CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_LN824141	Defluviitoga tunisiensis isolate L3 chromosome I	18 crisprs	cas3,csa3,DEDDh,cas6	0	14	4	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LN824141_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_1

13315-13443

Orphan

Consensus_repeat	Method
GGCGGAGCCCTCCCTCTGCCTTTGGTACAAGTACCAAAAAAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_1

>merge|NZ_LN824141|1|13315-13443|CRISPRCasFinder
GGCGGAGCCCTCCCTCTGCCTTTGGTACAAGTACCAAAAAAGATTGTAATTATTAATTATCGTTTTTGAAATTTATAGTGGGTCCAGGGCGGAGCCCTCCCTCTGCATTTGGTACAAGTACCAAAAAAG

>NZ_LN824141|1|1|13315-13443|CRISPRCasFinder
GGCGGAGCCCTCCCTCTGCCTTTGGTACAAGTACCAAAAAAG	ATTGTAATTATTAATTATCGTTTTTGAAATTTATAGTGGGTCCAG
GGCGGAGCCCTCCCTCTGCATTTGGTACAAGTACCAAAAAAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_171820561.1\|12816_13200_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045086996.1\|19993_21064_+\|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase	unknown	unknown	gnl\|CDD\|340818
NZ_LN824141.1\|WP_052670173.1\|13574_15077_+\|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase	unknown	unknown	gnl\|CDD\|234660
NZ_LN824141.1\|WP_171820562.1\|25878_26490_-\|ComF-family-protein	unknown	unknown	gnl\|CDD\|223970
NZ_LN824141.1\|WP_045086997.1\|21125_22481_+\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_LN824141.1\|WP_045086995.1\|18879_20007_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	unknown	unknown	gnl\|CDD\|274232
NZ_LN824141.1\|WP_045086998.1\|23184_25872_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|223690
NZ_LN824141.1\|WP_045087000.1\|26497_27766_-\|HEAT-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|237512
NZ_LN824141.1\|WP_045086994.1\|17573_18893_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	unknown	unknown	gnl\|CDD\|223842
NZ_LN824141.1\|WP_045086987.1\|7306_8662_-\|HlyC/CorC-family-transporter	unknown	unknown	gnl\|CDD\|224173
NZ_LN824141.1\|WP_045086992.1\|15077_16367_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|273468
NZ_LN824141.1\|WP_045088481.1\|3426_4839_-\|cysteine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234705
NZ_LN824141.1\|WP_045086990.1\|11582_12590_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224338
NZ_LN824141.1\|WP_045086993.1\|16632_17577_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	unknown	unknown	gnl\|CDD\|234638
NZ_LN824141.1\|WP_144403439.1\|9616_10741_-\|molecular-chaperone-DnaJ	unknown	unknown	gnl\|CDD\|274090
NZ_LN824141.1\|WP_052670494.1\|2721_3135_-\|chemotaxis-protein-CheX	unknown	unknown	gnl\|CDD\|381734
NZ_LN824141.1\|WP_045086986.1\|6933_7332_-\|cytidine-deaminase	unknown	unknown	gnl\|CDD\|223372
NZ_LN824141.1\|WP_045086985.1\|6352_6886_-\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|239516
NZ_LN824141.1\|WP_052670172.1\|10740_11394_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|366423
NZ_LN824141.1\|WP_045086984.1\|4847_6314_-\|glutamate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234953

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045086995.1\|18879_20007_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	gnl\|CDD\|274232	TIGR02614, Putative_lipid_II_flippase_FtsW, cell division protein FtsW. This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	7.45999e-62
NZ_LN824141.1\|WP_045086996.1\|19993_21064_+\|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase	gnl\|CDD\|340818	cd03785, GT28_MurG, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	2.7705e-87
NZ_LN824141.1\|WP_052670173.1\|13574_15077_+\|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase	gnl\|CDD\|234660	PRK00139, murE, UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional.	6.42763e-156
NZ_LN824141.1\|WP_171820562.1\|25878_26490_-\|ComF-family-protein	gnl\|CDD\|223970	COG1040, ComFC, Predicted amidophosphoribosyltransferases [General function prediction only].	9.52375e-34
NZ_LN824141.1\|WP_045086997.1\|21125_22481_+\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	6.58801e-141
NZ_LN824141.1\|WP_045086998.1\|23184_25872_+\|CBS-domain-containing-protein	gnl\|CDD\|223690	COG0617, PcnB, tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis].	1.30829e-54
NZ_LN824141.1\|WP_045087000.1\|26497_27766_-\|HEAT-repeat-domain-containing-protein	gnl\|CDD\|237512	PRK13800, PRK13800, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	6.12063e-05
NZ_LN824141.1\|WP_045086994.1\|17573_18893_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	gnl\|CDD\|223842	COG0771, MurD, UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell envelope biogenesis, outer membrane].	1.0773e-103
NZ_LN824141.1\|WP_045086987.1\|7306_8662_-\|HlyC/CorC-family-transporter	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	2.31374e-125
NZ_LN824141.1\|WP_052670172.1\|10740_11394_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|366423	pfam01025, GrpE, GrpE.	4.95979e-23
NZ_LN824141.1\|WP_045088481.1\|3426_4839_-\|cysteine--tRNA-ligase	gnl\|CDD\|234705	PRK00260, cysS, cysteinyl-tRNA synthetase; Validated.	0
NZ_LN824141.1\|WP_045086990.1\|11582_12590_-\|hypothetical-protein	gnl\|CDD\|224338	COG1420, HrcA, Transcriptional regulator of heat shock gene [Transcription].	1.80762e-47
NZ_LN824141.1\|WP_045086993.1\|16632_17577_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	gnl\|CDD\|234638	PRK00108, mraY, phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional.	1.6139e-101
NZ_LN824141.1\|WP_144403439.1\|9616_10741_-\|molecular-chaperone-DnaJ	gnl\|CDD\|274090	TIGR02349, Chaperone_protein_DnaJ, chaperone protein DnaJ. This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.	5.66388e-150
NZ_LN824141.1\|WP_052670494.1\|2721_3135_-\|chemotaxis-protein-CheX	gnl\|CDD\|381734	cd17906, CheX, chemotaxis phosphatase CheX. This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.	9.57504e-31
NZ_LN824141.1\|WP_045086986.1\|6933_7332_-\|cytidine-deaminase	gnl\|CDD\|223372	COG0295, Cdd, Cytidine deaminase [Nucleotide transport and metabolism].	1.11228e-60
NZ_LN824141.1\|WP_045086985.1\|6352_6886_-\|NUDIX-hydrolase	gnl\|CDD\|239516	cd03424, ADPRase_NUDT5, ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.	8.79281e-53
NZ_LN824141.1\|WP_045086992.1\|15077_16367_+\|hypothetical-protein	gnl\|CDD\|273468	TIGR01143, murF, UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase. This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	1.95628e-84
NZ_LN824141.1\|WP_045086984.1\|4847_6314_-\|glutamate--tRNA-ligase	gnl\|CDD\|234953	PRK01406, gltX, glutamyl-tRNA synthetase; Reviewed.	0

>NZ_LN824141.1|WP_171820561.1|12816_13200_+|hypothetical-protein
MIISDKINCGTHITVQQVRRNNRRLQKFYDAKYFDLRTGEKVNGQELNCGRRTRNKNLNTENLRKYSEKKVSPGRISIRKRRYPYKLGDTVLYDWQKCIIKGVQKLGTYIKLSKISNPVKISQVRVL
>NZ_LN824141.1|WP_045086990.1|11582_12590_-|hypothetical-protein
MNIRLQERQKEILKSIVEIYIKTNKPVSSEDVLNNSNIKASSATIRNDMQKLQKLGYIYQQHSSGGRIPLDPALKIYFEMIKEAYDVKVNHIELPKKYKFYDLNLLFQNLALLISQVLEGLVIFEYPNPKYVYITRVTVTPLTEENSVITILTNLGLAISRTVEIYGLPVSEELEKILNNALVGKSFEKIFSFLSTKQIEIEDLRITNFVEILEHLTDEFKRVRYISVGLEKIISKSQPDLDTIVTLAILVENDKIKEEFFTRLDFSPDIKVFFGKDINSKTLKNLAFFTTTYILNTNILGKVLFITEKYCNYEKIYLILKEYTSRLSEIISKNF
>NZ_LN824141.1|WP_052670172.1|10740_11394_-|nucleotide-exchange-factor-GrpE
MEDKKEVIEKNCGKNNMNGESNSNVTKNVDSLDENVEALQREIQELKDRIEKIKDEREKYKDSLYRLSAKFEHYKEMVEKEKRNIQFNTKKNIVELFLIPFEKLKISMKYKDDPEFIKAIEMIYKDIINVFKNLNLEFIVPEKGDQFDPFEHEVVEKFETDEVNEYCIYDVQSIGYKLEGEVIKPARVVVAIKPKDIIEKGCKSQNSEEEEDKEGDQ
>NZ_LN824141.1|WP_144403439.1|9616_10741_-|molecular-chaperone-DnaJ
MMPERKDYYKILGVDRNATPDEIKQAYRQKVKEWHPDRHIEDKDIAEEKFKEIQEAYEVLSDPEKRKLYDRFGFVPDESTTYANQRTGGGFEDVFRDFFGDAGSPFGDFFDMFFGSEPGRSGSSTKKRRRQERGEDIHVVMNLRLEEILYDVKKIVEYNRYVICESCKGTGAENGTNFETCPRCNGEGIIREEVRSFFGSYVRSYTCPTCDGVGEIINRKCSNCNGTGKIFKKENVEVNIPAGVLDGYTMKVRGKGNAVKNGGPYGDLIVQVRVLPHEKFIRRGSDLETEVTINYIKAVLGGKIKIPTLEGVIEEEIKEGTNPGTVIRIKNLGLPEFGGGRRGDLYVKINVEIKKPSRKEKKILQQLAEEMNVE
>NZ_LN824141.1|WP_045086987.1|7306_8662_-|HlyC/CorC-family-transporter
MDDPGSLWGSLIFLIVLLIMSGFFSASEISLTAIGRYKIRELIDNEKNDKKKKKYKDFIDNPNHYLTTILVMNNIVNILATSMATVFAVRLIPSSQGTTVGVVTAIMTLLILIFGEITPKVYAREISVKFFNFSFPIIYYLNTILSPIVWLLVSLSNIVIRTFGGETIKNAPPLITENEIISYLDISHEEGVIEKSEKYLMQRSLEMKDTPVKEIMTPRVDIVAIENTETVEELINIINEEGYSRIPVYKESLDNIVGIVYAKDIFQKIEELGDLEKVMKIRVSDIMRRPFFVPLTMNIRDVFKLFLTYHTHIAIVVDEYGGTAGLVTLEDIIEEMTGDIFDEYDDFSDEINIKKIEENSILVDGATPINDIERELDIDFPETEFETIGGFLLEHFKRFPKPGEKFTIDNYEFEIISVTVNRIDKVKITVHPEKNVEEGDEKKDEESNDSK
>NZ_LN824141.1|WP_045086986.1|6933_7332_-|cytidine-deaminase
MKNQTIVNKLYEEALKARENAYAPYSKYKVGAALLTEDDEIITGCNVENASYGLTICAERNAIFSAVARGKTKFKSLLVVAEGEGLAKPCGACRQVMNEFGDFDVYLANTKGDIEKSTVSELLPKSFGPKDL
>NZ_LN824141.1|WP_045086985.1|6352_6886_-|NUDIX-hydrolase
MKLMEQEVSKELIFKGKILNLEKYNVRLPNGNISTREVVDNPGAVAVLPIDEEGYIYFVKQYRFPIREVLIEIPAGKFDSPNEDPLECGKRELEEETGLMAKEWIYLGYIYTTPGFSNEKIHLYAAKELHNVGSKPDDDEFVEVVKIYSDDVEQMIKTGGITDSKSICAFYRYKLLT
>NZ_LN824141.1|WP_045086984.1|4847_6314_-|glutamate--tRNA-ligase
MISDVVRTRFAPSPTGFLHVGGARTALFNYLFSKRYNGEFILRIEDTDLERSTKESEDQLLRTLKWLDLKWDEGPIVGGPYGPYRQSERLDLYQTKAYELVNNDRAYEAYIYPEEMEEIKSQLLSVGKPPHYTYELISKYNTQERINEYKEKGLKPVVFLKMPQKDYQINDLIKGEVVFKKGAIGDFIILRSNGVPTYNFAVVVDDIAMKITHVIRGDDHLSNTLRQVAIYEAFSAEIPEFAHVSMILGPDGKKLSKRHGATSVEEFIKKGILPEALVNYLALLGWSHPEGKEIMDIEEIIFNFSLDRVSSSPAIFDEAKLKWMNGQYLHSKSIEEIYSLAEPFIIESNLLTKEQYEVNKTWIMKAIETIITSVETLSEIPDAISVFLKDITPNLGDQEFLDYFNKDGVREAITLFYEYTQETDKWDTEMITENLKKAIKEAKPQKKAFYMALRKILTDSFHGPDLVNTIYLIGRNRIIQRLERVVQV
>NZ_LN824141.1|WP_045088481.1|3426_4839_-|cysteine--tRNA-ligase
MKIYDTLLGKVVDFIPLKEDEVKIYLCGPTVYNLIHIGNARPIITFDAYRRFLEYIGYKVTIVQNFTDIDDKIINQAYKEQVSFDKIAKRYIIEYWKDMVALKVRAFNFHPKTSNYIEEIICYIDNLIKKGFAYTAENGDVYFNVRKLTNYGELSHRNTKDLISGSRIEISEYKKDPLDFALWKSSKEGEPFWVSPWGKGRPGWHIECTVMATELLGDAFDIHAGGNDLIFPHHENERAQAIASEKQFAKYWMHNGMIQLSQNKMSKSLGNVWLVRDLLKQFDSDVLKVFIFSKHYRAPIDVNEELLRSQEISVKRVRQSLKESEEYFQGVVPYSKEGEYFKEQEHYLLEQLSNDFNTPSAMARLFDLSRELNKALKSKNDTMIIDNYYLIKNVYGSVFGIFESDAEIEMHEVDAENIIKILLEVRSSLRDNKLYELSDYIRDSLQEIGIELKDTPEGTKYIFKSGKSEA
>NZ_LN824141.1|WP_052670494.1|2721_3135_-|chemotaxis-protein-CheX
MAKKELKVDKPKLVQEIQKDYDVVTNIGFTGVLEGNIIYSFSEKEAINLVNEMMQGIMNINELDDMAISAIGEFGNMISGAIATHLEQYGYLIKVTPPSVMRGKIVKVNVRGTILLFPLYVSGNNEMDLYFVYKETR
>NZ_LN824141.1|WP_052670173.1|13574_15077_+|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase
MKLKANDFKLLLEGNIKSFSLNGEEIIVEGIKDNSSEVKNNDIFIAVKGHKADGHDYINYALGNGASLIIAENEDKLPKDKLINYIIVKDIKKATADLVYSLNNISIDDFSIVGVTGTNGKSTSVSLVHHILTESGLNSTLISTVEIKINNQIIKQPRNTTPGILEIAELLKLSSESNSKIINIEVSSHAIDQRRIENLKFDIISYTNITRDHLDYHKNFEDYKKTKLSLMNFLKENGKIIINIDKLNKKDFYSSNKALITYGFDESADYVIKNFEQNIHQVKFTMKTIDNEFVEIVSPLVGKFNIYNIVNAFIIAKLLGIETELIIKAVSSFKGIPGRFQLVPSSKSLGFNCVIDFSHTPDALEQVLSTAASLTDGRIIIVFGAGGNADQGKRKIMGEVVSQKADVIILTNDDPKDEDPQKIIEDVLEGIDQTKQFLVIPDRKTAIEAALSFANKGDIVLITGRGHEQFQLFANGKKVKFNDYEVATKCIETIKRGLRR
>NZ_LN824141.1|WP_045086992.1|15077_16367_+|hypothetical-protein
MLEELKKKGYKFQIDSRKIKSGEVFLCLKGENTDGHFFIEDALKNGADFVVIDNPSFVNNLPNNKIIKVDNVLEEMLISSSKIVNNNSKIKIGITGSTGKTTTKECLYHLLSPFFTTFRNELNMNTEIGIPLSILNQYSNEDVSIIEIGLKQKGDLDFVTRFYKLDVAFITNVGPSHLEFLETIENVAQEKMKITNNMNKGLLILNGDYPILKELAPKRLKTLSFGLKKSNDAVLEGYEYNLNYTTTFYAKILGNHLMLTLNKYWSEGQILDLLSTLLFLTYIELPLDPFIICNIDIPEGRFQTITRENTLVINDSYNASYDSFNSAFKSISQIDFYPKILVMGEMKELGEYSKYYHEKVLSEAKEIFDEIYIYDPDNKLNYLLQNQDKIIKFESLDDITKIISEIKEGLIYIKASNSTGIYEYLKNNL
>NZ_LN824141.1|WP_045086993.1|16632_17577_+|phospho-N-acetylmuramoyl-pentapeptide--transferase
MNYTLFLLSVCAFGLLIFLYPIYINWLKKKQFGQYIRPEGPDLHNYKQGTPTMGGLLFVIAMFLLLLVTFFLTNDFLFLLMAISIILFGLVGFIDDYSSIKKKNATGLNVIQKLGLQLLFSAFIVILIYKFNYHTHLKIPFSRNIIDLKYFYPVWGVLYLTGMTNATNLTDGLDGLAGGIYIISAFFTAIVAGLNFESTSILILPVIAYLFFNIKPAKIFMGDTGSLALGGLLGCLALYSSIELFTLFTCFIFILEMFSVIIQVGSFKLRKKRVFLMAPIHHHFELKKWSEERVVMIFWLVNFLVGFIALGGLL
>NZ_LN824141.1|WP_045086994.1|17573_18893_+|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase
MKICLVGYGISNKDLLNKIKNSKDEIFVSQNRDFSKEEKIFFEANNIKYEIEHGDLLKKCDLAIVSPGISPQSDAAKIIFDYNINYTTEVEYSWQLIKKVNKESIFIAITGTDGKSTTTSLIGHILKHYEPLTFVGGNLGIPLINAPEDLQNYVVEVSSFQIFWSKIFSPEISVLINLAPDHLNWHHDLKDYYSTKEKLLRRSVDNGGIAIVNEDAKNNLTIHEHKNENSLLFFSKDMFDGKYVTYKNKNVKIDNDIFMLDILKEDLIAAVVTSLNLGIPENLISEAVSSFKPLKYRLEFVDEINKIKFYNDSKATNAHSAYNAYKSFRGKKYIAILGGIPKNEDLSSLLNELDQYAKAVFVFGKMRDELIKYSLDDKFIFYDNLEDVFLHLPEFWEPNDNIVFSPAGASFDLYNNFEERGKHFEFLVNKLRKLYYESF
>NZ_LN824141.1|WP_045086995.1|18879_20007_+|FtsW/RodA/SpoVE-family-cell-cycle-protein
MRASKENIKTNFLFFFIVLGITLFVGIMFVYSSLFAMQNIKEINPEQKFKTYIIGLIIGFIGAIFAFLFGNLFIKNSLIMLAFYIFLNMFLGIVLFAPPIAGVTRWMNFGPFQFQPSELAKLILPAFLAFYYSKLKNKKNILTNVLIPLILCLLSIFLIFLEPDLSTTLLILVISLITMFLGIEDKSVLIFFIVFMLVLGITIFIFQDKFLQSYQISRLTKEDPFQSQRARDAITGGGLAGKGPFAGEEKYYVPESYSDFIIAVIGEEWGKIGIAIVVTLFLFLCHELVYMAYLTKDSATFIFCGATASWIFIQVMINTLVGLGIPWMPVTGVTLPLMSYGNSSMIVTLTAIGWALGLIYNNSDIRKTGEENEEQ
>NZ_LN824141.1|WP_045086996.1|19993_21064_+|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase
MKNNKRLKVVFCGGGTGGHYYPALALLKYLDTNYQNLDIIYFATKGRIEEHNLAKDFPKAKMYTLDTKGLERPIYNPKNITRMFAVLKDTQKVRKIIKTFNPDFAFLTGGYVTVPVGLALTKEKIPFYLHEQNSIMGISNKFLTKYAKKVFVSFEETLINEKCILSGNPVRTPDEKLTREYLKKFGINNLNKRCILVFGGSLSSEEIDDIMYRVYLQDKSTNYIHITKNPDKFSKFENVHTFDYINDLYKIMAVCDGVVCRAGATTIAEILFYDLQAALIPWKGAAENHQFKNALSLQKLGKAEVFDDQNIDLTKLINFINSIKIKSQNYEYVPKHNQAIEIIINNIEEIKKFNNF
>NZ_LN824141.1|WP_045086997.1|21125_22481_+|UDP-N-acetylmuramate--L-alanine-ligase
MRYYFSGIGGIGMSSLALYKYYVSGVENVCGSNNEINERVEYLQRKGIKVKLEQNYSLPDVDILVRSTAVKDNNPEILEAKKRNIKVLYRMQLLNEILKNHLSIGITGTDGKTTTTAMLSQIFKDAKKDPTVFLGGIHSSLEDGNFRYGNDLIIAEVDESDGFIKDTCTDYSIVTNLRPDHLEHYDNKFKNLEYSIFQFINNTRRLIFLCKDDPVLSSWNLVGKNVLYFGLRNDSDYILKNRVQNEKIQEFEVYKKDKLFGKITLKLPGLHYAYDALASCALALEFGIDFQSIRDSLYNYISVDRRFNIIFKNDDICIIDDYAHTPDEILATIKATKEYFPGKKIITIFQPHRFSRLYFHLNDFVEVLKNSDKVYVYRLYSAFEEPLNGVDERTIVELLKAQNTPSQFYNAEEAIFSDLLEEQNAILLFVGAGDITNVARKFAKIKDNSLT
>NZ_LN824141.1|WP_045086998.1|23184_25872_+|CBS-domain-containing-protein
MKPKVLITTHKNPDFDAFAASIAASLLYQDSIIIIDSEPQQNLKEFLNIYDIPYKKSHEFEDEFEEQIKNKNFDKIVVVDTSDINRIPESIKFLIEEGLPVDIYDHHPELKEQNINGNNFSKPVGSSTTILVEILFEKGVPFSDTLKTLFLIAIHEDTGNFVYPTTSWEDHDIAARLIKTGARVEEIEEFVSLEMTQEQKILFDKLYNNIEEFYLDEICVNIAYAESEKFIGGLNIITHKLFETLTPDVLFVIVKIAKTIYIVARSKSNQIDLNKILTSFGGGGHKKAGAAKVKGQSPTKVINKIKSELKSSFIPVLKAKHIMSSPVRTILSNETVQRAYEIMYQTGHSGLPVIENNKLVGMVTKKDIEKAMNHGLKNAPVKSVMSTNLKVADVETSLSQIRRMMAEEDIGRIPIIKDGILVGIITRTDLVRASNGVFNFSVNPLLKEKYESQNLKKYMEEFLPPSILNLLRLLGDYGNEQNVNVYVVGGFVRDLLLAIKSKQQNDKNTKKFLFMDYDIDIVVEAEALTFGRYAAKQLNAKYVEHEKFHTCSLFYRISHKIIRIDIATARTEYYEEAGELPTVEFSTIKKDLARRDFTINAMAIKLNPESFGILLDFFNSRKDLDEKQIRILHPLSFIEDPTRVLRAIRFEQRFGFEIEPYTLNKLIEAVEGKYLEKVTGMRLREEFEKILNEPEPLKAIERMGNLNIISHLFEKTYYTPTLQKELEKLFQVIDFFNNNLKSYTKNVRIFHVVLYVLVQYTPVESLKRVVQRYGLPKDYISKLQQVNSLYEEINDLIKESFGKQYKDIFKPSFFYERCSSLDNEQLIFMATKIPDDILSYFYNYLKKLDELTLLISGKDLLKKGYKGKEIKIKLEEIKKKLLDDEIKPGEELSLI
>NZ_LN824141.1|WP_171820562.1|25878_26490_-|ComF-family-protein
MDTMFEPYCIICKSKISFGKIVCENCLKKTYAPSLTEGDFKVYHYGKYEEPLSQLITEFKYNSHPKIGKIFGEKLASLFLKLNFPALNYYVSYVPSNYISKFEKGFVPAKLIAIYFSSILGFPLIDLFISKALKKQAQLSYKQRSKNVHNKIRLIQSPPENIIVVDDVYTTGSTMNEIANLLENKCEVIIGLTMAKTIHNHSL
>NZ_LN824141.1|WP_045087000.1|26497_27766_-|HEAT-repeat-domain-containing-protein
MANEIIETYKLLEERIRSENVQIYFDMLDSPYPAFKSKAIQELTKQKIQTPIVKDFLQDPDKDVRFAAYRYLEKMGLLDEKTVKESLKDISPNIRKEAIISYISMGMEPIEYILDFAKDPDPIVRYQLLTTFLEFYPEDSNKLIEILKDDPYIKIRQLIYALDNISDTLVSINIEKSVKTMALKRYYEASDSITFFNTLKEVYFECDIDTKNLIIKFFSGIPCEIINQFMDKVMNEESNLIILQNAAKTSKKVCGIDAIPSWLIEKFIQSDDARIVKYGLSLATEKEDMGYVELCREFLDAIDDDLVIGATDYLLHFQDYSLVDYVSDFLNSLSSKRIREGLKIIRKLKLENFVGDASNIASNKIYPVSIRKSAINLLKFFKAKDYWEIPHQILKDPYESGSLKLAALNALLRLNAEMVVNI

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Crispr_ID: NZ_LN824141_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_2

28927-29049

Orphan

Consensus_repeat	Method
AACTATTTGGTACTTAAGGAAGGAAGGAGGGCTTTGCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_2

>merge|NZ_LN824141|2|28927-29049|CRISPRCasFinder
AACTATTTGGTACTTAAGGAAGGAAGGAGGGCTTTGCCCTAGACCCTTATAAATCAAAATTCCTTACTAATTATTCTTTCTTTAAACTATTTGGTACTTAAGGAAGGAAGGAGGGCTTCGCCC

>NZ_LN824141|2|2|28927-29049|CRISPRCasFinder
AACTATTTGGTACTTAAGGAAGGAAGGAGGGCTTTGCCC	TAGACCCTTATAAATCAAAATTCCTTACTAATTATTCTTTCTTTA
AACTATTTGGTACTTAAGGAAGGAAGGAGGGCTTCGCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_052670498.1\|37262_39761_-\|alpha-amylase	unknown	unknown	gnl\|CDD\|200459
NZ_LN824141.1\|WP_045086995.1\|18879_20007_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	unknown	unknown	gnl\|CDD\|274232
NZ_LN824141.1\|WP_045086996.1\|19993_21064_+\|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase	unknown	unknown	gnl\|CDD\|340818
NZ_LN824141.1\|WP_045086994.1\|17573_18893_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	unknown	unknown	gnl\|CDD\|223842
NZ_LN824141.1\|WP_045087004.1\|29747_30518_-\|patatin-like-phospholipase-family-protein	unknown	unknown	gnl\|CDD\|366777
NZ_LN824141.1\|WP_045087005.1\|30514_31318_-\|patatin-like-phospholipase-family-protein	unknown	unknown	gnl\|CDD\|132844
NZ_LN824141.1\|WP_045086997.1\|21125_22481_+\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_LN824141.1\|WP_045087003.1\|29127_29751_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087000.1\|26497_27766_-\|HEAT-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|237512
NZ_LN824141.1\|WP_171820563.1\|35848_37210_+\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|240542
NZ_LN824141.1\|WP_045087007.1\|33459_35157_-\|PEGA-domain-containing-protein	unknown	unknown	gnl\|CDD\|285503
NZ_LN824141.1\|WP_045087002.1\|28270_28786_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_171820562.1\|25878_26490_-\|ComF-family-protein	unknown	unknown	gnl\|CDD\|223970
NZ_LN824141.1\|WP_045087010.1\|40272_40830_-\|elongation-factor-P	unknown	unknown	gnl\|CDD\|234788
NZ_LN824141.1\|WP_045087001.1\|27810_28257_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087008.1\|35167_35611_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_LN824141.1\|WP_045087011.1\|41168_41366_+\|cold-shock-protein	unknown	unknown	gnl\|CDD\|224197
NZ_LN824141.1\|WP_045086993.1\|16632_17577_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	unknown	unknown	gnl\|CDD\|234638
NZ_LN824141.1\|WP_045087006.1\|31383_33456_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274009
NZ_LN824141.1\|WP_045086998.1\|23184_25872_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|223690

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_052670498.1\|37262_39761_-\|alpha-amylase	gnl\|CDD\|200459	cd11320, AmyAc_AmyMalt_CGTase_like, Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	3.20646e-94
NZ_LN824141.1\|WP_045086995.1\|18879_20007_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	gnl\|CDD\|274232	TIGR02614, Putative_lipid_II_flippase_FtsW, cell division protein FtsW. This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	7.45999e-62
NZ_LN824141.1\|WP_045086996.1\|19993_21064_+\|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase	gnl\|CDD\|340818	cd03785, GT28_MurG, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	2.7705e-87
NZ_LN824141.1\|WP_171820562.1\|25878_26490_-\|ComF-family-protein	gnl\|CDD\|223970	COG1040, ComFC, Predicted amidophosphoribosyltransferases [General function prediction only].	9.52375e-34
NZ_LN824141.1\|WP_045087005.1\|30514_31318_-\|patatin-like-phospholipase-family-protein	gnl\|CDD\|132844	cd07205, Pat_PNPLA6_PNPLA7_NTE1_like, Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.	3.98594e-46
NZ_LN824141.1\|WP_045086997.1\|21125_22481_+\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	6.58801e-141
NZ_LN824141.1\|WP_045086994.1\|17573_18893_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	gnl\|CDD\|223842	COG0771, MurD, UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell envelope biogenesis, outer membrane].	1.0773e-103
NZ_LN824141.1\|WP_045087000.1\|26497_27766_-\|HEAT-repeat-domain-containing-protein	gnl\|CDD\|237512	PRK13800, PRK13800, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	6.12063e-05
NZ_LN824141.1\|WP_171820563.1\|35848_37210_+\|MATE-family-efflux-transporter	gnl\|CDD\|240542	cd13137, MATE_NorM_like, Subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins similar to Thermotoga marina NorM. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	2.72424e-129
NZ_LN824141.1\|WP_045087007.1\|33459_35157_-\|PEGA-domain-containing-protein	gnl\|CDD\|285503	pfam08308, PEGA, PEGA domain. This domain is found in both archaea and bacteria and has similarity to S-layer (surface layer) proteins. It is named after the characteristic PEGA sequence motif found in this domain. The secondary structure of this domain is predicted to be beta-strands [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].	0.000320666
NZ_LN824141.1\|WP_045086993.1\|16632_17577_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	gnl\|CDD\|234638	PRK00108, mraY, phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional.	1.6139e-101
NZ_LN824141.1\|WP_045087008.1\|35167_35611_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	2.211e-24
NZ_LN824141.1\|WP_045087004.1\|29747_30518_-\|patatin-like-phospholipase-family-protein	gnl\|CDD\|366777	pfam01734, Patatin, Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.	1.5923e-15
NZ_LN824141.1\|WP_045087011.1\|41168_41366_+\|cold-shock-protein	gnl\|CDD\|224197	COG1278, CspC, Cold shock proteins [Transcription].	2.84928e-31
NZ_LN824141.1\|WP_045087010.1\|40272_40830_-\|elongation-factor-P	gnl\|CDD\|234788	PRK00529, PRK00529, elongation factor P; Validated.	5.07817e-90
NZ_LN824141.1\|WP_045087006.1\|31383_33456_-\|hypothetical-protein	gnl\|CDD\|274009	TIGR02169, chromosome_segregation_protein_related_ptotein, chromosome segregation protein SMC, primarily archaeal type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	1.18651e-10
NZ_LN824141.1\|WP_045086998.1\|23184_25872_+\|CBS-domain-containing-protein	gnl\|CDD\|223690	COG0617, PcnB, tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis].	1.30829e-54

>NZ_LN824141.1|WP_045087002.1|28270_28786_-|hypothetical-protein
MKKFFISAIVLLFSLLCFSQVRYDLGFSVLNEKSEFDLALRVGLESNDFNFSFDFSPSFNDTLSLITIMDVSAEIWEINDNLSLDAGLLWMNDKSKRGTYAYSALDIYFKGISSKICVGYPFKSKKEFLDYFVIKIGYEVPKPLNFIDDLKMELRLVNGRIDFSIFLVEPF
>NZ_LN824141.1|WP_045087001.1|27810_28257_-|hypothetical-protein
MKRKEGFLLVESIFELFIVSISMLIVLSTFIGTFFLLKDALEEIIDLNILSNTVMEIIIVSKNEMKNVTSLSSGQFSSSILGDSVEGGKVGFSFDSLTQKLLRYKYSNITKGYTFISQKITAFSYDGKFIIVTLDRDYIIKLFVKDLR
>NZ_LN824141.1|WP_045087000.1|26497_27766_-|HEAT-repeat-domain-containing-protein
MANEIIETYKLLEERIRSENVQIYFDMLDSPYPAFKSKAIQELTKQKIQTPIVKDFLQDPDKDVRFAAYRYLEKMGLLDEKTVKESLKDISPNIRKEAIISYISMGMEPIEYILDFAKDPDPIVRYQLLTTFLEFYPEDSNKLIEILKDDPYIKIRQLIYALDNISDTLVSINIEKSVKTMALKRYYEASDSITFFNTLKEVYFECDIDTKNLIIKFFSGIPCEIINQFMDKVMNEESNLIILQNAAKTSKKVCGIDAIPSWLIEKFIQSDDARIVKYGLSLATEKEDMGYVELCREFLDAIDDDLVIGATDYLLHFQDYSLVDYVSDFLNSLSSKRIREGLKIIRKLKLENFVGDASNIASNKIYPVSIRKSAINLLKFFKAKDYWEIPHQILKDPYESGSLKLAALNALLRLNAEMVVNI
>NZ_LN824141.1|WP_171820562.1|25878_26490_-|ComF-family-protein
MDTMFEPYCIICKSKISFGKIVCENCLKKTYAPSLTEGDFKVYHYGKYEEPLSQLITEFKYNSHPKIGKIFGEKLASLFLKLNFPALNYYVSYVPSNYISKFEKGFVPAKLIAIYFSSILGFPLIDLFISKALKKQAQLSYKQRSKNVHNKIRLIQSPPENIIVVDDVYTTGSTMNEIANLLENKCEVIIGLTMAKTIHNHSL
>NZ_LN824141.1|WP_045086998.1|23184_25872_+|CBS-domain-containing-protein
MKPKVLITTHKNPDFDAFAASIAASLLYQDSIIIIDSEPQQNLKEFLNIYDIPYKKSHEFEDEFEEQIKNKNFDKIVVVDTSDINRIPESIKFLIEEGLPVDIYDHHPELKEQNINGNNFSKPVGSSTTILVEILFEKGVPFSDTLKTLFLIAIHEDTGNFVYPTTSWEDHDIAARLIKTGARVEEIEEFVSLEMTQEQKILFDKLYNNIEEFYLDEICVNIAYAESEKFIGGLNIITHKLFETLTPDVLFVIVKIAKTIYIVARSKSNQIDLNKILTSFGGGGHKKAGAAKVKGQSPTKVINKIKSELKSSFIPVLKAKHIMSSPVRTILSNETVQRAYEIMYQTGHSGLPVIENNKLVGMVTKKDIEKAMNHGLKNAPVKSVMSTNLKVADVETSLSQIRRMMAEEDIGRIPIIKDGILVGIITRTDLVRASNGVFNFSVNPLLKEKYESQNLKKYMEEFLPPSILNLLRLLGDYGNEQNVNVYVVGGFVRDLLLAIKSKQQNDKNTKKFLFMDYDIDIVVEAEALTFGRYAAKQLNAKYVEHEKFHTCSLFYRISHKIIRIDIATARTEYYEEAGELPTVEFSTIKKDLARRDFTINAMAIKLNPESFGILLDFFNSRKDLDEKQIRILHPLSFIEDPTRVLRAIRFEQRFGFEIEPYTLNKLIEAVEGKYLEKVTGMRLREEFEKILNEPEPLKAIERMGNLNIISHLFEKTYYTPTLQKELEKLFQVIDFFNNNLKSYTKNVRIFHVVLYVLVQYTPVESLKRVVQRYGLPKDYISKLQQVNSLYEEINDLIKESFGKQYKDIFKPSFFYERCSSLDNEQLIFMATKIPDDILSYFYNYLKKLDELTLLISGKDLLKKGYKGKEIKIKLEEIKKKLLDDEIKPGEELSLI
>NZ_LN824141.1|WP_045086997.1|21125_22481_+|UDP-N-acetylmuramate--L-alanine-ligase
MRYYFSGIGGIGMSSLALYKYYVSGVENVCGSNNEINERVEYLQRKGIKVKLEQNYSLPDVDILVRSTAVKDNNPEILEAKKRNIKVLYRMQLLNEILKNHLSIGITGTDGKTTTTAMLSQIFKDAKKDPTVFLGGIHSSLEDGNFRYGNDLIIAEVDESDGFIKDTCTDYSIVTNLRPDHLEHYDNKFKNLEYSIFQFINNTRRLIFLCKDDPVLSSWNLVGKNVLYFGLRNDSDYILKNRVQNEKIQEFEVYKKDKLFGKITLKLPGLHYAYDALASCALALEFGIDFQSIRDSLYNYISVDRRFNIIFKNDDICIIDDYAHTPDEILATIKATKEYFPGKKIITIFQPHRFSRLYFHLNDFVEVLKNSDKVYVYRLYSAFEEPLNGVDERTIVELLKAQNTPSQFYNAEEAIFSDLLEEQNAILLFVGAGDITNVARKFAKIKDNSLT
>NZ_LN824141.1|WP_045086996.1|19993_21064_+|UDP-N-acetylglucosamine--N-acetylmuramyl--(pentapeptide)-pyrophosphoryl-undecaprenol-N-acetylglucosamine-transferase
MKNNKRLKVVFCGGGTGGHYYPALALLKYLDTNYQNLDIIYFATKGRIEEHNLAKDFPKAKMYTLDTKGLERPIYNPKNITRMFAVLKDTQKVRKIIKTFNPDFAFLTGGYVTVPVGLALTKEKIPFYLHEQNSIMGISNKFLTKYAKKVFVSFEETLINEKCILSGNPVRTPDEKLTREYLKKFGINNLNKRCILVFGGSLSSEEIDDIMYRVYLQDKSTNYIHITKNPDKFSKFENVHTFDYINDLYKIMAVCDGVVCRAGATTIAEILFYDLQAALIPWKGAAENHQFKNALSLQKLGKAEVFDDQNIDLTKLINFINSIKIKSQNYEYVPKHNQAIEIIINNIEEIKKFNNF
>NZ_LN824141.1|WP_045086995.1|18879_20007_+|FtsW/RodA/SpoVE-family-cell-cycle-protein
MRASKENIKTNFLFFFIVLGITLFVGIMFVYSSLFAMQNIKEINPEQKFKTYIIGLIIGFIGAIFAFLFGNLFIKNSLIMLAFYIFLNMFLGIVLFAPPIAGVTRWMNFGPFQFQPSELAKLILPAFLAFYYSKLKNKKNILTNVLIPLILCLLSIFLIFLEPDLSTTLLILVISLITMFLGIEDKSVLIFFIVFMLVLGITIFIFQDKFLQSYQISRLTKEDPFQSQRARDAITGGGLAGKGPFAGEEKYYVPESYSDFIIAVIGEEWGKIGIAIVVTLFLFLCHELVYMAYLTKDSATFIFCGATASWIFIQVMINTLVGLGIPWMPVTGVTLPLMSYGNSSMIVTLTAIGWALGLIYNNSDIRKTGEENEEQ
>NZ_LN824141.1|WP_045086994.1|17573_18893_+|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase
MKICLVGYGISNKDLLNKIKNSKDEIFVSQNRDFSKEEKIFFEANNIKYEIEHGDLLKKCDLAIVSPGISPQSDAAKIIFDYNINYTTEVEYSWQLIKKVNKESIFIAITGTDGKSTTTSLIGHILKHYEPLTFVGGNLGIPLINAPEDLQNYVVEVSSFQIFWSKIFSPEISVLINLAPDHLNWHHDLKDYYSTKEKLLRRSVDNGGIAIVNEDAKNNLTIHEHKNENSLLFFSKDMFDGKYVTYKNKNVKIDNDIFMLDILKEDLIAAVVTSLNLGIPENLISEAVSSFKPLKYRLEFVDEINKIKFYNDSKATNAHSAYNAYKSFRGKKYIAILGGIPKNEDLSSLLNELDQYAKAVFVFGKMRDELIKYSLDDKFIFYDNLEDVFLHLPEFWEPNDNIVFSPAGASFDLYNNFEERGKHFEFLVNKLRKLYYESF
>NZ_LN824141.1|WP_045086993.1|16632_17577_+|phospho-N-acetylmuramoyl-pentapeptide--transferase
MNYTLFLLSVCAFGLLIFLYPIYINWLKKKQFGQYIRPEGPDLHNYKQGTPTMGGLLFVIAMFLLLLVTFFLTNDFLFLLMAISIILFGLVGFIDDYSSIKKKNATGLNVIQKLGLQLLFSAFIVILIYKFNYHTHLKIPFSRNIIDLKYFYPVWGVLYLTGMTNATNLTDGLDGLAGGIYIISAFFTAIVAGLNFESTSILILPVIAYLFFNIKPAKIFMGDTGSLALGGLLGCLALYSSIELFTLFTCFIFILEMFSVIIQVGSFKLRKKRVFLMAPIHHHFELKKWSEERVVMIFWLVNFLVGFIALGGLL
>NZ_LN824141.1|WP_045087003.1|29127_29751_-|hypothetical-protein
MKKFISFVLVSFFIFISILSFPATINVKADSVKGEEKRYILTGNVFIQKDDLIITTDYATISLVNDDWRDVETNKVHIKGDSFEATSDYLIFDLQTEKGTLRYNVESNISIEESFIQIFCDELVLDNSKKLYEGFSKEHVLITKDDYSIKSKRFKYEESATLLSLFDNVKIVNESKKIDMDSQVAYFNTKTNEIEAQSVNLILQVED
>NZ_LN824141.1|WP_045087004.1|29747_30518_-|patatin-like-phospholipase-family-protein
MNLVMGGFFEGFYWESGVLEFLAKHEENLTIYTSSVGSLRGLFYSMYGENFFGRLKDFINKKNNPIKDIISSFELYNNLYAQTTALIRLGRGKMSLYEPQILKEFLKDYFGKDTLKSLNKDINFEVFELKSKKVVNLDKNTSIVDMLMMELAFPPYYPYYLYEDGYFIPSSFLSLIPQKFSSDSLIISFDSNLDYPIPKNTVEILLKVSYSRSLKNYQILTEKFTKIEPKKNLTSYFDMSAFFDGQSRIKEWWDNK
>NZ_LN824141.1|WP_045087005.1|30514_31318_-|patatin-like-phospholipase-family-protein
MKKYGLALGSGGARGAAHVGLIEIINKREINIEVVTGSSAGAIVGAFFALYPKANLVRVFDRVIKKNIDIINSNFKILNKKITNFPKMIAGKSFLQNDFVYDIYKELYGRKRFSECKIKLGIVSYDLESGQEIEITEGYIIDAVMASSNVPGVFPPLRLGGMQHLDGGVLNPIPVNFAKKLGANYVIASDLSYQSNNNIKYDNGLDFLLSIDDNKNDLMNRYELKNANEIYKYPLTYSWVDFSAFNDIYIQSKSYIIEQLEREGIQS
>NZ_LN824141.1|WP_045087006.1|31383_33456_-|hypothetical-protein
MQIRLFFTLLILVFSITIFSQVNIVDLPTSSPLYSQVIKMVETGIMSIDNQGRFRGTQEVLRYDLAEFGVNMLDYFDKRYNSQLNELSKKLLSLENQNLNSRINNIESTLFAYDDRLSYLNSSIIQLEQNVSDILAVIQPGHPLNKDNIVFQNILQSSKAVAQQAAEEEVRNIANDTLASLSMFEDRLIEFEKEVNMLNEKYDKSLESLSSLIVTVPQDTKEEFQNYIDITIEKEIDALKTSLRSIAKYQTALLESSLDSTLTSLDVRVTTLEGRISPYDSSLYDLRKKVEENEAKINYILTNYSSEATSLKRPDEYDLLGIKTDIEALKIRTDNFASDLSLLSDQVYENKSHIDTFEARQVLYDNKINEMQKKYESLVEQIINQNKKLDNIMYELSSLSQTGTQSQTIETSPIDIKNLQERVASLERTFGVYYDQVSQLSYYAVTFEDIQNNYSDLKRILDKNSTQVEELKQNLEVLSAQIKAITSLTDLNQDSLTTLKNMSTISQKLYSIESNLEILNRNNYNISNEVVALDNRLSNIEKTLGDFQVSSSEIKELKSAYDQLLSKYYDLKIEAEYYTDPKLLKDDLKIELYNELSSEIIVLDKNIVELDNNLKNLESRILQIEKAMIYYDENMSQVTFNTQETATKVVELEKKIEQKESKDFSTTFITSLLGVAVGALVTWLVLSTGD
>NZ_LN824141.1|WP_045087007.1|33459_35157_-|PEGA-domain-containing-protein
MNKKWNISNLAILVLLVVLCNILAFSSFGFSYIINIDALPGSAVYFGGNLLGIVKEVPAKFEIIDNSSGVLRILKNGYTDYIVSLSLIGSEATIVAEQVPLSKLLLNSELDELYLEYEYKGKKESVNIQGVKEIELPYIIDQIILKSEGYHEKIVKLDLKPFGKEEINVDLLGLDEIILDSLPQGADVYVEDMKVGTTPLKLKKDKLNKVIVKKEGYIEQTLENVNVNDKITIELKRGIEVFIDSTPKESGVFLNNKYIGTTPYYGIFEPGDYILTISKAGYETKELRSQFTENGINKYYVELNETKKLVGLLNSEDFEFNIDGKYLGKNIDYINLDNNMHLVKLSSDSGKMDFLISKDLIESNYYYDLRKISAINVYSIEEKVASLLGKTQNIPAFFVFHTLNGGQFVNVRTVSRTFSVFAEPSNSLDIFVDKGFGALFVTTNVKNPLIYIDDKFVSNDRLLGYPLKSGVHKVELRYLNEVRTQKVLIKEGDKTFLNFDFDIKIPVNVVCSEGRFAVNSQEYLSTSQLLYLKAGPNVFSNGTYSIVVFIYEPQYIDLDKLITGV
>NZ_LN824141.1|WP_045087008.1|35167_35611_-|MarR-family-transcriptional-regulator
MENDLLGQPAQMEKLIREICSKIKSEGRKVLKDFDISPAQFDVMQIIYFRGPKMLSDISKRLGITKSTTTGIVSRLETMGYLTKEKSPEDRRVYMVNITQKGKNIIEEVIETRVKLIEKVYNKLGDKVRTIEILNEINKIMNETKLS
>NZ_LN824141.1|WP_171820563.1|35848_37210_+|MATE-family-efflux-transporter
MEKDLTQGPLLRQILTMSIPTMIGYAAQMVYDLVDIYWVGKISSEAVAGVTLFSTIFWIVTALNEIIGSSSISLISQAYGQKDYEQTKIAIEQTISFKFLMASIAAVLIAVLLKPLMLLFSEADVVQHGLDYGYIRLFFLPIMFSSYSINTVFRCIGDSKIPMSIMILVSFLNVILDAVFMFETIPFTNLKGLNLGVFGAGLATVVSQTISFLIGFIILFTRTHNVKPSIKGLFKLNPQIDKKLLTIGLPNGIEIFFRNLSNIVVLGFVSMFGTAAIAANGIAGRLFGFAFVPLSGLTSGSSSVVGQCLGAENIQRAEKASHLAAVVATIIMSGSIFLAFGFGKEVILFFTKDPEVIKLGSDFLKFGSLGLVALGYGMGLASVFSASGYNFPYLVSSIFSRWAVQFVILVITIKFLNLSIIWIWLSYMFGDIAEALVFIYFYLRGDWKRKRAW
>NZ_LN824141.1|WP_052670498.1|37262_39761_-|alpha-amylase
MFWSIVIVILGFSSTVSPVWEDQIIYFIMIDRFANGDTSNDVLTESGIDSGYVNSKYNGGDIQGLINQLDYIAELGVTAIWVTPPVANQWWDGLVDYGGYHGYWARDFKNVDEHFGDIELYKKFVEEAHKRGIYVIQDIVTNHTGNFISYRDGKYYLNDQSYPTNKPEQYPFNMNDYNDPEQRNLNIYHWPSEVKEPNRYNTEFSDLDDLNTENPIVIEALKDSYSFWIKEADVDGFRIDTAIYVEPEFWPEFLEGEKGIFEVASELGKNDFLTYGEAWLNPMPFSNDAEKEIEQFFNWGFNSMLDFPLHTDIKRVFKEGKPTSYIKYRLEQREIMYSNPARMVTFVDNHDMDRFLKASDINSLKQALSLIFTIPGIPTIYYGTEQNFIETRATMFANGFASGGQDHYDINTPTFQFIKELSELRKNTPTFKHGKIEVLFSDDLGPGPLVYKIFDDSKMYIVMMNTSSNKKHATGMDFNIEDGSVLRPLVVNNMVNKEIVYSNPYNILLNAKSLGIFEVTDQKEEVAKSGISVEINNLSENNTFTDNFVLTGTASGAKSVRIIVDGEEKEYAKIDLKQGINEPWEVTINISDFTPGTHKIIAKAYGKTPMIVEYSKEYTVNFDIPMISLKVVEDPKGDDKGPYGTYFYPKDSTFSSQMDIRKVELVQIGTMLRMIITMDTVTDSWTPANGFDHVTFQIFFDDPSKPGIIELPLQNATMPDGYDWNYGMWATGWGIYLYSANNASAEKFGDPVTPSPEAQVNKKENTITFFIPLSVLETNDLSGWNIYITTYDYDGIEGVLRPLTPEGGQWAFGGGKTTDPKIIDDLFIKIDR
>NZ_LN824141.1|WP_045087010.1|40272_40830_-|elongation-factor-P
MLDVGDLRRGHYILYQGSIYKVIEANKHFMGRGSGLIRTRLKDVKTGLIKEVTFPSGEKVEEADISFQKAQYLYNDGDHYYFMTLDDYEQFALPKEEIEDVKFYLIENLEVDLVFHEGVPVSVELPVVVELTVVETEPNFKGNTVSGGGKPAILETGLKTTVPFFVERGERIKVDTRTGEYIERA
>NZ_LN824141.1|WP_045087011.1|41168_41366_+|cold-shock-protein
MKGKVKWFDSKKGYGFITGEDGNDVFVHFSAIQMDGYKKLEEDQDVEFEVVKGDKGPQASKVRPL

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Crispr_ID: NZ_LN824141_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_3

90413-90518

Orphan

Consensus_repeat	Method
TTTTTCTACTTGTACCAAGGGAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_3

>merge|NZ_LN824141|3|90413-90518|CRISPRCasFinder
TTTTTCTACTTGTACCAAGGGAAAGGGGAGGGCTGCGCCCTGTTACCCTTTTAAATTCAAAAACAATAATTAACCATTGCATTTTTTCTACTTGTACCAAGGGAAA

>NZ_LN824141|3|3|90413-90518|CRISPRCasFinder
TTTTTCTACTTGTACCAAGGGAAA	GGGGAGGGCTGCGCCCTGTTACCCTTTTAAATTCAAAAACAATAATTAACCATTGCAT
TTTTTCTACTTGTACCAAGGGAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_052670180.1\|83659_84058_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087046.1\|96979_98113_+\|cysteine-desulfurase	unknown	unknown	gnl\|CDD\|224029
NZ_LN824141.1\|WP_144403445.1\|88993_89620_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087039.1\|85943_86414_-\|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein	unknown	unknown	gnl\|CDD\|176643
NZ_LN824141.1\|WP_045087043.1\|91794_93291_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087050.1\|100052_100244_+\|DNA-directed-RNA-polymerase-subunit-omega	unknown	unknown	gnl\|CDD\|234744
NZ_LN824141.1\|WP_052670504.1\|84639_85371_-\|Nif3-like-dinuclear-metal-center-hexameric-protein	unknown	unknown	gnl\|CDD\|223404
NZ_LN824141.1\|WP_052670181.1\|84075_84606_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366483
NZ_LN824141.1\|WP_045087041.1\|87602_88973_-\|tyrosine-phenol-lyase	unknown	unknown	gnl\|CDD\|237313
NZ_LN824141.1\|WP_045087038.1\|85376_85868_-\|adenosine-specific-kinase	unknown	unknown	gnl\|CDD\|377190
NZ_LN824141.1\|WP_045087045.1\|94905_95580_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_LN824141.1\|WP_045087048.1\|99130_99418_+\|DUF370-domain-containing-protein	unknown	unknown	gnl\|CDD\|179823
NZ_LN824141.1\|WP_045087044.1\|93316_94774_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087047.1\|98151_99030_+\|YicC-family-protein	unknown	unknown	gnl\|CDD\|236993
NZ_LN824141.1\|WP_144403446.1\|89892_90285_-\|RidA-family-protein	unknown	unknown	gnl\|CDD\|129116
NZ_LN824141.1\|WP_045087049.1\|99421_100069_+\|guanylate-kinase	unknown	unknown	gnl\|CDD\|234719
NZ_LN824141.1\|WP_052670183.1\|90985_91570_-\|DUF2179-domain-containing-protein	unknown	unknown	gnl\|CDD\|235234
NZ_LN824141.1\|WP_045087037.1\|82934_83579_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235080
NZ_LN824141.1\|WP_052670184.1\|95542_96889_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_LN824141.1\|WP_045087040.1\|86679_87474_-\|Nif3-like-dinuclear-metal-center-hexameric-protein	unknown	unknown	gnl\|CDD\|376614

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087046.1\|96979_98113_+\|cysteine-desulfurase	gnl\|CDD\|224029	COG1104, NifS, Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes [Amino acid transport and metabolism].	3.74898e-164
NZ_LN824141.1\|WP_045087047.1\|98151_99030_+\|YicC-family-protein	gnl\|CDD\|236993	PRK11820, PRK11820, YicC family protein.	1.07712e-88
NZ_LN824141.1\|WP_045087039.1\|85943_86414_-\|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein	gnl\|CDD\|176643	cd00865, PEBP_bact_arch, PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea. PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in bacterial and archaea. Members here include Escherichia coli YBHB and YBCL which are thought to regulate protein phosphorylation as well as Sulfolobus solfataricus SsCEI which inhibits serine proteases alpha-chymotrypsin and elastase. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). In a few of the bacterial members present here the dimerization interface is proposed to form the ligand binding site, unlike in other PEBP members.	4.6273e-70
NZ_LN824141.1\|WP_045087050.1\|100052_100244_+\|DNA-directed-RNA-polymerase-subunit-omega	gnl\|CDD\|234744	PRK00392, rpoZ, DNA-directed RNA polymerase subunit omega; Reviewed.	2.09618e-05
NZ_LN824141.1\|WP_052670504.1\|84639_85371_-\|Nif3-like-dinuclear-metal-center-hexameric-protein	gnl\|CDD\|223404	COG0327, COG0327, Uncharacterized conserved protein [Function unknown].	6.62726e-59
NZ_LN824141.1\|WP_052670181.1\|84075_84606_-\|hypothetical-protein	gnl\|CDD\|366483	pfam01135, PCMT, Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT).	4.30408e-07
NZ_LN824141.1\|WP_045087041.1\|87602_88973_-\|tyrosine-phenol-lyase	gnl\|CDD\|237313	PRK13237, PRK13237, tyrosine phenol-lyase; Provisional.	0
NZ_LN824141.1\|WP_045087038.1\|85376_85868_-\|adenosine-specific-kinase	gnl\|CDD\|377190	pfam04008, Adenosine_kin, Adenosine specific kinase. The structure of a member of this family from the hyperthermophilic archaeon Pyrobaculum aerophilum contains a modified histidine residue which is interpreted as stable phosphorylation. In vitro binding studies confirmed that adenosine and AMP but not ADP or ATP bind to the protein.	6.40857e-99
NZ_LN824141.1\|WP_045087045.1\|94905_95580_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	1.12146e-72
NZ_LN824141.1\|WP_045087048.1\|99130_99418_+\|DUF370-domain-containing-protein	gnl\|CDD\|179823	PRK04323, PRK04323, hypothetical protein; Provisional.	7.1128e-44
NZ_LN824141.1\|WP_045087049.1\|99421_100069_+\|guanylate-kinase	gnl\|CDD\|234719	PRK00300, gmk, guanylate kinase; Provisional.	5.22583e-101
NZ_LN824141.1\|WP_144403446.1\|89892_90285_-\|RidA-family-protein	gnl\|CDD\|129116	TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other].	2.76438e-63
NZ_LN824141.1\|WP_052670183.1\|90985_91570_-\|DUF2179-domain-containing-protein	gnl\|CDD\|235234	PRK04164, PRK04164, hypothetical protein; Provisional.	3.84753e-73
NZ_LN824141.1\|WP_045087037.1\|82934_83579_-\|hypothetical-protein	gnl\|CDD\|235080	PRK02868, PRK02868, hypothetical protein; Provisional.	9.88799e-07
NZ_LN824141.1\|WP_052670184.1\|95542_96889_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.42065e-50
NZ_LN824141.1\|WP_045087040.1\|86679_87474_-\|Nif3-like-dinuclear-metal-center-hexameric-protein	gnl\|CDD\|376614	pfam01784, NIF3, NIF3 (NGG1p interacting factor 3). This family contains several NIF3 (NGG1p interacting factor 3) protein homologs. NIF3 interacts with the yeast transcriptional coactivator NGG1p which is part of the ADA complex, the exact function of this interaction is unknown.	1.50588e-22

>NZ_LN824141.1|WP_144403446.1|89892_90285_-|RidA-family-protein
MRRRIILKEQITTSEAPKAIGPYSQAVRVDGFLFISGILPIDPKTGQMVEMNIRDQTLQVMNNLEAILEAAGLKISNVVKTTIFLKDLSHFNEVNDIYGSFFSEIPPARSCIEVSRLPKDALIEIEAIAI
>NZ_LN824141.1|WP_144403445.1|88993_89620_-|hypothetical-protein
MKPVQKPLKDATFMSTIRWKLVNALMCDYTYGYITKSKRVSLGLEKTHYNDAFCIAGGINQQRIEPIYFEQIRRNNRSLEKFYDAKYVDIRDKSIKTGQELFCGRRTRNKNLNEENLHKYRGAKKSKGRRNIRKQRYAYQPKDIVIFESKKYSVQGVQNKGKYIKLMEMSKPVKTDLVKPYMFRKGFGMFYNCNSSPTYRSGSLLAGK
>NZ_LN824141.1|WP_045087041.1|87602_88973_-|tyrosine-phenol-lyase
MMYPPEPFKIKSVETIKMTTKEERAQVLKEAGYNTFLIPSKKVYIDLLTDSGTSAMSDHQWASMMIGDEAYGGSENWYHLRDAVQEVYGFEYVVPTHQGRGAENLLSQIMIKHGDYIPGNMYFTTTRTHIELNGGKFVDVIIDEAHQPEIELPFKGNVDLKKYQNLIDEVGANRIPYICVGVTVNMAGGQPVSMENLRKVKEISEKNGIKVMFDATRCVENAYFIKEREPGYGDKSIAEILKEMMSYADGCTMSGKKDCLVNIGGFLALRDQDLYEKATSLVVVYEGMPTYGGMAGRDMEAMATGIYESLDFHYIEHRIKQVRYLGDKLDEAGIPIIKPVGGHAVFLDAKRFLPHLSQDELPAQALSAEIYLDSGVRSMERGIVSAGRDEKGRNRYPKLETVRLTIPRRVYTYSHMDVVADSVISLFDKRNSIKGLEFVYEPPVLRFFTARFKPIE
>NZ_LN824141.1|WP_045087040.1|86679_87474_-|Nif3-like-dinuclear-metal-center-hexameric-protein
MEITVQDVINAIVLPKLSSEATVDKLLFGDPETIVTGISVTFLATQEVIEQSIKLGNNFIITHEGIFYSHIGNTEFLKSDPVFKQKLHLIESNSLSIFRFHDNIHRYQPDGIMAGLLKRLSLDIYEVNRSQTYSIIEIPKKSLLEIIQDIKKSLDIDYIRYMGDLSMECRRVGILVGYRGTGEMIIPLFHKESLDLVIYGEGPEWEAPEYVRDAIRQGNHKALIVLGHAESEKPGMEYVANLIKLKFPSIPVHYIDLEPLFCVY
>NZ_LN824141.1|WP_045087039.1|85943_86414_-|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein
MGMKISSPVFKNNDYIPSKYSCEGRDINPPLIIEEIPNNTKYLALIMDDPDAPRGTFVHWVAWNIEAVNEIPEAIPKMHVVTSPISMRQGKNSAYQIGYIGPCPPVGHGVHHYHFKIYALDTELDLPESSKKEDLLEAMNGHIIEQAEIVGLYKRT
>NZ_LN824141.1|WP_045087038.1|85376_85868_-|adenosine-specific-kinase
MDFKLDLVQVTIPEDANVIIGQSHFIKTVEDIYECIVTTNPSLKFGIAFIEASGPRLIRFDGNDEELIKIAVENAQKIGAGHCFVIVLKEGFPINIKNQLQNVQEVIGIFAATANPLQIIIAESEQGRGILGVIDGFKPLGIENQKDIENREDFLRKITQYKR
>NZ_LN824141.1|WP_052670504.1|84639_85371_-|Nif3-like-dinuclear-metal-center-hexameric-protein
MNIFELENFLNSILKPWDYDDFCHNGIQIEGAHTINKIAVGVSFNEEFISTAIKENCDLLLVHHGIFGKDFFELKGYLKRRVEKVIKNNLTLMAYHLPLDGHEEYGNNVSILKSLNLNIKEKVDVTFIGEYEDPILFMDFHKQVEKLFNPQPLLVYQNNKFVKTVGVCSGGGSSFLESVENKIDTFITGEVKEQTRNIVAEMGINFINAGHYSTEVFGIKNIGDLIRNSFGIEVEFIDIYNEI
>NZ_LN824141.1|WP_052670181.1|84075_84606_-|hypothetical-protein
MWIVLIFVIITIGYFLFFWIIPFSLKGAIYDPSNKEAVKKMVELAQIKPGEKSVDLGSGDGRVVIEFAKKGIQAHGYEINPLLVIISRINIRKAGLKGKAFIHWNNFWKVDLSQYDIITVFQVSFAMDRLEKKLMYELKPGARVISNYWTFPNWRPSKYEKDVYVYEKKINYIFYE
>NZ_LN824141.1|WP_052670180.1|83659_84058_-|hypothetical-protein
MTKYFFILLIFIPLVCFSFNLYYFPATLHIEDDRLVNFSNQFCIKFNEQIAVLEASSLEEFTELTKLPYSYYAGALIVSKNDYYIVTLPFDVLHKKGIFYSTLVHEIMHYYLESYFDFSEEEQEDIISQFIN
>NZ_LN824141.1|WP_045087037.1|82934_83579_-|hypothetical-protein
MKIQLYNVFVEPFKIAFSKEPIILIPLFISILLTIIFDIIGQFGPVAYFVSVMLTGIFNTFFYAWTTILYNEFKEYEKADMRDSFARIKKLFLDITILSIFVGFLISIGFMAFVIPGIILALFLIFSPCVFVVEDVSLADSIRKSFSFVFKAEHFFQILIVLVAIFLLGLIPYIGVYISTLLEFLWLPYLYVYYHDNNQVVAPQKPQVKENKQD
>NZ_LN824141.1|WP_052670183.1|90985_91570_-|DUF2179-domain-containing-protein
MAAWMDSSIFNYVVLPFIIFLMRLTDVTLMTLRIIFVSKGYKLWSSVMGFFEVSVWLVAISQVMNNLDKPLYAIAYAVGFACGNYLGAYLDEKIALGVNLLQIITNKDAEQLVKYLRDNDFGVTSINAEGARGPVKVIYSVVRRKDLNKIIQIVNEFNPNAFYSVAEVRSVNKGIFPVKTPKDKKLGRFIKNGK
>NZ_LN824141.1|WP_045087043.1|91794_93291_+|hypothetical-protein
MKKVCFFLIVLTISSLCFSLKIDKYFINIDLIDYKEVVVPFVFVNDKNYEQIIQIKNLSKNDFVDISYPKTIYLNPYETQNVNFVVSPTKINVGSYFFFFQFSIENNFINEIGNIYFPILFRINIIPQFDYHPTVEIYSGDLHISYEDKLGTIFPFTITNDSNLILEISGNFRLTSKENSNFIVEKPLFEGYQSAILPQTEKDFEIFIDRYLKPGKYRIRMELNYGYKNYLQEKYVLEKEFTIPETIYLDRKAINFVVNKNKLYISVPKEMSTREYITTPQQETLTILNNDYIDANLSIDFISSTVDIPLERSINPKYISENPSKISLKPDEKGEINLIADYRRANLQNLEGEFFGTVQLISEGYSREKIFYNTTKIPTVINFGNNKYEVKSNVTSIELIPINKFNKNLNFKIDIENTGNSTLLYQIKINKFNKQIGKKVGEEIRILPEKPILPEQSISINNQLIVELGVDTIIIDIEYYSYTDPKSIIKTYSYSFTL
>NZ_LN824141.1|WP_045087044.1|93316_94774_+|hypothetical-protein
MRKVFFLLLIFITGITGFSNIQITLPNIALKEALKALEEISGSTILTSPDIKGTIHTTINAINLENALDSLLYSTNYEYKKISEDLYLVGNFNIKMQNMQKEILQMEFNNLDLKKILNLLTLLSEKVFVIQNLNIILLNKNDEMHKYIKALFEFLETQDKSNDYFLFFSIYEISDNVYQFLKENEKVEYEKTFFIKNKKSTIILENNFEYLTRIKELEYHQLKMPSSQEITYYKTLTNNNIVLDFSNNKLLIKHLIMKENNSILLNTNEIGYLAIENEEKYYILAITYLNLSDIYIKKNLENIDNSESLFNFGIGYLIPDAKFIVISGINLGNNYIEISSNFKEHLDFSLSTNLVNNMNLGILFKKNSKESNTNIFVNDLQHYDNFDLYGNIILGGTVSFSNTLTNSLDYISYDLLVLKDIIKSENNSHIVTFAPGVGIKVSRNDKLKPYINFGVQYKYKLLKSKISLLYYYQMNIHKMTCSLEF
>NZ_LN824141.1|WP_045087045.1|94905_95580_+|response-regulator-transcription-factor
MCKIMVVEDDRSISRLLELELTHAGYKVKIAKDGEEALEFYENFKPHIILLDIMLPKLDGFEVAEAIRGYDPDVGIIMLTARGELENKIEGLKKADDYVVKPFEIEEILARIESLLRRMGKTTDYIKVGDIEIYPQKMQVIVKGDEIHLSLTEFNILKLLAINKNLVISKEKIMEEVWGYYDEENNNLVEVYINYLRKKIKNSSQNIETIRGVGYVIRERKKET
>NZ_LN824141.1|WP_052670184.1|95542_96889_+|HAMP-domain-containing-histidine-kinase
MDTSLGREKKKPSAVFRQTIVFTSVTMAIVFAMVIIIRIFYVQFTIRTYSDLYATELNIATGKKEKTNEPQDTLNLLYQLMQDSNVIRRSLVSNKIVILDGVLISDPYGLIKDKFKIPYLPYLYEYQGLYYLFIGVPIFDSSYLIIGNPSLEITALLKSFREVTTLILIFGFFLSLVVSYFLAKNTLKPVVKISDQISKIDIDNINQRIPEQNTKEFDIFANKLNSMLNRIQQAFELQNQFVSDVSHELRTPLTSINGYVKMLKRWGKNDPTVMEESLDSIESSSEYLSDLVEKLLLLTKTDYQIEKEEINLYSVIEDILDFFKLSLQEFSVQIKGKDFKVNTSKEYLSIILKVLIENAIKYSKDIKKIDIELNPLQKKLIIKDYGIGIEEEKLKNIFERFYKADSSRSQKGHGLGLSIAKKLADALDIKITVESEINKGTTFTLHFK
>NZ_LN824141.1|WP_045087046.1|96979_98113_+|cysteine-desulfurase
MIYFDNNATTPVDKEVAEVILKYMTELYANPNSIHSFGVQIEQYLEESRKTISEILQVLPTEIFFTSCATESINTVIRGVARANKNIGKRIITSTIEHSAVINTLKDLERNGFDVIYINVDKTGVIDLEQLANSINQNTILVSLMLANNEIGTIEPINEAYNLVKKINSNTYFHIDAVQALGKIPFNIEIFKCDFASFSAHKFHGPKGVGILYKKRGTRMYPLLTGGTQENAMRAGTQNVPGIIGTALALEKAVDQLEYMKTYIKQIRNYLADNLEKIGAKILTPLENSIPNTLGFFFPNIRGDIIVNALSEEEIFVSTTSACASKTRTESRIMKSLGYDDTNAKGLVRISLSHLNNLNEAEIFLNKLKNILNFLNY
>NZ_LN824141.1|WP_045087047.1|98151_99030_+|YicC-family-protein
MRSMTGYGRINKNIGDYGYNLEIKSLNSKSLNLNVIISPIFSPLEINIQNFIKKHFQRGRINIYIDIKLLKSDDVIDIDLGLAKAYYNALNVLANELHLSGEVNLEILLKFKDILKVSLTDEKIAQIWCGLEKVLEEATNIVINFQEEEGKNLEKVIVEYLKEMKRIVDEISQHADKMKDTYRELINNNLNSLLTDFTNIDEKRMEMEITLLSERSDITEEIDRLNSHIKRFKNLLESSEPSIGQDLDFICQEMHREFNTIASKSKLLEITNLSLEGRSLVNKIREQVQNVH
>NZ_LN824141.1|WP_045087048.1|99130_99418_+|DUF370-domain-containing-protein
MYGLINIGFGNLVVGDRVIAIVNPSSQPLKRLKDIADQQGKLLEVNHGRKTRAYIITDSGHVIASAIQPETITNRFLQNFYEIEKVLDKIRKENF
>NZ_LN824141.1|WP_045087049.1|99421_100069_+|guanylate-kinase
MHGLLYVISGPSGVGKSTLIKNALKSLNGFDFSVSYTTRPKRDGETEGIDYFFVDEKTFFEMRDKDEFLEWAKVHGNYYATSKSFVEKKLKECRGLVLDVDVQGALNIQKKYEEAIYIFILPPSIKDLEKRLKNRGTETAEIMQIRLNNAKWEMSKIDNFDYIVVNHEVSESSQQLTSILVAEQLKRERYNELTSQFFFFKKQETEGVKANGFRN
>NZ_LN824141.1|WP_045087050.1|100052_100244_+|DNA-directed-RNA-polymerase-subunit-omega
MDLEINYDKILNIVKLKFAVPVIVAKRAETLKNIDQLKGVSQKKDYVAIALKELEEGKIVLKK

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Crispr_ID: NZ_LN824141_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_4

237029-237143

Unclear

Consensus_repeat	Method
GAAAGAGGGAGGGCTCCGCCCTTAACCCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_4

>merge|NZ_LN824141|4|237029-237143|CRISPRCasFinder
GAAAGAGGGAGGGCTCCGCCCTTAACCCACTAAAAATTCAAAAACGATTATTAATAAGTGCAACTTTATTTAGTACTTATAACTGAGAAAGAGGGAGGGCTCCGCCCTTAACCCA

>NZ_LN824141|4|4|237029-237143|CRISPRCasFinder
GAAAGAGGGAGGGCTCCGCCCTTAACCCA	CTAAAAATTCAAAAACGATTATTAATAAGTGCAACTTTATTTAGTACTTATAACTGA
GAAAGAGGGAGGGCTCCGCCCTTAACCCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_052670208.1\|227582_228143_-\|chromate-transporter	unknown	unknown	gnl\|CDD\|376780
NZ_LN824141.1\|WP_045087167.1\|232902_233670_-\|4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol-kinase	unknown	unknown	gnl\|CDD\|224858
NZ_LN824141.1\|WP_084217073.1\|238058_239054_-\|FtsH-protease-activity-modulator-HflK	unknown	unknown	gnl\|CDD\|259802
NZ_LN824141.1\|WP_144403449.1\|230948_231575_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087172.1\|242648_245153_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226406
NZ_LN824141.1\|WP_045087162.1\|228268_228976_-\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225099
NZ_LN824141.1\|WP_045087173.1\|245255_246305_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223674
NZ_LN824141.1\|WP_045088518.1\|237196_238048_-\|protease-modulator-HflC	unknown	unknown	gnl\|CDD\|259803
NZ_LN824141.1\|WP_045087165.1\|231593_232631_+\|low-specificity-L-threonine-aldolase	unknown	unknown	gnl\|CDD\|99748
NZ_LN824141.1\|WP_045087174.1\|247720_248692_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|223521
NZ_LN824141.1\|WP_045087168.1\|233693_235880_-\|1,4-alpha-glucan-branching-protein-GlgB	unknown	unknown	gnl\|CDD\|235445
NZ_LN824141.1\|WP_052670211.1\|229800_230667_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|223769
NZ_LN824141.1\|WP_045088521.1\|246346_247714_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224094
NZ_LN824141.1\|WP_045087175.1\|248684_249716_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|226967
NZ_LN824141.1\|WP_045087166.1\|232633_232897_+\|EscU/YscU/HrcU-family-type-III-secretion-system-export-apparatus-switch-protein	unknown	unknown	gnl\|CDD\|235569
NZ_LN824141.1\|WP_045087170.1\|240205_241147_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187566
NZ_LN824141.1\|WP_052670219.1\|239241_239937_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|226608
NZ_LN824141.1\|WP_052670217.1\|235884_236805_-\|DNA-protecting-protein-DprA	unknown	unknown	gnl\|CDD\|376794
NZ_LN824141.1\|WP_045087171.1\|241121_242360_+\|replication-associated-recombination-protein-A	unknown	unknown	gnl\|CDD\|237355
NZ_LN824141.1\|WP_045087163.1\|229136_229592_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377295

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_052670208.1\|227582_228143_-\|chromate-transporter	gnl\|CDD\|376780	pfam02417, Chromate_transp, Chromate transporter. Members of this family probably act as chromate transporters. Members of this family are found in both bacteria and archaebacteria. The proteins are composed of one or two copies of this region. The alignment contains two conserved motifs, FGG and PGP.	8.43297e-41
NZ_LN824141.1\|WP_045087167.1\|232902_233670_-\|4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol-kinase	gnl\|CDD\|224858	COG1947, IspE, 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate synthase [Lipid metabolism].	1.84902e-64
NZ_LN824141.1\|WP_045087175.1\|248684_249716_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|226967	COG4608, AppF, ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism].	1.67984e-124
NZ_LN824141.1\|WP_045087172.1\|242648_245153_+\|hypothetical-protein	gnl\|CDD\|226406	COG3889, COG3889, Predicted solute binding protein [General function prediction only].	4.96492e-105
NZ_LN824141.1\|WP_045087162.1\|228268_228976_-\|GntR-family-transcriptional-regulator	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	8.11998e-45
NZ_LN824141.1\|WP_045087173.1\|245255_246305_+\|ABC-transporter-permease	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	1.46332e-76
NZ_LN824141.1\|WP_052670217.1\|235884_236805_-\|DNA-protecting-protein-DprA	gnl\|CDD\|376794	pfam02481, DNA_processg_A, DNA recombination-mediator protein A. The SMF family, of DNA processing chain A, dprA, are a group of bacterial proteins. In H. pylori, dprA is required for natural chromosomal and plasmid transformation. It has now been shown that DprA is found to bind cooperatively to single-stranded DNA (ssDNA) and to interact with RecA. In the process, DprA-RecA-ssDNA filaments are produced and these filaments catalyze the homology-dependent formation of joint molecules. While the E.coli SSB protein limits access of RecA to ssDNA, DprA alleviates this barrier. It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation.	7.95177e-98
NZ_LN824141.1\|WP_045088518.1\|237196_238048_-\|protease-modulator-HflC	gnl\|CDD\|259803	cd03405, SPFH_HflC, High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.	4.77022e-111
NZ_LN824141.1\|WP_045087165.1\|231593_232631_+\|low-specificity-L-threonine-aldolase	gnl\|CDD\|99748	cd06502, TA_like, Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.	7.10133e-135
NZ_LN824141.1\|WP_045087174.1\|247720_248692_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|223521	COG0444, DppD, ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	2.20961e-160
NZ_LN824141.1\|WP_045087168.1\|233693_235880_-\|1,4-alpha-glucan-branching-protein-GlgB	gnl\|CDD\|235445	PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.	0
NZ_LN824141.1\|WP_052670211.1\|229800_230667_+\|DMT-family-transporter	gnl\|CDD\|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	6.87069e-10
NZ_LN824141.1\|WP_045088521.1\|246346_247714_+\|ABC-transporter-permease	gnl\|CDD\|224094	COG1173, DppC, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	6.50746e-78
NZ_LN824141.1\|WP_045087166.1\|232633_232897_+\|EscU/YscU/HrcU-family-type-III-secretion-system-export-apparatus-switch-protein	gnl\|CDD\|235569	PRK05702, flhB, flagellar type III secretion system protein FlhB.	3.41826e-24
NZ_LN824141.1\|WP_045087170.1\|240205_241147_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187566	cd05256, UDP_AE_SDR_e, UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	2.03559e-134
NZ_LN824141.1\|WP_052670219.1\|239241_239937_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|226608	COG4123, COG4123, Predicted O-methyltransferase [General function prediction only].	1.7374e-31
NZ_LN824141.1\|WP_084217073.1\|238058_239054_-\|FtsH-protease-activity-modulator-HflK	gnl\|CDD\|259802	cd03404, SPFH_HflK, High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.	1.52204e-119
NZ_LN824141.1\|WP_045087171.1\|241121_242360_+\|replication-associated-recombination-protein-A	gnl\|CDD\|237355	PRK13342, PRK13342, recombination factor protein RarA; Reviewed.	7.19556e-177
NZ_LN824141.1\|WP_045087163.1\|229136_229592_-\|hypothetical-protein	gnl\|CDD\|377295	pfam04308, RNaseH_like, Ribonuclease H-like. RNaseH_like is a family of uncharacterized eubacterial proteins that are distant homologs of Ribonuclease H-like. The family maintains all the core secondary structure elements of the RNase H-like fold and shares several conserved, presumably active site residues with RNase HI. This finding suggests that it functions as a nuclease.	1.99793e-46

>NZ_LN824141.1|WP_052670217.1|235884_236805_-|DNA-protecting-protein-DprA
MPTVFKEDYEEKKRNIFKRLNQVKDLKILTYWDEAYPDLLKETNDPPIIIYYFGDISLMKSMKVSIVGSRKPTSYGKTVCENIAKTLDSYTIVSGMAYGIDSIAHINSKKTIAVLGNGIDVVYPKSNENLYARIKNEGLILSEYFPGTRPARYTFPYRNRIIAGLSEKTIVVEASKKSGSLITARYALDYGREVLAVPGDITRINSYGTNYLIYSGATPIISLEQLRELFRVNKTFDNNNTIIEDKNSILENHILQSIMNGKDNLDLICDSINEDVSLILSTIMKMEIEGVIGQENGVYYILKEGE
>NZ_LN824141.1|WP_045087168.1|233693_235880_-|1,4-alpha-glucan-branching-protein-GlgB
MPILTDDEIKMLINAECHDPFIYLGLRKLDEKNLIVRTIQPFAKEAYLITQDKKIKLDKIHPSGLFEKKIEGTEFFEYEFEYVAQDGHKWRTVDPYSFLPVISEYDRYLFNEGNHYKIYEKLGAHPMKIKGVNGVLFATWAPNAKRVSVVGNFNNWDGRVHQMRVLGVSGIWEIFIPNVVEGDLYKFEIKTQNGEILLKTDPYGTYFEVRPNTAAIVYDVDDKHKWQDEEWMEKREGINWFEEPISIYEVHLGSWARKDGNEFLNYRDLAQKLVKHVKEHNFTHIELLPIAEHPLDISWGYQVTGYFAPTSRFGKPEDFMYFVDVMHQNNIGVFIDWVPGHFPKDSFALGRFDGTALYEHFDPRLGEHKDWGTYIFNYGRYEVKNFLLSNALFWLEKYHIDGLRVDAVASMVYLDYSRKDGEWIPNKYGGRENLEAIDFLKQLNTVAYQYFPGILTIAEESTAFPGVTKPVHLGGLGFSFKWNMGWMNDTLRYFSKDPIFRKYHQNDLTFSLLYAFSENFILSISHDEVVYGKRSLLEKMPGDDWQKFANLRLFYSYMYAHPGKKLLFMGAEIAQRKEWDCLHSLDWHLLQYEPHEKTSVFLKDLNKIYKKYKSLFEVDHSYDGFEWIDFNDTENSVISFVRKSKNQEELIVCIFNFTPVPRENYRIGVPKKGVYQEILNSDWKEYYGSGIDNPKEVYSQDVPMHGREQSIILTLPPLAGMYFKYIIK
>NZ_LN824141.1|WP_045087167.1|232902_233670_-|4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol-kinase
MMLKAYGKVNLYLDVIKKRDDGYHDILTLFQSIKEHDIIYVDFSEKEFFESEPELSIPWKDNILKQTIEIFKKETGIYDFNLKIKLVKKLPLGGGVGGGSADSAALLRFLAKNFNISERDIFDIAKKIGSDVPFLLNGGTAIGRGKGDILEYLEPLDINIKLYPMPLRIDTKKMYELLDQQWKEIKHKGDPHLLYCSLKNKNVEVAKKNAFNVFEQIVFKINPQLQEQKHEIEKEKGTIFALMSGTGSTIFRVCE
>NZ_LN824141.1|WP_045087166.1|232633_232897_+|EscU/YscU/HrcU-family-type-III-secretion-system-export-apparatus-switch-protein
MMEKKKVVALRYKKGVDNAPKVVAKGMDLIAQRILEIAEKENIPIIKNEKAVEDFYGIDLDDEIPSELYEIAAEIIAFVYKLDKQHI
>NZ_LN824141.1|WP_045087165.1|231593_232631_+|low-specificity-L-threonine-aldolase
MKYIDIRSDTVTQPTQEMRDAMYNAVVGDDVYDEDPTIKKLEVYAAEIVGKEAALFVPSGTFGNQLSIFTHCERGNEVILDDSCHIVIHEVGASSVIAGVQLRTIKSDKGIMSPQEVRSKIRKGEEDIHFPSTGLICLENAHSNGRVIPLENMKEIHEIAKENKIPVHLDGARIFNASTYLKVDPKEITQYCDSIMFCLSKGLCAPVGSMVAGSKSFIEKAKKKRKLMGGGMRQAGFLAAAGLVALEKMRDRLHEDHENARYMGKELSKIPEISINLDDIQINMVFFTLNIDNVEEMVSYFLDKGIKINPPENGMFRFVTNYWVTKRDIDYIIKTLKDFLSLKAR
>NZ_LN824141.1|WP_144403449.1|230948_231575_+|hypothetical-protein
MKPVQKPLKDATFMSTIRWKLVNALMCDYTYGYITKSKRVSLGLEKTHYNDAFCIAGGINQQRIEPIYFEQIRRNNRSLEKFYDAKYVDIRDKSIKTGQELFCGRRTRNKNLNEENLHKYRGAKKSKGRRNIRKQRYAYQPKDIVTFESKKYSVQGVQNKGEYIKLMEMSKPVKTDLVKPYMFRKGFSMFYNCNSSPTYRSGSLLAGK
>NZ_LN824141.1|WP_052670211.1|229800_230667_+|DMT-family-transporter
MLLQQKYKAYINLFLVTLIWGSTFPLHKAVLTDEYTFPYLFVRFFIAGIFSFIIWRKQSFKYGMILGVILGLGHALQTYGINFTDASKSGFITSLYIPFTPIISFLIEKEKPNLIQWICFPLSLLGSYMLFGGISGFNFGDFLTFIGAVLFALHIVLITKFSKKVQETSLLAYQFLFAAVINLLLSFNSNWSLTNTIIATTLYTSIIATVLVNFVQVKYQKVVGSNSTVLIFIGEPIFASLFSFIFLKERFSYLQLIGAILMILVILLTSFSDKIIVHFTKPINTKEL
>NZ_LN824141.1|WP_045087163.1|229136_229592_-|hypothetical-protein
MNFRLKNPTIGFVESLEISDFIKEFSSEEEVKIWVGTDSHSRNGNVVFATAIVIYKTGSGGTYFYYLTRENKRYDMYNRLIKEAELSLETAKFLEEELQLKRPEIHLDIGLNGKSKDIFNSLTGYVKGLGYDCKTKPYSFAATNIAHIYTK
>NZ_LN824141.1|WP_045087162.1|228268_228976_-|GntR-family-transcriptional-regulator
MAKNKVPIYKIIADEITTRIYEGVYSLNSYLPSENELAEEFHVTRTTIRKVLEVLKHQGTIKSYPGRGYKVQSLLWEQSLLKFYSFGRSIATKIENSKTKLISINKVDGLGDVDKFEQLELWEITRIGMVGEIPLILETSYIPCDYLKKVDNKKLLQTKSLYDVLEREGIRCVRAKEYLEPVLPSLEAQKLLEVEENVPLFQTTRYTYDSDDRFVEFRESLIRADYFKFYTELSL
>NZ_LN824141.1|WP_052670208.1|227582_228143_-|chromate-transporter
MTTKKEKNKLFSMFITFLKIGLFTFGGGYAMIPLMEKEIVDNNKWLEKEKFTETVSLTQTIPGSVSVNLSILLGYNIEGIIGSIVSAIGVILPSFVIILLIALALTNLGELALLEKAFNGIRPAVAAFILYAAFSLSKSIKWSTVLFLVFLISFLLTTIFSVNPIYIIAGAFIIGSLSNRIKNKDK
>NZ_LN824141.1|WP_045088518.1|237196_238048_-|protease-modulator-HflC
MTIWAVTIIIVFLGLFFGLTSFYIVEQTQQAVVLRFGEIKNVRTEPGVYVKAPFIDNVVKFEKRFMIYDIPVERVITFDRRTVLADTYAIWRIEDPKRFIETLGTMEVAMTRIDDIVYSHVRDVIGTYSFSEVLSIQRLKILEEIKKRSVNSLKDFGISIIDVRLKRTDLPQENTQAVYERMKSERYAMAAQLRAEGEKEAQKMKAEADKKVSIIKSDAQKEAEIIRGTGEASATNIYSEAYSQDMDFYELQKITQIYKESFEKSILVIPNDSPLLKYFYNMK
>NZ_LN824141.1|WP_084217073.1|238058_239054_-|FtsH-protease-activity-modulator-HflK
MAEYEVFDPVDPNDEFKEYSNDRKHRWRNIIILVIIIAVGAYLLTGVYQVGPSEVALVKTFGAYSSTTGPGIHLHLPYPFQSHVIVDVRTINKIEIGFRTTSSGRTTSYVFVEEEAEMITGDQNIISIEAIVQYRVSDPVDYAFNVIQGDDLVKLTSESVLREMVALLELEKVLTTERDKVAMETARRIQEIMNDYEAGIQIENVYLQDVTPPDPVVPAFDDVNNARQDQQTSINEAQRYANDVIPRAEGEAVKILNDAQAYAYEQISKATGEAERFRIMLEEYRKSEEITKNRLILDSIQKMLENSKIKVISEKGDTLNFINIAEVMGDD
>NZ_LN824141.1|WP_052670219.1|239241_239937_-|methyltransferase-domain-containing-protein
MDALEFKNKIQKIDQIYRSISLYSPSVTHFPTHASVFLLATSPFKDGYKIVELGSGIGHVCLALSKLVENSLIYGIEVQKDLYLASLKNIQNNCIKNVEFYNLDVKEIKSLFTAECADLVISNPPHYFDGLKSDKKDRRVARSADNLKVMEDFIYAAKYLLKNKRLGCFVIHPSILSDVFIYLEKNNLEPQHMYIGYGNKNKDAQLISLIFRKNGGKNFVIHPPVFFDDLK
>NZ_LN824141.1|WP_045087170.1|240205_241147_+|NAD-dependent-epimerase/dehydratase-family-protein
MADKSKYKILVTGGAGFIGSNLVDKLLEEGHSVVVVDNLSTGNINLLSPLALFYQQDIRDYKVMDIIFETHHFDYVFHLAAQISVPESVENPKKDAEINILGTLNILSLSVKYGIKKIIFSSSGGAIYGENAPIPTTEDYCPNPISPYAISKLACEHYIKFFSKEFSLDYTILRYSNVYGPKQTPKGEAGVVAIFTENMLNNQEVTIYGTGEQIRDFVHVYDVIQANILSLDRAKNEIINISTNEATSINELFKIMKEEINYKKTPIYQQKRPGDLEVSVLSNEKAKEILNWQPSFNLKKGVKNTIEWYRTSV
>NZ_LN824141.1|WP_045087171.1|241121_242360_+|replication-associated-recombination-protein-A
MNGIEPLYEKIRPKNIDEILGNEKLKEVLKTWIKNKKIRSFIIYGEPGTGKSTIVKALLNEIKELYDIYTISGALEGKKTIKSIIEKENNLFSKPKLLFVDEIHRLNKAEQDTLLLSIETGDLTLIGATTENPAISINPALLSRVLIFKTQELSEKDYELLFERIKDYYKDINITDEAKKALVDYAGKDLRRIINLIETAKEASINEIDLQFLSDFTGFKLNYNKNAKYSFISAYIKSVRGSDPDAAILYLAYMLESGEDPLYVARRMVILAAEDVGLADPNALNIAVSAMIATEHIGYPECYLPLSEATLYLCACPKSNSSYLAYSKAKDFINKSNFEIPKKLINPLNKKMQKQGFGENYKYPHDYGGFVRESYMPETYEKTQFYHPKDIGYEKKIKERFIQLWKNYKNYT
>NZ_LN824141.1|WP_045087172.1|242648_245153_+|hypothetical-protein
MKKVSVLLIALVCLLSVFSFAEKGPMPDKVYFDVRMQEDVAIQDVAAGNVDVFFSGVGAPTINALPQSTLDKLDIYSIPSGSWSLLFNPVPNAAPYTVKVGDKEYFNPLAIKDVRFAMNFLINRQYIVDEIQQGAGEVMYTVATPGQPGTQPYIDIAAKMGFAPEGNEELALETIENAMNEAANLPENKGRLVKKGQWWTFDGEPVTIKFLIRVDDPEGRLKAGRYIADQIEKAGIKVERLERDRTAIQIAYYSNPADLEWHIYTEGWGAGATRKFWHHIVAQMYAPWYANMPGGQDPANWNYVQDEIDYLTQKVYSGNFATEEEYWDSILRATELGLEDSVRIYISYQDQFFVANKDRFNRRMVYGLGDGLNQWSVITADTKDRILRATQFSSQGALFMSAWDPIGTDGFNDVFSINIASTMYDYGMFESPASADIVPAKVIPRLETLDTKFEVDEEGELVGLIEVPQDAIKFDTVSKKWVPVEPGLKSLSVCTYDITYGIWNHGIQESLADYMYAFAYAWDLSTQGDANDTRYDPTYSASATPGLIVEVARRINPDGSITVWFNYNFPVDDMYLASWGAPMFSVSQSGQPIGVSWEIVEALTRLVEHGGVSGRGYTLSATAAKGNVYEIDVIETAAVNDIKVELQKMINEKYVPVYINEYVTPDEAVKRYQTALDFINKYGHAYIGSGPFYMSKYDPVARYVELTAIRDERYPFERGYWNEFFETVRLNVDSVDLAFAAIGGLDLPVYINVSEVLYPYDTYTPATEGNVEVSLITPDGEKVFKAEVESPGRFLATIPGGVLAELDSGTYTVVVTAKSEGAIPSTYSSTIIIY
>NZ_LN824141.1|WP_045087173.1|245255_246305_+|ABC-transporter-permease
MYWRYAIKRILMGIIIYVIIIFIYSFLFNTVMEETLNGQIIEQVNGEMVKISQVGTDPDYLLEYRERRIRELRDIYHLDDPLLSRVFWRAIDTLTFNYGRSTIMRSFKGETDVIKIVLERIPNTLMLFTTSIILDILIGVWLGIKKAQRAGKFLDKSTSIITMTVYGLPSWWFGMVMIMIFAFMIPIFPSGGISSVPPPETFFAKLVDLLYHMALPVITLVFIGFWGRAYLTRNIVLGNLQEDFIMSARARGIPERSVLYGHALRTSAPPILTMSLLSLLASFSGALVFEGIFSWPGMGNLYWAAVQQNDIPVLLGNLSITTLIYISGIVLLDLIYGFLDPRIKVGGKA
>NZ_LN824141.1|WP_045088521.1|246346_247714_+|ABC-transporter-permease
MQLADFWKEFKQVKFGIIGLIFLVIFILITIFEHFLIPFPEASTRWRDITYWEDNPRNAPPVWINWFTEKDYTPTTYMNNLEFEEKTISPTMSVSTAILEYDYNYDVPPIDLIYRGRFKGSFTLNIVLERPDGNTINLVNKNFSSPTWKDFRVAISNEAKNAVQSFAKRFQNVSSQTIKVNSTIFSEANKEIITNPVPLKGTYKFNINIIKTSEDTVIEDPKFIFSGAVSGILGTDNAKRDIWSGLIAGTKWALFIGLLTSAISISVGVIYGVVSAYYGGFVDSIMQRIWEIFMNIPLLPVLIVLSAIFKPSIWSLITMMCLFFWVGPVKTVRSMALQIKEETYVEAAKALGASNGRIIFKHMVPILIPYAFASMALNVPSAILYEATVSLLGLGDATIVTWGQILHDAMNGGAVTNGLWWWVVPPGISIALIGMTFAFIGFAMDTILNPKLRTR
>NZ_LN824141.1|WP_045087174.1|247720_248692_+|ABC-transporter-ATP-binding-protein
MSEVLTVNNLKLYYFTRKGVVKALDDVSFSLKEGETLGLVGESGCGKTTLGMGLLRMPSPPGKIVDGEIIIDNENIIHLKENELRKRIRWNKISMIFQGAMNSLTPVYNIKKQMLETLLNHREMEEEQTLEIIKKYINYVGLSEDVLKRYPHELSGGMKQRVVIATALFLEPKIVIADEPTTALDVVVQAQIINLLKKLKHDLNLSFIFITHDLATEAEVADRIMVMYAGKIAEIGTNDQIYGKQGPSHPYTKGLLGATPKLREKVEELAFIPGTPPDLLNPPTGCRFHERCPVAFDKCILNEPPLKEIEPEHFVACWRCYDE
>NZ_LN824141.1|WP_045087175.1|248684_249716_+|ABC-transporter-ATP-binding-protein
MNDEIILSVKNIKKWFPLRRSITEVFKGKKRWVKAVDGVTFNIKKGEIFALIGESGCGKTTTGRLIMKIEELTSGQIIFKGTDTSTLSSSTEIKKYREEVQMVFQDPYASMNPRFRVRDVLYEPLIIHKKTKDSREMEKIARRALEEVKLTPPEEFLDRFPHMLSGGQRQRVATARTLVLSPNLIIADEPVSMIDLSTRAEILHMMKEVQENLNLTYLYITHDLSTARYFCDRIAVMYLGRIVELGTSDEIIENPLHPYTKALIAAVPEPIAGKENIIKDIPIKGEIPSAANIPKGCRFHNRCIYSKPLCYENVDDPELVEDSNGHYVACYRYKEINQEVQNI

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Crispr_ID: NZ_LN824141_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_5

624747-624890

Orphan

Consensus_repeat	Method
GTACTTGTAGGTAGGAAGGGCGGAGGGCTTCGCCCTAAACCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_5

>merge|NZ_LN824141|5|624747-624890|CRISPRCasFinder
GTACTTGTAGGTAGGAAGGGCGGAGGGCTTCGCCCTAAACCCTTTATAAATTCAAATGCTTACTTTTAGAAAATCTTCATTTTTTAATTTTTTTACTTTTAAGTACTTGTAGGTAGGAAAGGGCGGAGGGCTTCGCCCTAAACC

>NZ_LN824141|5|5|624747-624890|CRISPRCasFinder
GTACTTGTAGGTAGGAAGGGCGGAGGGCTTCGCCCTAAACCC	TTTATAAATTCAAATGCTTACTTTTAGAAAATCTTCATTTTTTAATTTTTTTACTTTTAA
GTACTTGTAGGTAGGAAAGGGCGGAGGGCTTCGCCCTAAACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087456.1\|628411_629644_-\|U32-family-peptidase	unknown	unknown	gnl\|CDD\|223896
NZ_LN824141.1\|WP_045087448.1\|617624_618872_-\|glycerate-kinase	unknown	unknown	gnl\|CDD\|225254
NZ_LN824141.1\|WP_045087454.1\|625956_627627_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374899
NZ_LN824141.1\|WP_052670306.1\|625069_625960_+\|AEC-family-transporter	unknown	unknown	gnl\|CDD\|223751
NZ_LN824141.1\|WP_045087449.1\|618888_620007_-\|sensor-domain-containing-diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635
NZ_LN824141.1\|WP_045087461.1\|633356_635036_+\|methylmalonyl-CoA-mutase-family-protein	unknown	unknown	gnl\|CDD\|239652
NZ_LN824141.1\|WP_045087458.1\|631012_631987_-\|AI-2E-family-transporter	unknown	unknown	gnl\|CDD\|223701
NZ_LN824141.1\|WP_045087447.1\|617019_617628_+\|CoA-pyrophosphatase	unknown	unknown	gnl\|CDD\|239518
NZ_LN824141.1\|WP_045087450.1\|620143_621112_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381369
NZ_LN824141.1\|WP_045087462.1\|635360_635762_+\|cobalamin-B12-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|239022
NZ_LN824141.1\|WP_045087451.1\|621235_621601_-\|DUF4180-domain-containing-protein	unknown	unknown	gnl\|CDD\|379371
NZ_LN824141.1\|WP_084217299.1\|616614_617007_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|224867
NZ_LN824141.1\|WP_045088570.1\|614886_616038_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340928
NZ_LN824141.1\|WP_045087457.1\|629640_630996_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087455.1\|627595_628348_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_LN824141.1\|WP_045087459.1\|632037_632592_-\|DUF4416-family-protein	unknown	unknown	gnl\|CDD\|379590
NZ_LN824141.1\|WP_045087460.1\|632578_633181_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087452.1\|621648_623007_-\|dihydrolipoyl-dehydrogenase	unknown	unknown	gnl\|CDD\|273568
NZ_LN824141.1\|WP_144403463.1\|623645_624614_-\|ExsB-family-protein	unknown	unknown	gnl\|CDD\|224522
NZ_LN824141.1\|WP_045087453.1\|623011_623353_-\|carboxymuconolactone-decarboxylase-family-protein	unknown	unknown	gnl\|CDD\|223672

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087456.1\|628411_629644_-\|U32-family-peptidase	gnl\|CDD\|223896	COG0826, COG0826, Collagenase and related proteases [Posttranslational modification, protein turnover, chaperones].	2.31642e-139
NZ_LN824141.1\|WP_045087448.1\|617624_618872_-\|glycerate-kinase	gnl\|CDD\|225254	COG2379, GckA, Putative glycerate kinase [Carbohydrate transport and metabolism].	1.98381e-161
NZ_LN824141.1\|WP_045087454.1\|625956_627627_-\|hypothetical-protein	gnl\|CDD\|374899	pfam16949, ABC_tran_2, Putative ATP-binding cassette. This is a family of putative two component ABC exporters. This is the membrane protein of approximately 573 residues and twelve transmembrane domains. It is encoded adjacent to an ATPase.	0.00205154
NZ_LN824141.1\|WP_052670306.1\|625069_625960_+\|AEC-family-transporter	gnl\|CDD\|223751	COG0679, COG0679, Predicted permeases [General function prediction only].	9.85741e-29
NZ_LN824141.1\|WP_045087449.1\|618888_620007_-\|sensor-domain-containing-diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	4.74156e-46
NZ_LN824141.1\|WP_045087461.1\|633356_635036_+\|methylmalonyl-CoA-mutase-family-protein	gnl\|CDD\|239652	cd03680, MM_CoA_mutase_ICM_like, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA mutase (ICM)-like subfamily; contains archaeal and bacterial proteins similar to the large subunit of Streptomyces cinnamonensis coenzyme B12-dependent ICM. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA, intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis.	0
NZ_LN824141.1\|WP_045087458.1\|631012_631987_-\|AI-2E-family-transporter	gnl\|CDD\|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	2.56262e-28
NZ_LN824141.1\|WP_045087447.1\|617019_617628_+\|CoA-pyrophosphatase	gnl\|CDD\|239518	cd03426, CoAse, Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved Nudix fold and requires a single divalent cation for catalysis. In addition to a signature Nudix motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.	8.26238e-49
NZ_LN824141.1\|WP_045087450.1\|620143_621112_+\|aldo/keto-reductase	gnl\|CDD\|381369	cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.	0
NZ_LN824141.1\|WP_045087451.1\|621235_621601_-\|DUF4180-domain-containing-protein	gnl\|CDD\|379371	pfam13788, DUF4180, Domain of unknown function (DUF4180).	3.09665e-55
NZ_LN824141.1\|WP_084217299.1\|616614_617007_+\|GAF-domain-containing-protein	gnl\|CDD\|224867	COG1956, COG1956, GAF domain-containing protein [Signal transduction mechanisms].	1.63039e-47
NZ_LN824141.1\|WP_045088570.1\|614886_616038_+\|MFS-transporter	gnl\|CDD\|340928	cd17370, MFS_MJ1317_like, MJ1317 and similar transporters of the Major Facilitator Superfamily. This family is composed of Methanocaldococcus jannaschii MFS-type transporter MJ1317, Mycobacterium bovis protein Mb2288, and similar proteins. They are uncharacterized transporters belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	9.55319e-112
NZ_LN824141.1\|WP_045087462.1\|635360_635762_+\|cobalamin-B12-binding-domain-containing-protein	gnl\|CDD\|239022	cd02071, MM_CoA_mut_B12_BD, methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.	2.00906e-58
NZ_LN824141.1\|WP_045087455.1\|627595_628348_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	1.16567e-88
NZ_LN824141.1\|WP_045087459.1\|632037_632592_-\|DUF4416-family-protein	gnl\|CDD\|379590	pfam14385, DUF4416, Domain of unknown function (DUF4416). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 176 and 187 amino acids in length. There is a conserved DPG sequence motif.	3.20625e-62
NZ_LN824141.1\|WP_045087452.1\|621648_623007_-\|dihydrolipoyl-dehydrogenase	gnl\|CDD\|273568	TIGR01350, Dihydrolipoyl_dehydrogenase, dihydrolipoamide dehydrogenase. This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.	1.33064e-178
NZ_LN824141.1\|WP_144403463.1\|623645_624614_-\|ExsB-family-protein	gnl\|CDD\|224522	COG1606, COG1606, ATP-utilizing enzymes of the PP-loop superfamily [General function prediction only].	2.46961e-32
NZ_LN824141.1\|WP_045087453.1\|623011_623353_-\|carboxymuconolactone-decarboxylase-family-protein	gnl\|CDD\|223672	COG0599, COG0599, Uncharacterized homolog of gamma-carboxymuconolactone decarboxylase subunit [Function unknown].	2.3155e-20

>NZ_LN824141.1|WP_144403463.1|623645_624614_-|ExsB-family-protein
MSRNINDTINNIKEEIKQIVGNQPLYIAFSGGMDSTVVALLARDALPNDQITLVNVCFGAYSYSKAIEAVLLLSKELKLKLNFISSNNEQEIIMYHGPNCNQCTREVKIRKVKEFAHNGIIASGANMSDSWGKTGIKFMDGIYSPLINLNKNEIKEILNFYNFTIPKIGENSIREGCKFKHLLKMAVNSQYHSRSAVIANEVLIDILDFYDIKREIANVKIIGPLSQNIALINIRPLPENYIINEVVYNLEKEKSIDKIDVVDRPLKLKILANPGIYNNEESRHWILNGRLAPEFAMPLTAEWKKSSNQKLWTFSVYGYEKI
>NZ_LN824141.1|WP_045087453.1|623011_623353_-|carboxymuconolactone-decarboxylase-family-protein
MSMKEAYSQAQKWMSEFAKKSPEKMQAFQKMVEAIEKEEGESLDKKTKELIAVALSIARDCEWCIAFHVKEAINEGASEEEILEAAWMAILMGGGPALMHAGLVLDALKEFRG
>NZ_LN824141.1|WP_045087452.1|621648_623007_-|dihydrolipoyl-dehydrogenase
MYDVIIIGAGPAGYVSAIRLSQLGKKVAIIEKEYLGGTCTNKGCIPTKTLLSCAHLYDEIISKSNKFGININSVSYDLNKMDNYLTTVVTQTRKGIEYLIKKNKIDFINATAEIVDTNHVKTGNNILETKNIILAHGSEPAVFPPFNSIEGIWTSDDFFINLKDIPNSILIVGGGVIGVEFATFLASLGKKVYIVELMDHILPTEDLDVSQEIKRSLLRKGVEIYEKNKVINVEKDGKMYISKIEENGKITEINSEKILLAVGRKPVIPEDVKKIGIEINKGIKTDLNMRTNISNIYAIGDIRADIMLAHVAMYEGIVAAHNIAGEKKIMDYNAVPNVIFSNPEIATVGIKEKDANPEEVIVSKFPVSANARARTINEKNGFVKVIADKRSKKIIGISIVSQNATEMIMEGVLAVKYGMTTNQLTDAIHPHPTLSEIILEAVEGVEGKAIHI
>NZ_LN824141.1|WP_045087451.1|621235_621601_-|DUF4180-domain-containing-protein
MTINIVKENNIKIAIVNSQEVIIKDVQSALDFMMTMLYKTGCDRIIINKEAICEDFFDLKTKIAGEILQKFVNYQVKIAIVGDFSKYSSKSLKDFIYESNNGNHFFFLPDELTAVRKLSSF
>NZ_LN824141.1|WP_045087450.1|620143_621112_+|aldo/keto-reductase
MKYNNLGKAGIKVSEISLGSWLTFGNQLDTEGVKQTMRTAYEHGINFFDNAEAYANGLSESLMGMAIKEYRREDLVISTKIFWGGKGPNDLGVSRKHLLEGIWNSLKRLQLDYVDLIFCHRPDPTTPIEETVFAMDYIIRNGLALYWGTSEWSAKQLEEAYTIADKRNLIPPSMEQPQYNMFVREKVEKEFLPLYQKYGLGLTTFSPLASGLLTGKYNEGIPENSRLAKFKGLKDDLEKDGLLSSKNIEKVKRLSKIANDLGATMAQLAIAWILKNPHVSTVIIGASRPEQVIENVKATEVKDKLTEDVMLEIENILDNKPL
>NZ_LN824141.1|WP_045087449.1|618888_620007_-|sensor-domain-containing-diguanylate-cyclase
MYLVLIYLTFVTFLLALILFRGIQTVKYIKRLTSNKERFFIFIPPSPKKTVINRFKSILYETALYCLEDEKEKSDILRIFIEHLPDFLKSDSWSFLLTPTKAHWTFLTWSKNLDFLPLEDIAYELENEGENIRNVLESNSSLFIKNVKENVTWKQENPLTVSWLGIPIKIGDEIVGVLNIDWFKTKKFTKIEKELARSFKIEIENVLTKVFKLNELFLNFHLDPLTEIYNRKALEDYMKNRQIITDNIALVFIDIDGFKKINDTFGHTVGDQILKTIVKRIKNVLRVEDYFFRYGGDEFILILKNINNHEDIKKIITRLQSIVSDTIIIDDYIIKSSCSMGYCLLPLETNNIQRAIEIADKKMYLQKSNLNH
>NZ_LN824141.1|WP_045087448.1|617624_618872_-|glycerate-kinase
MNKLREDALRIINNSIDSVLPEHAVKSQLSSMSLGENIYLVAIGKAAWRMAKAAKDFLKEKIKNGIVITKYEHSQGIIEGLQIYEAGHPIPDENTLKATRKVIEMIKNLGKDDEVLFLVSGGGSSLFELPNEGIELEDLQKLNNDLLKSGANIVEINTIRKHISQVKGGQFAKIAEPAKIYALILSDVIGDRLDSIASGPAYPDSTTLEDVKKIISKYNLSLPENLLHAFSETPKSLRNVDTYIIGSVNKVCENAKLIAEQLGYNSIILTTTLDCEAKEAGLFLASIARELIEKDRPINKPCAVILGGETVVKVQGNGLGGRNQELALSAARGIYNYEDVIIVSVGTDGTDGPTDAAGGIVDGQTINKLIKQNIDVEFALKNNDSYTALDAIGGLIRTGPTGTNVNDLIFILCGA
>NZ_LN824141.1|WP_045087447.1|617019_617628_+|CoA-pyrophosphatase
MYKDKIVRVYENYLPKALGIESYFSVLISLIEVEGSTHLLFEQRSNHLTRQPGEISFPGGKVEPGETPEYAALREAQEELNLEPNFVKIIGPSDYLVTPFNDLIYSFVGFLEVDLEEIKPNDEVESIFTVPLEYFLIHEPIKYEAYIIHEINDDFPYELIPKGKDYEWRIGKYPIYFYIYENHVIWGITARFTYEFVKKLKL
>NZ_LN824141.1|WP_084217299.1|616614_617007_+|GAF-domain-containing-protein
MQRIVELLSERIDYYNWVGFYLVDNKDKGLLTLGPFVGEPTEHEKIKFGQGICGQAASSKKTFIVGDVTKEENYLSCSPKTKSEIVVPIFDKKGNIVGEIDIDSHQKDAFDQDDKLFLEEIARLITDRFY
>NZ_LN824141.1|WP_045088570.1|614886_616038_+|MFS-transporter
MGIISLLGDIVYEGARSISGPYLAFLGAGASIIGIVGGIGEFVGYALRLVFGYFADKTKAYWTLTIIGYGLLLSIPLLAFSNSWQIAAFLLIMERMGKAIRSPARDAILSHATKQVGRGWGFGIHEALDQIGAIIGPLIFSAVFLLNSQYKTGFGILIIPVVILLMLLFFARSKVPSPQKLEVSIESDKQINSYDNKNKWSKTFWLYTFFTLLSVMGFVQYPIIAYHLNVNSIISNVWIPIFYAIAMGIDGITALIIGRTYDNIGLKTLLIIPIATLVIPFFAFSYSKIFILFSIIIWGIVMGIHETIMRAAIADLIPLERRGTAYGIFNTVYGLSMFIGGTSIGFLYEISLSYVVTFVVIIEIISLIFLYSLIRNVNQRANA
>NZ_LN824141.1|WP_052670306.1|625069_625960_+|AEC-family-transporter
MTALINFVVIVLMGYMFKKLFPKNTGEILSTLIVNFTLPMTVFIGISSSKVLLSDLYFILIGFLGCLLTFFGGKILVNLLNIEDKNVSTVILLSFCGLNIGLFMYPLAEMLWGINAITYFALYDLGNSIILYGIGKSVAEGKKGGFRILDLLKFPPFIALILGLVFNLFGVTLPDLIMSPIKIIKDANNFLIMFLVGFYFSVSTIKKHSKILTITLSTKYLIGLAISLLTLLIPVRNQLERVSLFISPMLPTAMMVIVYSIENNYDSELASSIVSLTAIISFILVFLASAMFNFGI
>NZ_LN824141.1|WP_045087454.1|625956_627627_-|hypothetical-protein
MKKLTSLSLIELDQHYKISKNKYLLKHTKDETIPFFALIAVLATLIIIYFPFYLDFIRVNLEYYSLKNIEPLFIAEFIMITGFIGFFLGAFVLIGEFFLKKDMKLLITLPLKPSEVILGKLSVVLCDQMIISLIFLLPALIYFGIYNHLSIGYYLSMILVVLFSQIFPVLLVLVFILPISHLFKKLKNKELILYILTSLLMVLALIYIFSSKDIFFIVATNPQDMPDIYINPQGIFSRLAWIYPPAFLGAKSLINTNIYRFTWTIAFIGFHIILLTLSLYIGEKLYYSTYVNFLEASTSAEKKASKNIDLLFNKALSPNKALLKREWLYFLKTPSFSVNGFTNVLIFPGLCILLAIIDAGIGINLQKELVGPLIKIKMFLVVFISAIAGSLSGLSYSCFSREGKFIKELKVLPITSSQIVISKFLHIMQLSSIGIISGALIGYILFNLNFLEFINVLTFSIIISIFFNLLQMLIDAFKPTFDWDNPQKAMKQNANGLFSILVIFGILILLGFLYYYISIYFDLHFVLIISSCIFVIFDILLYKLLKNRTTKLLKED
>NZ_LN824141.1|WP_045087455.1|627595_628348_-|ABC-transporter-ATP-binding-protein
MIEIVGLTKVFSEKIIAVDNIDLKINEGKVVGFLGPNGAGKTTTLNMIVGLCKPTSGKIFINGIDVREEPEKVKKVIGFVPDEPLLFEKITGISYLNFICDIFEVPLEERRKRGGWLLQAFKLLDAIKDPISTYSHGMRQKLALISALIHKPKILILDEPIVGLDPESASILKQIMKRHASNGNLVFFTTHIMEIAEKICDEIAIIDKGKIVFQGTINELRQLKGDKSLEQLFLEVTKSENEEIDFSFLD
>NZ_LN824141.1|WP_045087456.1|628411_629644_-|U32-family-peptidase
MKKIELLSPAGDLEKLETVFHYGADAAYIGGKFLNLRAFSKNFDNDELKKAVKLAHKLGKKIFVTLNAIPNNSELELLPDYIQYLESIKVDSIIVSDLGVFNLAKQYSDIPITISTQANNMNWASVKMWKELGAKRVILARELSLREINEIRQKVTDIELEVFIHGAMCISISGRCLLSNYLTARDANRGECTQPCRWKYYLMEEKRPGEYFQVFEDERGSYIMNSKDLCTIEFLDKIIETGVDSLKIEGRMKSSYYAGITTKIYREAIDSYFEGTYSEDKIKEWKNELKNVSHRPYTSGFYLDKTNYNSQNYETSSYIRKYNYVGIVKEKISENSYLIEVKNKIKRGETIEIIRSKGEKISILLSEIINYENNDIIEEANPNQKIILEVGSSIQSGDLIRSLKTNATAN
>NZ_LN824141.1|WP_045087457.1|629640_630996_-|hypothetical-protein
MKKITLFLYLSAIFISGFASARLLSKNDPEYYYQVLNGVNLKYPIYYESENIPKEYRNYIHTSIDLKYENRIIGSYTLEGGWYRPSNLTDILFRDFVLKNGNLFNFGFKTYYGNNFFAQFIADFRLGDTTYFKYGNYNIFNIPRIDYISLDFPTFSYLSYKKDKMDFLIGRIPLSYGPMKYNLVLSDNSPYYDTMNISYSFSDNLSYDFAILSMVPQLSKDEQEKMEEKYIASRNAFYNGINYKFNENLFFGLSSLNQVAGKLPNPINIFVKSDVGIYGGYLKLIPFYDINFNGEYAINYNTLKSSYGLGVSKTFRTKSSRFKVGYERYWIEDNFFSNEKPYQNLYYRTIALSNEPGARIFFDYPFGFKYGENSKIGSLELILAFEKASISYIWDNGTNSFGKLNNHNISFLWNTKIGKIGIDWMHLKNAENEFETFNLKYLFEVNIRLPK
>NZ_LN824141.1|WP_045087458.1|631012_631987_-|AI-2E-family-transporter
MSLGGWLSLTYLIIFLFLSHFAPYVMGALILGFFLSLLINVPTNLFSKIMNDKVASILSHLLVLGAFFYAAISFFPLVINEGKKLFSVLSTFAFPKSGEIDNFPSWILDVIDEFSKNISNFGFNLINKLISVTPSLLMSIIVLIVTTVAIGSLKSLMKDNSWKLYPANERDKGVKFLKSFYGEVEKFVHGRFLSATIVGFVIGLATYIAGIPNSLFIAIVAWIGDFIPYLGSIAAGILLAILGFTEKGLMGLIIGLLIALISNQIEMWFLYPKIQSKVLDLHWFIILISSLLFGELFGFIGVLIALPLVIYVINFWEYWVVRIK
>NZ_LN824141.1|WP_045087459.1|632037_632592_-|DUF4416-family-protein
MGNPKPPDFVNYVAHIFTAGDSDLWLYKMGLKGILEENFGPIDYVSPVLDFQRFTYFYNEEMGKNILIEARMISFEYLSSPAFLSNAKLITNDIERRFSVNNKRKVNIDIGYIHHTQFVLASTKHWGNRIYIGKNIYAEITLMYNFGKWEPLEYTYANFRDPNYLKELEIIRNNYLKKRKKFDS
>NZ_LN824141.1|WP_045087460.1|632578_633181_-|hypothetical-protein
MKRIKIYFNKNIKTLIENSNYSLKEVSLNLKIPLSSLEKILEGKLEGFSVVSLKDIANRLSHLLNEEILLICEDDETTKPVQSMNKKIFNKSISFKLIISTFLIINLVFLYFLVKDLNFYIGLLYKNLYTLTISNHASTEVMVNETKLAPQDSIKMELTPGQSIKVKGNKNNEEIVVTTPNAIYTINLENFEVILSNGKS
>NZ_LN824141.1|WP_045087461.1|633356_635036_+|methylmalonyl-CoA-mutase-family-protein
MFDKNKLEEIENKKNEWKEKTLKKTIQRFPERKQSFLTTYDENIDVVYTPKDIENINYLEDVGFPGEYPFTRGVQPTMYRGKLWTMRQYAGFGTAEESNERYKYLLEQGQTGLSIAFDLPTQIGYDSDDSISEGEVGKVGVAVDSLMDMEILFDGIPLDEVSVSMTINSTAIILLAMLVVVANKQGVPLEKLRGTIQNDILKEYIARGTYIFPPQESMKIIVDIFDYGSKHLPKFNLISISGYHIREAGANSVQEVAFTLADGISYVEAAIKAGLDPNEFGKNLSFFFSSHNNFLEEIAKFRASRKLWSKVMKKRFGVSNENAMKLKFHTQTAGSTLTAQQPLNNIVRVTLQALAAVLGGTQSLHTNSFDEALGLPTEQAVTIALRTQQIIAHESGISDTVDPFAGSYVIEKMTLEIEEKVEEYLKKIDELGGMVKAIEIGYPQQEILNTAYRTQRRIEEKEEIIVGVNEYKSENDEKIEILKLDEDIEKKQKEQLRALKTDRNQKEVYYSLERLKKAACENENLFPYVIKCVESYATIGEITKVLKEIYGEYHENLSI
>NZ_LN824141.1|WP_045087462.1|635360_635762_+|cobalamin-B12-binding-domain-containing-protein
MNKKIRVMIAKPGLDGHDRGAKIIARALRDAGMEVIYTGIRRTPEEIVEAAIQEDVDLIGLSILSGAHKILCKKIISLLKEREVEIPVILGGIIPEEDVSELKEMGIIEVFSPGTSINEIVEKVKAIAMARKV

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Crispr_ID: NZ_LN824141_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_6

907885-907998

Orphan

Consensus_repeat	Method
GCCCTAGACCCAGCATAAATTCAAAAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_6

>merge|NZ_LN824141|6|907885-907998|CRISPRCasFinder
GCCCTAGACCCAGCATAAATTCAAAAAAAAATAATTAATAATAGCGAACTTTTTTGGTACTTGTATTGGGAAAGGAAAAGGGCTCCGCCCTAGACCCAGTATAAATTCAAAAAA

>NZ_LN824141|6|6|907885-907998|CRISPRCasFinder
GCCCTAGACCCAGCATAAATTCAAAAAA	AAATAATTAATAATAGCGAACTTTTTTGGTACTTGTATTGGGAAAGGAAAAGGGCTCC
GCCCTAGACCCAGTATAAATTCAAAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087664.1\|902690_903785_-\|BMP-family-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380577
NZ_LN824141.1\|WP_045087668.1\|911211_912630_-\|protein-translocase-subunit-SecD	unknown	unknown	gnl\|CDD\|273456
NZ_LN824141.1\|WP_045087665.1\|905102_906593_+\|glycerol-kinase-GlpK	unknown	unknown	gnl\|CDD\|234594
NZ_LN824141.1\|WP_045087676.1\|918152_919151_-\|methionine-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224058
NZ_LN824141.1\|WP_171820588.1\|906685_907792_-\|alanyl-tRNA-editing-protein	unknown	unknown	gnl\|CDD\|225427
NZ_LN824141.1\|WP_045087662.1\|898215_899499_-\|alkaline-phosphatase	unknown	unknown	gnl\|CDD\|224699
NZ_LN824141.1\|WP_045087675.1\|917512_918151_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224922
NZ_LN824141.1\|WP_084217309.1\|901710_902526_-\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|223810
NZ_LN824141.1\|WP_045087673.1\|916039_917044_+\|M42-family-metallopeptidase	unknown	unknown	gnl\|CDD\|349906
NZ_LN824141.1\|WP_045087661.1\|897850_898132_+\|DUF503-domain-containing-protein	unknown	unknown	gnl\|CDD\|377364
NZ_LN824141.1\|WP_045087667.1\|910285_911212_-\|protein-translocase-subunit-SecF	unknown	unknown	gnl\|CDD\|237275
NZ_LN824141.1\|WP_045087672.1\|915009_916056_+\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349906
NZ_LN824141.1\|WP_045087669.1\|912683_913106_-\|preprotein-translocase-subunit-YajC	unknown	unknown	gnl\|CDD\|235518
NZ_LN824141.1\|WP_052670360.1\|901121_901709_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|224627
NZ_LN824141.1\|WP_045087663.1\|899773_900955_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340891
NZ_LN824141.1\|WP_045087660.1\|897312_897840_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	unknown	unknown	gnl\|CDD\|376665
NZ_LN824141.1\|WP_045087674.1\|917085_917469_+\|methylglyoxal-synthase	unknown	unknown	gnl\|CDD\|179969
NZ_LN824141.1\|WP_045087670.1\|913343_913946_+\|semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|237580
NZ_LN824141.1\|WP_052670362.1\|904120_905047_+\|inorganic-phosphate-transporter	unknown	unknown	gnl\|CDD\|223383
NZ_LN824141.1\|WP_045087671.1\|913972_915013_+\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349906

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087664.1\|902690_903785_-\|BMP-family-ABC-transporter-substrate-binding-protein	gnl\|CDD\|380577	cd06354, PBP1_PrnA-like, periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. Periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. The members of PnrA-like subgroup are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold.	3.04453e-100
NZ_LN824141.1\|WP_045087668.1\|911211_912630_-\|protein-translocase-subunit-SecD	gnl\|CDD\|273456	TIGR01129, Protein_translocase_subunit_SecD, protein-export membrane protein SecD. Members of this family are highly variable in length immediately after the well-conserved motif LGLGLXGG at the amino-terminal end of this model. Archaeal homologs are not included in the seed and score between the trusted and noise cutoffs. SecD from Mycobacterium tuberculosis has a long Pro-rich insert. [Protein fate, Protein and peptide secretion and trafficking].	6.99529e-127
NZ_LN824141.1\|WP_045087665.1\|905102_906593_+\|glycerol-kinase-GlpK	gnl\|CDD\|234594	PRK00047, glpK, glycerol kinase GlpK.	0
NZ_LN824141.1\|WP_045087676.1\|918152_919151_-\|methionine-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224058	COG1135, AbcC, ABC-type metal ion transport system, ATPase component [Inorganic ion transport and metabolism].	9.90753e-135
NZ_LN824141.1\|WP_171820588.1\|906685_907792_-\|alanyl-tRNA-editing-protein	gnl\|CDD\|225427	COG2872, COG2872, Predicted metal-dependent hydrolases related to alanyl-tRNA synthetase HxxxH domain [General function prediction only].	1.03207e-43
NZ_LN824141.1\|WP_045087662.1\|898215_899499_-\|alkaline-phosphatase	gnl\|CDD\|224699	COG1785, PhoA, Alkaline phosphatase [Inorganic ion transport and metabolism].	8.19609e-139
NZ_LN824141.1\|WP_045087675.1\|917512_918151_-\|ABC-transporter-permease-subunit	gnl\|CDD\|224922	COG2011, AbcD, ABC-type metal ion transport system, permease component [Inorganic ion transport and metabolism].	7.73413e-80
NZ_LN824141.1\|WP_084217309.1\|901710_902526_-\|M23-family-metallopeptidase	gnl\|CDD\|223810	COG0739, NlpD, Membrane proteins related to metalloendopeptidases [Cell envelope biogenesis, outer membrane].	1.95403e-44
NZ_LN824141.1\|WP_045087673.1\|916039_917044_+\|M42-family-metallopeptidase	gnl\|CDD\|349906	cd05656, M42_Frv, M42 Peptidase, endoglucanases. Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.	7.97639e-123
NZ_LN824141.1\|WP_045087661.1\|897850_898132_+\|DUF503-domain-containing-protein	gnl\|CDD\|377364	pfam04456, DUF503, Protein of unknown function (DUF503). Family of hypothetical bacterial proteins.	9.50538e-19
NZ_LN824141.1\|WP_045087667.1\|910285_911212_-\|protein-translocase-subunit-SecF	gnl\|CDD\|237275	PRK13022, secF, protein translocase subunit SecF.	2.99822e-92
NZ_LN824141.1\|WP_045087672.1\|915009_916056_+\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349906	cd05656, M42_Frv, M42 Peptidase, endoglucanases. Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.	2.85799e-115
NZ_LN824141.1\|WP_045087669.1\|912683_913106_-\|preprotein-translocase-subunit-YajC	gnl\|CDD\|235518	PRK05585, yajC, preprotein translocase subunit YajC; Validated.	2.68785e-32
NZ_LN824141.1\|WP_052670360.1\|901121_901709_+\|HD-domain-containing-protein	gnl\|CDD\|224627	COG1713, COG1713, Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism].	1.18756e-38
NZ_LN824141.1\|WP_045087663.1\|899773_900955_+\|MFS-transporter	gnl\|CDD\|340891	cd17333, MFS_FucP_MFSD4_like, Bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4, and similar proteins. This family is composed of bacterial L-fucose permease (FucP), eukaryotic Major facilitator superfamily domain-containing protein 4 (MFSD4) proteins, and similar proteins. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. The MFSD4 subfamily consists of two vertebrate members: MFSD4A and MFSD4B. The function of MFSD4A is unknown. MFSD4B is more commonly know as Sodium-dependent glucose transporter 1 (NaGLT1), a primary fructose transporter in rat renal brush-border membranes that also facilitates sodium-independent urea uptake. The FucP/MFSD4 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.65297e-47
NZ_LN824141.1\|WP_045087660.1\|897312_897840_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	gnl\|CDD\|376665	pfam01923, Cob_adeno_trans, Cobalamin adenosyltransferase. Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.	6.78959e-73
NZ_LN824141.1\|WP_045087674.1\|917085_917469_+\|methylglyoxal-synthase	gnl\|CDD\|179969	PRK05234, mgsA, methylglyoxal synthase; Validated.	6.8444e-69
NZ_LN824141.1\|WP_045087670.1\|913343_913946_+\|semialdehyde-dehydrogenase	gnl\|CDD\|237580	PRK13992, minC, septum site-determining protein MinC.	3.54821e-30
NZ_LN824141.1\|WP_052670362.1\|904120_905047_+\|inorganic-phosphate-transporter	gnl\|CDD\|223383	COG0306, PitA, Phosphate/sulphate permeases [Inorganic ion transport and metabolism].	3.91378e-47
NZ_LN824141.1\|WP_045087671.1\|913972_915013_+\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349906	cd05656, M42_Frv, M42 Peptidase, endoglucanases. Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.	2.20813e-89

>NZ_LN824141.1|WP_171820588.1|906685_907792_-|alanyl-tRNA-editing-protein
MQGKIEIIEVKKEKQYYFAKINHSPFYPDGKGGQIGDRGFVGEAKIVEVRDDGLLLDREINIGEHAFEIDEDRRFEISQQHTAQHILSAAFEKIADLKTVGFKMGEEHSTIDLNGIDIDDKIFSEAENLSNKIIAECIIVEEITTSKEEANHFTLRKPLSEKVEGPVRIIKIGEFDESACGGFHVKNTGNINLLKIINTEKVKGNLTRIYFVAGKRALQDYSLKHNLIEKLSLKLTSGISQLDEKIEILIQENKEYKNKIKKICEYAAPFIVNEIIKTPLIVKEHKIIYYKKENDIADFISNLVDLNEYTLIVEDQENSTFIIFSKKINCKEFINRLKEKYDIKGGGSEVRGNIKGKISLDQIIDNLK
>NZ_LN824141.1|WP_045087665.1|905102_906593_+|glycerol-kinase-GlpK
MNKYILSIDQGTTSSRAIIFDHEGNIVNSSQREFSQLYPKPGWVEHNPDEIWGTTIGVIANVLGVSNIQPEQISAIGITNQRETTIIWDAKTGEPVYNAIVWQDRRTSSICDGLREKGYEELIRNKTGLLIDAYFSGTKIKWILDNVEGVRKRAENGELRFGTVDSWIIWKLTRGKVHVTDYTNASRTMIYNIFDLKWDDDLLNMLDIPRSLLPVVKESSEIYGYTDSSVFGANVPISGIAGDQQAATFGQLCFEKGMAKNTYGTGCFMLLNTSEVPVKSKSGLLTTIAWGLNGKVEYALEGSVFVAGAAIQWLRDQLRLIDTSADSEYFATKVEDNGGVYFVPAFTGLGAPYWDMYARGAIFGLTRGSRKEHIIRATLESIAYSTKDVLEAMEKDSGLSLKKLRADGGASENNFLMQFQADILGIEVERPLIVETTALGAAFLAGLAVGYWKDREELKKIWRCEKCFQPNMIEEDREKLYAGWKKSVDRVKNWEK
>NZ_LN824141.1|WP_052670362.1|904120_905047_+|inorganic-phosphate-transporter
MIFLYIIPSLLLGWSLGTNNAGHIFGPPVVSGLVSYKKVRIVASIFVFIGAIIGGGAGLKTLGQLTNLEVGYLSLSMFSAFLTMMIMTLLALPASATQAVVGALIGASILKGQVNLGLLVGIFVSWLLTPLGAIFFSYILYRVIAFFFRKFLTLATQDMFIRVLTWFVIVYSSYSLGANNVANVTGVFTDVLLSPLILSIIGGLSIAVGIFTTNQKVLYTVGKGILEMDHFSSAISIFGVSVSLWLFSLIGIPVSASQAIIGSIIGVGLATGTKTFDYKLILKIVFGWIGTPLASGLISVLLIRIFKL
>NZ_LN824141.1|WP_045087664.1|902690_903785_-|BMP-family-ABC-transporter-substrate-binding-protein
MKKSLVIFCLVACIVSAFGFKAIMVTDAGGLGDRSFNDGTWEGIQMAIRELDGVEGDVFVSKEQTDYLQNLTKAAEQADVVIGVGFLMSDILFNVAAQYPDTYFIGIDIEPSPGQNVPPNLALYTFKEEEGGFLLGYIAASMSKTNTVGFIGGLEVPPVKRYEIGYRTGIKAYNQIKNASVECITGYVGSFTDASKTKQIALSQYERGADIIFTGVTTGAVIDAAKEKGSYFYGLNNNAPLNSIIDAYFEKGRGYFVIGYDMDQDYMAPGYVLVSSRKKVDVATFNGIKSAKEDRIFKSGVQVLGLAEDGVGISQMKYTKGLVPNEVLAELVMLKNIVKNGELIIPKSEAELSAVDFSDIEFPF
>NZ_LN824141.1|WP_084217309.1|901710_902526_-|M23-family-metallopeptidase
MLTFFYLILLVSSFASYSVVTHKIQQNETLFSISIKYNVSISTILDWNPGISPNSLRVGQSLKIPQPDGYLYEVKKGDTLSSIAKLFFADVEDIKKINGLTSSTIVPGQKIFIPNSAIGKGFNNEKSIIWPTYGTISSLYGYRVNPISKEYTLHKGVDIAAPTGTPVFASEDGVVEFVGENNGYGLMIQIDSNSNTFIYGHLSQINVYKGQYVKKGQLIGRVGSTGVSTGPHLHFEVRREDKLYDPLVLLPSRNNIYVLDERESAYGVGGE
>NZ_LN824141.1|WP_052670360.1|901121_901709_+|HD-domain-containing-protein
MNINKIILEIEQYLKLMINSKERLNHIYSVVDFSNKLAEVHNISQERVKIAALGHDLFRDVKPSKLITIARIYNIPITQIELAAPILLHGMISAEFLKRKYGIDEEIYEAIYYHTSGYEYMGDIGRILVISDSAGDDREYRGVKKLRQESIKSLNLGYKLAIKNKIQYAIKKDRYVLEQTYKTWNRILLNKVENY
>NZ_LN824141.1|WP_045087663.1|899773_900955_+|MFS-transporter
MLALLIIIYISFISLGLPDSLLGSAWPVMYEELSVPVSHAGILSMIVSLGTVVSSFLSAKLIERFGTGRVTLVSVAMTAIALIGFGLSHSFIPLLFFAIPLGLGAGSVDAALNNFVALHYKAKHMNWLHSFWGVGATTGPVIMSFWLAKKNNWNMGYITIGIIQSFLVIALMFSLPLWNNSQIEKKGTQNKDNKKDDIKVLSLPKIFQIPKAKMALLAFFSYCSLELTTGLWVGSYAVNNYGVSSEVAAFWTSIYYLGITIGRFLSGFMSVRFSNTKLIKIGLSGIFIGITLIVLPLPVWKIPIGLSLIGLGCAPIYPSMLHQTPRIFGKELSQSMMGIQMAFAYIGSTFTPPLFGFVAEHIGISLFPFFLLMLAFVLFFATETVSSKVFVHE
>NZ_LN824141.1|WP_045087662.1|898215_899499_-|alkaline-phosphatase
MKKRSILLVLLVFLVSLLSFASGVNNVIFFIGDGMGANHMLLASYLEGYELTMMKAPYTGYALTYSADSNVTDSAAAGTALATGYKTNNGMIGILPNGEIVSTISEVLAKEGYKTGIIATSRITHATPASYYGHVLDRDDEDKLAEQLVNSNLSVVLGGGSKNFNPTTRKDGKDLIAVAKENGFDYITSKQELNSYSGDKVLGLFNSNHMNSVTERSDNEPLLPEMTAKALEILSKEGTPFFLMVEGSQIDWEGHDNDVYGVWKEVVELDQAVKVALDFAKDHPDTLIIVTADHETGGLGLSTGSPMNLEMVRSYQKTTDWIIANSSTSSKLKENVKKFYGYELADNELKYVENSSNKIESLSEVISKKANMGWTTHDHTGALVPILAFGSGSEEFTGIMDNTEFPKKIAYLLEVTFPDLIQIVPQN
>NZ_LN824141.1|WP_045087661.1|897850_898132_+|DUF503-domain-containing-protein
MFCLKLELKIKLFGLNSLKDKRSIVKNLTNRLRKKYNISIIEGNFNDSKNHLEIYISSVSKNKDYLLDLIEQIEQDIELMFGLEVEGEDYIIF
>NZ_LN824141.1|WP_045087660.1|897312_897840_+|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase
MSIYTKTGDSGETALWSGERVSKDDLRVESYGTIDELSAFISEATHYVNSQEIRKILKELQNDLFKVGGELASKGKQYIHPIEESDVERITNYVDYFEKRIQLKSFVIQGSTPQSSKLDICRTIARRAERRIISLDKKETVSPTIKKYINRLSDLLYVMARFEEFLQNKIEYKRW
>NZ_LN824141.1|WP_045087667.1|910285_911212_-|protein-translocase-subunit-SecF
MPNLNIVGKRKIFIYLSLAFIIFFVIVIFVKGFNFGVDFSGGSEIVISTQETYTIDQLRDALQKIDPSYATAKIVSVKPSDEEITKNFYVITVKDSFPSSQIKDEFINSLSTYLQSSDLEVEQFNDVSGYAAKEIRSFAWYAIIATLAVLLIYITIRFQFSFAIGAILALAHDVIVTLGFYSLFGIEMNLMAIAAFLTLVGYSLNNTIVVYDRIRENRAKSRATPIEEVMNQSINDVLVRCLHTSITTFIVVFLMLLMGGRSIASFAFGLTMGVVVGTYSSIFIASPIVIPMMKDKKKGTKKSSSKSR
>NZ_LN824141.1|WP_045087668.1|911211_912630_-|protein-translocase-subunit-SecD
MKSRRILLILSVAVFIFALLGIVLPLSENKNNISIFKYLPNIKLGLDIQGGSSLEYSMAIPEGARAEEIVNNVIAVLRRRLDSAGYTEAVVSEVVVGGERRVRVEIPGISDTRRAEELIGSKGKLYFAEVIETIESSTPPQITRNRKVKVDGEEIDLYSYVRDSRNPNVWYRVKNVFEFGTEPFQITGLDVTDARASLNPQGGGFVVNLSFSNQGKNKFELATANLIGKQIAIILDDEVIIAPVVRDKISEGRAEISGIESVQEAQNIAVLIKSGNLPVDLIKFQENTIGPTLGRDVVTTIVNAGIIGLVIVMVYLIIFYGWMGFVADIALLYNTLLLLGVLSWSGAILTLPGLAGIILTFGTTVDGNVIIYERIKEEMRVGRPPLTAIKFGFDKVFSTILDANITTVLAGIVLYFLTSGSIRGFAVTLIIGVLGSMFTNLVVTRVILEGSSNMIKPEKYLKGIVVGKGGNE
>NZ_LN824141.1|WP_045087669.1|912683_913106_-|preprotein-translocase-subunit-YajC
MYEKILNFVNFGPAGASDAQGVTEQAQAAPGGGFGSLIFLLVILVLMWVMLFLPQRRQEKKHKEMISSLKKGDKIVTSAGIIGKIVSISNDTIRIATGDRTEIDITKNAVAGILSSKSSAEEKVSEEENPDEKEDVEKKK
>NZ_LN824141.1|WP_045087670.1|913343_913946_+|semialdehyde-dehydrogenase
MDELVYAKIIDGEIIFYFAKGHTQKDLFESFKKELVKMKSFFNIGDSFYVYFEDGSQYNLINSIIKFAKNFDLNVAGAYFGKLPEGKVGNKELTLSSTKIYRKHLRSGQVVQNPGDIIIFGNVNQGAEVNAGGSVIIFGKVFGTVRAGITNKKNVFIIAYEMESPLVEIAGIPFYNYEWPKTPISIRVEGDKALVETLEL
>NZ_LN824141.1|WP_045087671.1|913972_915013_+|M20/M25/M40-family-metallo-hydrolase
MDTKDLIKNLSDSFGVTSFENCTFPLIEQFLLEINQDIKLEKIGIGNLVATYGQGNPKIAFFAHVDEIGIVISNIIDDTFARIEAVGGVDPRTLVGKRVCFRTENGEKLGVIGFLAPHLQKPEDKDKSPSFDELFVDFSVSGGTKDINVGDIGVINVEAKDLENDQIVGKAIDNRAGVAVLIKSFEYLQNLKFDGQLMLSFNKGEEVGLVGAKGAAEYLQPDYAVVVDVTFGERLPENVESFKIGEGPVITIGAPINRCVYDDLVKTAKDNNIKYQIEAVPSRSGTETDIVQIVGQGIKTGLVSVPILNMHSPSEVVNINDIDRAAKLLAMFALNMSLKTKGSLNV
>NZ_LN824141.1|WP_045087672.1|915009_916056_+|M20/M25/M40-family-metallo-hydrolase
MRKYLKDLTELSGISSREEKVREYIKSQVEGKVNNITIDNLGNLICFVKGKDSSKKMMVDAHMDEVGFMVTKINDDGTLGISPVGGVDPRVIKSQRLKIEGVLNAVVNSTPIHLDKDIKRVVKYEEIKVYAGFSSKEEASKKVNLGDMVTFDTTYVEEGNYALSKAFDDRVGCSIMLDIIDYIYENKLQPAFDTYFNFATQEEVGLRGTGVAAARIKPDFALVLEGTTAGDNPENPPEKWATHIGNGPVITFMHSGLVIKKEMFETIVNAAKALNIKFQYKMRTAGGTNAAKLAKTMYGIPAGVISVPCRYIHSPLAILNIDDYNNTYSLVKELVTNNERWVNYERAH
>NZ_LN824141.1|WP_045087673.1|916039_917044_+|M42-family-metallopeptidase
MKELIKNITELYGPSGREHEVREFIKKEIEDYVDEIKIDKLGNLIAIKKGHSGKTILFDAHMDEIGVVVTHIIDGGFLKIEQVGGQFPLNLVGARLNFKGRIGVVGIEGETDKELRENYKNVSLDNIYVDIGVSSKEEAEKYAPIGTFGVFADGFVDYGEYCLSKALDDRIGCASLIETIKQMKDNKHTVIFAFTVQEEVGLVGAFVSAYDYNVDRAIAIDVTDSLDTPKALKRMSMKLGYGPCIKIKDLASVSDREVVDWIKDTAVNNNIKYQLEVLTLGGTNAAGYQRTKSGIPSCTISIPTRYIHSPHEMICYSDVVDTVELILALSEADF
>NZ_LN824141.1|WP_045087674.1|917085_917469_+|methylglyoxal-synthase
MVNVALIAHDKKKLDLVMFVKEWKNVFSQCKLYATKTTGSVLKDKVGLEIQTFESGPLGGDLQIGALAVSGKIDFVLFLRDPLTAQPHEPDVSAVLRICDVHNIPLATNLATAEALVLEIEKKFTNK
>NZ_LN824141.1|WP_045087675.1|917512_918151_-|ABC-transporter-permease-subunit
MVQDLIFATLETLYMTLVSALFAILLGIPLGIALYMLSKSEKKSSKTFYSVLDWVVNIFRSIPFIILIILIIPLTRLLTGTIIGSTAAIVPLSIAAIPFMARLAENSFNNLSQGLWDTAVSMGMTNWQFISKVLLPETASEMVANITLLIINLITYTAIAGAVGAGGLGAMAINYGYQRFRMDVLIYDVIILVLLTQVIQFAGTKIANSLRK
>NZ_LN824141.1|WP_045087676.1|918152_919151_-|methionine-ABC-transporter-ATP-binding-protein
MLEIKDLNLIYEDNYHVLKDINFKVEDGEIVGIIGLSGAGKTSLLRTLNLLQVPTSGKILLDGVDLTSLDKEELRKIRKKISIVFQHFNLLSSRTVFQNVALPLEIEDLSKKEIEEKVNKMLESMNLIPRKDAYPSQLSGGEKQRTAIARALISNPDIILFDEPTSSLDPKTTQKILDLILEINQSTRKSILIVTHEMDVIKKICDKVVYLKNGYVNFVGPVHEFFIEKETELNNEFYQEINIDWSKTWEMVRNKNQKLLKIVFWGSKTHEPVLYDVAKKYDVSVNILYGKIEHLKDSPYGTMIIAINSDNSHVENFLKELSENVYKVEVLN

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Crispr_ID: NZ_LN824141_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_7

966300-966380

Orphan

Consensus_repeat	Method
GCGTATAGCACGTCTCTACAACT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_7

>merge|NZ_LN824141|7|966300-966380|CRISPRCasFinder
GCGTATAGCACGTCTCTACAACTAATAATCAACGCTGGTTTATAATAAAACGAAATGAGCGTATAGCACGTCTCTACAACT

>NZ_LN824141|7|7|966300-966380|CRISPRCasFinder
GCGTATAGCACGTCTCTACAACT	AATAATCAACGCTGGTTTATAATAAAACGAAATGA
GCGTATAGCACGTCTCTACAACT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087703.1\|962633_963959_+\|phosphoglucosamine-mutase	unknown	unknown	gnl\|CDD\|100095
NZ_LN824141.1\|WP_045087698.1\|956226_957645_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340830
NZ_LN824141.1\|WP_045087712.1\|972863_973634_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
NZ_LN824141.1\|WP_045087706.1\|966469_967222_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|378820
NZ_LN824141.1\|WP_045087701.1\|959487_960729_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270453
NZ_LN824141.1\|WP_045087700.1\|958196_959129_-\|sugar-kinase	unknown	unknown	gnl\|CDD\|238571
NZ_LN824141.1\|WP_045087707.1\|969069_970014_-\|DUF1385-domain-containing-protein	unknown	unknown	gnl\|CDD\|377780
NZ_LN824141.1\|WP_045087711.1\|971853_972867_+\|iron-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|376439
NZ_LN824141.1\|WP_045087714.1\|976834_977776_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087702.1\|960849_961752_+\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_LN824141.1\|WP_045087713.1\|974083_976273_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_LN824141.1\|WP_045087708.1\|969991_970246_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087705.1\|965498_966107_-\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|273579
NZ_LN824141.1\|WP_084217142.1\|967240_968566_-\|transcription-termination-factor-Rho	unknown	unknown	gnl\|CDD\|236490
NZ_LN824141.1\|WP_045087715.1\|977791_978160_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224639
NZ_LN824141.1\|WP_045087704.1\|964025_965390_-\|Do-family-serine-endopeptidase	unknown	unknown	gnl\|CDD\|273938
NZ_LN824141.1\|WP_171820590.1\|954567_956175_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|223571
NZ_LN824141.1\|WP_045087710.1\|970966_971857_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|223687
NZ_LN824141.1\|WP_045088614.1\|961778_962618_+\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_045087699.1\|957655_958183_-\|dihydrofolate-reductase	unknown	unknown	gnl\|CDD\|223340

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087703.1\|962633_963959_+\|phosphoglucosamine-mutase	gnl\|CDD\|100095	cd05802, GlmM, GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0
NZ_LN824141.1\|WP_045087698.1\|956226_957645_-\|glycosyltransferase	gnl\|CDD\|340830	cd03800, GT4_sucrose_synthase, sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.	7.2727e-94
NZ_LN824141.1\|WP_045087712.1\|972863_973634_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	1.57946e-94
NZ_LN824141.1\|WP_045087706.1\|966469_967222_-\|alpha/beta-hydrolase	gnl\|CDD\|378820	pfam12146, Hydrolase_4, Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.	1.61716e-55
NZ_LN824141.1\|WP_045087701.1\|959487_960729_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270453	cd14750, PBP2_TMBP, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold. This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.14554e-158
NZ_LN824141.1\|WP_045087700.1\|958196_959129_-\|sugar-kinase	gnl\|CDD\|238571	cd01166, KdgK, 2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.	7.79006e-68
NZ_LN824141.1\|WP_045087707.1\|969069_970014_-\|DUF1385-domain-containing-protein	gnl\|CDD\|377780	pfam07136, DUF1385, Protein of unknown function (DUF1385). This family contains a number of hypothetical bacterial proteins of unknown function approximately 300 residues in length. Some family members are predicted to be metal-dependent.	1.25309e-110
NZ_LN824141.1\|WP_045087711.1\|971853_972867_+\|iron-ABC-transporter-permease	gnl\|CDD\|376439	pfam01032, FecCD, FecCD transport family. This is a sub-family of bacterial binding protein-dependent transport systems family. This Pfam entry contains the inner components of this multicomponent transport system.	2.28572e-73
NZ_LN824141.1\|WP_045087715.1\|977791_978160_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|224639	COG1725, COG1725, Predicted transcriptional regulators [Transcription].	8.15559e-24
NZ_LN824141.1\|WP_045087702.1\|960849_961752_+\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	5.85332e-86
NZ_LN824141.1\|WP_045087713.1\|974083_976273_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	1.185e-57
NZ_LN824141.1\|WP_045087705.1\|965498_966107_-\|orotate-phosphoribosyltransferase	gnl\|CDD\|273579	TIGR01367, Orotate_phosphoribosyltransferase, orotate phosphoribosyltransferase, Thermus family. This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis].	6.14082e-67
NZ_LN824141.1\|WP_084217142.1\|967240_968566_-\|transcription-termination-factor-Rho	gnl\|CDD\|236490	PRK09376, rho, transcription termination factor Rho; Provisional.	0
NZ_LN824141.1\|WP_045087704.1\|964025_965390_-\|Do-family-serine-endopeptidase	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	6.91663e-155
NZ_LN824141.1\|WP_171820590.1\|954567_956175_-\|AAA-family-ATPase	gnl\|CDD\|223571	COG0497, RecN, ATPase involved in DNA repair [DNA replication, recombination, and repair].	2.12079e-125
NZ_LN824141.1\|WP_045087710.1\|970966_971857_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|223687	COG0614, FepB, ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism].	4.94224e-47
NZ_LN824141.1\|WP_045088614.1\|961778_962618_+\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	1.58598e-91
NZ_LN824141.1\|WP_045087699.1\|957655_958183_-\|dihydrofolate-reductase	gnl\|CDD\|223340	COG0262, FolA, Dihydrofolate reductase [Coenzyme metabolism].	6.47367e-27

>NZ_LN824141.1|WP_045087705.1|965498_966107_-|orotate-phosphoribosyltransferase
MTQNEKTDYKESDVLAILKETEAFLQGHFLLSSGLHSDTYIQCAKVLQYPKYAELFGRLIANQINTKIDLVVSPALGGIIIGYEVARALKVPFIFTEREESGDMTLRRGQKIDKGLKVVIVEDVITTGKSSLEVAKVVNESEGEVVLFSCIVNRSEKSTLLDRKIISLVNIKTNIYTPDVCPLCKKGYELVKPGSRKMINPE
>NZ_LN824141.1|WP_045087704.1|964025_965390_-|Do-family-serine-endopeptidase
MKKSFMVVIMAILISLTSFAAVNLDYESPIVNVVEVAAPAVVNIETTRTVAVQIDPFTQYFFERFFGLDIPEYQTKGLGSGFIFHEDGYILTNYHVIEKAKEITVTLSNGKKYEAELIGGDSDLDLAIIKLKTDEKLPILELGNSDNVKIGEWVIAIGNPLGLQNTVTVGVLSATNRTITKPEGDGSYYGLLQTDASINPGNSGGPLLNIHGEVIGINTAIAVDPELGNVNIGFAIPINIAKRFALSVMEIGTFQRGYLGVHIQNVTEDLKKSLGLKVDYGAYVTHVDQGSAAEKSGIQPQDVIIEFDGKKIETMNDLSSLVSTYPAGTEVEVVVDRFGERLTFKVKLEGQTAVAKAQEYFGIRVRNITDEDRKTYNIKKDIQGVLVEEIVDNKYVLGLKVGDVITEIAVNGVYYDIKNVSDWEKIASSVEKNSYVALIVYRSNVRYVIQFFYR
>NZ_LN824141.1|WP_045087703.1|962633_963959_+|phosphoglucosamine-mutase
MKSLFGTDGIRDVVNEKLTCELAMKLGNAVANLFSNKYKKLYLARDTRNSGKMLELAIASGALAGGMNVESCGVLTTPALAYITHKERALGIVISASHNPPIYNGLKVICEGYKISDEIEEKLEEIMLGGLLKYCNYTEIGTYIEDSSKQEYINYILSTYNNKLSSINYKIAVDVANGAAGAIIDDVFGRLGLSYDVYFNTPNGLNINDNCGSTSWKSLSNIVKEDGYDLGILFDGDADRCLFLDSQGNLVDGDALIAINALKLKEQGRLNNNIVVTTVMSNLGLEYYLKSHGLILLRADVGDKYVFELMTQKNGTIGGEQSGHIIFLDRSTTGDGIITALETLETLKFFSKSIEDLVAELPKFPQDLENITVKDKIKIMKDKRLEELKRKYEHIDNFRVLVRPSGTEHIIRVMSEGTDKNIVKQCINEFSQLIRKLDSEY
>NZ_LN824141.1|WP_045088614.1|961778_962618_+|carbohydrate-ABC-transporter-permease
MKAKKTTQKTILYIIVILMVIFYIFPFYWAIKSSFTSDKFLFTKDIKFWPQGFTFENYKKVFTERPFGLNILNSIIVAGATTIFSLIVGSFSAYAIARLKIPGKSALMLLILAVSMFPQVSILGGLFQLLRKMGLINSYPGLIIPYIALNLPLTTWILQNFFRELPKEIEESAYIDGCSKFETLWRIVLPLSAPGLVTTGLLAFIQAWNEFLFALTFMQTPEKYTVPVAIAMFTGKTFYEVPWGQLMAASVIVTTPLVVLVLIFQNKIVQGLTAGSVKG
>NZ_LN824141.1|WP_045087702.1|960849_961752_+|sugar-ABC-transporter-permease
MNVKGKYKRQDMNLAFWLILPTLLAIGITAFYPLGQTIYDSFFKWSLRPGFQREFVGFQNYINLFKDQRFLSALWNTIYFTIFSVLIEFILGLATALVLNADFKLRGLVRAAVLIPWAIPTAVSSQMWKWMYNDQYGVISLMLYNIGLLEPGTPILGTPGLAMAAIIAVDVWKTTPFVALLLLAGLQTISTELYEAARIDGAGLWKQFTSITLPILRPTIGVTLIFRTLDALRVFDVVYIMTQGAVGTETLAVYNRSLLMDNIFSPRGLFGYGSALSVVIFLIIGVFTIIYMRSLNIKLD
>NZ_LN824141.1|WP_045087701.1|959487_960729_+|ABC-transporter-substrate-binding-protein
MKKVFALLVILVLAFSAFSVTITMTAGAVGTELETLYKQIDMFMQENPDITVQVMPMPNSSTDRHDLYVTYLASGVPDPDVLMLDVIWPAEFAPFLVDLTDDYNYFELDEFFPGTVDSNTVDGRLVSVPWFTDAGILYYRKDLLQKYGYDVPKTWDELFNIAKDISAKEGINGFVWQGARYEGLTCDVMEFVHSFGGEIIESGDVVVDDPRYFDKNVAAIAFMKKLVDDGVTPKGVTTYMEEEARRVFQNGDAVFMRNWPYAWSLANAPDSPVAGKVGITVLPKGPEPDGRNSATLGGWNLGINRNSSKAEIEAAKKLIKFLTSHEQQVFKAVHAGQTPTRISAYNDPRTLEANDFYAEILDVFLSAEPRPISPIYNEISYEIQVAVHSVLTGQAQPKAAVESLAKNLKSLVY
>NZ_LN824141.1|WP_045087700.1|958196_959129_-|sugar-kinase
MYDLISFGEVLIDFISTDYVNTLKDASSFSKFLGGSPSNIAVNIAKQGFNTAIISRVGYDPFGDYIISQLKKYKVDTSTVIQDNLFQTDVVYVLKSILSPEFCAYRSASLHLDLPSNSSDMIKNTQAFHLSSWSISTDYNLKNAIYLLKNAKKNNVLTGFDPNYRKILWKTSLDIEDVLKIVLPYVDIIKPSLDDCYHLFSTTKKDEKYYIETFHSLGVKYVVLTLGEKGATVSDGSKMMHLDSLATNVVDTTGAGDAFWSGLYIGLIEGYDIFTASKLGNAFSAEKLKHVGAISEIGNYKELVNKYNIY
>NZ_LN824141.1|WP_045087699.1|957655_958183_-|dihydrofolate-reductase
MKVILIMVQSINGKVRLIINKNQPWSSQEDKKHFSKVTKEIGVVIMGRKTFEEIGKPLDKRKNIVLTGEPEKYQKLEKTYQGSLFFTDEKPESLLNRLEKEGYQTVALIGGPTINALFLEKNLIDEIYLTIEPVIIEGDLSLFSYVQGTYQFKLNEVINLNNDAILLKYQKQQGR
>NZ_LN824141.1|WP_045087698.1|956226_957645_-|glycosyltransferase
MKVLFLNPQGNFDKHDSHLTEHPDFGGQLVYVKEVSRELAKMNVSVDIVTRQIIDENWPEFAKTIDYFDDTKNPRIIRIAFGGKKFLNKELLWPFLNEYVENIITFYNGEKIDFVTTHYADGGYAGVLLKSKKDIDFSFTGHSLGAQKMDKMGVNYENFEKFDTEYNFSKRIMAERLAMKYAYKIIVSTNMERFEQYSHPLYIDVSDVNNDNKFKVVPPGVNTQIFNDNFKEIDEDTIQKITEKTKGIFKPFIILSSRLDEKKNHIGVVKAYASSKRLQEIANLGIFLRGISNPFEDINHLSEKEQGILKPILQVIKEAKIEDKVYFFDFRSQKALASAYKYFAQLKSIFAITAFYEPFGLAPIEAGACGLAVVATKNGGPSEIFSDGSGVLVDPFDIEDIERGLVEALQNFEIYSKKVKNRVLQKYTWKKTAEGYLEVIKEGIKNKTPKINLSNFELNAKELILKYLKDRE
>NZ_LN824141.1|WP_171820590.1|954567_956175_-|AAA-family-ATPase
MDGMLVSLSMNNFGLFKKANIDFSDSFNVITGESGTGKSMFLNSINVFLTGNVPQNLKTTEGSVSAFFIVNNQIKEIVQEYAPVQENELILSVNFTPKKTLFRINDTIVPRDIVQEISKFLIELHSQESNIALRDETYQNSLIFKVLRENFPDYFESYDLKYQEYLRLKKRYDNLPSNINEVLRNIDLLDYQIKVIEEVDPKPFEDDELSERFKTLNNKEEIKEKIYESLNILKDNEVHNMDIDIGTVVFNLSKIADFGFKDEYNMALSMQEQIDFLYNILQSKVDDLDLDPQELQTISDRLNKIMDLKRKYGPTLEDVLENLEKYKKEKEDLEEIKKDFNELEPKLNKLSKELIEESENIIDKTKPFLNNLKDSIEEHLKDLNMGNAEIDFSIEKLKEPKKEGAHRICFLLKTNPKSDFLPLSEIASGGELSRIILALEVVLGNTHTIDTMIFDEIDSGVGPRMADVVGKKLKELSKNKQIIVITHMPQVANLADTHFKIIKSLNEDDINSEIIHLNQDEKQKEIKEMYGSIIY
>NZ_LN824141.1|WP_045087706.1|966469_967222_-|alpha/beta-hydrolase
MRIFYRYFISNKPSKNEQPKLYIVHGLGEYSGRYEKFIKIFNELGFDVFIFDLPGHGYSYGKKGDIGNFYEIYYFLENYIQEDYFLFGHSLGGLLAARFVEITENKPKKLVLSSPALGDISQMKWLLNMLSVFPKLTFSNRIDPFDLSTNRKVCEEYKRDPLVHDKITVESAIGMFAQAELALKDIDKIDVQTLLLYGTDDKVVNISEYEKIQNPNINIISFNKGKHELFECVYNKNKFLETILNFYLSS
>NZ_LN824141.1|WP_084217142.1|967240_968566_-|transcription-termination-factor-Rho
MDETDSNLVSKKQTKDNIQAVEIDMAKLNEMSRKDLYDLARKFEIANYSKMTKNELKFAILRKQTESIGYFFYEGILEILPDGYGFLRSIDNSLLPGSDDVYVSQSQIKKFNLFTGDIVAGQVRPPKEGERFFALLRIEAINSLPPENARDRISFENLTPEYPTERMVLEHKNSPLSSRIIDLFSPVGFGQRGLIVAPPKAGKTTLLKDIANSIAANYPETRRYILLIDERPEEVTDIRDTVDAHVIAAPFDMDPQNQIKITEMALDHFKRLVEFGHDVVVLIDSLTRFAREYNLYVPSSGKLLSGGLDPAAIIFPKKFFGAARKIREGGSLTMIATALVETGSKMDEVIFEEFKGTGNMELVLARELANERIFPAINLKLSGTRKEELLYSKNELKNVIILRKFINDMSPKEALEFILSLMKKFKTNDEIMASIENQKVF
>NZ_LN824141.1|WP_045087707.1|969069_970014_-|DUF1385-domain-containing-protein
MVSKEKPKTVGGQAVIEGVMMKGVNTVVAVKRSDGKIAVKKINDDSWGIWEKIPFIRGIFVLIHSMIIGMGALSYSAKVSGEDEEELTTKDMVFAILIAVVVATLGFGVLPVLVTKPFHIESEFLFALIEGLIRAFLVLAYIWAISFMKDIKRVFQYHGAEHKSVYTYENGEPLDVTHAKKYTTLHPRCGTSFLIITVFASVVVFAISGGLGWNSTIEKIISRIVLLPVVAGVAYEFQRFTAKIINTKIGKILAYPGLMLQKLTTKEPDDEQLKIALVSLNYALDENFEGEIVLDLATNTITPVTAIPGTTLTK
>NZ_LN824141.1|WP_045087708.1|969991_970246_-|hypothetical-protein
MSDYEQLIEEISDVCQKNQELLEIVKKIAEMESTKRYEFRKRASKILKRENGIDKEALKFYYFITEENAAEEILRRINGVKRET
>NZ_LN824141.1|WP_045087710.1|970966_971857_+|ABC-transporter-substrate-binding-protein
MKKGIKKYVVLLLLTVLSVLTFAQLALVDDLGRFVKFDSQVQRVVSAAPLVSDYIKYLGLEEKVVGVTDWDTSIESEKIGDMFPLNIEKIISLNPDLVFLSGGFQEPEIERLQRYNIKSFVINPVGFNDIYKTITIIGSILGEPERAVEISNKFRQQYLGIAKNAFLWTKKPTVLYLMVQNNVGEMWTAGTGSYINELIAYAGGLNLAAPYSGNNGFFQIGPEFVVAQNPDIIIVDAYFEGDETAKNTLLNAPQLKNVKAIKNGKIVTVDGNKMSQASPSIIDVLSQLNQYFGDNR
>NZ_LN824141.1|WP_045087711.1|971853_972867_+|iron-ABC-transporter-permease
MKSTQKQGGQLPLVLFLVFISFVLIIVFTSFGSVKIDAKDVFLSLIGKQENEIYKNLIVNIRLPRVIGTFIVGAILAVSGNVLQLLVQNPLADPYMLGISSGASFGAVLYTALNSIYGFTLFLGLEGFSFLFAVLSTFIVLLIARQGKRLPILSLILSGVIVSFLFNSFTTLFTVMYWKNLIHVNLWLMGSTGNLAWNSNLKLLTILLVQFFIALLFSKELNVLAMGEEMAVYSGLNPESVKMLLILTTVLAVSFTVSQVGIIGFVGLIIPHIVRMIKGPYSFISNLYSVFFGGIFLMFADFIARTLFAPTELPIGVVTSIVGAPIFIYVMRRKERL
>NZ_LN824141.1|WP_045087712.1|972863_973634_+|ABC-transporter-ATP-binding-protein
MIDIDKLQFTYNNGFNLYIKKLDIKKGDIVSIIGPNGAGKSTLIKIISKIIKNYTGKIMIENKELSNYSYKELSRKIAIVPQEFNTTFEYDVESVISTARLPYSRRFSFFETQEDKKIINEVLELVGLVKYKNKPFSQLSGGEKQKVMIARAFAQKTPILLLDEFSSHLDPGYTQNLLKLVKSMAEKEGKTVLAVFHDINSAAIFSDKIVVMKDGEIKYQGTPKEIFKETLMKEIFDIEVYIIEHPIKKIPQILYK
>NZ_LN824141.1|WP_045087713.1|974083_976273_-|methyl-accepting-chemotaxis-protein
MKIQGKLVSRNVILFVAGFIAFLIIILYSITNYIVDNSAEKLIISSELKKQYFENFFNNIEKDLNIISNRPDLSNNLNLLLFQFNNINKRYSNNAKQYLQDMYITNNPFENRNELNSLLDIKNFELIESYSIVREYGAQHEKVHPELNILLKEKEYDDILFITTNGDIIYTTSKNNDIGCNVIQDLSETNLNQLFNSLTQSEDTTVKFVDFAEYPPTGKPEAFAGKAMLNAIGYPMGYLIFEISIEQIDKIMQDTTGMNELTQMYVVGEDLLMRSNSIYSDTPTILTQKVETAQVIKALNGEEGWIKSTDYTGESVLAVYQPFKYKEINWAMIGETKYTNIKEQINSFSKITILIFGLITIAVIISSIAFSRATVKPIKQITNKIQNFAKGDLTTSFEIESDDEIGEMSKALNEMSLSLKNSIENIMTFSKKIQNLSNELKSFFTVLEENSKALTLETQKTNKETEDTAVSLEEVSAGIEQVSATSEKVLGDLNILLQNSQKLAKDAQQGRKKIDEMRDTLKKSVDKTKDTSEIVKALSKNALDVGNIVETINAITDQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESRNSTEKISKILETIRKYTQEASNSTDETYDTVKETSEKTASILEHFNNILENVQGINESINEITVSFDQQAKITNEIAQAMDKASTSVSNISERINKIAKDIEEQDKQTSEISKNIQELTILATELKNQFEIFKI
>NZ_LN824141.1|WP_045087714.1|976834_977776_+|hypothetical-protein
MKRVEYLLKLVFALVLGVLALFAPSVFLKAILSIVALILLATNMRNYKILFLILSIVLFIVPASFFSNYISNRSFWRWINSDNFFQSSNNGETLKPDTYIDAADNLIISGPGFRILFDETSDKIYIPHEIKQSRSGDTLSLSSNSVNKSAFIEVGTKSPYNSIRIEASGLSISGNLTVKDMNIQTLGLSSYVDLQATNFIVNCAGLDLGGELSVDNIEINATGVSWKGTVDAQKVKVQGIGMDINLLVKRAEDIVIQATALNGSLKYLDEWAGTRNMSIYVTHGNFTLIEPSDNEGSLELNISGMINVDRKKY
>NZ_LN824141.1|WP_045087715.1|977791_978160_+|GntR-family-transcriptional-regulator
MFYEVDKHSGIPSYIQIMNQIKKEIIIGNLKKGDSLPPVRELSKIFNVNVNTILRALERLEFEGYLEAQHGVGYFVRTDMDLKNSVFNEVSSFVEKMKKENIDLETIKLLLEEVWRNEQFSE

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Crispr_ID: NZ_LN824141_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_8

973648-973735

Orphan

Consensus_repeat	Method
AGCGTTGATTATTAGTTGTAGAGACGTGCTA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_8

>merge|NZ_LN824141|8|973648-973735|CRISPRCasFinder
AGCGTTGATTATTAGTTGTAGAGACGTGCTATACGCGCGTCTCGTTTTATTATATTTAGCGTTGATTATTAGTAGTAGAGACGTGCTA

>NZ_LN824141|8|8|973648-973735|CRISPRCasFinder
AGCGTTGATTATTAGTTGTAGAGACGTGCTA	TACGCGCGTCTCGTTTTATTATATTT
AGCGTTGATTATTAGTAGTAGAGACGTGCTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087703.1\|962633_963959_+\|phosphoglucosamine-mutase	unknown	unknown	gnl\|CDD\|100095
NZ_LN824141.1\|WP_045087719.1\|980637_980850_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_LN824141.1\|WP_045087712.1\|972863_973634_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
NZ_LN824141.1\|WP_045087710.1\|970966_971857_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|223687
NZ_LN824141.1\|WP_045087720.1\|980864_982190_-\|acetylxylan-esterase	unknown	unknown	gnl\|CDD\|224423
NZ_LN824141.1\|WP_045087717.1\|978727_979564_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_LN824141.1\|WP_045087716.1\|978140_978731_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087711.1\|971853_972867_+\|iron-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|376439
NZ_LN824141.1\|WP_045087718.1\|979600_980608_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087714.1\|976834_977776_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087721.1\|983158_984835_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374899
NZ_LN824141.1\|WP_045087713.1\|974083_976273_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_LN824141.1\|WP_045087708.1\|969991_970246_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087705.1\|965498_966107_-\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|273579
NZ_LN824141.1\|WP_045087707.1\|969069_970014_-\|DUF1385-domain-containing-protein	unknown	unknown	gnl\|CDD\|377780
NZ_LN824141.1\|WP_045087715.1\|977791_978160_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224639
NZ_LN824141.1\|WP_045087704.1\|964025_965390_-\|Do-family-serine-endopeptidase	unknown	unknown	gnl\|CDD\|273938
NZ_LN824141.1\|WP_045087706.1\|966469_967222_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|378820
NZ_LN824141.1\|WP_084217142.1\|967240_968566_-\|transcription-termination-factor-Rho	unknown	unknown	gnl\|CDD\|236490
NZ_LN824141.1\|WP_144403473.1\|982448_982928_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087703.1\|962633_963959_+\|phosphoglucosamine-mutase	gnl\|CDD\|100095	cd05802, GlmM, GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0
NZ_LN824141.1\|WP_045087719.1\|980637_980850_-\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	5.0192e-06
NZ_LN824141.1\|WP_045087712.1\|972863_973634_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	1.57946e-94
NZ_LN824141.1\|WP_045087710.1\|970966_971857_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|223687	COG0614, FepB, ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism].	4.94224e-47
NZ_LN824141.1\|WP_045087720.1\|980864_982190_-\|acetylxylan-esterase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	2.65373e-09
NZ_LN824141.1\|WP_045087717.1\|978727_979564_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	5.18902e-57
NZ_LN824141.1\|WP_045087711.1\|971853_972867_+\|iron-ABC-transporter-permease	gnl\|CDD\|376439	pfam01032, FecCD, FecCD transport family. This is a sub-family of bacterial binding protein-dependent transport systems family. This Pfam entry contains the inner components of this multicomponent transport system.	2.28572e-73
NZ_LN824141.1\|WP_045087715.1\|977791_978160_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|224639	COG1725, COG1725, Predicted transcriptional regulators [Transcription].	8.15559e-24
NZ_LN824141.1\|WP_045087721.1\|983158_984835_-\|hypothetical-protein	gnl\|CDD\|374899	pfam16949, ABC_tran_2, Putative ATP-binding cassette. This is a family of putative two component ABC exporters. This is the membrane protein of approximately 573 residues and twelve transmembrane domains. It is encoded adjacent to an ATPase.	1.95909e-05
NZ_LN824141.1\|WP_045087713.1\|974083_976273_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	1.185e-57
NZ_LN824141.1\|WP_045087705.1\|965498_966107_-\|orotate-phosphoribosyltransferase	gnl\|CDD\|273579	TIGR01367, Orotate_phosphoribosyltransferase, orotate phosphoribosyltransferase, Thermus family. This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis].	6.14082e-67
NZ_LN824141.1\|WP_084217142.1\|967240_968566_-\|transcription-termination-factor-Rho	gnl\|CDD\|236490	PRK09376, rho, transcription termination factor Rho; Provisional.	0
NZ_LN824141.1\|WP_045087704.1\|964025_965390_-\|Do-family-serine-endopeptidase	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	6.91663e-155
NZ_LN824141.1\|WP_045087706.1\|966469_967222_-\|alpha/beta-hydrolase	gnl\|CDD\|378820	pfam12146, Hydrolase_4, Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.	1.61716e-55
NZ_LN824141.1\|WP_045087707.1\|969069_970014_-\|DUF1385-domain-containing-protein	gnl\|CDD\|377780	pfam07136, DUF1385, Protein of unknown function (DUF1385). This family contains a number of hypothetical bacterial proteins of unknown function approximately 300 residues in length. Some family members are predicted to be metal-dependent.	1.25309e-110

>NZ_LN824141.1|WP_045087712.1|972863_973634_+|ABC-transporter-ATP-binding-protein
MIDIDKLQFTYNNGFNLYIKKLDIKKGDIVSIIGPNGAGKSTLIKIISKIIKNYTGKIMIENKELSNYSYKELSRKIAIVPQEFNTTFEYDVESVISTARLPYSRRFSFFETQEDKKIINEVLELVGLVKYKNKPFSQLSGGEKQKVMIARAFAQKTPILLLDEFSSHLDPGYTQNLLKLVKSMAEKEGKTVLAVFHDINSAAIFSDKIVVMKDGEIKYQGTPKEIFKETLMKEIFDIEVYIIEHPIKKIPQILYK
>NZ_LN824141.1|WP_045087711.1|971853_972867_+|iron-ABC-transporter-permease
MKSTQKQGGQLPLVLFLVFISFVLIIVFTSFGSVKIDAKDVFLSLIGKQENEIYKNLIVNIRLPRVIGTFIVGAILAVSGNVLQLLVQNPLADPYMLGISSGASFGAVLYTALNSIYGFTLFLGLEGFSFLFAVLSTFIVLLIARQGKRLPILSLILSGVIVSFLFNSFTTLFTVMYWKNLIHVNLWLMGSTGNLAWNSNLKLLTILLVQFFIALLFSKELNVLAMGEEMAVYSGLNPESVKMLLILTTVLAVSFTVSQVGIIGFVGLIIPHIVRMIKGPYSFISNLYSVFFGGIFLMFADFIARTLFAPTELPIGVVTSIVGAPIFIYVMRRKERL
>NZ_LN824141.1|WP_045087710.1|970966_971857_+|ABC-transporter-substrate-binding-protein
MKKGIKKYVVLLLLTVLSVLTFAQLALVDDLGRFVKFDSQVQRVVSAAPLVSDYIKYLGLEEKVVGVTDWDTSIESEKIGDMFPLNIEKIISLNPDLVFLSGGFQEPEIERLQRYNIKSFVINPVGFNDIYKTITIIGSILGEPERAVEISNKFRQQYLGIAKNAFLWTKKPTVLYLMVQNNVGEMWTAGTGSYINELIAYAGGLNLAAPYSGNNGFFQIGPEFVVAQNPDIIIVDAYFEGDETAKNTLLNAPQLKNVKAIKNGKIVTVDGNKMSQASPSIIDVLSQLNQYFGDNR
>NZ_LN824141.1|WP_045087708.1|969991_970246_-|hypothetical-protein
MSDYEQLIEEISDVCQKNQELLEIVKKIAEMESTKRYEFRKRASKILKRENGIDKEALKFYYFITEENAAEEILRRINGVKRET
>NZ_LN824141.1|WP_045087707.1|969069_970014_-|DUF1385-domain-containing-protein
MVSKEKPKTVGGQAVIEGVMMKGVNTVVAVKRSDGKIAVKKINDDSWGIWEKIPFIRGIFVLIHSMIIGMGALSYSAKVSGEDEEELTTKDMVFAILIAVVVATLGFGVLPVLVTKPFHIESEFLFALIEGLIRAFLVLAYIWAISFMKDIKRVFQYHGAEHKSVYTYENGEPLDVTHAKKYTTLHPRCGTSFLIITVFASVVVFAISGGLGWNSTIEKIISRIVLLPVVAGVAYEFQRFTAKIINTKIGKILAYPGLMLQKLTTKEPDDEQLKIALVSLNYALDENFEGEIVLDLATNTITPVTAIPGTTLTK
>NZ_LN824141.1|WP_084217142.1|967240_968566_-|transcription-termination-factor-Rho
MDETDSNLVSKKQTKDNIQAVEIDMAKLNEMSRKDLYDLARKFEIANYSKMTKNELKFAILRKQTESIGYFFYEGILEILPDGYGFLRSIDNSLLPGSDDVYVSQSQIKKFNLFTGDIVAGQVRPPKEGERFFALLRIEAINSLPPENARDRISFENLTPEYPTERMVLEHKNSPLSSRIIDLFSPVGFGQRGLIVAPPKAGKTTLLKDIANSIAANYPETRRYILLIDERPEEVTDIRDTVDAHVIAAPFDMDPQNQIKITEMALDHFKRLVEFGHDVVVLIDSLTRFAREYNLYVPSSGKLLSGGLDPAAIIFPKKFFGAARKIREGGSLTMIATALVETGSKMDEVIFEEFKGTGNMELVLARELANERIFPAINLKLSGTRKEELLYSKNELKNVIILRKFINDMSPKEALEFILSLMKKFKTNDEIMASIENQKVF
>NZ_LN824141.1|WP_045087706.1|966469_967222_-|alpha/beta-hydrolase
MRIFYRYFISNKPSKNEQPKLYIVHGLGEYSGRYEKFIKIFNELGFDVFIFDLPGHGYSYGKKGDIGNFYEIYYFLENYIQEDYFLFGHSLGGLLAARFVEITENKPKKLVLSSPALGDISQMKWLLNMLSVFPKLTFSNRIDPFDLSTNRKVCEEYKRDPLVHDKITVESAIGMFAQAELALKDIDKIDVQTLLLYGTDDKVVNISEYEKIQNPNINIISFNKGKHELFECVYNKNKFLETILNFYLSS
>NZ_LN824141.1|WP_045087705.1|965498_966107_-|orotate-phosphoribosyltransferase
MTQNEKTDYKESDVLAILKETEAFLQGHFLLSSGLHSDTYIQCAKVLQYPKYAELFGRLIANQINTKIDLVVSPALGGIIIGYEVARALKVPFIFTEREESGDMTLRRGQKIDKGLKVVIVEDVITTGKSSLEVAKVVNESEGEVVLFSCIVNRSEKSTLLDRKIISLVNIKTNIYTPDVCPLCKKGYELVKPGSRKMINPE
>NZ_LN824141.1|WP_045087704.1|964025_965390_-|Do-family-serine-endopeptidase
MKKSFMVVIMAILISLTSFAAVNLDYESPIVNVVEVAAPAVVNIETTRTVAVQIDPFTQYFFERFFGLDIPEYQTKGLGSGFIFHEDGYILTNYHVIEKAKEITVTLSNGKKYEAELIGGDSDLDLAIIKLKTDEKLPILELGNSDNVKIGEWVIAIGNPLGLQNTVTVGVLSATNRTITKPEGDGSYYGLLQTDASINPGNSGGPLLNIHGEVIGINTAIAVDPELGNVNIGFAIPINIAKRFALSVMEIGTFQRGYLGVHIQNVTEDLKKSLGLKVDYGAYVTHVDQGSAAEKSGIQPQDVIIEFDGKKIETMNDLSSLVSTYPAGTEVEVVVDRFGERLTFKVKLEGQTAVAKAQEYFGIRVRNITDEDRKTYNIKKDIQGVLVEEIVDNKYVLGLKVGDVITEIAVNGVYYDIKNVSDWEKIASSVEKNSYVALIVYRSNVRYVIQFFYR
>NZ_LN824141.1|WP_045087703.1|962633_963959_+|phosphoglucosamine-mutase
MKSLFGTDGIRDVVNEKLTCELAMKLGNAVANLFSNKYKKLYLARDTRNSGKMLELAIASGALAGGMNVESCGVLTTPALAYITHKERALGIVISASHNPPIYNGLKVICEGYKISDEIEEKLEEIMLGGLLKYCNYTEIGTYIEDSSKQEYINYILSTYNNKLSSINYKIAVDVANGAAGAIIDDVFGRLGLSYDVYFNTPNGLNINDNCGSTSWKSLSNIVKEDGYDLGILFDGDADRCLFLDSQGNLVDGDALIAINALKLKEQGRLNNNIVVTTVMSNLGLEYYLKSHGLILLRADVGDKYVFELMTQKNGTIGGEQSGHIIFLDRSTTGDGIITALETLETLKFFSKSIEDLVAELPKFPQDLENITVKDKIKIMKDKRLEELKRKYEHIDNFRVLVRPSGTEHIIRVMSEGTDKNIVKQCINEFSQLIRKLDSEY
>NZ_LN824141.1|WP_045087713.1|974083_976273_-|methyl-accepting-chemotaxis-protein
MKIQGKLVSRNVILFVAGFIAFLIIILYSITNYIVDNSAEKLIISSELKKQYFENFFNNIEKDLNIISNRPDLSNNLNLLLFQFNNINKRYSNNAKQYLQDMYITNNPFENRNELNSLLDIKNFELIESYSIVREYGAQHEKVHPELNILLKEKEYDDILFITTNGDIIYTTSKNNDIGCNVIQDLSETNLNQLFNSLTQSEDTTVKFVDFAEYPPTGKPEAFAGKAMLNAIGYPMGYLIFEISIEQIDKIMQDTTGMNELTQMYVVGEDLLMRSNSIYSDTPTILTQKVETAQVIKALNGEEGWIKSTDYTGESVLAVYQPFKYKEINWAMIGETKYTNIKEQINSFSKITILIFGLITIAVIISSIAFSRATVKPIKQITNKIQNFAKGDLTTSFEIESDDEIGEMSKALNEMSLSLKNSIENIMTFSKKIQNLSNELKSFFTVLEENSKALTLETQKTNKETEDTAVSLEEVSAGIEQVSATSEKVLGDLNILLQNSQKLAKDAQQGRKKIDEMRDTLKKSVDKTKDTSEIVKALSKNALDVGNIVETINAITDQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESRNSTEKISKILETIRKYTQEASNSTDETYDTVKETSEKTASILEHFNNILENVQGINESINEITVSFDQQAKITNEIAQAMDKASTSVSNISERINKIAKDIEEQDKQTSEISKNIQELTILATELKNQFEIFKI
>NZ_LN824141.1|WP_045087714.1|976834_977776_+|hypothetical-protein
MKRVEYLLKLVFALVLGVLALFAPSVFLKAILSIVALILLATNMRNYKILFLILSIVLFIVPASFFSNYISNRSFWRWINSDNFFQSSNNGETLKPDTYIDAADNLIISGPGFRILFDETSDKIYIPHEIKQSRSGDTLSLSSNSVNKSAFIEVGTKSPYNSIRIEASGLSISGNLTVKDMNIQTLGLSSYVDLQATNFIVNCAGLDLGGELSVDNIEINATGVSWKGTVDAQKVKVQGIGMDINLLVKRAEDIVIQATALNGSLKYLDEWAGTRNMSIYVTHGNFTLIEPSDNEGSLELNISGMINVDRKKY
>NZ_LN824141.1|WP_045087715.1|977791_978160_+|GntR-family-transcriptional-regulator
MFYEVDKHSGIPSYIQIMNQIKKEIIIGNLKKGDSLPPVRELSKIFNVNVNTILRALERLEFEGYLEAQHGVGYFVRTDMDLKNSVFNEVSSFVEKMKKENIDLETIKLLLEEVWRNEQFSE
>NZ_LN824141.1|WP_045087716.1|978140_978731_+|hypothetical-protein
MNNFLNKLEVFIQKEFTEKSGRIFLFSLIFLFVIPLHISFLTWFFVFLFLTNMLGSDIKNKKFSLIISLPYSYAEVFFSSYIFSLLMILIPGTIGVAFINFSAVTAFLNILRALIFATAYYGVILISVTLGGDNFGIPFLILLADLILGSFGSGYNVNPYRLISPYYQGNIWGSLIFSLVILSLSLYLFEKRGVNK
>NZ_LN824141.1|WP_045087717.1|978727_979564_+|ABC-transporter-ATP-binding-protein
MIIEVNDLVKNFNSKPVLNKINFKVDVGEIFSLIGPNGAGKTTTLRCLYGELKPDSGSIRLFSDELNSKIKTKISVMTEDRLTFSNFKGSDYHKVWRMLYPNFDDETFSNFVLHYNLDMSQKVERYSMGMKTLFYIALTISSGADLLLLDEPTQNLDPVIRAEILSVLRKYANEANKTIVISSHEIYELEEISSSFAIIREGKILYTDDVDLAKEKHRMIRKGETIPSGEVVANFEQEVLVKTDEDIGRFPTFNEIVLAYLKSSQTFDPFGVKKSLES
>NZ_LN824141.1|WP_045087718.1|979600_980608_+|hypothetical-protein
MKKNIYLSNFIFALVLAVLAVLVPQVGLKAILGICSVLFFGWNMKNHKFAFVILALIFLIIPSVSFAILKSMDVSWSSLWERWGKNIFSNQNDYMVLEPDTYIDSAENVYIKGVSLEITFDENSDQIYIPHQVRQNRISNTLNLTSDINNRHKSIIVIGTKNPYNTIQINSTSLRLKGILKATYFKTNTTSLNIDADIETSNFSVGSTSFRLNQELKAHNVQIDATSININSDIYADDIEIDGTSIKWFGYIDSRNIRLDGTSLNLDMTVNCSESININGTSINVRIKYADTWNGDRFLSVYGTHGNLKILEPLSNTGNLTLRAEGKIKATRDKY
>NZ_LN824141.1|WP_045087719.1|980637_980850_-|alpha/beta-hydrolase
MQVPLLIINGTQDLKTPYELLKEKENQLKQKKDLEIVYIENMGHELYRSDTGVFEDSVIDQIVNWLKKVL
>NZ_LN824141.1|WP_045087720.1|980864_982190_-|acetylxylan-esterase
MKKLMLITLSIILVPMFIFSETYTYYVYQNNVEMGNISVDVDPHSYTGKTTTVLQVGLNTVKYIAQTKYDNDWTFKEYNLDIYVDNQKQVSFKSSYDGQKINNYFDGISLKNYEVSDAIILDNNLILDHIFAIYYKQLTDGTYTSFIPQLVLNQLTWDYAVLNIDIKYIDSENFVISSPGVDQKVTFKDNKLIRLEIPSQLIEVTESKKEVKEKSYIEEEITFPSFDEFELNGSLMFPKEIQKNEKIPAIVLVHGSGANDRNESISYMAPFLQLSEGLVNNGYIVLKYDKRNYTMMKNKQDTLNVMPLDFIKDAQAAIKYLKTIPEVDSDKIIVIGHSEGGSFLPHIVKGEKVAAAVALSPGLIEITDLMVYQIDYQINYLKKLNVDKSQDYTITMLENLLAQLKEVNNDMKNGKIDPDKVYLDYYKGSYLIQWSELTKKL
>NZ_LN824141.1|WP_144403473.1|982448_982928_-|hypothetical-protein
MKPVQKPLKDATFMSTIRWKLVNALMCDYTYGYITKSKRVSLGLEKTHYNDAFCIAGGINQQRIEPIYFEQIRRNNRSLEKFYDAKYVDIRDKSIKTGQELFCGRRTRNKNLNEENLHKYRGAKKSKGRRNIRKQRYAYQPKDIVTFESKKYSVQGVQN
>NZ_LN824141.1|WP_045087721.1|983158_984835_-|hypothetical-protein
MKVKKLISLISIELDQHFNITKRRHTVKKNKGELASLIAMIASISILIVVYFLFYINILKTNLALYTEMNLQQLFLNNFIMMSGLFGFFLGAFVLIGEFFSNKDLKVLITLPLEPHETIFGKLFIVLFDQMIISLLILLPALIYYGIYTKQTTVYYIISIIVFLLSQVFPVMTVLLYTLIISKLLKRFKRRELLLYLSTALFMIIVAVLLFFSGNTFSINIENSQELPDITINPEGILSRLAWIYPPAFFATKALSTIGVNQLIWLLMFLGFHMLLFVLTYFLGNRFYYSFYSILSEQVSSKKTGANFEEETWFSKASNPEKALLKREWYYFLKTPAFSVNGFANVLVFPIMIIIFAIIFSKIGVPEEIFEQILSYNIFIVGMISVLSSSLNGLSYSCFSREGHLLKELKMLPIEIEQILKAKIIHIYQISSIGFLSGLIIGTIFFKLNFFEFLGTVLFSIMVNIFLNLIQMLIDVSNPYLDWDNPQKAMKENVNGLFATLIIFGFLGVFGFLIYKLVPIVNSYVLLASLSLLFLILNFLIWRLLKSQLPTAPRGGGL

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Crispr_ID: NZ_LN824141_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_9

1059459-1059722

Orphan

Consensus_repeat	Method
TTTAAAACCAGGAGACGCCCATATAGGTCGTCTCTACA	CRISPRCasFinder

3 spacers

The CRISPR arrays of NZ_LN824141_9

>merge|NZ_LN824141|9|1059459-1059722|CRISPRCasFinder
TTTAAAACCAGGAGACGCCCATATAGGTCGTCTCTACAGTTGTTTGAATTGAGGTTTGAAGCAATATTAAACGTATTGATTTTTGGAATGTGTTTAAAACCAGGAGACGCCCATGTAGGTCGTCTCTACAAAAAGATAAATTCATAAAATGTTTTGTTATGATTAAACCATGAGACGTGCGTATAGCACGTCTCTATAAAAAAATCAATTCACATTTTTTGCTACGTTTGAACCTAGGAGATGCGCATGTAGCACGTCTCTACA

>NZ_LN824141|9|9|1059459-1059722|CRISPRCasFinder
TTTAAAACCAGGAGACGCCCATATAGGTCGTCTCTACA	GTTGTTTGAATTGAGGTTTGAAGCAATATTAAACGTATTGATTTTTGGAATGTG
TTTAAAACCAGGAGACGCCCATGTAGGTCGTCTCTACA	AAAAGATAAATTCATAAAATGTTTTGTTAT
GATTAAACCATGAGACGTGCGTATAGCACGTCTCTATA	AAAAAATCAATTCACATTTTTTGCTACG
TTTGAACCTAGGAGATGCGCATGTAGCACGTCTCTACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087780.1\|1050743_1051838_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340831
NZ_LN824141.1\|WP_052670384.1\|1062920_1063913_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227265
NZ_LN824141.1\|WP_045087787.1\|1061230_1061452_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087788.1\|1067761_1067962_-\|type-II-toxin-antitoxin-system-HicB-family-antitoxin	unknown	unknown	gnl\|CDD\|374224
NZ_LN824141.1\|WP_045088627.1\|1068323_1068524_+\|type-II-toxin-antitoxin-system-HicB-family-antitoxin	unknown	unknown	gnl\|CDD\|224514
NZ_LN824141.1\|WP_084217315.1\|1066739_1067381_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236344
NZ_LN824141.1\|WP_052670379.1\|1049659_1050127_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379098
NZ_LN824141.1\|WP_084217170.1\|1060304_1060691_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274805
NZ_LN824141.1\|WP_084217157.1\|1050051_1050546_+\|DDE-type-integrase/transposase/recombinase	unknown	unknown	gnl\|CDD\|366234
NZ_LN824141.1\|WP_084217313.1\|1054872_1055043_+\|transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|376415
NZ_LN824141.1\|WP_045087781.1\|1051894_1053286_+\|O-antigen-ligase-family-protein	unknown	unknown	gnl\|CDD\|377422
NZ_LN824141.1\|WP_045087786.1\|1057031_1058486_+\|lipopolysaccharide-biosynthesis-protein	unknown	unknown	gnl\|CDD\|240533
NZ_LN824141.1\|WP_045087785.1\|1055629_1056817_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340828
NZ_LN824141.1\|WP_052670381.1\|1053795_1054209_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|132997
NZ_LN824141.1\|WP_171820592.1\|1061050_1061197_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_084217174.1\|1070026_1072399_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_LN824141.1\|WP_084217155.1\|1049293_1049575_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_052670383.1\|1061748_1062909_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|284995
NZ_LN824141.1\|WP_045087784.1\|1055085_1055598_+\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|275030
NZ_LN824141.1\|WP_045087789.1\|1069343_1069970_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|369778

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087780.1\|1050743_1051838_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	5.29755e-59
NZ_LN824141.1\|WP_045087788.1\|1067761_1067962_-\|type-II-toxin-antitoxin-system-HicB-family-antitoxin	gnl\|CDD\|374224	pfam15919, HicB_lk_antitox, HicB_like antitoxin of bacterial toxin-antitoxin system. This is a family of HicB-like antitoxins.	4.53697e-20
NZ_LN824141.1\|WP_045088627.1\|1068323_1068524_+\|type-II-toxin-antitoxin-system-HicB-family-antitoxin	gnl\|CDD\|224514	COG1598, COG1598, Predicted nuclease of the RNAse H fold, HicB family [General function prediction only].	8.32018e-06
NZ_LN824141.1\|WP_084217315.1\|1066739_1067381_+\|hypothetical-protein	gnl\|CDD\|236344	PRK08869, PRK08869, polar flagellin E.	2.48497e-39
NZ_LN824141.1\|WP_052670379.1\|1049659_1050127_+\|hypothetical-protein	gnl\|CDD\|379098	pfam13276, HTH_21, HTH-like domain. This domain contains a predicted helix-turn-helix suggesting a DNA-binding function.	0.00680622
NZ_LN824141.1\|WP_084217170.1\|1060304_1060691_+\|hypothetical-protein	gnl\|CDD\|274805	TIGR03830, transcriptional_regulator_XRE_family, putative zinc finger/helix-turn-helix protein, YgiT family. This model describes a family of predicted regulatory proteins with a conserved zinc finger/HTH architecture. The amino-terminal region contains a novel domain, featuring two CXXC motifs and occuring in a number of small bacterial proteins as well as in the present family. The carboxyl-terminal region consists of a helix-turn-helix domain, modeled by pfam01381. The predicted function is DNA binding and transcriptional regulation.	8.13594e-26
NZ_LN824141.1\|WP_084217157.1\|1050051_1050546_+\|DDE-type-integrase/transposase/recombinase	gnl\|CDD\|366234	pfam00665, rve, Integrase core domain. Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.	8.04198e-10
NZ_LN824141.1\|WP_084217313.1\|1054872_1055043_+\|transglycosylase-domain-containing-protein	gnl\|CDD\|376415	pfam00912, Transgly, Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.	8.23338e-06
NZ_LN824141.1\|WP_045087781.1\|1051894_1053286_+\|O-antigen-ligase-family-protein	gnl\|CDD\|377422	pfam04932, Wzy_C, O-Antigen ligase. This group of bacterial proteins is involved in the synthesis of O-antigen, a lipopolysaccharide found in the outer membrane in gram-negative bacteria. This family includes O-antigen ligases such as E. coli RfaL.	2.91959e-09
NZ_LN824141.1\|WP_045087786.1\|1057031_1058486_+\|lipopolysaccharide-biosynthesis-protein	gnl\|CDD\|240533	cd13128, MATE_Wzx_like, Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).	6.24564e-27
NZ_LN824141.1\|WP_045087785.1\|1055629_1056817_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340828	cd03798, GT4_WlbH-like, Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.	6.02637e-86
NZ_LN824141.1\|WP_052670381.1\|1053795_1054209_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|132997	cd00761, Glyco_tranf_GTA_type, Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.	1.122e-41
NZ_LN824141.1\|WP_052670384.1\|1062920_1063913_+\|hypothetical-protein	gnl\|CDD\|227265	COG4928, COG4928, Predicted P-loop ATPase [General function prediction only].	0.00197447
NZ_LN824141.1\|WP_084217174.1\|1070026_1072399_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	3.36871e-24
NZ_LN824141.1\|WP_052670383.1\|1061748_1062909_+\|AAA-family-ATPase	gnl\|CDD\|284995	pfam07693, KAP_NTPase, KAP family P-loop domain. The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.	5.12318e-44
NZ_LN824141.1\|WP_045087784.1\|1055085_1055598_+\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|275030	TIGR04176, hypothetical_protein, EPS-associated transcriptional regulator, MarR family. Members of this family of MarR-family transcriptional regulators are associated with long genomic loci consisting of genes encoding enzymes for the biosynthesis of exopolysaccharides. These genes include glycosyl transferases, sugar modifying enzymes (epimerases, isomerases, methyltransferases, aminotransferases, etc.), and exopolysaccharide polymerases (wzx, wzy). In Leptospira interrogans, borgpeterenii and biflexa, this gene is observed first in unidirectional EPS biosynthesis loci as long as 90 genes. MarR genes (pfam01407) are known to bind to DNA regions with palindromic or pseudopalindromic sequences as homodimers, and to bind small molecules as triggers for conformational changes controlling on/off states.	1.97435e-15
NZ_LN824141.1\|WP_045087789.1\|1069343_1069970_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|369778	pfam08242, Methyltransf_12, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	1.21594e-06

>NZ_LN824141.1|WP_045087786.1|1057031_1058486_+|lipopolysaccharide-biosynthesis-protein
MSKEREFIKSFFEFSIGQWIAALISFITTPITTWLIIPEEFGKASMFTLAFNLLLNVALLGADQSFVRMFYEKEEDKRRDLLWNALIPSLTLGFVVFILIGIFWKQLSFVLFGDYSHFLPIFLLGITIIIGTIERFATLVVRMKQRGIAFSTLRVVNGLSNAVFTILYALLVSRTFYAVIVGLFFSHVASLLLAIFLEKDMWVGKFKINTGLVKEIIKYGLPFVPTFLITWLFQSFDKLALRNYSDFTEIGLYSAAFKVVAIMNLIQTGFTTFWTPVSYESYENDPESTGLFEKVSLFISASMFVLGMLIIVFKDVIFLLLAKSYRSAAQISPFLILMPIMYTTSEVSVVGINFKKKTFWHMLIAAISAGCNIVGNVLLVPLYGAKAAAFTTGVSYIVFFCMRTFISKKLYPVNYHLGKFFSATAVFVIVAFINTFVGNVVWQISSALIGLILILLVYNNEVRYVFDLVVDALKRVKNKVVNKA
>NZ_LN824141.1|WP_045087785.1|1055629_1056817_+|glycosyltransferase-family-4-protein
MRVLFITNLFPYPQNPTSGVFITNRLKALRNLEVDFDAYGLISQDSSTVKLARKVLGKKGISVNEAFYEVNGIKYKFAFFNRNIYDVFSDKILKRNKVYFYSENAANQIFNNSKEFDIIHAHGMYNLPAGLVAKLVSEKLKVPYVITCHGSDINLAMPNNKELYNNVLEQAGKVIFVSNALLNKAKSLGYSGKNAVVIPNGMEPETFKPLDKEKIKRELGLSKKVVGFVGNLVFIKRADKFPEIFENISSNKDVEFLVVGDGELRENIEKECQKRNLNVKFVGRVSQDKVPYYMNAMDVMILPSKNEGWPCVVLEAQACGVPVVGSSNGGIPEAIGDGGIVIEEGEDFEKRFADAVVELLKNPIERDYLRERALGFSWENIVKQEVAVYEEVLKK
>NZ_LN824141.1|WP_045087784.1|1055085_1055598_+|winged-helix-turn-helix-transcriptional-regulator
MEENELLILEIIENNASVTQREISKKSGLSLGMVNLLLKKFVKKGLVKLERLDGKSFRYILTPEGFKEKSKKTIDYIKRYYNKTMIIKQNIERVIRTYGRNRTYALFGNDKEMKEIIEGILKELNVDYIIENNLQNINNSQIIIFWDIDDKEKLNEFNCEFLLGNYNNEW
>NZ_LN824141.1|WP_084217313.1|1054872_1055043_+|transglycosylase-domain-containing-protein
MLITYLENVYFGRSNFGIYTTSENYLGTSAFVLNRGQSFFLAERIALPNIFRKNVV
>NZ_LN824141.1|WP_052670381.1|1053795_1054209_+|glycosyltransferase-family-2-protein
MSKISVIIPPYNVEKYVERTLRSLMAQTFKDFEVIIINDGSTDNTEKIIQEVLQNANFQWKLINQENQGVSAARNRGIIESKGGYVCFLDADDYYHPTFLEKMYNKAKEKNYDLVFCNFSYVDENGKTILEPKQSKK
>NZ_LN824141.1|WP_045087781.1|1051894_1053286_+|O-antigen-ligase-family-protein
MDRNANENTKFIDFIKALFFLFIVIQALIFNNAFITFGLFILLFFLEKKYLLSIILVSPIIETILIVVEGVTITKLLVIFYTFYFLYVIVKENAVIIDKKSWILLVYLFIVIFGLFNAITFGPFLSLVDWDYNAIINENFISYIPKILFSILLYSYIKIKGYNYLRDNLRYLAVLISIALIIIAVYFFITISNESSNWWNVARRFTFKGADPNNFASILSSLSIFPLYLILKSRTKREIVVGIISVALIYFSIFLTLSKGGTLTLIFSIILTFFVLSKKNVKRSFFVLSLGIIIIAILVNFEIIDFSPLYERFFGEHIYDISSFTTRRSDWWLAGIKAIKQRPILGFGGSFYAGMWINYTAYGEMFVMHSLYIEILVQYGILGLIVFLWIIVRILKDFKQLINKLNKGQLKDTIFLIPFISLLTCLFAGLSLSWQWRDLLWFFISICLGVGSLTGENIKMSNI
>NZ_LN824141.1|WP_045087780.1|1050743_1051838_+|glycosyltransferase-family-4-protein
MQVTHVISSCIPGGAQVFVKSLPKQLYLEGNEVELWVMIKAKDIPYTNDQSICFEEKFIEELENTNIPVRFIWKRPNKDWYKTSKNLNKLFLQFRPDIVHSHSESGTFHICRALDTKVKIIQTIHSRKITQKFIRKFYINPRCSIFVAISNKVRIILEDNLKISPEKIKLIYNGIDTNDFLYENRNVKNKVKSIVSIGRFTKAKDCPNLLSAFSLLKSLLENERLDVPNLLLVGEGELRNQIKDEVKEKKLSENVKFLGVRNDIPEILKHSDIYVMSLQWEGLSISLIEALASGIPIVTTDAGSNNEIVENNVSGLIVPIKDPEVLANGLYKLIIDDQIWKKFSEEASKRAKLFTIEECAKKTC
>NZ_LN824141.1|WP_084217157.1|1050051_1050546_+|DDE-type-integrase/transposase/recombinase
MYFYNERWFFPILDIIDKTIVSSQIGHSSKLKDFIKAVHTGISYRKVNPKELIIRTDNGPQFKSKATEAFMNELEITHEFGYKNNPNSQDFIELHHFNLEREFVQLNSFENIEEIFQAYNAYMFFYHNLRRYGSLNYMTPSEFSKMFEINSDTYFNSKTIFVKK
>NZ_LN824141.1|WP_052670379.1|1049659_1050127_+|hypothetical-protein
MSSSSFYFKTRFFFVVECIKAKSKQKRFPGFSYTINGQIVEDERIKEIIISIYENSNPNDPTFYFKSVIDKKLFVVFKNQLGIIVNHKKICRLRKELGVVRAYKNHFKHAKKRPNNQEIDALNGFREGNIKFISTTKDGFSPYWILLIRQLFLHR
>NZ_LN824141.1|WP_084217155.1|1049293_1049575_+|hypothetical-protein
MLFLSGYKRSNYNDSFFDVKKGRAKSIISDYSKIPPIIYESAGIDRSDDYNTSNDSVYLKRKLSYYEKILLEKELQLRIIMDELELKKNMNHK
>NZ_LN824141.1|WP_084217170.1|1060304_1060691_+|hypothetical-protein
MIITLNFIYHFLCDSLVDYEIIEKKEVYNLRGDLIEINSYVAKCKTCNSELFEPYLENENLKQLYRKYAKKHNLVLPEDIKSMREKYDVSQTLFAIILGIGEATIERYESGSLPSESISNLIKNEFST
>NZ_LN824141.1|WP_171820592.1|1061050_1061197_+|hypothetical-protein
MIMIVENAFIFSFILRFKFESIPNVIANNSYKRWLVKKFITFILRAKS
>NZ_LN824141.1|WP_045087787.1|1061230_1061452_+|hypothetical-protein
MALYYLNLTPKSEGKGLHYEIHKEDCKWLEQVEHFELIGNFFNCRGAINKAKLDHPDWKIDGCFYCCKDCHNL
>NZ_LN824141.1|WP_052670383.1|1061748_1062909_+|AAA-family-ATPase
MFKPDQPIQSSKDDILGRSSFAKSLGDAVLSYTEKESIVVGLFGEWGSGKTSIINMMLEHIENVSKEKNNEKPIIFRFNPWNFSDQNQLISLFFTQMSITLGRQDYSENIKKTGEKLETYSKLFSLLKIIPVINTIAELLENSGDALKSLGDIKSHDLDSLKEELNELLSKQKQKILIIIDDIDRLNNTEIRQIFQLVKSLGDFPNTIYLLSFDKEVVIKALEKVQEGSGTVYLEKVVQIPFEIPAISEQDVNHLLLKELNELLKDFPENRFDEKHWNHVFHGGFKYFFRNIRDVTRYINSLKFSFGLVKDEVNFVDYLAITAIQVFMPEVYYGIRDNKEVFIGVHNQYYRQIDNYYSHYYRSIKDFDKKICDEIIKKGIDFQKKF
>NZ_LN824141.1|WP_052670384.1|1062920_1063913_+|hypothetical-protein
MILFPKLEYFYYDTSNYTNTSLDTWRRECRICSPEMVDVYFKLALPKGSFSQKEIYEILELGNNSELFSNRLLKLKEEGRIIFFLDRLEDYTVKDIPEENIEPIISSLMDVGDLIIKKGGLFSGTDSSIFRIVHKLLHRFKDQEIRFNIIKRAIEHAKRSLYIIVFEVGELEGECDKHASKESSITDGNLTVNSEQLEELKNLVCRKIETWADNGGLAEHLQMDYILYYWKVWGDIEKVDSFVRNMIKDDIGLINFVSRFLNHNIFYYREGTDTRLKMNLEIIKEFVDLEEIEPRIREIYSSDIEKLDEQQRKAIELLLDTYDGKIKENF
>NZ_LN824141.1|WP_084217315.1|1066739_1067381_+|hypothetical-protein
MITATLDDLDKENIGYYSDDGIFLLKSTNPLSPGETALDLEIGSWREEVFSTEAGYYYEDTLLWKTDSPFDVDDLNNWKSFEEAGFEVGYYDPEGKLIFATNMAFENDRRITKGIDVSTQEAADEAISKIDNAINYVSNERSNLGAMQNRLEHTIRNLQVSSENLSAAESRIRDADMAKEIMEFTKQQILMQTSNAMLAQSNTIPQNVLKLLQ
>NZ_LN824141.1|WP_045087788.1|1067761_1067962_-|type-II-toxin-antitoxin-system-HicB-family-antitoxin
MQKLTYRILLRKEPEGGYTVLVPALPGCITYGKIIEEAIKMAKEAIELYLESMIENGEEIPTEEGA
>NZ_LN824141.1|WP_045088627.1|1068323_1068524_+|type-II-toxin-antitoxin-system-HicB-family-antitoxin
MKVTVVVQKEDNWYVAKCIENNVVSQGKSIEESLESLKEALELYYEDTMPEEKNPVTLITIMEVPL
>NZ_LN824141.1|WP_045087789.1|1069343_1069970_-|class-I-SAM-dependent-methyltransferase
MENKSNFFLKINSSREYWEQRYSMGGTSGAGSYDKLAEFKAEVINSFMKNYQINSVIEFGCGDGNQLSMFDFPSYIGLDVSRTAIKLCIERFKYDKSKSFFLYDSICYKDNHAIFKADLAISLDVLYHLVEDNIFELYMNHLFESAERYVIIYASNFNSKQTNHIKHRQFSIWIDNNLSNWKLIDIIKNKYPNESLADFFIYQNIEND
>NZ_LN824141.1|WP_084217174.1|1070026_1072399_-|methyltransferase-domain-containing-protein
MYDKIFKLIQNGELNKAQEQLENTPENDPKRYNISGLIYYQKKEFDKAKEEFEKGLKINPVDSDLLFNYGYLLKNINQEKEAWRYLMRIHNKDWATYDLLGDIEYKNRSKLASLRFYKKAAELPNSPNEMKKKFIDMRNIVKQDTKIAFLCLPGLDNFLKDIVETFSLGYDVKLVVTTNGNQISEAIKWADIVWLEWANEMTVFATNQVPEIQNKKVVCRLHGYEIFGGYPQKINWTNIDQLIFVNGHKKELFGKVYPNAKIEKVVINNGIDLNKFTFNVHNKNHNLLIMGNINYRKGFETLLLCFEQLLKEDNRYKLCIKGKFQDLRYEDYILNAIKEMNIERNITFIDKYIEDIDLWGEQFGYILSTSIEESFHYTVGEFMAKGIKPVINSWPSAREVWPNECIFTTIDQFKEKILEDKYDSNFYRRFIEDNYSLEEQIGSINNIFKITESHERKIVKNEHESDNNLSLNYIISKFIEYTPYTDNYINSFDFENSKITIGKVEKITKDFSLIEFIVKNNDCKQLALQNIWFDKSSGKLILPDYILKSKNKTKIEAFIYDVLSYNLKFNNNIASFILDEAILNDIKENQLAYTWERGIPATPFMPALGYLKTMFRYNFAANFIEKDDVILDAACGFGYGSAYFSKLCKKVYALDIAKENIEFGRNTYSFDNIEWMEGDVTNLPFKNEKFDVYVSFETFEHLPLNILDKYLREAIRVVKKDGFFILSTPNKETRKNIHNPFHIKEYNFEELSSILRKYFKDIDYYSHIGYNIEKGFDDRANNFIVICRKQ

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Crispr_ID: NZ_LN824141_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_10

1088665-1088754

Orphan

Consensus_repeat	Method
AGACGCCCGTATAGGGCGTCTCTACAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_10

>merge|NZ_LN824141|10|1088665-1088754|CRISPRCasFinder
AGACGCCCGTATAGGGCGTCTCTACATCTGATTTAATCGAAGGTTAAATGATCTATTATTGGTAGACGCCCGTATAGGGCGTCTCTACAT

>NZ_LN824141|10|10|1088665-1088754|CRISPRCasFinder
AGACGCCCGTATAGGGCGTCTCTACAT	CTGATTTAATCGAAGGTTAAATGATCTATTATTGGT
AGACGCCCGTATAGGGCGTCTCTACAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087809.1\|1093549_1094980_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_LN824141.1\|WP_052670386.1\|1080831_1082286_+\|lipopolysaccharide-biosynthesis-protein	unknown	unknown	gnl\|CDD\|225153
NZ_LN824141.1\|WP_144403483.1\|1096667_1096916_+\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|277319
NZ_LN824141.1\|WP_045087814.1\|1102495_1103632_+\|ROK-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224851
NZ_LN824141.1\|WP_045087799.1\|1083163_1084264_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340825
NZ_LN824141.1\|WP_045087810.1\|1094969_1095653_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_LN824141.1\|WP_045087802.1\|1086132_1086567_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087812.1\|1096959_1099584_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133005
NZ_LN824141.1\|WP_052670388.1\|1085137_1085536_+\|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	unknown	unknown	gnl\|CDD\|374105
NZ_LN824141.1\|WP_045087803.1\|1086865_1087750_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|100043
NZ_LN824141.1\|WP_052670387.1\|1082347_1082809_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|182167
NZ_LN824141.1\|WP_045087806.1\|1089872_1091564_-\|iron-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224099
NZ_LN824141.1\|WP_045087800.1\|1084503_1084851_-\|Variant-SH3-domain-containing-protein	unknown	unknown	gnl\|CDD\|369452
NZ_LN824141.1\|WP_045087801.1\|1085591_1086167_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_171820593.1\|1082844_1083021_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087813.1\|1099711_1101259_-\|flagellin	unknown	unknown	gnl\|CDD\|183761
NZ_LN824141.1\|WP_045087805.1\|1088779_1089859_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|226361
NZ_LN824141.1\|WP_045087808.1\|1092792_1093560_-\|DUF3919-family-protein	unknown	unknown	gnl\|CDD\|372450
NZ_LN824141.1\|WP_045087807.1\|1091628_1092612_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270262
NZ_LN824141.1\|WP_045087804.1\|1088045_1088543_+\|outer-membrane-beta-barrel-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087809.1\|1093549_1094980_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.20726e-55
NZ_LN824141.1\|WP_052670386.1\|1080831_1082286_+\|lipopolysaccharide-biosynthesis-protein	gnl\|CDD\|225153	COG2244, RfbX, Membrane protein involved in the export of O-antigen and teichoic acid [General function prediction only].	8.28268e-29
NZ_LN824141.1\|WP_144403483.1\|1096667_1096916_+\|metallophosphoesterase	gnl\|CDD\|277319	cd00840, MPP_Mre11_N, Mre11 nuclease, N-terminal metallophosphatase domain. Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	3.64393e-14
NZ_LN824141.1\|WP_045087814.1\|1102495_1103632_+\|ROK-family-transcriptional-regulator	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	6.78616e-58
NZ_LN824141.1\|WP_045087799.1\|1083163_1084264_-\|glycosyltransferase	gnl\|CDD\|340825	cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.	1.17125e-26
NZ_LN824141.1\|WP_045087810.1\|1094969_1095653_-\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	4.40552e-78
NZ_LN824141.1\|WP_045087808.1\|1092792_1093560_-\|DUF3919-family-protein	gnl\|CDD\|372450	pfam13057, DUF3919, Protein of unknown function (DUF3919). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 251 and 262 amino acids in length. There is a conserved YLNG sequence motif.	2.31324e-15
NZ_LN824141.1\|WP_045087812.1\|1096959_1099584_-\|glycosyltransferase	gnl\|CDD\|133005	cd02511, Beta4Glucosyltransferase, UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.	2.45942e-47
NZ_LN824141.1\|WP_052670388.1\|1085137_1085536_+\|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	gnl\|CDD\|374105	pfam15781, ParE-like_toxin, ParE-like toxin of type II bacterial toxin-antitoxin system.	1.13262e-14
NZ_LN824141.1\|WP_045087803.1\|1086865_1087750_+\|hypothetical-protein	gnl\|CDD\|100043	cd03352, LbH_LpxD, UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).	9.30648e-59
NZ_LN824141.1\|WP_045087806.1\|1089872_1091564_-\|iron-ABC-transporter-permease	gnl\|CDD\|224099	COG1178, ThiP, ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism].	3.42758e-105
NZ_LN824141.1\|WP_045087813.1\|1099711_1101259_-\|flagellin	gnl\|CDD\|183761	PRK12806, PRK12806, flagellin; Provisional.	7.80717e-68
NZ_LN824141.1\|WP_045087800.1\|1084503_1084851_-\|Variant-SH3-domain-containing-protein	gnl\|CDD\|369452	pfam07653, SH3_2, Variant SH3 domain. SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.	2.16863e-05
NZ_LN824141.1\|WP_052670387.1\|1082347_1082809_+\|hypothetical-protein	gnl\|CDD\|182167	PRK09956, PRK09956, ISNCY family transposase.	0.000537111
NZ_LN824141.1\|WP_045087805.1\|1088779_1089859_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|226361	COG3842, PotA, ABC-type spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism].	3.81517e-162
NZ_LN824141.1\|WP_045087807.1\|1091628_1092612_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270262	cd13544, PBP2_Fbp_like_1, Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	1.81848e-133

>NZ_LN824141.1|WP_045087804.1|1088045_1088543_+|outer-membrane-beta-barrel-protein
MPHDALGINIAGTYWFTDTLGVEANLDFAKGDVINMSSEDFSIKASSQLIGPSVAVKYLVLKSPVFVNVKAGAGYYFYNSTTKVTGTSEGTTVETTSKMKGNGFGMLVGAEMLHPVTTSLAIKANAGYKLFTNIKNLKDQDGNEITDTAISMNGLKLGFGVIYSF
>NZ_LN824141.1|WP_045087803.1|1086865_1087750_+|hypothetical-protein
MYLSEISGIAIKKDGFFENFGKLGRIYLENSISFIHSEKYLPDIDQNISCIVCNEELLPFFLDKDMGIVVSKEPKNTFYEIYYTIYSEGKLNYSENKISDSATISPKATIASSGVVIGDNCVIGDNVVIREGTILGNNVHIGNNCVLGSDGYEVAKIYGSSKIVPHTGFCILKDNVEILNNCCVCKGLFRGYDTIIEENVKIDNIVQIAHAVKIGKNTEIGAGAVISGNTIIGENVWIGPNVTLSNKIKVGNNAFVSLGAVLINDISDGERVAGNFAYDTKKFMKEFKMKKSEE
>NZ_LN824141.1|WP_045087802.1|1086132_1086567_+|hypothetical-protein
MKISNLQLEWDRIKKFEYQIDDEIIGKKLTPKLKLEVQHNFLEKTNDNPYRATLLLKYNARFKEGKKIYLKMNIELEGSFIGSPKLDDTEFKKLVIQSGILNLIQITRAKVTAISANFGFIQPIYLPMIDATDLVNKKMKEVLG
>NZ_LN824141.1|WP_045087801.1|1085591_1086167_+|hypothetical-protein
MISIGELISIFSELSATNKKRLYNFLINEFSKVKSEEYIEFVGLLRDLEEDLLYSDEIDEKEENEKLYFTQDDLAIMTGLSKRQVQRILKSNNIEPLNPGQKPLFYDLNEFEKYYFIAKNTFREQQVEDNSFVIEERKQLKVETLFNNTTNIKKEIGPLIDLNIIYDKNSFISEFKGREESENQQFAVRVG
>NZ_LN824141.1|WP_052670388.1|1085137_1085536_+|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin
MGEFSSKTIKELISLINEETSSNSLKLFKNDVKKLKDRNLLLKIFSAVREIKIDYSVGDLKTGDLCGVRTVKINYNNVAYRIAYYVDKPILDSEKVNIMFIHVGSRGNFYKELRDYFRNQKSILKYINNKAI
>NZ_LN824141.1|WP_045087800.1|1084503_1084851_-|Variant-SH3-domain-containing-protein
MYYKVAEAHESNYPNPITIKKGTKVKVGDKYNGPENWEKWRYCYTLDNRTEGWVPEQLLVIENEYGIILEDYTAKELNVEKNEIVKGIKELNGWLWCVKLIDNDEGWLPKEKLRS
>NZ_LN824141.1|WP_045087799.1|1083163_1084264_-|glycosyltransferase
MKILIIGYMHPKLDKRVSRTVSSLSKSHEIIYQYWTDREEKKYQDGNITYIPIKYTKGTKGNPLRKLLNRRALDKIICDLIKNEDYDILYMHHFLASRPLEPFKIAKKRNKKIVYDIHEYHPENFLAELPAIIGDLKTAVLWHLFKKQLKLSDLAIFVSGETRNDVIDKVGITKDKTFIMPNYANFILKPDIQKKQKEIVLVGKVTRKIEDEKKLLNILINKGFSFKVIGMDSQEFDDIPHASTSFLPYNEMMEELSKAAFSLISYNTVKDRHYKNDIFALPHKYYDSIAAGTPVIVKESFISMAKQVEELGIGLVINPSNTEQSIEKIQKAYENYETILKNIEKYQKYFVWSQEKEQEFLKIIEL
>NZ_LN824141.1|WP_171820593.1|1082844_1083021_-|hypothetical-protein
MKKANIDSPIDVTFSVFDLVILILKILAKICFNSNKKDVRIERPYNCGLILIIIHLSD
>NZ_LN824141.1|WP_052670387.1|1082347_1082809_+|hypothetical-protein
MVIEVMRSAFEKDIERFYKAFRLIVELINKMQDKEKADEVFEMCIKYLLNVRDDIEIEELERTAKEESVERGELIMSIAEKLREEGIEKGIKKGKIEGKKEIAINVLSQRFGNELTEELTEKIRNADDETINYIGDNLLEITIEELKEILNLK
>NZ_LN824141.1|WP_052670386.1|1080831_1082286_+|lipopolysaccharide-biosynthesis-protein
MSKEREFIKSFFQFSIGQWIAALISFITTPITTWLIIPEEFGKASMFTLAFNLLLNISLLGTDQSFVRMFYEKPEEERRNLLWESLMPSLSVGFIVFIIIGLFWKELSFVLFEDYSHFLPIFLLGLTILIAIIERFATLVVRMKQRGIAFSALRVVNGASNAAFTILYALLVSKTFYAVIVGLFFSHVLSALLAIFFERDLWFGKFKINTGSVKEIIKYGLPFVPTFLITWIFQSFDKLALRNYCDFTEIGLYSAAFKVVSVMSLIQVGFSNFWTPVSYESYENDPESTGLFEKVSLFISAAMFVVGMLIIVFKDVIFLLLAKSYRQAAGISSFLLLIPIMNTTSQVTGVGIGFKKKTYWHMIISAVPAVANVIGNTLLVPQYGAKGAAFTTGLSYILYYCMKTFISKNLYPVNYHLGKFFTATVVFVIVAFINTFVGNLVWQVLSAVIGLVIVLLVYNTEVKYALDLVIDELKRVKNKVANRA
>NZ_LN824141.1|WP_045087805.1|1088779_1089859_-|ABC-transporter-ATP-binding-protein
MSLELKNIYKVFKSENTETVAVKDFSLKIEKGQLVTLLGPSGCGKTTTLRMIAGFETPTSGKIFLEGKDITNDPPNKRDISMVFQSYALFPHMTVKENIEFGLKIKKLPKNAIEEKVRSIISLTGLEGMENRRPDQISGGQQQRVALARSLVMEPKVLLFDEPLSNLDAKLRESMRSEIRRIQKELNITSVYVTHDQTEAMSISDIIIVMNKGEIMQVGNPFDIYSYPLNRFVADFIGKVNFIEGEVVKKNENYYEVYNKELNKTFVGISKKNLQINENVLIALRPEALTYEKKENSISGIIKKVVYLGSQVEYEFETEHNKIINGILFNPVENKIPQVNEKINLYFGLKASWLIKSKE
>NZ_LN824141.1|WP_045087806.1|1089872_1091564_-|iron-ABC-transporter-permease
MEIANKEFSNKFKSLMKNPSLLILLIAIFVVLFIFIIYPLFKVLIISFTDNNNNFSLDVYKSILSNDYMKQGFKNSILVATLTAVIGTLIGYLYAYTINRTNIPFKKFFRTIAIVPMVFPPFIGAMSIIMLFGFNGLITSKLFGIRTFPVYGLWGLMIAQVITFFPVAFITLDGVLSTISPTLEDAAFNLKASRWQVFTKVTLPLSVPGIASTMLVLFIESLADFGNPLILAGASFPVLSVQAYLEITGMFNLKNGAALAVWLLVPSLIAFILQKYWVNKKKYITVTGKPTTSQVKSVSTSAKWILFTLCMIVSIFIVLIYATIFWGAFTKAWGMNNQFTLDNFKYVFDVGKESIKDTLAIALTSTPISALLGMIIAFLIVRKSFPGKKALEFISLLNFAVPGTVVGIGYILGFNTKPLLLTGTFAILVLNFIFRYIPVGIQSGISLLNQVDPAIEEAAYTLGANDSQVFLKITLPLIIPAFFSALVYSFVRAMTAISAAIFLVSADWNLMTVQILSQTDSGRLSEACAFSVILILLILAFILILKIFLKNKVSLVDNNFGIE
>NZ_LN824141.1|WP_045087807.1|1091628_1092612_-|ABC-transporter-substrate-binding-protein
MKKVALVGLMLVLLVFSFAELVIYSSVDEANARKILNAFSKDTGIEVKYIFLSSGPALARLEAEKNNPQADVWFGAPMSNHIIAKERDLTEPYKSTSVYGIDPNFYDVDGYFHAFYMNPLGVGVNLKVLEQIKAELPKSWADLLKPEFKNMIQYPNPQTSGTAYTFITGLISVYGEDGAMDYLKKLAKNIQSYTQSGTGPSKAVGIGQAAVAIQFTPAFFEFKEQGYPIEVVFPVEGVPYESACVSIVKGAAHKTEANTLIDWLLSKKGQQVIVDEKTYFYPVRADVNFGSLQPLSTIKLISVDEAWAAENKNRIIERWIKEVLPVK
>NZ_LN824141.1|WP_045087808.1|1092792_1093560_-|DUF3919-family-protein
MKNNKYMYIFVILFAFVVVLGIYTLNKSFNKVYFIKDNETLMSRYSSSTPVKIVFSMKYFPPYEINDSKIILDFWNRLSKLPAYKHIAIDKNQEYDLITGEIYFLDGSKKHFEISNSFSIEELSLGSSGNEETNYIKSQMKALILSTENISKELLNKENKVIGFKSNNDSFKIDYNNLIELANLLKSSTIITSTDEIGKVIQDNPYPVYIIAVLKGGDQFLTINVYNEDYFSIYYLDTLLYLIKGDLLSYLKITY
>NZ_LN824141.1|WP_045087809.1|1093549_1094980_-|HAMP-domain-containing-histidine-kinase
MKNSIRSQILFINIAFAVLILTIIFFVTLNTFQKNIIDITVDRMTEYSQETQIYLMNYLKDYEYSDVYDEFKKLSPFASDYFSKKFELYLEVYDIRKNLLSNTYTNEQYYVYQDIYYAINGMKNYIIKSEDDKKILFFASPVFYNNEVIGAIRFIYPMNSEFLLIDKIKVTLAIIGVLAIFVSLILNYFFSNTITRPIEKLKYETERIANGDLSTHIDIQSNEEINSLVNSFNIMVEKLEHYIQSLNEEKERQKIFTDNITHELKTPITAILGHADLLQRLTNEEDKKVSLNYVVSEGNRLLKLVEELLEISRINKDSFNFDFKNHNIKDLINECLGILNPRFKKFGIVVDNNVEEKSLIFDYEKIKQVVLNVLDNAIVHSKCSEITITSEVNEEYCYLIIQDNGIGIDEKTQERLFNPFFTPKKQKSFGLGLYISKEIMKKHHGDINIISQINNGTKAILKLPLNLKGDHYKHEK
>NZ_LN824141.1|WP_045087810.1|1094969_1095653_-|response-regulator-transcription-factor
MKILIIEDEKSISDLIRMNLILEGFETIVSDEGYKGLQMFKKEEPDLVILDLMLPDCDGFEILKEMQEANYRTPIVILTAKSDQNDKILGLGLGADDYITKPFDNKELILRIRNIFKRMKKSELNSSNEINIGVFKIINNSRQFFIDSQEIYLTKTEFDLMELLMNNHKQVLSREVLLNKIWGFESEVDTRAVDMTIQRLRKKLGSYGDCIQSLYGIGYKFEANDEE
>NZ_LN824141.1|WP_144403483.1|1096667_1096916_+|metallophosphoesterase
MDVLVISGDLYDRVVPPAEAINLLNETLSKIVLEFRIPTIIISGNHDSAERLEFLNGILSGMVLQIEGVLKGEVKEGSFIKY
>NZ_LN824141.1|WP_045087812.1|1096959_1099584_-|glycosyltransferase
MVSNNEGLLSVAMIVKDEEANIRHALESIKDVADEIIVVDTGSTDRTPEIVKEYTDKLYFHEWQNDFSEARNYSLQFPTCKWVLIYDADEEASESFRKNIRDFLKGLDKSVNTVYLPTISYLDIDLTKTEIASTPRIFRRGTISYKNVVHNQAIYQPKVVHANFPILHYGYIWTRALKKKKYERTGNLIREHLQTAKEPLERIYYLVQLYKTESIGGYTYKKNQVAWQTLEAIQKVGQIPAIGLEFMYLFGLDCIMGGLKDLSKQLLEKCIKVAPNYPDPYFAMMVAYEREKDWNELLKWGRKFFEVLDDAMKNVEKFEWTIMSFKQIPLANILMARSSLKTGDFEGFNQYLKDTFSEENVTLERNNVYVLLQDINETVKTKSELESIIPGIKILVDNLEKEGMVIYYDSLIEKIADLNLEVDNDLLDKLTHKNEISRYILKKLQTGEDQLLDFLTKDDHLEFVEKTEIPGLLLFYSILKNTQDTIGILKTLSSFRKIENEKVQGVLYALLGDCYLRVKRFKEAIDQYRKAMEILPELSRFIKPVVEDLSTKLDPLMDGVYEEMYSYFSSGKEFIFNIIEYIGQEQCQRLYLISDSPFALYTSGISYIQKDSEKAKKLLNKIENTEEFPFYYYRLAKIYEKEDMKKAFELHIKSLEENNKLADFALGRYTYSGLYPNTRFNFMKNNDEIIWVGNISEKLSTLGIIHPIRSWKKANNFMYAVPYPSDEALKIYEEREKEIYKTKPFEIKKEYILKGLIDSGINDLQIVGFDEEKYKSVFDDLEITVNEDSKNLLILGEFEKNFDMSKHLNNAEKVLAFVYVPDLNDRDNIIWYGPNFRVLRTTKQLKELLEKEGFKILRLEALNDNLRCILAQKQ
>NZ_LN824141.1|WP_045087813.1|1099711_1101259_-|flagellin
MRINHNISALNAWRSLDQVNSSMGKTLEKLSSGLRINRAGDDAAGLAISEKMRGQIKGLDMAVKNAQDAISLIQTAEGALTETHSILQRMRELSVQAASDTNTNVDRNQIQAEIDQLREEIDRIARTTEFNTMKLLDGKIESFRPEADVKVVTGGNFDLQASLKGTALGAMTVASGTSLGEVEVESGDNTAVVSLELNDLELGAVTVKLIDTGESNADGIGTIQITYNNVNFNIEGLDLNTNQTVSTTVGDLKFDFVLSDSKIDSIKVSLATSKAVDAPEGSYVVEVGQFKGEGTSPLDVRVNYFNDEGLVTSPIVDFSEGKASIDNVSMTASKEDGFSVSVKALSFTWNTDVYDINDFNGALPMEAVIDSGVVRAEERWYDDTSLVLQIGANEGHNIVLGIDDMSAKALGLTTSSLKATDQDSAERSIMVVDAAIHKVSTARASLGAVQNRLEHTISNLGVASENLTAAESRIRDVDMAKEMMAFTKQQILMQSANAMLAQSNMIPQNVLQLLR
>NZ_LN824141.1|WP_045087814.1|1102495_1103632_+|ROK-family-transcriptional-regulator
MEPDNVLEVFKTVQKKSLISRTEIAKITKLSPSTVGRCTQRLLEKNFFVEKRVGKSSGGRPPILLDINRENGFSVGIEVGESHIDAVLLNLVNEMKDSNSKRLSNHLSPNALADDIKNMIDELVNKAHISQEDIISVGVGLPGIVSADQKRLLLSPNLKWKDVDMARLLEGKLNKPVFLDNGANLMTFAEYHYNKLSSNAMVLGIIVGRGIGTGLVVKESIFRGVNGAALEAGHSVIKTDGPLCSCGRRGCAEALASLPRLIESYNKQSKSKKIDNVRELNELFLKKDKLAVELINEEAFYLSVLSANLANIFNPSHIIIGGEISPILPLMIKTIKTSFLDQVLTTNRCELLTSQLNEKSIAYGAAIMAIEKEIEGYI

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Crispr_ID: NZ_LN824141_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_11

1134429-1134639

Orphan

Consensus_repeat	Method
TAATTATTAGTTGTAGAGACGTGC	CRT
TTATACCCACCATTAATTATTAGTTGTAGAGACGTGCTACACGCGCGTCTC	PILER-CR

3 spacers

The CRISPR arrays of NZ_LN824141_11

>merge|NZ_LN824141|11|1134429-1134639|CRT,PILER-CR
CTTAAAATTATTATAGAGACGCACAACGCGTACATCTTCTCTATTATACCTAACAGTAATTATTAGTTGTAGAGACGTGCTACATGCGCGTCTCGTTTTTTTGTTTTAACCACCATTAATTATTAGTTGTAGAGACGTGCAACGCATACATTTGCTCTATTTATACCCACCATTAATTATTAGTTGTAGAGACGTGCTACACGCGCGTCTC

>NZ_LN824141|11|1|1134429-1134625|CRT
CTTAAAATTATTATAGAGACGCAC	AACGCGTACATCTTCTCTATTATACCTAACAG
TAATTATTAGTTGTAGAGACGTGC	TACATGCGCGTCTCGTTTTTTTGTTTTAACCACCAT
TAATTATTAGTTGTAGAGACGTGC	AACGCATACATTTGCTCTATTTATACCCACCAT
TAATTATTAGTTGTAGAGACGTGC

>NZ_LN824141|11|1|1134472-1134639|PILER-CR
TTATACCTAACAGTAATTATTAGTTGTAGAGACGTGCTACATGCGCGTCTC	GTTTTTTTG
TTTTAACCACCATTAATTATTAGTTGTAGAGACGTGCAACGCATACATTTG	CTCTATTTATACCCACCATT
AATTATTAGTTGTAGAGACGTGCTACACGCGCGTCTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087836.1\|1142757_1143783_-\|anthranilate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234682
NZ_LN824141.1\|WP_045087838.1\|1144376_1145906_-\|anthranilate-synthase-component-I-family-protein	unknown	unknown	gnl\|CDD\|223225
NZ_LN824141.1\|WP_045087841.1\|1147634_1148855_+\|peptidase-T	unknown	unknown	gnl\|CDD\|235484
NZ_LN824141.1\|WP_045087837.1\|1143775_1144360_-\|aminodeoxychorismate/anthranilate-synthase-component-II	unknown	unknown	gnl\|CDD\|235552
NZ_LN824141.1\|WP_045087829.1\|1129721_1130978_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270451
NZ_LN824141.1\|WP_045087824.1\|1121531_1122170_-\|class-II-aldolase/adducin-family-protein	unknown	unknown	gnl\|CDD\|376358
NZ_LN824141.1\|WP_045087831.1\|1132508_1133369_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_045087833.1\|1139538_1140714_-\|tryptophan-synthase-subunit-beta	unknown	unknown	gnl\|CDD\|235288
NZ_LN824141.1\|WP_045087840.1\|1146816_1147569_+\|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|336781
NZ_LN824141.1\|WP_045087834.1\|1141218_1141839_-\|phosphoribosylanthranilate-isomerase	unknown	unknown	gnl\|CDD\|238237
NZ_LN824141.1\|WP_045087830.1\|1131107_1132133_-\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_LN824141.1\|WP_045087835.1\|1141831_1142596_-\|indole-3-glycerol-phosphate-synthase-TrpC	unknown	unknown	gnl\|CDD\|234710
NZ_LN824141.1\|WP_052670393.1\|1128772_1129651_-\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_LN824141.1\|WP_045087827.1\|1125439_1126855_-\|L-fucose/L-arabinose-isomerase-family-protein	unknown	unknown	gnl\|CDD\|238323
NZ_LN824141.1\|WP_045087826.1\|1124390_1125386_-\|exo-alpha-sialidase	unknown	unknown	gnl\|CDD\|372469
NZ_LN824141.1\|WP_045087832.1\|1138642_1139419_-\|tryptophan-synthase-subunit-alpha	unknown	unknown	gnl\|CDD\|237285
NZ_LN824141.1\|WP_045087839.1\|1146394_1146820_+\|large-conductance-mechanosensitive-channel-protein-MscL	unknown	unknown	gnl\|CDD\|234795
NZ_LN824141.1\|WP_052670392.1\|1127934_1128756_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_045087828.1\|1126952_1127861_-\|4-hydroxy-tetrahydrodipicolinate-synthase	unknown	unknown	gnl\|CDD\|188630
NZ_LN824141.1\|WP_045087825.1\|1122851_1124372_-\|FGGY-family-carbohydrate-kinase	unknown	unknown	gnl\|CDD\|198372

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087836.1\|1142757_1143783_-\|anthranilate-phosphoribosyltransferase	gnl\|CDD\|234682	PRK00188, trpD, anthranilate phosphoribosyltransferase; Provisional.	0
NZ_LN824141.1\|WP_045087838.1\|1144376_1145906_-\|anthranilate-synthase-component-I-family-protein	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	1.31516e-149
NZ_LN824141.1\|WP_045087841.1\|1147634_1148855_+\|peptidase-T	gnl\|CDD\|235484	PRK05469, PRK05469, tripeptide aminopeptidase PepT.	0
NZ_LN824141.1\|WP_045087837.1\|1143775_1144360_-\|aminodeoxychorismate/anthranilate-synthase-component-II	gnl\|CDD\|235552	PRK05670, PRK05670, anthranilate synthase component II; Provisional.	3.62342e-86
NZ_LN824141.1\|WP_045087829.1\|1129721_1130978_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270451	cd14748, PBP2_UgpB, The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold. This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	2.84326e-74
NZ_LN824141.1\|WP_045087824.1\|1121531_1122170_-\|class-II-aldolase/adducin-family-protein	gnl\|CDD\|376358	pfam00596, Aldolase_II, Class II Aldolase and Adducin N-terminal domain. This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.	4.83303e-56
NZ_LN824141.1\|WP_045087831.1\|1132508_1133369_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	8.31456e-75
NZ_LN824141.1\|WP_045087833.1\|1139538_1140714_-\|tryptophan-synthase-subunit-beta	gnl\|CDD\|235288	PRK04346, PRK04346, tryptophan synthase subunit beta; Validated.	0
NZ_LN824141.1\|WP_045087840.1\|1146816_1147569_+\|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein	gnl\|CDD\|336781	pfam07722, Peptidase_C26, Peptidase C26. These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C-terminus.	9.48637e-75
NZ_LN824141.1\|WP_045087834.1\|1141218_1141839_-\|phosphoribosylanthranilate-isomerase	gnl\|CDD\|238237	cd00405, PRAI, Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.	1.15666e-73
NZ_LN824141.1\|WP_045087830.1\|1131107_1132133_-\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	5.94806e-101
NZ_LN824141.1\|WP_045087835.1\|1141831_1142596_-\|indole-3-glycerol-phosphate-synthase-TrpC	gnl\|CDD\|234710	PRK00278, trpC, indole-3-glycerol phosphate synthase TrpC.	6.00666e-110
NZ_LN824141.1\|WP_052670393.1\|1128772_1129651_-\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	3.92953e-70
NZ_LN824141.1\|WP_045087827.1\|1125439_1126855_-\|L-fucose/L-arabinose-isomerase-family-protein	gnl\|CDD\|238323	cd00578, L-fuc_L-ara-isomerases, L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.	1.79883e-95
NZ_LN824141.1\|WP_045087826.1\|1124390_1125386_-\|exo-alpha-sialidase	gnl\|CDD\|372469	pfam13088, BNR_2, BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.	1.82169e-32
NZ_LN824141.1\|WP_045087832.1\|1138642_1139419_-\|tryptophan-synthase-subunit-alpha	gnl\|CDD\|237285	PRK13111, trpA, tryptophan synthase subunit alpha; Provisional.	3.09365e-125
NZ_LN824141.1\|WP_045087839.1\|1146394_1146820_+\|large-conductance-mechanosensitive-channel-protein-MscL	gnl\|CDD\|234795	PRK00567, mscL, large-conductance mechanosensitive channel protein MscL.	7.96877e-57
NZ_LN824141.1\|WP_052670392.1\|1127934_1128756_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	3.41381e-80
NZ_LN824141.1\|WP_045087828.1\|1126952_1127861_-\|4-hydroxy-tetrahydrodipicolinate-synthase	gnl\|CDD\|188630	cd00408, DHDPS-like, Dihydrodipicolinate synthase family. Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.	1.86804e-103
NZ_LN824141.1\|WP_045087825.1\|1122851_1124372_-\|FGGY-family-carbohydrate-kinase	gnl\|CDD\|198372	cd07804, FGGY_XK_like_1, uncharacterized xylulose kinase-like proteins; a subgroup of the FGGY family of carbohydrate kinases. This subgroup is composed of uncharacterized bacterial and archaeal xylulose kinases-like proteins with similarity to bacterial D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17), which catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. The presence of Mg2+ or Mn2+ is required for catalytic activity. D-XK exists as a dimer with an active site that lies at the interface between the N- and C-terminal domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Members of this subgroup belong to the FGGY family of carbohydrate kinases.	0

>NZ_LN824141.1|WP_045087831.1|1132508_1133369_-|carbohydrate-ABC-transporter-permease
MKAKKKIKVARILLHIFIIFMMLIWILPTLGLLITSFRPAQEVSKTGWWTVFNSPLKFTQFTLNNYKEVITKAGLGTAFKNSFMITIFGTLLPVIIGAFAAFGLAKIEFKGKSLIYSLIVGLLVVPLQLTFIPILRLYNKLKLSGTFVGLWFAHTAYGLPFAIFMLHNFFVSLPNDLFDSARIDGASLWTSFYKLALPLSVPAIASLVIFQFLWVWNDLLVALIYLGGTKDVAPLTVVLANMVGSYGQNWHLLTAAAFISMVVPLIVFLSLQKYFVKGILAGSVKG
>NZ_LN824141.1|WP_045087830.1|1131107_1132133_-|LacI-family-DNA-binding-transcriptional-regulator
MDRPTIKDIAKVLNISPSTVSRALSGKPGASEELRKKVLETAEEMGYMKNLSAQSLKNSKSKIIGIIAFDIRNPFFLDFLKGVEDVLFPREYKILLSSVDESADKEKTYLNWMVSQGVDGILSSPITEKNGKSNLKLYNNFYKMGVPIVFYDRMFYNQEQFDYVIVDNQDAIIQALMHLKENGHENVSIFLSKKGVFTIEERLKGFLKGCELLNIQTRKEWICEDIYPHEKAFDILKMLKDKNNLPSAIIATNNNITKNIVSSSRKLNVKIPDKLSLIGFDDTPENELIDPPLTTIKQPILEIGKIAATALLSRIEDRFAKPMKVVLKAELIKRGSVKNLK
>NZ_LN824141.1|WP_045087829.1|1129721_1130978_-|ABC-transporter-substrate-binding-protein
MRFKKLLLVSLLMLMLSFSFAAEKTTLYYTTLFHSGDAQAMEKIVQRINQESDDIFVVLVQGAWENYYAQLINQVVAGNAPQVGVVHSNMFPSMRDALTPLNASSAGNLLEKSGFKREDFLTDVWDSSTFDDLHYGIPLDTHMWAMWYNKDIFVKAGLDPDKPPTNAEELKYAAEKIKDAGYYAVHFAEDGVARKLMRAWYILYWQQGGELFDENYSKATFNNEKGIKALQYLVDSVQKWGWNTKGTDGFKQFASGQLGILFAGNWYYYSAEEAKINYGVAKVPTIFDKPATWGNSHNLVIPKQAANNPQMYEQAIELIRRITDLSYMWGMFGGHIPAYNNSRTSSELLNAPVWEKSLNVFSQMAEEGYLHYPPNHVKAAELEDAIQVYVQQAYNGTITPSEALKRAEAECNRILSEN
>NZ_LN824141.1|WP_052670393.1|1128772_1129651_-|sugar-ABC-transporter-permease
MKKAVRDQWSGMLFALPFMIIWGVFTLWPVISGFIISLHNWDPLRGSEFIGFGNYKYLFSSQRFWNAFVNTFEFALIMIPMTLILALLFAFYLYFSKGKAKAFVESALFFPYLLNVSIISLIWKWLFDPDFGLITESLKMIGITNPPQFLNNPIWVIPAIALASSWWLMGYRMTIFRAALESQPVEIVEAATIDGANKRQIMFKILFPLIRPQFLFTTVLTVISGFDVLGQVMIMTEGGPGRSSEVLALLLYKEAFSYFRMGRAAAIGFILFVIIFIFTLIALRFMGKDVQQ
>NZ_LN824141.1|WP_052670392.1|1127934_1128756_-|carbohydrate-ABC-transporter-permease
MKKNEESKILDIIMIIFSILWLIPVLWMIDTAIKPTPEIFTTPPKWLPEKFTLQHIKDVINNWPFGTWLLNSIIVSGLSTLFSLFLSILAAYSFSRIEWKGRDVIFIILLASMLIPWQINAVPLYFLMNNLNLLNKLIAVILPITAMPISVFLLRQFFIGLPSELEDAARIDGCNRMDILFRIIVPISGPALAALAIYMFIFSWNEYFWSLIALQRIGKFTLPIGLNMLQGAYDIEYGLLMAAAFLASIPVMIVFALLRKQIIKGMSWSGVTK
>NZ_LN824141.1|WP_045087828.1|1126952_1127861_-|4-hydroxy-tetrahydrodipicolinate-synthase
MNLEGIITALVTPFDEKGKIVESSLRKLCKFQLNKQVNGLLILGTTGEGISLNLEERKLVAEIVVDELKGKLPIMVHVGSSNINEVFSLAKHAVDIGADSITSITPYFFKMSDKEIFDFYLELSKNVPNDYPVYLYNFPTATGNDITPEVIKKLIEETNNILGIKYSSDNMMRIQEYLKLQNPNFKVFTGADQLFYPMLCLGCDGLVSGNANIFPELFVTVFKSFKKNDHKTAKLFHQYGNEIAKLFKYGNIPAIKAGMKLREIDGGYVRRPFRNLCEEEKNKLQKEFSLIFDQILNLKPLE
>NZ_LN824141.1|WP_045087827.1|1125439_1126855_-|L-fucose/L-arabinose-isomerase-family-protein
MKKRKVGIITFSDGRDFVHEETLEMNKKFEDRLVKALERTNEIEVVRASDIVNKPSKAKKAGKEMMKAEVEMTIFNYSIWCWPHLSVIASLYAPGPYLIYGQINPKYPGMVGMLAAAGALEQIGIFPERVWGEPEDPEVMKRLLKFVRGASAAHRLKGERYGMFGGRPMGMYTASANGDQWMKEFGIDVEQIDQYALVLKAEKVPTEKKRKAREWLERYATVQYDGKRLTPAILEKQIGLYYAALEIIKEEELDFVGFKGQPEMTNNYATMDIAEAFLNDPYDFDGPKEPIVAATETDMDGALTMEIFKHIAQTPVLFADVRHYFKEEKLLDLANSGQHATYFAGKSNNPEENLKNVIIHPEDFYFPAGGGAVKHFAAPGRVTLARLARQDGEYVMTIVPAEFVELSDKEKKRLSEQVQIEWPHAYAKLDTTIDTYLEYYPCNHIHGVYGNYIEELVHFCKVKGIAFQILD
>NZ_LN824141.1|WP_045087826.1|1124390_1125386_-|exo-alpha-sialidase
MKIINKSFVFDKIPSKPSSHSVSLCKINDNEIIAFWFAGSWEGEKDVDILSSRYDINADKWDTPKLFIHDPSRSLGNTAPVLFEKTFRVYYCAMEGKDWTESSLWYTDSYDQGYSWKKPKPFSLQGENLLFGTKILKLSDNRFIFPMYNEKLWISTPYITNNISSNKWEKIGEIKTEKGNIQQDMVEMNGQIFSLLRTRDGFIYKTLYNFENKKWSTTISINIPNPNSRLALEKTRDLLICCCNPLGLNKENLTHDPRKLSDIEEGFWGKREKLSIFVSSDGGNTWNEEIILEESQDKEYSYPWIQIIDETKIMIAYTYERQKIAYAIIEI
>NZ_LN824141.1|WP_045087825.1|1122851_1124372_-|FGGY-family-carbohydrate-kinase
MYLIGIDIGTQSTKSVITDEEGKVISESSKEYAVLTPQPNWAEQWPDVWFNAVIDTLKRVIEKSQIQPKNITGVAISGLYGGSGIPVDKDFNPLRPCLIWMDRRATKETKFVKQNIPKDKIFRITGNYVDSYFGFTKMMWIKNNEPEVWNKTYKFMTPKDFVIYKLTGENIIDYSSAGNIGGVFDIHKKYWSQEMCEILGIDLDKLPEKIVKSSDIVGTMSGKYAQETGLLEGTPIIAGGIDAPVAQLSAGAVYEGEHVAMVGTSTCWGNIHDGKYLTPELVSYPYVVDDLTKIYTFGGGATSGAIIRWFREEFGEYEKEYENKRGVSAYTLLELGSKDIPAGSDGIIVLPYFMGERSPIWDSKAKGTIIGLSLYHNRNHLYKAFMEAVAYSLRHNIEEAQNAGIVLDPECYLVGGTAKSDIWTQIFSDVTGYVMKRTKQDVEAPLGDAFLAGLGTGIFKQPEDIKKWTLFKEDTLPNNSNKQIYDKYFNLYKQLYKNTKEIMEQL
>NZ_LN824141.1|WP_045087824.1|1121531_1122170_-|class-II-aldolase/adducin-family-protein
MSESQLKKQVALFAKLVWDRKLTDGTGGNMSIRNKDKIYITPTSTIKHFLTENDIITVDKNGNKIEGEKEPSSERRMHIKIYEKASDVNAIIHAHPRYATSFAVTFQKLPVYALPESALVLDPITYIEYQMPGTQEFADAFAKGLEEGSRVFVLQNHGVTVAGKDIEEAYMKLETLEFLAEVSVISKLYSGINEIPTEKIKAFIEFFNKRGD
>NZ_LN824141.1|WP_045087832.1|1138642_1139419_-|tryptophan-synthase-subunit-alpha
MSKIQQIFNNNKALITYITAGDPDLETTKDIIFELNNDGVDIIEIGIPFSDPLADGPVIQEASQRALKNGVNLRKIFNTLESIKGRIHTPLVLMGYYNSIFNYGEDKFIEDCKRTGISGVIIPDLPFDEEIEFYEKLKENGIDGILLVAPNTSEERLKEISNYATGFLYCVSLMGVTGDSRGPVEYINEYVQKIRKYVNIPLAIGFGIDTPEKVKLIINYVDGIIVGSALIKIIDKNKENKNKMFEEIKTFIQNLKVW
>NZ_LN824141.1|WP_045087833.1|1139538_1140714_-|tryptophan-synthase-subunit-beta
MKKGYYGQYGGQYVPETLIPALKELEAAYEEYSKDPDFLKEYNGLLADYSGRPTPLYYADRFTEYLNGAKIYLKREDLNHTGAHKINNALGQVLLAKRMGKKRIIAETGAGQHGVATATAATKFGLECVIYMGAEDIKRQSLNVYKMEMLGAKVVPVYNGSQTLNEAVNEAIRDWVTNVEDTHYVIGSVVGPHPYPKIVRDFQRIIGDEAKKQIIEKEGRLPDYIIACVGGGSNAIGIFYPFVEDQEVKLIGVEAAGKGLETGLHAAALTAGKIGVLHGSKSYVLQDENGQIKLAYSISAGLDYPGVGPEHSYLRDIKRATYTSVTDEEAIEAFELLTKLEGIIPAFESSHALAYTMKLAPQLDKNKIIIVNLSGRGDKDVDAYRNLNRNK
>NZ_LN824141.1|WP_045087834.1|1141218_1141839_-|phosphoribosylanthranilate-isomerase
MVRIKVCGITNITDAVNIANLNIHALGFILSESPRKVELSEVAKISKLLPPFVSRVAVVVDITLNELEEIQNSKLFDYIQFHGSEDISLIKKCNLKTIKAIKIENEKSLSDIALYQNFVDYILFDTKIENKIGGTGKAFEWNILKKANITKPYILAGGIGPENVSQAIATLKPAAIDLNSKVEKSPGKKDINLIKQTLEIIKNTEK
>NZ_LN824141.1|WP_045087835.1|1141831_1142596_-|indole-3-glycerol-phosphate-synthase-TrpC
MFLQEIIKTKNEELSKLTQKKRSLKSALKKSELTLIAEIKKASPSKGLISKNFDPEKQLQAYSQGGADAISILTDEKYFNGSTEILRQLRGKTSLPILRKEFIIHPLQIYESLFLGADIVLLIAAILTKQQIISFLDISNQLGLEALVEVHDHDDLEKIIDTKTEILGINNRNLDNFTVDITNTEKIINELEKMNIRNNFYIVSESGVKDKNDVDYLESLGVNGVLIGEALMKSNKPQEKIKELFPKKEHVRNG
>NZ_LN824141.1|WP_045087836.1|1142757_1143783_-|anthranilate-phosphoribosyltransferase
MFNYFLTKVVKKQDLSMEEMEKAMNMVMEGKTTHSQLAGFLVGLNMKGETVDEITASAKVMREKALPFNYQSDNLLDTCGTGGDGKGTFNISTAVAFVLAAAGVSVAKHGNRSVSSKSGSADVLESLGVNISLSVNLVEECLKEINIAFLFAPDFHKATQYAAVPRKELGIRTIFNLLGPLTNPAKVKYQLMGIYDPTLVYPIAEVLRNLGVKRAMVVHGAGGVDEFSLAGKNKVAFLSDEKIEELEIAPEDVGLKRYDLEEIKGGTAQENKEIILSIFNGAKGPKRDVVLFNSAAALLVTHVVENFEDGVRYAQEIIDSKKALRKLQDMIEFTNFLTVQN
>NZ_LN824141.1|WP_045087837.1|1143775_1144360_-|aminodeoxychorismate/anthranilate-synthase-component-II
MILLIDNYDSFTYNIYQTISELDDVVICKNDKVSINQIESMNPSHIIISPGSGLPNAKDISIDIIKHFAKKTPILGIGSGHQCIAKIFGGELIRTSEIHHGRISKIFVTTEDVIFDGINNPFNAVRYDSLVVSQDSFPAELKILALSDQNEIMAIRHQFYSIYGVQFHPESILTSIGFQLLENFINIGRSVNYV
>NZ_LN824141.1|WP_045087838.1|1144376_1145906_-|anthranilate-synthase-component-I-family-protein
MKTIEVKVLSCSLPFENINSPVIYKKTAFNNDYSFLFENLKYNGKTFSMIGIIPEKIIQYIKTSEDNLVITLKEREKKAEKILEQDYLTFLEKELGKINFQHIEGIPPFFCSFFGYFVYEMSYLWEELLSKNTNSFSQNAELPLSILCLPKVSLIIDHEDKMLHIFNCLYFDNEETADEIEESVSIAQSEIDELKEHIIEILKIRDSKDNTSNNQSNLKRQYTPLNITYHTKKDDFLEQVKKAIEQINSSGAFQIVLSQKFSTHVESHPFEIYEILRTINPSPYMFYLNFPEAKILGCSPEMLVKVEGDKIISRPLAGTRTRGQKAEEDTYLEQELLNDEKEKAEHVMLVDLARNDLGKVCKRGSVKVTKLFGIEKYSHVMHIYSQVEGIKRGDVGPLGILKSVFPAGTVSGAPKIQAMEIINYLESKPREVYAGSIGYVAPNGDLDAAIAIRTIVYKNSEAFIQAGAGIVSYSIPENEYEETLNKAKAMFKAIEIAEHQRKEVQQLTK
>NZ_LN824141.1|WP_045087839.1|1146394_1146820_+|large-conductance-mechanosensitive-channel-protein-MscL
MAKKFWEEFKNFAIKGNVIDLAVGVIIGGAFGKIVTSLVNDLLMPLIGILIGGVDFSDLQFKIGEATIRYGAFIQTVVDFLIISFSIFLFVRFLNKLKLEHEKQAEVEEAKTPPPPPPPSKEEILLTDIKNILEEIKDKKS
>NZ_LN824141.1|WP_045087840.1|1146816_1147569_+|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein
MKKTVIGISSSYKYQKSTNEQSGNPLQEVHSLADEYVTAVIRAGGIPVIVPILDDLDIIREILENVDGLILSGGEDIDPKYYKKRAVSEVSLIIPKRDKQDLFCAKYMVENTDKPLLGICRGAQVMNVALGGTLYQHLPASGFEQHSLINYPACEVSHYIQIEEDSLLYRITKSNIIGVNSYHHQAVETVAPSLRVVATSVEDNLCEAIELKDSSPNRFVLGVQWHPEKMACQAKVQQEIINAFVNSCKQ
>NZ_LN824141.1|WP_045087841.1|1147634_1148855_+|peptidase-T
MKDIVERFKTYIAIDTKSDESSTTIPSTPGQLELGRLLVNELKELGLENAKQDEHGYVYATLKSNIQKEVPSIGFIGHMDTSPDLDGKCTNPKIFLYQGGNIRLNDKYTTTVDEFPFLEKLKGKELITTDGTTLLGADDKAGIAAIMSAIEYLVNHPEIEHGNVQIAFTPDEEIGRGTDFFDIEGFGADFAYTVDGGPLGELEYENFNAASVKLKIYGKNVHPGTAKDVMINALRIALEIESMLPVNEKPEYTEKYEGFFHLTKLSGTVDYAEVEYIIRDHSKTKFEAKKQLFQEIVKFLNYKYNREIIKIEITDSYYNMREKIEPHMEIIELAKKSMIDLGIEPIIKPIRGGTDGARLSYMGLPCPNIFTGGYNFHSRFELIPVEDMKLASKTIVKIIENNAKQE

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Crispr_ID: NZ_LN824141_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_12

1134826-1138285

Orphan

Consensus_repeat	Method
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CRISPRCasFinder
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CRT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	PILER-CR

51 spacers

The CRISPR arrays of NZ_LN824141_12

>merge|NZ_LN824141|12|1134826-1138285|CRISPRCasFinder,CRT,PILER-CR
TTTTCCGTTCCTCATAGGTAGGATAAGAACCAGCGTCGTTGAAGAAAGGACTAGCTGATGCCATGTTTCCATTCCTCATAGGTAGGATAAGAACCGACTAATAAGTTACTCCGAGCTTTTATTTAAAAAAGTTTCCATTCCTCATAGGTAGGATAAGAACAGGAATTGAAACAAATTCGGGCTTTGCAACAACTTCTCGTTTCCATTCCTCATAGGTAGGATAAGAACGAGCAATTAAAGGTAACTTCTTTGAAGTCTAGGTTCGTTTCCATTCCTCATAGGTAGGATAAGAACTGGGAGGAAAGCTATGGAACATACAAGAAAGCTAAGTTTCCATTCCTCATAGGTAGGATAAGAACGCAATCTGGGTTCTTAGATATATTAGTACCCAGGGCATGTTTCCATTCCTCATAGGTAGGATAAGAACGAAAAATTATTGATGAAGAAAGTTTTGAATACGAAAAATTTGTTTCCATTCCTCATAGGTAGGATAAGAACATTTTTACATTGTAAATTTTCCGTTTAATGATCAATTGTTTCCATTCCTCATAGGTAGGATAAGAACGAACAAAAAGAAACAAAAGAAGTAAAAGGAGTAATAACGTAGTTTCCATTCCTCATAGGTAGGATAAGAACTGGAACGAGCAACTTCAAGAAAGTTGGAAAAAATTACCTAAAGTTTCCATTCCTCATAGGTAGGATAAGAACGCGACAAAAGGCAAGAATTAGTAGAAACTGAATTTAAATTGTTTCCATTCCTCATAGGTAGGATAAGAACGGATGCTATTTCAAAATCAGGTGCAGTAGGTTTGATGGTTTCCATTCCTCATAGGTAGGATAAGAACGCGACAAAATGCAAGAATTAGTAGAAACTGAATTTAAATTGTTGCCATTCCTCATAGGTAGGATAAGAACAGATGCTATTTCAAAATCATGTGCATTAGGTTTGATGGTTTCCATTCCTCATAGGTAGGATAAGAACAATTCATTTGTTTAGGCGAAGTTTTTCTAATTGTTTAGTTTCCATTCCTCATAGGTAGGATAAGAACCAGACAAAGATGGTTTCAAAGTTGTAGTAGAATACATGTTTCCATTCCTCATAGGTAGGATAAGAACTTTATAATCATCGGGTTGAAGTTGTGGATCTCAAGTTTGTTTCCATTCCTCATAGGTAGGATAAGAACGGGACAATATAGCATGGCTTGTAGAACTATTGAGAAAGTTTCCATTCCTCATAGGTAGGATAAGAACGAAACCTAGAACTGTCTACATTAGAAACTATAGGAAAATAGTTTCCATTCCTCATAGGTAGGATAAGAACACATAAAACACTTGACAAATATAATATATTATATTAGTTTCCATTCCTCATAGGTAGGATAAGAACGCAAACAAGGTAATCATACAGGCAAGGGTAGTGAAACGTTTCCATTCCTCATAGGTAGGATAAGAACATAATCTTTTGGAATACAATCAAAGTTTGATAGAGGTTTCCATTCCTCATAGGTAGGATAAGAACAAAAGATAGTAGATGATTTAGGAGGAGGTAAACAGAGTTTCCATTCCTCATAGGTAGGATAAGAACAAAGAAAACTGACAAAAGAATTGATAAAAGAAGCGTAGTTTCCATTCCTCATAGGTAGGATAAGAACGGGAAATAGCTCCCCTCTTTTTTGTACGAATATGTTGTTTCCATTCCTCATAGGTAGGATAAGAACTATTATGGATATAGAACATCCTGATATTCTTATAATGTTTCCATTCCTCATAGGTAGGATAAGAACCATTTTCAACTGATACCGAAGAATTATTTATTGGAAAGTTTCCATTCCTCATAGGTAGGATAAGAACATATTTTAGCTTTGTGTATTTGTCTGTTATGCTTTCTGTTTCCATTCCTCATAGGTAGGATAAGAACCTGTCATTTCAGTCACAAACTTTTGCATATCTTCCTTGTTTCCATTCCTCATAGGTAGGATAAGAACTTAGATAAGAATTATATAGTTAGAGCTGGCAATACAAGAGTGTTTCCATTCCTCATAGGTAGGATAAGAACTTATATTGCTATGGGAGGATTTTTGACAGATGGGAGTTTCCATTCCTCATAGGTAGGATAAGAACCAAAGTCATATCCAAATTGATTAGATATATTTGTAGTTTCCATTCCTCATAGGTAGGATAAGAACCCTCATAATCCAACTCTGTTTTTGCACCTTTAACTTGTTTCCATTCCTCATAGGTAGGATAAGAACTTGGTCTCCCTCGCAAATCTATTGCCATTGACCATAAGTTTCCATTCCTCATAGGTAGGATAAGAACAAATATAGTTTAACATTTTTTCACTCCAACCGCTAAAGTTTCCATTCCTCATAGGTAGGATAAGAACCAAAGCATACGCAAACTCGAATTTTGATATCTTTTGTTTCCATTCCTCATAGGTAGGATAAGAACCAATTATAGTCAGAAATTATATATTAGATTAGGAGGTTTCCATTCCTCATAGGTAGGATAAGAACTTGGATTTAGATGAGCCAGAAAGCATATATGAAGAATTGTGTTTCCATTCCTCATAGGTAGGATAAGAACGATTGTTGCAGATAAAAACTCATCAGGATTGCTTACGTTTCCATTCCTCATAGGTAGGATAAGAACGAAAATATAACCCGTCACTTAGAGTTACAACGTGGGTTTCCATTCCTCATAGGTAGGATAAGAACATAGAAGATTTTAAGAAAGTGATTGATAATAGAGTCGAGTTTCCATTCCTCATAGGTAGGATAAGAACGGAGTACCACCTGAAATTATGGGGATTGTCGAAAATTCGTTTCCATTCCTCATAGGTAGGATAAGAACTTATACCAGAAAACATTCGAAAAAAATTTAAAAGAGTTTCCATTCCTCATAGGTAGGATAAGAACTTAAACTGGAAGGGTTAACCCCCTTCCATTATAAAAAAGTTTCCATTCCTCATAGGTAGGATAAGAACGGTATGATATAAGCTATTTTGTGAAGAAAATTACCGTAAAGTTTCCATTCCTCATAGGTAGGATAAGAACCAAGGTGTTTCCGAAGAATTTCGGAAAGATATGGGAGGTTTCCATTCCTCATAGGTAGGATAAGAACTAAACCCTGTGAAAGATTTACACATAAAGATAAAGGGGTTTCCATTCCTCATAGGTAGGATAAGAACTGGTATTTTATAAATCAAATGCGATACGCATATTATTATTATGTTTCCATTCCTCATAGGTAGGATAAGAACTGAGGAAGGAAGCATATATTGGGGAAAGATGAGCCAGTTTCCATTCCTCATAGGTAGGATAAGAACAAAACATATAAAATATGATATAATCTGTAATAGAAAAGTTTCCATTCCTCATAGGTAGGATAAGAACCCACGTATCCATGTATAGACGATTAAATGAAACAAGTTTCCATTCCTCATAGGTAGGATAAGAAC

>NZ_LN824141|12|11|1134826-1138285|CRISPRCasFinder
TTTTCCGTTCCTCATAGGTAGGATAAGAAC	CAGCGTCGTTGAAGAAAGGACTAGCTGATGCCAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CGACTAATAAGTTACTCCGAGCTTTTATTTAAAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AGGAATTGAAACAAATTCGGGCTTTGCAACAACTTCTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAGCAATTAAAGGTAACTTCTTTGAAGTCTAGGTTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGGAGGAAAGCTATGGAACATACAAGAAAGCTAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCAATCTGGGTTCTTAGATATATTAGTACCCAGGGCAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAAAATTATTGATGAAGAAAGTTTTGAATACGAAAAATTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATTTTTACATTGTAAATTTTCCGTTTAATGATCAATT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAACAAAAAGAAACAAAAGAAGTAAAAGGAGTAATAACGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGAACGAGCAACTTCAAGAAAGTTGGAAAAAATTACCTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCGACAAAAGGCAAGAATTAGTAGAAACTGAATTTAAATT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGATGCTATTTCAAAATCAGGTGCAGTAGGTTTGATG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCGACAAAATGCAAGAATTAGTAGAAACTGAATTTAAATT
GTTGCCATTCCTCATAGGTAGGATAAGAAC	AGATGCTATTTCAAAATCATGTGCATTAGGTTTGATG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AATTCATTTGTTTAGGCGAAGTTTTTCTAATTGTTTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAGACAAAGATGGTTTCAAAGTTGTAGTAGAATACAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTTATAATCATCGGGTTGAAGTTGTGGATCTCAAGTTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGGACAATATAGCATGGCTTGTAGAACTATTGAGAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAACCTAGAACTGTCTACATTAGAAACTATAGGAAAATA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ACATAAAACACTTGACAAATATAATATATTATATTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCAAACAAGGTAATCATACAGGCAAGGGTAGTGAAAC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATAATCTTTTGGAATACAATCAAAGTTTGATAGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAAGATAGTAGATGATTTAGGAGGAGGTAAACAGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAGAAAACTGACAAAAGAATTGATAAAAGAAGCGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGGAAATAGCTCCCCTCTTTTTTGTACGAATATGTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TATTATGGATATAGAACATCCTGATATTCTTATAAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CATTTTCAACTGATACCGAAGAATTATTTATTGGAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATATTTTAGCTTTGTGTATTTGTCTGTTATGCTTTCT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CTGTCATTTCAGTCACAAACTTTTGCATATCTTCCTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTAGATAAGAATTATATAGTTAGAGCTGGCAATACAAGAGT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTATATTGCTATGGGAGGATTTTTGACAGATGGGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAAGTCATATCCAAATTGATTAGATATATTTGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CCTCATAATCCAACTCTGTTTTTGCACCTTTAACTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTGGTCTCCCTCGCAAATCTATTGCCATTGACCATAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAATATAGTTTAACATTTTTTCACTCCAACCGCTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAAGCATACGCAAACTCGAATTTTGATATCTTTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAATTATAGTCAGAAATTATATATTAGATTAGGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTGGATTTAGATGAGCCAGAAAGCATATATGAAGAATTGT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GATTGTTGCAGATAAAAACTCATCAGGATTGCTTAC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAAATATAACCCGTCACTTAGAGTTACAACGTGG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATAGAAGATTTTAAGAAAGTGATTGATAATAGAGTCGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGAGTACCACCTGAAATTATGGGGATTGTCGAAAATTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTATACCAGAAAACATTCGAAAAAAATTTAAAAGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTAAACTGGAAGGGTTAACCCCCTTCCATTATAAAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGTATGATATAAGCTATTTTGTGAAGAAAATTACCGTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAGGTGTTTCCGAAGAATTTCGGAAAGATATGGGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TAAACCCTGTGAAAGATTTACACATAAAGATAAAGGG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGTATTTTATAAATCAAATGCGATACGCATATTATTATTAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGAGGAAGGAAGCATATATTGGGGAAAGATGAGCCA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAACATATAAAATATGATATAATCTGTAATAGAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CCACGTATCCATGTATAGACGATTAAATGAAACAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC

>NZ_LN824141|12|2|1134826-1138285|CRT
TTTTCCGTTCCTCATAGGTAGGATAAGAAC	CAGCGTCGTTGAAGAAAGGACTAGCTGATGCCAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CGACTAATAAGTTACTCCGAGCTTTTATTTAAAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AGGAATTGAAACAAATTCGGGCTTTGCAACAACTTCTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAGCAATTAAAGGTAACTTCTTTGAAGTCTAGGTTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGGAGGAAAGCTATGGAACATACAAGAAAGCTAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCAATCTGGGTTCTTAGATATATTAGTACCCAGGGCAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAAAATTATTGATGAAGAAAGTTTTGAATACGAAAAATTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATTTTTACATTGTAAATTTTCCGTTTAATGATCAATT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAACAAAAAGAAACAAAAGAAGTAAAAGGAGTAATAACGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGAACGAGCAACTTCAAGAAAGTTGGAAAAAATTACCTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCGACAAAAGGCAAGAATTAGTAGAAACTGAATTTAAATT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGATGCTATTTCAAAATCAGGTGCAGTAGGTTTGATG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCGACAAAATGCAAGAATTAGTAGAAACTGAATTTAAATT
GTTGCCATTCCTCATAGGTAGGATAAGAAC	AGATGCTATTTCAAAATCATGTGCATTAGGTTTGATG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AATTCATTTGTTTAGGCGAAGTTTTTCTAATTGTTTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAGACAAAGATGGTTTCAAAGTTGTAGTAGAATACAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTTATAATCATCGGGTTGAAGTTGTGGATCTCAAGTTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGGACAATATAGCATGGCTTGTAGAACTATTGAGAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAACCTAGAACTGTCTACATTAGAAACTATAGGAAAATA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ACATAAAACACTTGACAAATATAATATATTATATTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GCAAACAAGGTAATCATACAGGCAAGGGTAGTGAAAC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATAATCTTTTGGAATACAATCAAAGTTTGATAGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAAGATAGTAGATGATTTAGGAGGAGGTAAACAGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAGAAAACTGACAAAAGAATTGATAAAAGAAGCGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGGAAATAGCTCCCCTCTTTTTTGTACGAATATGTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TATTATGGATATAGAACATCCTGATATTCTTATAAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CATTTTCAACTGATACCGAAGAATTATTTATTGGAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATATTTTAGCTTTGTGTATTTGTCTGTTATGCTTTCT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CTGTCATTTCAGTCACAAACTTTTGCATATCTTCCTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTAGATAAGAATTATATAGTTAGAGCTGGCAATACAAGAGT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTATATTGCTATGGGAGGATTTTTGACAGATGGGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAAGTCATATCCAAATTGATTAGATATATTTGTA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CCTCATAATCCAACTCTGTTTTTGCACCTTTAACTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTGGTCTCCCTCGCAAATCTATTGCCATTGACCATAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAATATAGTTTAACATTTTTTCACTCCAACCGCTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAAGCATACGCAAACTCGAATTTTGATATCTTTT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAATTATAGTCAGAAATTATATATTAGATTAGGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTGGATTTAGATGAGCCAGAAAGCATATATGAAGAATTGT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GATTGTTGCAGATAAAAACTCATCAGGATTGCTTAC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GAAAATATAACCCGTCACTTAGAGTTACAACGTGG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	ATAGAAGATTTTAAGAAAGTGATTGATAATAGAGTCGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGAGTACCACCTGAAATTATGGGGATTGTCGAAAATTC
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTATACCAGAAAACATTCGAAAAAAATTTAAAAGA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TTAAACTGGAAGGGTTAACCCCCTTCCATTATAAAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	GGTATGATATAAGCTATTTTGTGAAGAAAATTACCGTAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CAAGGTGTTTCCGAAGAATTTCGGAAAGATATGGGAG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TAAACCCTGTGAAAGATTTACACATAAAGATAAAGGG
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGGTATTTTATAAATCAAATGCGATACGCATATTATTATTAT
GTTTCCATTCCTCATAGGTAGGATAAGAAC	TGAGGAAGGAAGCATATATTGGGGAAAGATGAGCCA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAAACATATAAAATATGATATAATCTGTAATAGAAAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CCACGTATCCATGTATAGACGATTAAATGAAACAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC

>NZ_LN824141|12|2|1134827-1138285|PILER-CR
TTTCCGTTCCTCATAGGTAGGATAAGAACC	AGCGTCGTTGAAGAAAGGACTAGCTGATGCCATG
TTTCCATTCCTCATAGGTAGGATAAGAACC	GACTAATAAGTTACTCCGAGCTTTTATTTAAAAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	GGAATTGAAACAAATTCGGGCTTTGCAACAACTTCTCG
TTTCCATTCCTCATAGGTAGGATAAGAACG	AGCAATTAAAGGTAACTTCTTTGAAGTCTAGGTTCG
TTTCCATTCCTCATAGGTAGGATAAGAACT	GGGAGGAAAGCTATGGAACATACAAGAAAGCTAAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	CAATCTGGGTTCTTAGATATATTAGTACCCAGGGCATG
TTTCCATTCCTCATAGGTAGGATAAGAACG	AAAAATTATTGATGAAGAAAGTTTTGAATACGAAAAATTTG
TTTCCATTCCTCATAGGTAGGATAAGAACA	TTTTTACATTGTAAATTTTCCGTTTAATGATCAATTG
TTTCCATTCCTCATAGGTAGGATAAGAACG	AACAAAAAGAAACAAAAGAAGTAAAAGGAGTAATAACGTAG
TTTCCATTCCTCATAGGTAGGATAAGAACT	GGAACGAGCAACTTCAAGAAAGTTGGAAAAAATTACCTAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	CGACAAAAGGCAAGAATTAGTAGAAACTGAATTTAAATTG
TTTCCATTCCTCATAGGTAGGATAAGAACG	GATGCTATTTCAAAATCAGGTGCAGTAGGTTTGATGG
TTTCCATTCCTCATAGGTAGGATAAGAACG	CGACAAAATGCAAGAATTAGTAGAAACTGAATTTAAATTG
TTGCCATTCCTCATAGGTAGGATAAGAACA	GATGCTATTTCAAAATCATGTGCATTAGGTTTGATGG
TTTCCATTCCTCATAGGTAGGATAAGAACA	ATTCATTTGTTTAGGCGAAGTTTTTCTAATTGTTTAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	AGACAAAGATGGTTTCAAAGTTGTAGTAGAATACATG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TTATAATCATCGGGTTGAAGTTGTGGATCTCAAGTTTG
TTTCCATTCCTCATAGGTAGGATAAGAACG	GGACAATATAGCATGGCTTGTAGAACTATTGAGAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	AAACCTAGAACTGTCTACATTAGAAACTATAGGAAAATAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	CATAAAACACTTGACAAATATAATATATTATATTAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	CAAACAAGGTAATCATACAGGCAAGGGTAGTGAAACG
TTTCCATTCCTCATAGGTAGGATAAGAACA	TAATCTTTTGGAATACAATCAAAGTTTGATAGAGG
TTTCCATTCCTCATAGGTAGGATAAGAACA	AAAGATAGTAGATGATTTAGGAGGAGGTAAACAGAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	AAGAAAACTGACAAAAGAATTGATAAAAGAAGCGTAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	GGAAATAGCTCCCCTCTTTTTTGTACGAATATGTTG
TTTCCATTCCTCATAGGTAGGATAAGAACT	ATTATGGATATAGAACATCCTGATATTCTTATAATG
TTTCCATTCCTCATAGGTAGGATAAGAACC	ATTTTCAACTGATACCGAAGAATTATTTATTGGAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	TATTTTAGCTTTGTGTATTTGTCTGTTATGCTTTCTG
TTTCCATTCCTCATAGGTAGGATAAGAACC	TGTCATTTCAGTCACAAACTTTTGCATATCTTCCTTG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TAGATAAGAATTATATAGTTAGAGCTGGCAATACAAGAGTG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TATATTGCTATGGGAGGATTTTTGACAGATGGGAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	AAAGTCATATCCAAATTGATTAGATATATTTGTAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	CTCATAATCCAACTCTGTTTTTGCACCTTTAACTTG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TGGTCTCCCTCGCAAATCTATTGCCATTGACCATAAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	AATATAGTTTAACATTTTTTCACTCCAACCGCTAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	AAAGCATACGCAAACTCGAATTTTGATATCTTTTG
TTTCCATTCCTCATAGGTAGGATAAGAACC	AATTATAGTCAGAAATTATATATTAGATTAGGAGG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TGGATTTAGATGAGCCAGAAAGCATATATGAAGAATTGTG
TTTCCATTCCTCATAGGTAGGATAAGAACG	ATTGTTGCAGATAAAAACTCATCAGGATTGCTTACG
TTTCCATTCCTCATAGGTAGGATAAGAACG	AAAATATAACCCGTCACTTAGAGTTACAACGTGGG
TTTCCATTCCTCATAGGTAGGATAAGAACA	TAGAAGATTTTAAGAAAGTGATTGATAATAGAGTCGAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	GAGTACCACCTGAAATTATGGGGATTGTCGAAAATTCG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TATACCAGAAAACATTCGAAAAAAATTTAAAAGAG
TTTCCATTCCTCATAGGTAGGATAAGAACT	TAAACTGGAAGGGTTAACCCCCTTCCATTATAAAAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACG	GTATGATATAAGCTATTTTGTGAAGAAAATTACCGTAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	AAGGTGTTTCCGAAGAATTTCGGAAAGATATGGGAGG
TTTCCATTCCTCATAGGTAGGATAAGAACT	AAACCCTGTGAAAGATTTACACATAAAGATAAAGGGG
TTTCCATTCCTCATAGGTAGGATAAGAACT	GGTATTTTATAAATCAAATGCGATACGCATATTATTATTATG
TTTCCATTCCTCATAGGTAGGATAAGAACT	GAGGAAGGAAGCATATATTGGGGAAAGATGAGCCAG
TTTCCATTCCTCATAGGTAGGATAAGAACA	AAACATATAAAATATGATATAATCTGTAATAGAAAAG
TTTCCATTCCTCATAGGTAGGATAAGAACC	CACGTATCCATGTATAGACGATTAAATGAAACAAG
TTTCCATTCCTCATAGGTAGGATAAGAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087836.1\|1142757_1143783_-\|anthranilate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234682
NZ_LN824141.1\|WP_045087838.1\|1144376_1145906_-\|anthranilate-synthase-component-I-family-protein	unknown	unknown	gnl\|CDD\|223225
NZ_LN824141.1\|WP_045087841.1\|1147634_1148855_+\|peptidase-T	unknown	unknown	gnl\|CDD\|235484
NZ_LN824141.1\|WP_045087837.1\|1143775_1144360_-\|aminodeoxychorismate/anthranilate-synthase-component-II	unknown	unknown	gnl\|CDD\|235552
NZ_LN824141.1\|WP_045087829.1\|1129721_1130978_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270451
NZ_LN824141.1\|WP_045087824.1\|1121531_1122170_-\|class-II-aldolase/adducin-family-protein	unknown	unknown	gnl\|CDD\|376358
NZ_LN824141.1\|WP_045087831.1\|1132508_1133369_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_045087833.1\|1139538_1140714_-\|tryptophan-synthase-subunit-beta	unknown	unknown	gnl\|CDD\|235288
NZ_LN824141.1\|WP_045087840.1\|1146816_1147569_+\|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|336781
NZ_LN824141.1\|WP_045087834.1\|1141218_1141839_-\|phosphoribosylanthranilate-isomerase	unknown	unknown	gnl\|CDD\|238237
NZ_LN824141.1\|WP_045087830.1\|1131107_1132133_-\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_LN824141.1\|WP_045087835.1\|1141831_1142596_-\|indole-3-glycerol-phosphate-synthase-TrpC	unknown	unknown	gnl\|CDD\|234710
NZ_LN824141.1\|WP_052670393.1\|1128772_1129651_-\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_LN824141.1\|WP_045087827.1\|1125439_1126855_-\|L-fucose/L-arabinose-isomerase-family-protein	unknown	unknown	gnl\|CDD\|238323
NZ_LN824141.1\|WP_045087826.1\|1124390_1125386_-\|exo-alpha-sialidase	unknown	unknown	gnl\|CDD\|372469
NZ_LN824141.1\|WP_045087832.1\|1138642_1139419_-\|tryptophan-synthase-subunit-alpha	unknown	unknown	gnl\|CDD\|237285
NZ_LN824141.1\|WP_045087839.1\|1146394_1146820_+\|large-conductance-mechanosensitive-channel-protein-MscL	unknown	unknown	gnl\|CDD\|234795
NZ_LN824141.1\|WP_052670392.1\|1127934_1128756_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_045087828.1\|1126952_1127861_-\|4-hydroxy-tetrahydrodipicolinate-synthase	unknown	unknown	gnl\|CDD\|188630
NZ_LN824141.1\|WP_045087825.1\|1122851_1124372_-\|FGGY-family-carbohydrate-kinase	unknown	unknown	gnl\|CDD\|198372

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087836.1\|1142757_1143783_-\|anthranilate-phosphoribosyltransferase	gnl\|CDD\|234682	PRK00188, trpD, anthranilate phosphoribosyltransferase; Provisional.	0
NZ_LN824141.1\|WP_045087838.1\|1144376_1145906_-\|anthranilate-synthase-component-I-family-protein	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	1.31516e-149
NZ_LN824141.1\|WP_045087841.1\|1147634_1148855_+\|peptidase-T	gnl\|CDD\|235484	PRK05469, PRK05469, tripeptide aminopeptidase PepT.	0
NZ_LN824141.1\|WP_045087837.1\|1143775_1144360_-\|aminodeoxychorismate/anthranilate-synthase-component-II	gnl\|CDD\|235552	PRK05670, PRK05670, anthranilate synthase component II; Provisional.	3.62342e-86
NZ_LN824141.1\|WP_045087829.1\|1129721_1130978_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270451	cd14748, PBP2_UgpB, The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold. This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	2.84326e-74
NZ_LN824141.1\|WP_045087824.1\|1121531_1122170_-\|class-II-aldolase/adducin-family-protein	gnl\|CDD\|376358	pfam00596, Aldolase_II, Class II Aldolase and Adducin N-terminal domain. This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.	4.83303e-56
NZ_LN824141.1\|WP_045087831.1\|1132508_1133369_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	8.31456e-75
NZ_LN824141.1\|WP_045087833.1\|1139538_1140714_-\|tryptophan-synthase-subunit-beta	gnl\|CDD\|235288	PRK04346, PRK04346, tryptophan synthase subunit beta; Validated.	0
NZ_LN824141.1\|WP_045087840.1\|1146816_1147569_+\|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein	gnl\|CDD\|336781	pfam07722, Peptidase_C26, Peptidase C26. These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C-terminus.	9.48637e-75
NZ_LN824141.1\|WP_045087834.1\|1141218_1141839_-\|phosphoribosylanthranilate-isomerase	gnl\|CDD\|238237	cd00405, PRAI, Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.	1.15666e-73
NZ_LN824141.1\|WP_045087830.1\|1131107_1132133_-\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	5.94806e-101
NZ_LN824141.1\|WP_045087835.1\|1141831_1142596_-\|indole-3-glycerol-phosphate-synthase-TrpC	gnl\|CDD\|234710	PRK00278, trpC, indole-3-glycerol phosphate synthase TrpC.	6.00666e-110
NZ_LN824141.1\|WP_052670393.1\|1128772_1129651_-\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	3.92953e-70
NZ_LN824141.1\|WP_045087827.1\|1125439_1126855_-\|L-fucose/L-arabinose-isomerase-family-protein	gnl\|CDD\|238323	cd00578, L-fuc_L-ara-isomerases, L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.	1.79883e-95
NZ_LN824141.1\|WP_045087826.1\|1124390_1125386_-\|exo-alpha-sialidase	gnl\|CDD\|372469	pfam13088, BNR_2, BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.	1.82169e-32
NZ_LN824141.1\|WP_045087832.1\|1138642_1139419_-\|tryptophan-synthase-subunit-alpha	gnl\|CDD\|237285	PRK13111, trpA, tryptophan synthase subunit alpha; Provisional.	3.09365e-125
NZ_LN824141.1\|WP_045087839.1\|1146394_1146820_+\|large-conductance-mechanosensitive-channel-protein-MscL	gnl\|CDD\|234795	PRK00567, mscL, large-conductance mechanosensitive channel protein MscL.	7.96877e-57
NZ_LN824141.1\|WP_052670392.1\|1127934_1128756_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	3.41381e-80
NZ_LN824141.1\|WP_045087828.1\|1126952_1127861_-\|4-hydroxy-tetrahydrodipicolinate-synthase	gnl\|CDD\|188630	cd00408, DHDPS-like, Dihydrodipicolinate synthase family. Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.	1.86804e-103
NZ_LN824141.1\|WP_045087825.1\|1122851_1124372_-\|FGGY-family-carbohydrate-kinase	gnl\|CDD\|198372	cd07804, FGGY_XK_like_1, uncharacterized xylulose kinase-like proteins; a subgroup of the FGGY family of carbohydrate kinases. This subgroup is composed of uncharacterized bacterial and archaeal xylulose kinases-like proteins with similarity to bacterial D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17), which catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. The presence of Mg2+ or Mn2+ is required for catalytic activity. D-XK exists as a dimer with an active site that lies at the interface between the N- and C-terminal domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Members of this subgroup belong to the FGGY family of carbohydrate kinases.	0

>NZ_LN824141.1|WP_045087831.1|1132508_1133369_-|carbohydrate-ABC-transporter-permease
MKAKKKIKVARILLHIFIIFMMLIWILPTLGLLITSFRPAQEVSKTGWWTVFNSPLKFTQFTLNNYKEVITKAGLGTAFKNSFMITIFGTLLPVIIGAFAAFGLAKIEFKGKSLIYSLIVGLLVVPLQLTFIPILRLYNKLKLSGTFVGLWFAHTAYGLPFAIFMLHNFFVSLPNDLFDSARIDGASLWTSFYKLALPLSVPAIASLVIFQFLWVWNDLLVALIYLGGTKDVAPLTVVLANMVGSYGQNWHLLTAAAFISMVVPLIVFLSLQKYFVKGILAGSVKG
>NZ_LN824141.1|WP_045087830.1|1131107_1132133_-|LacI-family-DNA-binding-transcriptional-regulator
MDRPTIKDIAKVLNISPSTVSRALSGKPGASEELRKKVLETAEEMGYMKNLSAQSLKNSKSKIIGIIAFDIRNPFFLDFLKGVEDVLFPREYKILLSSVDESADKEKTYLNWMVSQGVDGILSSPITEKNGKSNLKLYNNFYKMGVPIVFYDRMFYNQEQFDYVIVDNQDAIIQALMHLKENGHENVSIFLSKKGVFTIEERLKGFLKGCELLNIQTRKEWICEDIYPHEKAFDILKMLKDKNNLPSAIIATNNNITKNIVSSSRKLNVKIPDKLSLIGFDDTPENELIDPPLTTIKQPILEIGKIAATALLSRIEDRFAKPMKVVLKAELIKRGSVKNLK
>NZ_LN824141.1|WP_045087829.1|1129721_1130978_-|ABC-transporter-substrate-binding-protein
MRFKKLLLVSLLMLMLSFSFAAEKTTLYYTTLFHSGDAQAMEKIVQRINQESDDIFVVLVQGAWENYYAQLINQVVAGNAPQVGVVHSNMFPSMRDALTPLNASSAGNLLEKSGFKREDFLTDVWDSSTFDDLHYGIPLDTHMWAMWYNKDIFVKAGLDPDKPPTNAEELKYAAEKIKDAGYYAVHFAEDGVARKLMRAWYILYWQQGGELFDENYSKATFNNEKGIKALQYLVDSVQKWGWNTKGTDGFKQFASGQLGILFAGNWYYYSAEEAKINYGVAKVPTIFDKPATWGNSHNLVIPKQAANNPQMYEQAIELIRRITDLSYMWGMFGGHIPAYNNSRTSSELLNAPVWEKSLNVFSQMAEEGYLHYPPNHVKAAELEDAIQVYVQQAYNGTITPSEALKRAEAECNRILSEN
>NZ_LN824141.1|WP_052670393.1|1128772_1129651_-|sugar-ABC-transporter-permease
MKKAVRDQWSGMLFALPFMIIWGVFTLWPVISGFIISLHNWDPLRGSEFIGFGNYKYLFSSQRFWNAFVNTFEFALIMIPMTLILALLFAFYLYFSKGKAKAFVESALFFPYLLNVSIISLIWKWLFDPDFGLITESLKMIGITNPPQFLNNPIWVIPAIALASSWWLMGYRMTIFRAALESQPVEIVEAATIDGANKRQIMFKILFPLIRPQFLFTTVLTVISGFDVLGQVMIMTEGGPGRSSEVLALLLYKEAFSYFRMGRAAAIGFILFVIIFIFTLIALRFMGKDVQQ
>NZ_LN824141.1|WP_052670392.1|1127934_1128756_-|carbohydrate-ABC-transporter-permease
MKKNEESKILDIIMIIFSILWLIPVLWMIDTAIKPTPEIFTTPPKWLPEKFTLQHIKDVINNWPFGTWLLNSIIVSGLSTLFSLFLSILAAYSFSRIEWKGRDVIFIILLASMLIPWQINAVPLYFLMNNLNLLNKLIAVILPITAMPISVFLLRQFFIGLPSELEDAARIDGCNRMDILFRIIVPISGPALAALAIYMFIFSWNEYFWSLIALQRIGKFTLPIGLNMLQGAYDIEYGLLMAAAFLASIPVMIVFALLRKQIIKGMSWSGVTK
>NZ_LN824141.1|WP_045087828.1|1126952_1127861_-|4-hydroxy-tetrahydrodipicolinate-synthase
MNLEGIITALVTPFDEKGKIVESSLRKLCKFQLNKQVNGLLILGTTGEGISLNLEERKLVAEIVVDELKGKLPIMVHVGSSNINEVFSLAKHAVDIGADSITSITPYFFKMSDKEIFDFYLELSKNVPNDYPVYLYNFPTATGNDITPEVIKKLIEETNNILGIKYSSDNMMRIQEYLKLQNPNFKVFTGADQLFYPMLCLGCDGLVSGNANIFPELFVTVFKSFKKNDHKTAKLFHQYGNEIAKLFKYGNIPAIKAGMKLREIDGGYVRRPFRNLCEEEKNKLQKEFSLIFDQILNLKPLE
>NZ_LN824141.1|WP_045087827.1|1125439_1126855_-|L-fucose/L-arabinose-isomerase-family-protein
MKKRKVGIITFSDGRDFVHEETLEMNKKFEDRLVKALERTNEIEVVRASDIVNKPSKAKKAGKEMMKAEVEMTIFNYSIWCWPHLSVIASLYAPGPYLIYGQINPKYPGMVGMLAAAGALEQIGIFPERVWGEPEDPEVMKRLLKFVRGASAAHRLKGERYGMFGGRPMGMYTASANGDQWMKEFGIDVEQIDQYALVLKAEKVPTEKKRKAREWLERYATVQYDGKRLTPAILEKQIGLYYAALEIIKEEELDFVGFKGQPEMTNNYATMDIAEAFLNDPYDFDGPKEPIVAATETDMDGALTMEIFKHIAQTPVLFADVRHYFKEEKLLDLANSGQHATYFAGKSNNPEENLKNVIIHPEDFYFPAGGGAVKHFAAPGRVTLARLARQDGEYVMTIVPAEFVELSDKEKKRLSEQVQIEWPHAYAKLDTTIDTYLEYYPCNHIHGVYGNYIEELVHFCKVKGIAFQILD
>NZ_LN824141.1|WP_045087826.1|1124390_1125386_-|exo-alpha-sialidase
MKIINKSFVFDKIPSKPSSHSVSLCKINDNEIIAFWFAGSWEGEKDVDILSSRYDINADKWDTPKLFIHDPSRSLGNTAPVLFEKTFRVYYCAMEGKDWTESSLWYTDSYDQGYSWKKPKPFSLQGENLLFGTKILKLSDNRFIFPMYNEKLWISTPYITNNISSNKWEKIGEIKTEKGNIQQDMVEMNGQIFSLLRTRDGFIYKTLYNFENKKWSTTISINIPNPNSRLALEKTRDLLICCCNPLGLNKENLTHDPRKLSDIEEGFWGKREKLSIFVSSDGGNTWNEEIILEESQDKEYSYPWIQIIDETKIMIAYTYERQKIAYAIIEI
>NZ_LN824141.1|WP_045087825.1|1122851_1124372_-|FGGY-family-carbohydrate-kinase
MYLIGIDIGTQSTKSVITDEEGKVISESSKEYAVLTPQPNWAEQWPDVWFNAVIDTLKRVIEKSQIQPKNITGVAISGLYGGSGIPVDKDFNPLRPCLIWMDRRATKETKFVKQNIPKDKIFRITGNYVDSYFGFTKMMWIKNNEPEVWNKTYKFMTPKDFVIYKLTGENIIDYSSAGNIGGVFDIHKKYWSQEMCEILGIDLDKLPEKIVKSSDIVGTMSGKYAQETGLLEGTPIIAGGIDAPVAQLSAGAVYEGEHVAMVGTSTCWGNIHDGKYLTPELVSYPYVVDDLTKIYTFGGGATSGAIIRWFREEFGEYEKEYENKRGVSAYTLLELGSKDIPAGSDGIIVLPYFMGERSPIWDSKAKGTIIGLSLYHNRNHLYKAFMEAVAYSLRHNIEEAQNAGIVLDPECYLVGGTAKSDIWTQIFSDVTGYVMKRTKQDVEAPLGDAFLAGLGTGIFKQPEDIKKWTLFKEDTLPNNSNKQIYDKYFNLYKQLYKNTKEIMEQL
>NZ_LN824141.1|WP_045087824.1|1121531_1122170_-|class-II-aldolase/adducin-family-protein
MSESQLKKQVALFAKLVWDRKLTDGTGGNMSIRNKDKIYITPTSTIKHFLTENDIITVDKNGNKIEGEKEPSSERRMHIKIYEKASDVNAIIHAHPRYATSFAVTFQKLPVYALPESALVLDPITYIEYQMPGTQEFADAFAKGLEEGSRVFVLQNHGVTVAGKDIEEAYMKLETLEFLAEVSVISKLYSGINEIPTEKIKAFIEFFNKRGD
>NZ_LN824141.1|WP_045087832.1|1138642_1139419_-|tryptophan-synthase-subunit-alpha
MSKIQQIFNNNKALITYITAGDPDLETTKDIIFELNNDGVDIIEIGIPFSDPLADGPVIQEASQRALKNGVNLRKIFNTLESIKGRIHTPLVLMGYYNSIFNYGEDKFIEDCKRTGISGVIIPDLPFDEEIEFYEKLKENGIDGILLVAPNTSEERLKEISNYATGFLYCVSLMGVTGDSRGPVEYINEYVQKIRKYVNIPLAIGFGIDTPEKVKLIINYVDGIIVGSALIKIIDKNKENKNKMFEEIKTFIQNLKVW
>NZ_LN824141.1|WP_045087833.1|1139538_1140714_-|tryptophan-synthase-subunit-beta
MKKGYYGQYGGQYVPETLIPALKELEAAYEEYSKDPDFLKEYNGLLADYSGRPTPLYYADRFTEYLNGAKIYLKREDLNHTGAHKINNALGQVLLAKRMGKKRIIAETGAGQHGVATATAATKFGLECVIYMGAEDIKRQSLNVYKMEMLGAKVVPVYNGSQTLNEAVNEAIRDWVTNVEDTHYVIGSVVGPHPYPKIVRDFQRIIGDEAKKQIIEKEGRLPDYIIACVGGGSNAIGIFYPFVEDQEVKLIGVEAAGKGLETGLHAAALTAGKIGVLHGSKSYVLQDENGQIKLAYSISAGLDYPGVGPEHSYLRDIKRATYTSVTDEEAIEAFELLTKLEGIIPAFESSHALAYTMKLAPQLDKNKIIIVNLSGRGDKDVDAYRNLNRNK
>NZ_LN824141.1|WP_045087834.1|1141218_1141839_-|phosphoribosylanthranilate-isomerase
MVRIKVCGITNITDAVNIANLNIHALGFILSESPRKVELSEVAKISKLLPPFVSRVAVVVDITLNELEEIQNSKLFDYIQFHGSEDISLIKKCNLKTIKAIKIENEKSLSDIALYQNFVDYILFDTKIENKIGGTGKAFEWNILKKANITKPYILAGGIGPENVSQAIATLKPAAIDLNSKVEKSPGKKDINLIKQTLEIIKNTEK
>NZ_LN824141.1|WP_045087835.1|1141831_1142596_-|indole-3-glycerol-phosphate-synthase-TrpC
MFLQEIIKTKNEELSKLTQKKRSLKSALKKSELTLIAEIKKASPSKGLISKNFDPEKQLQAYSQGGADAISILTDEKYFNGSTEILRQLRGKTSLPILRKEFIIHPLQIYESLFLGADIVLLIAAILTKQQIISFLDISNQLGLEALVEVHDHDDLEKIIDTKTEILGINNRNLDNFTVDITNTEKIINELEKMNIRNNFYIVSESGVKDKNDVDYLESLGVNGVLIGEALMKSNKPQEKIKELFPKKEHVRNG
>NZ_LN824141.1|WP_045087836.1|1142757_1143783_-|anthranilate-phosphoribosyltransferase
MFNYFLTKVVKKQDLSMEEMEKAMNMVMEGKTTHSQLAGFLVGLNMKGETVDEITASAKVMREKALPFNYQSDNLLDTCGTGGDGKGTFNISTAVAFVLAAAGVSVAKHGNRSVSSKSGSADVLESLGVNISLSVNLVEECLKEINIAFLFAPDFHKATQYAAVPRKELGIRTIFNLLGPLTNPAKVKYQLMGIYDPTLVYPIAEVLRNLGVKRAMVVHGAGGVDEFSLAGKNKVAFLSDEKIEELEIAPEDVGLKRYDLEEIKGGTAQENKEIILSIFNGAKGPKRDVVLFNSAAALLVTHVVENFEDGVRYAQEIIDSKKALRKLQDMIEFTNFLTVQN
>NZ_LN824141.1|WP_045087837.1|1143775_1144360_-|aminodeoxychorismate/anthranilate-synthase-component-II
MILLIDNYDSFTYNIYQTISELDDVVICKNDKVSINQIESMNPSHIIISPGSGLPNAKDISIDIIKHFAKKTPILGIGSGHQCIAKIFGGELIRTSEIHHGRISKIFVTTEDVIFDGINNPFNAVRYDSLVVSQDSFPAELKILALSDQNEIMAIRHQFYSIYGVQFHPESILTSIGFQLLENFINIGRSVNYV
>NZ_LN824141.1|WP_045087838.1|1144376_1145906_-|anthranilate-synthase-component-I-family-protein
MKTIEVKVLSCSLPFENINSPVIYKKTAFNNDYSFLFENLKYNGKTFSMIGIIPEKIIQYIKTSEDNLVITLKEREKKAEKILEQDYLTFLEKELGKINFQHIEGIPPFFCSFFGYFVYEMSYLWEELLSKNTNSFSQNAELPLSILCLPKVSLIIDHEDKMLHIFNCLYFDNEETADEIEESVSIAQSEIDELKEHIIEILKIRDSKDNTSNNQSNLKRQYTPLNITYHTKKDDFLEQVKKAIEQINSSGAFQIVLSQKFSTHVESHPFEIYEILRTINPSPYMFYLNFPEAKILGCSPEMLVKVEGDKIISRPLAGTRTRGQKAEEDTYLEQELLNDEKEKAEHVMLVDLARNDLGKVCKRGSVKVTKLFGIEKYSHVMHIYSQVEGIKRGDVGPLGILKSVFPAGTVSGAPKIQAMEIINYLESKPREVYAGSIGYVAPNGDLDAAIAIRTIVYKNSEAFIQAGAGIVSYSIPENEYEETLNKAKAMFKAIEIAEHQRKEVQQLTK
>NZ_LN824141.1|WP_045087839.1|1146394_1146820_+|large-conductance-mechanosensitive-channel-protein-MscL
MAKKFWEEFKNFAIKGNVIDLAVGVIIGGAFGKIVTSLVNDLLMPLIGILIGGVDFSDLQFKIGEATIRYGAFIQTVVDFLIISFSIFLFVRFLNKLKLEHEKQAEVEEAKTPPPPPPPSKEEILLTDIKNILEEIKDKKS
>NZ_LN824141.1|WP_045087840.1|1146816_1147569_+|gamma-glutamyl-gamma-aminobutyrate-hydrolase-family-protein
MKKTVIGISSSYKYQKSTNEQSGNPLQEVHSLADEYVTAVIRAGGIPVIVPILDDLDIIREILENVDGLILSGGEDIDPKYYKKRAVSEVSLIIPKRDKQDLFCAKYMVENTDKPLLGICRGAQVMNVALGGTLYQHLPASGFEQHSLINYPACEVSHYIQIEEDSLLYRITKSNIIGVNSYHHQAVETVAPSLRVVATSVEDNLCEAIELKDSSPNRFVLGVQWHPEKMACQAKVQQEIINAFVNSCKQ
>NZ_LN824141.1|WP_045087841.1|1147634_1148855_+|peptidase-T
MKDIVERFKTYIAIDTKSDESSTTIPSTPGQLELGRLLVNELKELGLENAKQDEHGYVYATLKSNIQKEVPSIGFIGHMDTSPDLDGKCTNPKIFLYQGGNIRLNDKYTTTVDEFPFLEKLKGKELITTDGTTLLGADDKAGIAAIMSAIEYLVNHPEIEHGNVQIAFTPDEEIGRGTDFFDIEGFGADFAYTVDGGPLGELEYENFNAASVKLKIYGKNVHPGTAKDVMINALRIALEIESMLPVNEKPEYTEKYEGFFHLTKLSGTVDYAEVEYIIRDHSKTKFEAKKQLFQEIVKFLNYKYNREIIKIEITDSYYNMREKIEPHMEIIELAKKSMIDLGIEPIIKPIRGGTDGARLSYMGLPCPNIFTGGYNFHSRFELIPVEDMKLASKTIVKIIENNAKQE

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Crispr_ID: NZ_LN824141_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_13

1165895-1166012

Orphan

Consensus_repeat	Method
GCCCTGGACCCGTTATAAATTCAAAAACAGTAAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_13

>merge|NZ_LN824141|13|1165895-1166012|CRISPRCasFinder
GCCCTGGACCCGTTATAAATTCAAAAACAGTAATTAACAATTACAACTTTTTGGTACTTGCACCAAGGTAGTGGGAAGGGCTCTGCCCTGAACCCGTTATAAATTCAAAAACAGTAAT

>NZ_LN824141|13|12|1165895-1166012|CRISPRCasFinder
GCCCTGGACCCGTTATAAATTCAAAAACAGTAAT	TAACAATTACAACTTTTTGGTACTTGCACCAAGGTAGTGGGAAGGGCTCT
GCCCTGAACCCGTTATAAATTCAAAAACAGTAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045087852.1\|1162266_1162665_+\|PadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224609
NZ_LN824141.1\|WP_045087861.1\|1175968_1177054_-\|ROK-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224851
NZ_LN824141.1\|WP_052670397.1\|1174532_1175954_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366376
NZ_LN824141.1\|WP_045087855.1\|1167063_1169064_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_LN824141.1\|WP_045087858.1\|1172234_1173107_-\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_LN824141.1\|WP_045087854.1\|1166031_1166907_-\|DegV-family-protein	unknown	unknown	gnl\|CDD\|273257
NZ_LN824141.1\|WP_045087856.1\|1169121_1169610_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379228
NZ_LN824141.1\|WP_045087850.1\|1161542_1161869_+\|NifB/NifX-family-molybdenum-iron-cluster-binding-protein	unknown	unknown	gnl\|CDD\|224350
NZ_LN824141.1\|WP_052670395.1\|1157553_1158477_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|224292
NZ_LN824141.1\|WP_045087851.1\|1161888_1162254_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238431
NZ_LN824141.1\|WP_045087849.1\|1160534_1161401_+\|P-loop-NTPase	unknown	unknown	gnl\|CDD\|224071
NZ_LN824141.1\|WP_045087857.1\|1169781_1170969_-\|glycoside-hydrolase-family-18-protein	unknown	unknown	gnl\|CDD\|119365
NZ_LN824141.1\|WP_045087853.1\|1162713_1164636_-\|threonine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234752
NZ_LN824141.1\|WP_052670520.1\|1159692_1160538_+\|P-loop-NTPase	unknown	unknown	gnl\|CDD\|224071
NZ_LN824141.1\|WP_045087847.1\|1159313_1159601_+\|DUF5320-domain-containing-protein	unknown	unknown	gnl\|CDD\|379955
NZ_LN824141.1\|WP_052670396.1\|1158540_1159020_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|182623
NZ_LN824141.1\|WP_045087859.1\|1173223_1174429_-\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270450
NZ_LN824141.1\|WP_045088639.1\|1170975_1172229_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_LN824141.1\|WP_084217196.1\|1177378_1177843_+\|purine-binding-chemotaxis-protein-CheW	unknown	unknown	gnl\|CDD\|223905
NZ_LN824141.1\|WP_045088638.1\|1164659_1165724_-\|peptide-chain-release-factor-1	unknown	unknown	gnl\|CDD\|234801

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045087852.1\|1162266_1162665_+\|PadR-family-transcriptional-regulator	gnl\|CDD\|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	1.03301e-14
NZ_LN824141.1\|WP_045087861.1\|1175968_1177054_-\|ROK-family-transcriptional-regulator	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	5.57147e-21
NZ_LN824141.1\|WP_052670397.1\|1174532_1175954_-\|hypothetical-protein	gnl\|CDD\|366376	pfam00933, Glyco_hydro_3, Glycosyl hydrolase family 3 N terminal domain.	7.64598e-68
NZ_LN824141.1\|WP_045087855.1\|1167063_1169064_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	7.68431e-61
NZ_LN824141.1\|WP_045087858.1\|1172234_1173107_-\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	1.7293e-88
NZ_LN824141.1\|WP_045087854.1\|1166031_1166907_-\|DegV-family-protein	gnl\|CDD\|273257	TIGR00762, DegV, EDD domain protein, DegV family. This family of proteins is related to DegV of Bacillus subtilis and includes paralogous sets in several species (B. subtilis, Deinococcus radiodurans, Mycoplasma pneumoniae) that are closer in percent identity to each than to most homologs from other species. This suggests both recent paralogy and diversity of function. DegV itself is encoded immediately downstream of DegU, a transcriptional regulator of degradation, but is itself uncharacterized. Crystallography suggested a lipid-binding site, while comparison of the crystal structure to dihydroxyacetone kinase and to a mannose transporter EIIA domain suggests a conserved domain, EDD, with phosphotransferase activity. [Unknown function, General].	4.59736e-77
NZ_LN824141.1\|WP_045087856.1\|1169121_1169610_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379228	pfam13508, Acetyltransf_7, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	5.57918e-06
NZ_LN824141.1\|WP_045087850.1\|1161542_1161869_+\|NifB/NifX-family-molybdenum-iron-cluster-binding-protein	gnl\|CDD\|224350	COG1433, COG1433, Uncharacterized conserved protein [Function unknown].	4.62909e-24
NZ_LN824141.1\|WP_052670395.1\|1157553_1158477_-\|ATP-binding-protein	gnl\|CDD\|224292	COG1373, COG1373, Predicted ATPase (AAA+ superfamily) [General function prediction only].	3.6521e-40
NZ_LN824141.1\|WP_045087851.1\|1161888_1162254_+\|hypothetical-protein	gnl\|CDD\|238431	cd00851, MTH1175, This uncharacterized conserved protein belongs to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme. This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB) however, its function is still undetermined.The SCOP database suggests that this domain is most similar to structures within the ribonuclease H superfamily. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).	1.67959e-29
NZ_LN824141.1\|WP_045087849.1\|1160534_1161401_+\|P-loop-NTPase	gnl\|CDD\|224071	COG1149, COG1149, MinD superfamily P-loop ATPase containing an inserted ferredoxin domain [Energy production and conversion].	2.0088e-99
NZ_LN824141.1\|WP_045087857.1\|1169781_1170969_-\|glycoside-hydrolase-family-18-protein	gnl\|CDD\|119365	cd06548, GH18_chitinase, The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.	1.56281e-107
NZ_LN824141.1\|WP_045087853.1\|1162713_1164636_-\|threonine--tRNA-ligase	gnl\|CDD\|234752	PRK00413, thrS, threonyl-tRNA synthetase; Reviewed.	0
NZ_LN824141.1\|WP_052670520.1\|1159692_1160538_+\|P-loop-NTPase	gnl\|CDD\|224071	COG1149, COG1149, MinD superfamily P-loop ATPase containing an inserted ferredoxin domain [Energy production and conversion].	7.34994e-102
NZ_LN824141.1\|WP_045087847.1\|1159313_1159601_+\|DUF5320-domain-containing-protein	gnl\|CDD\|379955	pfam17253, DUF5320, Family of unknown function (DUF5320). A number of this family members have a coiled coil domain at the C terminal.	7.41606e-26
NZ_LN824141.1\|WP_052670396.1\|1158540_1159020_+\|hypothetical-protein	gnl\|CDD\|182623	PRK10657, PRK10657, isoaspartyl dipeptidase; Provisional.	7.01123e-70
NZ_LN824141.1\|WP_045087859.1\|1173223_1174429_-\|extracellular-solute-binding-protein	gnl\|CDD\|270450	cd14747, PBP2_MalE, Maltose-binding protein MalE; possesses type 2 periplasmic binding fold. This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.35662e-90
NZ_LN824141.1\|WP_045088639.1\|1170975_1172229_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	1.48512e-81
NZ_LN824141.1\|WP_084217196.1\|1177378_1177843_+\|purine-binding-chemotaxis-protein-CheW	gnl\|CDD\|223905	COG0835, CheW, Chemotaxis signal transduction protein [Cell motility and secretion / Signal transduction mechanisms].	1.11625e-41
NZ_LN824141.1\|WP_045088638.1\|1164659_1165724_-\|peptide-chain-release-factor-1	gnl\|CDD\|234801	PRK00591, prfA, peptide chain release factor 1; Validated.	0

>NZ_LN824141.1|WP_045088638.1|1164659_1165724_-|peptide-chain-release-factor-1
MLEFKEEVEKKLQELEIKLSDPNITSDLEKLKELGQEHARFSELNELFNNYESTLEDIDALHEMYNAGDVPEEEYLSLLNELETKKETLEKNITERLVPPDEYDERNIIMEIRAGTGGDEAALFAADLMRMYLRYAERKNWKHEILDINENELGGIKTAILRINGKGVYRRLKYESGVHRVQRVPQTEASGRIHTSTATVAVLPEPTDIDVHISEDELKIDTYRASGAGGQHVNKTDSAVRITHLPTGIVVTCQKERSQHQNKEKALNILKAKLFEIKLQEQQSKIIKERKSQIGTAERSEKIRTYNFPQNRVTDHRIQYTTYRINEILDGDLDEIIDKLIEYDLKEKIETLTI
>NZ_LN824141.1|WP_045087853.1|1162713_1164636_-|threonine--tRNA-ligase
MIKITFPDGSTKEYEEGVSPADIAKDISQRLYKNSIAAEVNGQLVDLNYSITQDATVKLITLEDDKAPNIYRHTMSHIMAQAVIHVFGKEKVKLAIGPVIEDGFYYDFDIEGYNISEEDFPKIEEEMKKIIDQDITIIRKEISKAQAKEIFKDQPYKLELLDDIDDDEVSVYIQGDFIDLCRGPHLPSTGYVKHFKLLSVSGAYWRGDEKNKMLQRIYGTAFAKKKDLDDYLNMLEEAKRRDHRKLGPQLNLFMLQPEMAPGMPFILPNGKIILNELMNYSRQVHKRYGYSEVETPQIMNIKLWHQSGHWDHYKENMFFTEKEDMPMAVKPMNCPGHILIYKNSFVSYKDLPIRMFEFGKVHRYERSGTLHGLFRVRAFTQDDAHIFCTKSQMEQEIIKVIELTNEIYSTFGFNYEAILSTMPDDHMGDIEAWERATQALKLALEKSQIKYKIAEGDGAFYGPKIDFHVTDSIGRKWQCTTIQLDFQMPERFEMVYANEKGEYERPVMIHRAIFGSLERFFGILIENFAGEFPTWLAPIQVSVVPVSEKFNEKAKEFARQLEKENIRTFVNDSDSTVSYKIRNEQMKKIPYMIVFGEKEMNSNTINVRTIKGNTAENISRDLFINKIKEEISSRSLNLSF
>NZ_LN824141.1|WP_045087852.1|1162266_1162665_+|PadR-family-transcriptional-regulator
MCANHRGGRGKGGRGRGKGRFLANYILLIIAEEPTYGYDIATKLDEMGIEKIEGTGQMGRIYRILSELESYGYIIPKWDTSKSPPVKVYTITPLGLEYLKYAVESVKQEIKVLETFISKYEDVLKKNDSADE
>NZ_LN824141.1|WP_045087851.1|1161888_1162254_+|hypothetical-protein
MKIAIPVIENNKEESRISEHFGRAPYFAFVELKDDKTHTFEIEENPFEDHSLGDIPRYLHDKNVDLIVVRNIGKKALNFFEEYNIKVIRGVEGNLKKIIQMAKSNELKDQDYTEDSKCCHE
>NZ_LN824141.1|WP_045087850.1|1161542_1161869_+|NifB/NifX-family-molybdenum-iron-cluster-binding-protein
MIVAIPTEMDSLNSKISERFARTAYFLIYNTNDDSYEFISHEMQQEHGAGTKIVNELSVRNVEAVISKNIGQNALQALKVGNIKAYIASAGNVKENIDFLKSKKLQEF
>NZ_LN824141.1|WP_045087849.1|1160534_1161401_+|P-loop-NTPase
MKQIAVVSGKGGTGKTTLSASLSYLFKNPVMSDCDVDASNFHLLFSPLEMIESYEYYGGKKANINYEKCTNCGICKNKCRFDAIDFKEGKYVINEYACEGCKLCVLTCPEKAIKLSENLAGNYYKSKCSNGILVHGDLNPGEETSGGLVAEVRKKSYSEAEKSKKDVIIIDGAPGIGCPATSSVAGVNLAVVVTEPTLSGFHDLKRMVDTLKKMRVKFAVVINKFDLNESAKLEEWCFSENIDLLGKIPFDEMVNVATKEAKPIILYENSIAAKAIKDIYLRILDKFF
>NZ_LN824141.1|WP_052670520.1|1159692_1160538_+|P-loop-NTPase
MKIAVLSGKGGTGKTTISTNLAKVLSKNRKVLLLDADVEEPNDHLFYNVTFKKEKSVNIFIPKVNKETCTLCGLCAKECQFGAINVFEKGVFVFQHLCHGCGVCSEICVLNAIDEVSKSIGQIKFGTSIFFDFGMGLMNIGEPSGVRIVRELKKYISNDYDVTIIDAPPGTSCPVVEVLQNVDFAILVTESSPFGLHDLKLAVSLVREMGIAFGVVINRYDPSFFELEEYIKSEDISLLMKIEFDKNIAKWYSQGFLIVDKSEELYKNFEVLFENIIEVLK
>NZ_LN824141.1|WP_045087847.1|1159313_1159601_+|DUF5320-domain-containing-protein
MPNLDRTGPWGLGPMTGRGLGRCARGYGRGRGYGRGFGYGLGAHGRWKGGYYYPQVSSLREDKAFLEEQREYLKDELNYIEKILKEIEVTEKKEE
>NZ_LN824141.1|WP_052670396.1|1158540_1159020_+|hypothetical-protein
MENLIAKAKSLNAEGVSCFAYTGSYHLPLKTFTKRIIDDVVYIEEIIGVGEIAISDHRGSQPTIEELTRLTSDARVGGILSKKAGIVNVHVGRGKNFVGPLIEVVKKSDLPIAQFLPTHMNKGKESMFDEKGNFLKLDVADVCTLFKEVKDCVIQEDTR
>NZ_LN824141.1|WP_052670395.1|1157553_1158477_-|ATP-binding-protein
MDKFGIYTIRGPRQIGKTTFIKLFIRKLIEDDINTLRILFFTCDMIKDNSELVDIIKIYLQSFNISKNERTYIFIDEITMVNNWQSAIKYLVDIGLIVNAVVILTGSSAYDLKVSSERMPGRRGEGKDLLFLPLTFNEYLKAIGIEIDPLNIRQILLLGEEDLKRLNFKYSFLQEYFLKYINSGGFPKVINEYMNENKITDQTKNIYRDFILGDAEKYMNSRGTIIEIFKKLPEIIGQRFSWRSILNDLGKSIKSVDTIQKYFEYLAYSFIISTVYFIDPSTKTIKFKKALNQTHPFLYGNLNSRDS
>NZ_LN824141.1|WP_045087854.1|1166031_1166907_-|DegV-family-protein
MKNNICLVADSGGYLPKEILTKYDISIVPFYITLDGKKYLVQGKDITDEELYKKMHSDPNLLPKTSAPNPEDWYNVLSEKVKKGYNNILITTMSSDLSASFNNANLAKDLFLKDYPNCNVKLFDTRTCTCGQSAMEIKLAQLIEKGKHTLEQLYDTAKDLISKTHTLFSVKTLKYMEAGGRIGEAAKFLGILLKINPISEFVNGVVKPIKISRTRKKALDSMVDIAVERIKDPTKTIICTRSALFEEDQEYLITKLKEKLNYKGKIYSGVLESVIGAHSGPGAIGIGFVTE
>NZ_LN824141.1|WP_045087855.1|1167063_1169064_-|methyl-accepting-chemotaxis-protein
MKTLRTKMLVLILVPIIALLVILASVLYVQINSVVSQEVTNLTIEIEKIGTKTVDEWLKGLLKEVQLLADTNAVKTAFQTKDWTSLMEEYLPPRLKERPDYEMFFIAYSDGTSPNTLGSVSNLADRQYFIDIMKNNKKYSISDVLVSKASGKNVFVITVPVKDNNKNIGVFGATVLLDTLTNFVSDIDIGKSGYAFIVDSTGMVIAHPDKSIVMNLNLLQSSKDNYQDLDKIGKKMISKESGYGQYKEPTGEIKNVFFSPIPSTTGWSFAAIIAEKDLKSSVNKLLGQILIVIAIIIAFAIGIIFFLSISISKPISQLAQSAQEFGQGDLTVKFEAKGKDEVVTMAKALQQMGDNLRNSFTQIVSYSEQVDTTAQELASSAEEMSATSEELSAQMENVNKNVQNVSASIEEATSGIQEVASSAQNVSRSAQELTEKASRVKEAADRGNLAVNNIVNMIEQTKASAGKTEKVVLELSNNAKNIWSIVETINSIAEQTNLLALNAAIEAARAGEAGKGFAVVADEIRKLAEDSKKATDKIASILNQVQSGTEKARSETIDASKQVEKTVEQSSIIKNEIFNILKEVNEISSMIESLAAGSEEMSAAAEEMSSAMDSAAKSVTEIAQQVEEMTSAVRQQANATLQVSSASEELSQIADKLVHQVKKFKI
>NZ_LN824141.1|WP_045087856.1|1169121_1169610_-|GNAT-family-N-acetyltransferase
MPDMLVKLYELPYDKTLFDNLEKENISVRRAKAPEKNYVVGWIQEKFGDYWASESDIAFSRSPISCFIAIDTAKNQIVGFACYDTTCKDFFGPMGVDENYRGKDIGKALLLISLKGMWDIGYAYAIIGSAGPVKFYEKVVNAIPIENSVPGIYKGIFRKNNP
>NZ_LN824141.1|WP_045087857.1|1169781_1170969_-|glycoside-hydrolase-family-18-protein
MKKIWIILMVLAVSLLSFSENLSNTKENITLEDKDYKIIAYLPCWVGKDWIAEDIQGDKLTHLYLAFARINNEFKISNHDVRIPGVPDTVSSQTIIDSIWEEVRRVQKKYPDLKIIVAVGGWGADGFSDMAATKATREIFVDSVVEYLKKYNLDGIDIDWEYPVDGGGGTIEARKEDKENFTEVIKLLRKKLGEDKEISFCTNVSGWFLDVIEWEEVVPLVNSINVMGYDYQGPWSENTAHHSNLYINPQDPVAHWGLSSDAAIKRFINRGIPAEKLVLGFPAYGREFHGAQPGENGDGLFQKYQDTIWPGGSIPYTILKQYYVNKNNFKRFWDDDAKVPYLYDGETFITYEDPQSVAEKARYVKEMDLGGIMYWEYVDDIENDLLNSAYETLKK
>NZ_LN824141.1|WP_045088639.1|1170975_1172229_-|carbohydrate-ABC-transporter-permease
MKKTVLLIISFCLLIIFLFPLVIMIYTSFIPQGNMTNIVKDYYLNDFEAGYMSVIKRTIAPLGNTDYLLAKESPTSTQSLKIESTSERNPGIKMIGATRDLRKIKTLNFWLKVETPDINKGYVRFEDVNGLFQDIPFTLEKNGQWQEIKIDKKELDQDKLNLKFVTGISVVLNNEKEVSNVAFLIDDIKVYNQYPTLMNYVIVWTEDMFGRYIINSVIISVVVVLANLLFSSMVAYAFARREFKGKNFLFGLILATMMIPFQVTTIPIFILMKNLNFLDTYWALILPQLVTPFGIFILKQYIEQLPLEIEQAAVVDGAGPFAVFFKIVMPLSSPALAVMGINTFITTWNDLFMPLILTSSREMRTAQVGLALYQQLTQLQWPYLMSATTIVGLPIMIAFLIFQKQIISGITAGSVKG
>NZ_LN824141.1|WP_045087858.1|1172234_1173107_-|sugar-ABC-transporter-permease
MKTKRKYNLITLAFLLPWIITFIIFSAYPIIFSIGISFTDYSGLNPAMNFVGLKNYTALFKDEIFLKAMKNTLIFVVGTIPFTTIISILLAVLINSKMVKCKGLFKAGFFLPSVMSMVVISTIWRYIYSADGILNYMLRIFGIEKNTGWLASPDTALLAIMIMDIWAAIGYYTIIFLSGLQSIPEELYESAAIDGASSTDAFFKITLPLVKPTLFFVIAINTIRSFQIFAEIFTMTGGGPLNSTQTIVHYLYITGFRQFKMGYASAMAYILVIIILIITLIQQRALRSEY
>NZ_LN824141.1|WP_045087859.1|1173223_1174429_-|extracellular-solute-binding-protein
MSKKVLLVFMLVGLTLLSFGKTKISVWQFMMDDNLSQQVKADFEKANPDIELEIVQLSWATGFDRIVTSIAAGTAPDVIELGNTWLATFASQGVLRPVDDLVGKAKDDYVAWNFVEYQDKYWGFPWLLAPRCMYYNLELLEKAGLDPDNPPKTWMELLNASAKIHALGPDIYGVGLCVGELYSPYQEWFLPAVWGNFGHFVSPDLKKATLNSDPVIEAAYYYRSLKDYALLGKESELAEAFGKGKLGFFFAGPAYINNTQRDYPETIFDVAFIPKPRENYGYHASFAGGEVLGISSQCKNIDEAWRVVEYLLGEKVAMQITRTTGEVFPTKVGIEKDPWFESHPLHRTFLEQNQYAVPFPPLAEANKIEQLFTNIVEEILLTNTPIENILQKYNEQIQSLL
>NZ_LN824141.1|WP_052670397.1|1174532_1175954_-|hypothetical-protein
MNKNDLGKFFILGFQHGIKKHHIDLIKEIKPAGIILYPSNMRSLSDLQLSIERLHEIIDDGVRLFISSDHEGGQLETVPGILPSPGNKALGASNEPHYAYIFGDFLGNELRKIGFNMLFAPVLDVRANKSSPVVGLRSFSDNPKIVAEYGVNFLKGLNNHIIGTCKHFPGHGKAMQDSHHEIPIIPNLDESDLFPFMKAIEAGAEAIMTAHIIYPQYDDNIIATLSKTILKNLLREKMGYQGLIITDALEMKAIHDNYSPREIVSKFFNATGDLLLVGDCDANFEPLYKELISLYSNGEIDKQLLENSFNRITSLQNQFVEPNYEARFLTEISKKAIKTNINEKLNFSEITFLVPQGDPLSPSDTSNKDYYEYTDLIRNLFENPQITTFNFENGKINGSLEKTELIVSFVVDSFLFEKQLKMQKEIKEYANQVIYIILRDERDLQNYKTEKYVLTNSTKAVSVYYALKTIFDI
>NZ_LN824141.1|WP_045087861.1|1175968_1177054_-|ROK-family-transcriptional-regulator
MQENLFSITKYLWSHKKATINQISEDLTLDKSTVSRHIRKLKQSNIVVTEGSLKPGSHGGRKTNVYSFNYDIFQVLGLEIEQNGIEGVITNFNGDIIDKFVIHQKINKSNLTELIINIVEDKKNFNLYAIGISLPGIIDPIKGKIVFSQALGIENYLLVKELSNKISLPILIDNDSNIGAAYYNSKLKNTARNILYIYTSIPYELKDLVGVGIGIIIDNHLYHGSNNCSGEYEFKFNLVKDKKYETDYFNFLKNFDEEEVFEAVKSFLDNLSEKIGLLGSILDPDTIIYDGNIRFLPELALSYLLEETRKKIFMKDKRKIKFLKESKDESVNAVGAAINFITKTFEEERYLKKFFKKLQTV
>NZ_LN824141.1|WP_084217196.1|1177378_1177843_+|purine-binding-chemotaxis-protein-CheW
MSSEIKIVTFTLGKEKFGLDIMNVDAVIEYEDTTKLPNTSDYFEGIINYRDEEVLPIINLRKKFKLPDFENKSHAKVIVVKIGDKKVGIMVDDVKNVRSINSSLIEEKPNIGGLRGAKFISGIARLDEGMLIILDIDKLISEEDKIEINEMVNS

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Crispr_ID: NZ_LN824141_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_14

1305995-1306123

Orphan

Consensus_repeat	Method
AGCTAAGAAGGGTGAGGGCTGCGCCCTGTTACCCTCATAAATTCAAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_14

>merge|NZ_LN824141|14|1305995-1306123|CRISPRCasFinder
AGCTAAGAAGGGTGAGGGCTGCGCCCTGTTACCCTCATAAATTCAAAAACAATAATTAAATTATGGCTTTTTAATACTTGCAGCTAAGAAGGGAGAGGGCTGCGCCCTGTTACCCTCATAAATTCAAAA

>NZ_LN824141|14|13|1305995-1306123|CRISPRCasFinder
AGCTAAGAAGGGTGAGGGCTGCGCCCTGTTACCCTCATAAATTCAAAA	ACAATAATTAAATTATGGCTTTTTAATACTTGC
AGCTAAGAAGGGAGAGGGCTGCGCCCTGTTACCCTCATAAATTCAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045088653.1\|1301578_1302214_-\|class-II-aldolase/adducin-family-protein	unknown	unknown	gnl\|CDD\|376358
NZ_LN824141.1\|WP_045087939.1\|1297817_1300142_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_LN824141.1\|WP_045087936.1\|1294543_1294798_+\|DUF4911-domain-containing-protein	unknown	unknown	gnl\|CDD\|379806
NZ_LN824141.1\|WP_045087941.1\|1300784_1301495_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087943.1\|1306428_1307178_+\|DeoR/GlpR-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224268
NZ_LN824141.1\|WP_045087951.1\|1321549_1322323_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_052670403.1\|1294772_1295888_+\|YqeG-family-HAD-IIIA-type-phosphatase	unknown	unknown	gnl\|CDD\|225090
NZ_LN824141.1\|WP_045087935.1\|1293201_1294491_+\|PhoH-family-protein	unknown	unknown	gnl\|CDD\|224787
NZ_LN824141.1\|WP_045087942.1\|1302778_1305892_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|153237
NZ_LN824141.1\|WP_045087940.1\|1300268_1300757_-\|peroxiredoxin	unknown	unknown	gnl\|CDD\|224146
NZ_LN824141.1\|WP_045087950.1\|1319772_1321500_+\|NAD+-synthase	unknown	unknown	gnl\|CDD\|237577
NZ_LN824141.1\|WP_045087947.1\|1316635_1317208_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293792
NZ_LN824141.1\|WP_045087945.1\|1313650_1314628_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176196
NZ_LN824141.1\|WP_045087938.1\|1296051_1296243_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237517
NZ_LN824141.1\|WP_045087946.1\|1314846_1316601_+\|M3-family-oligoendopeptidase	unknown	unknown	gnl\|CDD\|341073
NZ_LN824141.1\|WP_045087944.1\|1307225_1308683_-\|alpha-glucosidase/alpha-galactosidase	unknown	unknown	gnl\|CDD\|133433
NZ_LN824141.1\|WP_045088652.1\|1296287_1297499_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl\|CDD\|179745
NZ_LN824141.1\|WP_084217212.1\|1317572_1318742_+\|sulfate-adenylyltransferase	unknown	unknown	gnl\|CDD\|235227
NZ_LN824141.1\|WP_171820596.1\|1318758_1319628_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|197215
NZ_LN824141.1\|WP_045087952.1\|1322353_1324921_+\|alpha-glucan-family-phosphorylase	unknown	unknown	gnl\|CDD\|340852

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045088653.1\|1301578_1302214_-\|class-II-aldolase/adducin-family-protein	gnl\|CDD\|376358	pfam00596, Aldolase_II, Class II Aldolase and Adducin N-terminal domain. This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.	1.65265e-64
NZ_LN824141.1\|WP_045087939.1\|1297817_1300142_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	7.99603e-48
NZ_LN824141.1\|WP_045087936.1\|1294543_1294798_+\|DUF4911-domain-containing-protein	gnl\|CDD\|379806	pfam16256, DUF4911, Domain of unknown function (DUF4911). This family consists of uncharacterized proteins around 75 residues in length and is mainly found in various Thermotogav species. The function of this family is unknown.	1.82591e-05
NZ_LN824141.1\|WP_045088652.1\|1296287_1297499_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl\|CDD\|179745	PRK04135, PRK04135, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_LN824141.1\|WP_045087943.1\|1306428_1307178_+\|DeoR/GlpR-transcriptional-regulator	gnl\|CDD\|224268	COG1349, GlpR, Transcriptional regulators of sugar metabolism [Transcription / Carbohydrate transport and metabolism].	2.54217e-67
NZ_LN824141.1\|WP_052670403.1\|1294772_1295888_+\|YqeG-family-HAD-IIIA-type-phosphatase	gnl\|CDD\|225090	COG2179, COG2179, Predicted hydrolase of the HAD superfamily [General function prediction only].	2.85229e-42
NZ_LN824141.1\|WP_045087935.1\|1293201_1294491_+\|PhoH-family-protein	gnl\|CDD\|224787	COG1875, COG1875, NYN ribonuclease and ATPase of PhoH family domains [General function prediction only].	5.50987e-163
NZ_LN824141.1\|WP_045087942.1\|1302778_1305892_-\|hypothetical-protein	gnl\|CDD\|153237	cd03143, A4_beta-galactosidase_middle_domain, A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.	0.00245979
NZ_LN824141.1\|WP_045087940.1\|1300268_1300757_-\|peroxiredoxin	gnl\|CDD\|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	1.27855e-67
NZ_LN824141.1\|WP_045087950.1\|1319772_1321500_+\|NAD+-synthase	gnl\|CDD\|237577	PRK13981, PRK13981, NAD synthetase; Provisional.	0
NZ_LN824141.1\|WP_045087947.1\|1316635_1317208_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293792	cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.	3.94868e-49
NZ_LN824141.1\|WP_045087945.1\|1313650_1314628_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176196	cd08234, threonine_DH_like, L-threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.	5.35975e-111
NZ_LN824141.1\|WP_045087938.1\|1296051_1296243_+\|hypothetical-protein	gnl\|CDD\|237517	PRK13807, PRK13807, maltose phosphorylase; Provisional.	3.5402e-11
NZ_LN824141.1\|WP_045087946.1\|1314846_1316601_+\|M3-family-oligoendopeptidase	gnl\|CDD\|341073	cd09610, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid.	0
NZ_LN824141.1\|WP_045087944.1\|1307225_1308683_-\|alpha-glucosidase/alpha-galactosidase	gnl\|CDD\|133433	cd05297, GH4_alpha_glucosidase_galactosidase, Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.	0
NZ_LN824141.1\|WP_084217212.1\|1317572_1318742_+\|sulfate-adenylyltransferase	gnl\|CDD\|235227	PRK04149, sat, sulfate adenylyltransferase; Reviewed.	0
NZ_LN824141.1\|WP_171820596.1\|1318758_1319628_+\|hypothetical-protein	gnl\|CDD\|197215	cd09116, PLDc_Nuc_like, Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins. Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.	1.00384e-26
NZ_LN824141.1\|WP_045087952.1\|1322353_1324921_+\|alpha-glucan-family-phosphorylase	gnl\|CDD\|340852	cd04299, GT35_Glycogen_Phosphorylase-like, proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.	0

>NZ_LN824141.1|WP_045087942.1|1302778_1305892_-|hypothetical-protein
MLYPKNKRDISQELFKNPTSEYRGAPFWAWNSSLNKEDLLEQIDNFKIMGIGGFHIHSRTGLAVDYLSDEFMSLVKLCNEKAKEEDMLCWLYDEDRWPSGFAGGYVTKDDQYRQRFLVFTPIYYNDSEIVVEHLRANKRVEQGKKRKLLARYEIVLENGYLTRYKRLKDNEKSKDNSKIWYAYLEIAADDPWFNNQAYVDTLNKRAIETFVEITHEKYFQELGEDFGKSIPAIFTDEPQFTRKSYLQFSEDESEIILPFTDDFEESYFNSYNQSILDHLPELIWELPNDQISLVRYRYHDHLTERFTQAFADTIGDWCENHGILLTGHLMEEPTLESQTACVGEAMRSYRSFQLPGIDMLCDRREFTTAKQAQSAAHQYAREGVLSELYGVTNWDFDFRGYKLAGDWQAALGVTVRVHHLTWVSMQGEAKRDYPPSIGYQIPWYKEYSLIEDHFARLNTVLTRGTPEVKVGVIHPIESYWLYWGPQDKTAIKREELEDNFKNITEWLLFGLIDFDYIAESLLPSLSKIQENKTFQVGAMNYDVIIVPGCETLRSTTLDRLEAFQKTGGKIIFLGELPRFVDAVESNKAKKLAEKSTVIPFSKGKLMQELNQYRDIEIIKQDGSPSDNLFYQMRKDANNKWLFISHVYKMKNPDIAEKERIKIIIKGECNPVIYDTINGSIKETEAKIINGETIVDYEFYPHDSLLLKLESSNFTESEKKKENLSIVEKETKEIRLEDPVNYSLSEPNVLLLDMAEYSFDGRGWQQVDEILRIDNKFRELLNYPLRMNKLAQPWTIKKEEPFEHVLKLKFSIESDIELKNPCLALENVENTKIFVNKKHVEPEVVGWFVDKSIKKVKIPNLRLGISEIILEIPFNSKTNVEWCYLLGDFGVKVSGKHKKIVEPQKALTFGNWVNQGLPFYAGNVTYHCTIECNEGNLTIEVPQFRNPLLSISVDGQEKGKIAFAPYTLELGKVNKGKHDIDITAYGNRINAFGTVHNCDDTYFWFGPDAWRTTGSRWSYEYRLKPMGILVSPKIYLKQ
>NZ_LN824141.1|WP_045088653.1|1301578_1302214_-|class-II-aldolase/adducin-family-protein
MNEKQRLINICLSMEKNGLVKGTWGNASIKDGDKIFITPSGYPYDKMNEDDVMVIDIDGNILEGFRKPSSEYQLHLEIYKNRKDVNAIIHSHPIYSSVVSLVKEYIPPLIEDGVMICGERINVAKYGEPGTKDLALKAVEALEMNYAVILKNHGLVTIGENEIEALTTSIIAEKTAQIYIEALKIGEISELSPQDAKKLREKYLSSYRQKG
>NZ_LN824141.1|WP_045087941.1|1300784_1301495_-|hypothetical-protein
MKNLSRTLVSLIVIIVASLSFSQGFSGGEFGGLGGGDFGAKWMDLGELNKTLNDNNLPTFSNPAFYTGGGGYALIGKTLYGGEGYGITLSEKADDYTVELDVGYGLFDIGYLIYAKQSLRVYGMGGVGFGGMTFKVSEFPDSKKFEDLLTDYHENLFISGPIPIFKIGFGADYILTFKASSSTGGFAIGISAGYVFAPFDPIGGWKLSDTSVSNVPKFGPTGPYITIKIGGGGFAF
>NZ_LN824141.1|WP_045087940.1|1300268_1300757_-|peroxiredoxin
MKYFRLEEGDRLPTFSLKDANGELININDFLGKWLVIYFYPKDGSKGCLLEALDFSNKLSEFKKYNCEIIGISPDSEESHKKFIEKNDLKILLLSDPDHVVLEKLGVWQLKKMYGREHWGVIRTTILVDPDGFVRKIWENVKVKDHASNVLHSLIELIRSNK
>NZ_LN824141.1|WP_045087939.1|1297817_1300142_-|methyl-accepting-chemotaxis-protein
MKPRDRENMNIKWFNKFSNKISIILLVLGLLPCIFLVIYITLSIQNKTLENEANISYVVEDLNNEYLKQINEYNDAVQEQLNSYNNYLKSQITLIEEEVSKQMKEMYTQSFDNSLKTLGTIFSNFLDSEKRTLEKTGKLIASDTILKEKTASKSISLMERYSILEPFVTTQEYNGMQLWILYPPNTAGTGVEVTSKNQTYKLQKKAETYSKGYEYTKQLNLDDFLKEIFTNILEIGYLTPVVKTKSFNSIPYFIGVFPIVDPIATNTVNGFLVIIEEFENQKLLEISKLLDASVTLYDKNYNFIYSNFPKDEIYIDENKLNAKFVTEEILNKPKRSYYFQTEEFDGLYIQISKDYQDFDASINIPLETSFDLPTLTAKEVTFEIDLGLNKIIRNTIIILIILILIIIFVSYLLSRRFGTQIRNFTKNLQRLSEGDLTVEISHVTQIKDEFDQMNKELNKTISSLKMMIKNLLEDSEQIIVSSKNVDEKSKLLKNTQQNLNSLLEQIKDLGDTVSKISSRFSEKIDELISNSRKVKNATENISKISNETITFANEGKKFVGSVLNVSNSVEELVKNSSVSVDNFSKEVEKINEFVKNISDIAKQTNLLALNASIEAARAGEAGKGFAVVAEEIRNLSEETSMTAMGISDKMINILNSLKTLAQGIQETNKKTNDLGNTIKVFEEGFNNLENSSKSLTSVVNDLTQSVREQNQTIEEFKNEIQGIESQTNTTISKLNIVEEGIKADSDAINSLLEQVEILNKIAHNLKEETSRFKI
>NZ_LN824141.1|WP_045088652.1|1296287_1297499_-|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MSFDRQNIIKDLSIKTDSKIVLLVMDGVGDLPNEEGKTPLKAANKPIMDSLAKESELGQSIAVFQGITPGSGPGHLSLFGYDPLKYQIGRGILEALGLDVEVGPKDVVARANFATIKNGVIIDRRAGRPASEESKKIVELLSEKIKQIDDVKITFYPGKEHRFVVKFSGEGLFDEVSDADPQKEGHPMEWAKSLNPDSEKMAKIANKLLKEIGEVLKDQPKMNFALLRGFSKHPKLPTFKEIYKLDAAAIATYPMYRGLAKLVGMQIIKTGETIEDEIETLKANWNKYDFFFVHVKKTDSYGEDGNFNEKVKVIENTDRVLKDILALKPDVLIITGDHSTPAPMKSHSWHPVPVLINSKFVRKGLSNVFDEFECARGVLGTISALDLLPLALAHAGKLEKYGA
>NZ_LN824141.1|WP_045087938.1|1296051_1296243_+|hypothetical-protein
MNFKPWLPEQWKELSFKLRWRDAKLKVDILQDKIVFLSDQTLKIRVFSKDYILEQNKPFTCQR
>NZ_LN824141.1|WP_052670403.1|1294772_1295888_+|YqeG-family-HAD-IIIA-type-phosphatase
MNRMTGLFKYIPIPQEHSPDIYSVDYENLKKLGFTTILMDYDFTVTGWRDDNITDKTLKLFDKLIEEGFKVAIVTNAKREKVKIIEELTNGKVKVYTSMKKPNTKKLKEVLQEMDSKESETVIIGDLFITDISVGNKLGLYTILINPYTYGLESKFKKFVAGFSKFAYNVFFYTIGWFFRFIDLAAPNEFRENIFDIDYIQLKEKGYKMIIFDFDNTLNEYHKDFLTPEATDLIIRLKEMGFYLLIASNGRKSRFKSLEMDLDELGVDLLTAARKPLKFKIRKKIKYLGYKPSEIVMIGDQLFTDVVCGNAFKFYTIKVEPLTTNEGIWTRMIRFFEQIALKGIREKPTLSNNEEKKIGKDSSITKNKLTK
>NZ_LN824141.1|WP_045087936.1|1294543_1294798_+|DUF4911-domain-containing-protein
MPYDNSIPEFDIFIDIAEEDIHLLIYLIEAEAHIMNVRKRQKNGYFKIIVPAGFLDESLILLNSLKKSDIKLEVISVEPHDGII
>NZ_LN824141.1|WP_045087935.1|1293201_1294491_+|PhoH-family-protein
MVKNYILDTNVLIHDPNCIFKFEDNNLIIPFPVIEEIDKLKTRSDKVAKSARDVARILDSLRDGMPLQKGVKLQNGGTLKILAIEKNDPKYKMPSYLGESKDNFILYYALYLKEVDKNFKTIIVSKDLNLRIKADALGIESQDYLSDKIDIELLPDGYIIIDNPTKHLEIKDTYTYSELGLNEEPYPNTYLKYGEKLLRYNKKKQAFEKIQMTFNSVIFGITPRSAEQVFALDALLDPDIPFVTLVGIAGTGKTLLALAAGLYNILENKVYDRLLVSKPVIPMGKDIGYIPGGIEEKMRPWLQSIYDNLDFLFKGKGKKPDEYLTKRDLLEIEVLSYIRGRTIPNQYMIVDEAQNLTPSEVKTILTRAGEGTKIVFTGDPYQIDNLYLDSSSNGLVYAASKFKGIDLAANITMKKGERSELATISAEIL
>NZ_LN824141.1|WP_045087943.1|1306428_1307178_+|DeoR/GlpR-transcriptional-regulator
MNKIMRQDKILEILQNRNSVNLDDLAKELKVSMVTIRRDVAELYERGLIEKFYGGIRKRNHFTEALFFERVKINQDKKEKIAELALRFISRDSTVFLDASSTCYLLARKLAERYEFLNIVTNNLYTALALAENTTHNIIVIGGTLDNKNGVTMGVIPENMMKEIRVEKAFFSCSAFSVDEGAFENLPQSASIKKIVGENCDEIYMLVDSSKFDKRSIMKTFSIEEIDKFVSDSFDEKIYKVFKDNFIYQ
>NZ_LN824141.1|WP_045087944.1|1307225_1308683_-|alpha-glucosidase/alpha-galactosidase
MPGVKISIIGAGSASFSLRLVGDLCKTKGLSGSLVSLMDIDKNRLNAVHTLAKKYAEELGSDLRFETTMNLEDSIKDASFVVNTALVGGHSYFEKVRQISEKYGYYRGIDAQEFNMVSDYYTISNFNQIKFMFDVAKLIEKLSPKAWLLQAANPVFELTTLISRVVPINMVGICHGHHGVDYIIEKMGLEKQKVDWQVAGVNHGIWLTRFKYEGKDAHHLIDELLEKELKNFKPTNPFDDQISLVAKDMYEFYGRMPIGDTVRNGSWKYHYNLETKKKWFGEPWGGVDSELGWKWYQERQAERAIITQQVAKYFKENPKAKLLSKETQQAIISTAKDDLKKEYTKEVYELLDPEKKSGEQHILLANALLNDEKVDLVLNILNKGTIPGIADDVAVEIPVYADKNGIHPYKIDPDIPERIKKMYLMPRILRMEWALEAFLTGDRRVLEEFLIRDPRTRSYEQVVKVIDEILALPENEEMRKHYSKK
>NZ_LN824141.1|WP_045087945.1|1313650_1314628_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MKALYITEPHHIELIEKDDPEIRENESLLKILGCGVCGTDLKIYKGETLATYPIIPGHEIVGEIINSSKYEKGTKVTVDPNKPCGYCKYCREGKPHLCDDLKAVGVNRNGGFAELLSVPNDLIYPLNENIDVKSALFAEPLSCIIHGIDLSNFSFTDDIAIIGGGAIGLIFAMLFNKFSVGIKLIFEISQDKITYIEKEFGFDIVHPQEYKKFKEFDLVIECSGSISGLELAYTLVKKGGKIIVFGVTPKGLTTTELEPFQIYSEEITLTGSYINPFTMQKAVKIINSKEFPFHKLLTDQASLQDINEYISGNKHPFLKAAYINK
>NZ_LN824141.1|WP_045087946.1|1314846_1316601_+|M3-family-oligoendopeptidase
MPIWDLTFFYKSPHDDKIKKDLEEGLNKAEQLRQKYHNKLSDPTLSSSQLKNFFVECEELFNKVWLTIQYASLNYAADTSNELYQKLAAICDDYESKIEMELSFWKPAILKQSDSKLKEFMESEELKDYKHVIENLLKSKKHVLSADAEKVLAAMYNSSRGGFQDLYQRLTSSYIFEIEIDGMIKTLTEPQMRSLRMHPDKDVRRRAMKILFDRYEKDQLVIEKTYNSIVKNYDTEASLRNFQEPISMRNLENEVDDKIVSTVIEVTTENTPLVHQYYNWKTKKMGIPLTLADIYAPLEKEQKEYSFEEAKNLVLEAYYHFDEEFGEIVDSFFTEKRIDSDIRKGKRGGAFTSYVVPNKKPFILMNFTGNMNDVMTLAHELGHGIHGVLASKQNVWNYHPPLVMAEVASVFGEMLVMDAVLPTLSEEERIAFIASKIEDTFATMFRQNMFARFEISSHKMISDNGSATWKELSNLYSQELKIMFGDSVIIPDEYHFEWSSISHMFHTPFYVYAYNFANLLVLALYEQYKQEGRSFVPKYKELLSSGANDSPDRLLKKVGIDINQKAFWKRGFEFIEREFLNKLD
>NZ_LN824141.1|WP_045087947.1|1316635_1317208_+|MBL-fold-metallo-hydrolase
MEIQKLVTSKGFQTNTYIINNEIIIDPGEGVGQFVSKDHEFIVLLTHGHFDHILGLSEIKVKELYVHPLDVNLLQNPKENLSFLLDKPFSWLKPWKNISENYRVIHTPGHTPGSCVIHIGDYLFTGDTLFFDSIGRTDLPNSSTDDMKNSLKILKQYFKSLPRNTFIAPGHMRTGTLEEVLENNPFLKEI
>NZ_LN824141.1|WP_084217212.1|1317572_1318742_+|sulfate-adenylyltransferase
MIEPHGGKLINRIVSEQEKDEWLKKSKELKSITVSYYDLSELENISTGLFSPLEGFMNKNDYDSVLNNMRLESGIVWSIPIVLSVKKQIADNLKVGEDIIIKSEEDGKTYAVLHLEDKFIRRKEEEAKKVYKTNEDKHPGVKFLYEQGEVALGGKITLLSRINHENFQEYRFDPVETRRIFSENGWKTIVAFQTRNPIHRAHEYLQKTALEIVDGLFINPLVGKTQEEDIPSDVRMHSYEVILDKYYPKNRVCLGVFPVNMRYAGPREAVFHAICRKNYGCSHIIIGRDHAGVGNYYGTYEAQEIFDQFKPEEIGIIPLKFEHAFYCKRCENMATSKTCPHGNEEHVFLSGTKVREMLSRGEKPPKEFTRPEVAEILMKFYQEKNNVEK
>NZ_LN824141.1|WP_171820596.1|1318758_1319628_+|hypothetical-protein
MILLLAINIFSYEIFFSGEELVRFLKEKILESNSLRLVSFSLDDTISNELLKVKSEIFLEYEGGYSGVLFLPIIYDKNIEGYLHEKFIVFDDNSVLFGTGNFTKSGLLTDFNVFIYTDDQKIVNVFLQEISNFKKGKYANDKSKIKVNLKKTDLNNVKIVTGPSDQITKEILNNIKKAKKSIKVFSYSFTDPYFVEALERMSSKGVDVQILSDDWNKLYDSPIKYLSNINVRYNDKIHAKTIIIDEKKSIIGSYNLTYRAREKNDEIIMIIDNESVANILTKKFDLLFQ
>NZ_LN824141.1|WP_045087950.1|1319772_1321500_+|NAD+-synthase
MEIRVAIAQMNSIVGDYYGNINKIKNNIRQACNDHADIIVFPELCLNGYPPEDLLLKTQFLNDSLKSIKDVKDFTEDKDIVIILGAVECDEYYNIYNSAQIIFKGNLLGKYKKRLLSSFSFFDERRYFNPSDILTLIELNGSKIGITIGNEICFPNSSLYSAVNNETDLILNLSASVFYKNKINSIHNILKARALELSSWVVYCNMVGGQDELVFDGGSMVIDPYGVIEMNAPLFEEGIYFIDIDAEEAKRAKLKNSKSSSLCQVKNNVEIININKIVSKKRKIKSITSKIPDENELLYSAIKLGLRDYLVKNGFSSVVLGLSGGVDSALVASIAADSIGNKNVLALIMPSEFTSKKSVEDAVELSLNLGIEYKIISISELYNTYLDTLKESFKGKTFDETEENLQARIRGNIIMAFSNKFGHLALVCGNKSEVATGYSTLYGDTAGGFAPIKDLYKTELYKVAKKYNEIHNKEIITKSILEKPPSAELRPNQKDEDKLPPYDILDKILFNYIERGKSYNELLEMGLNEEIVKNVINMVEKSEWKRRQLPAGIKLSELSFGKERKMPITKKYRFW
>NZ_LN824141.1|WP_045087951.1|1321549_1322323_+|hypothetical-protein
MKENKIEEILEQKLKETEKEEFGSWKNLLIIIIAMGLIYAVALLLWNMYSGYLENRHYYPYIKLKDTGYEKISKYPYNAKDTNIIINKTDYSNIYSVKTPFGAFSVQTFDNRFFFFENSETAVISYPSYDFRGLEYSVINKNGDFFRFVIVPSEEVIPDIFDFVENLSEIKILDSSELIKYEFLSENDEAYIVKTKYEELDLPKNLIESVGESEKFVYLVSKKYGLFNKIYYIEKDTSKLRELIIISETSFPIRTIE
>NZ_LN824141.1|WP_045087952.1|1322353_1324921_+|alpha-glucan-family-phosphorylase
MNFINKITVVPKLPEEIVGLKELSENMWWTWNYKAQQLFKKIDENLWNSVQRNPVVFLKKVEQKKLNSAVASNDFMSLYQEVMNNFHNYMNEDQKTWFKKTHSHTNYGEIAYFCMEYGMHESFPMYSGGLGILAGDHIKSASDLGIPLVAVGLLYRKGYFIQKINSEGWQESIYLDYDFSDFPIHPAVDQNGEEVYVSITLPERTVYIKVWEIKVGRVKLYLLDTDLLQNDPEDRKITSTLYGGDLEMRIKQEMVIGIAGVRALRKLGYKPSVWHMNEGHSAFLGLERIREFVQEYNLSFSEAVQAVRAGNIFTTHTPVPAGNDLFPIYLIDKYFGDYWPQLKATRQDFLDLGLEKQKSGESLFSMAILALKLSGRANGVSKLHGTVSKKLWNHVWPGIEWVEVPITYVTNGVHINSWLNPLLQESFKKYLGEDWMLKIDDPDLWTKINDIPNEELWKIHMLLKKELIKFVRESIKAQRMRHGETVEQLEEVENIGNEEALTIGFARRFATYKRADLIFKDPERLKKILNNPERPVELIFAGKAHPADKPGQELMKKIYEYSRDPEFKNKIIILENYDMNMARFLVSGVDIWLNNPRRPLEASGTSGQKAGMNGAINFSVLDGWWNEGYNGKNGWTIGDDRDYENHELQDKIDSVSIYNQLEKQIVPLYYERGNGNIPQEWIEKMKESLKSVTSFFNTYRMLKEYTQKLYMPASEQHRNFCSNDFKVVKDFTKWLNLLKENWNSIKIHVMFDYEKSQIINAEEEIEIQAEIYMPGIGPDSIIAEIVVASLQNGKIEQLKTYDMKLVKEIQKDAYLYTGKIKIEDRGEYGINVRVTPNHPYMPHKNYLMGLVKYPE

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Crispr_ID: NZ_LN824141_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_15

1317329-1317447

Orphan

Consensus_repeat	Method
GATGTTTTTGATTTATATAGGGTCTAGGGCGAAGCCCCCCTTCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_15

>merge|NZ_LN824141|15|1317329-1317447|CRISPRCasFinder
GATGTTTTTGATTTATATAGGGTCTAGGGCGAAGCCCCCCTTCTACTTTGAGAAAAGTTTCAGATATTAAAAAATGATGTTTTTGATTTATATAGGGTCTAGGGCGAAGCCCCCCTTCT

>NZ_LN824141|15|14|1317329-1317447|CRISPRCasFinder
GATGTTTTTGATTTATATAGGGTCTAGGGCGAAGCCCCCCTTCT	ACTTTGAGAAAAGTTTCAGATATTAAAAAAT
GATGTTTTTGATTTATATAGGGTCTAGGGCGAAGCCCCCCTTCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045088653.1\|1301578_1302214_-\|class-II-aldolase/adducin-family-protein	unknown	unknown	gnl\|CDD\|376358
NZ_LN824141.1\|WP_045087954.1\|1328167_1328599_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087939.1\|1297817_1300142_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_LN824141.1\|WP_045087941.1\|1300784_1301495_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087943.1\|1306428_1307178_+\|DeoR/GlpR-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224268
NZ_LN824141.1\|WP_171820597.1\|1329207_1330044_+\|50S-ribosomal-protein-L11-methyltransferase	unknown	unknown	gnl\|CDD\|225173
NZ_LN824141.1\|WP_045087951.1\|1321549_1322323_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045087952.1\|1322353_1324921_+\|alpha-glucan-family-phosphorylase	unknown	unknown	gnl\|CDD\|340852
NZ_LN824141.1\|WP_052670406.1\|1330010_1330544_+\|DUF501-domain-containing-protein	unknown	unknown	gnl\|CDD\|377352
NZ_LN824141.1\|WP_045087942.1\|1302778_1305892_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|153237
NZ_LN824141.1\|WP_045087945.1\|1313650_1314628_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176196
NZ_LN824141.1\|WP_045087953.1\|1325028_1327542_+\|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase	unknown	unknown	gnl\|CDD\|236330
NZ_LN824141.1\|WP_045087940.1\|1300268_1300757_-\|peroxiredoxin	unknown	unknown	gnl\|CDD\|224146
NZ_LN824141.1\|WP_045087947.1\|1316635_1317208_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293792
NZ_LN824141.1\|WP_045087946.1\|1314846_1316601_+\|M3-family-oligoendopeptidase	unknown	unknown	gnl\|CDD\|341073
NZ_LN824141.1\|WP_045087955.1\|1328654_1329197_+\|folate-family-ECF-transporter-S-component	unknown	unknown	gnl\|CDD\|275311
NZ_LN824141.1\|WP_045087944.1\|1307225_1308683_-\|alpha-glucosidase/alpha-galactosidase	unknown	unknown	gnl\|CDD\|133433
NZ_LN824141.1\|WP_084217212.1\|1317572_1318742_+\|sulfate-adenylyltransferase	unknown	unknown	gnl\|CDD\|235227
NZ_LN824141.1\|WP_045087950.1\|1319772_1321500_+\|NAD+-synthase	unknown	unknown	gnl\|CDD\|237577
NZ_LN824141.1\|WP_171820596.1\|1318758_1319628_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|197215

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045088653.1\|1301578_1302214_-\|class-II-aldolase/adducin-family-protein	gnl\|CDD\|376358	pfam00596, Aldolase_II, Class II Aldolase and Adducin N-terminal domain. This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.	1.65265e-64
NZ_LN824141.1\|WP_045087939.1\|1297817_1300142_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	7.99603e-48
NZ_LN824141.1\|WP_045087943.1\|1306428_1307178_+\|DeoR/GlpR-transcriptional-regulator	gnl\|CDD\|224268	COG1349, GlpR, Transcriptional regulators of sugar metabolism [Transcription / Carbohydrate transport and metabolism].	2.54217e-67
NZ_LN824141.1\|WP_171820597.1\|1329207_1330044_+\|50S-ribosomal-protein-L11-methyltransferase	gnl\|CDD\|225173	COG2264, PrmA, Ribosomal protein L11 methylase [Translation, ribosomal structure and biogenesis].	6.20371e-55
NZ_LN824141.1\|WP_045087952.1\|1322353_1324921_+\|alpha-glucan-family-phosphorylase	gnl\|CDD\|340852	cd04299, GT35_Glycogen_Phosphorylase-like, proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.	0
NZ_LN824141.1\|WP_052670406.1\|1330010_1330544_+\|DUF501-domain-containing-protein	gnl\|CDD\|377352	pfam04417, DUF501, Protein of unknown function (DUF501). Family of uncharacterized bacterial proteins.	1.22205e-48
NZ_LN824141.1\|WP_045087942.1\|1302778_1305892_-\|hypothetical-protein	gnl\|CDD\|153237	cd03143, A4_beta-galactosidase_middle_domain, A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.	0.00245979
NZ_LN824141.1\|WP_045087945.1\|1313650_1314628_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176196	cd08234, threonine_DH_like, L-threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.	5.35975e-111
NZ_LN824141.1\|WP_045087953.1\|1325028_1327542_+\|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase	gnl\|CDD\|236330	PRK08665, PRK08665, vitamin B12-dependent ribonucleotide reductase.	0
NZ_LN824141.1\|WP_045087940.1\|1300268_1300757_-\|peroxiredoxin	gnl\|CDD\|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	1.27855e-67
NZ_LN824141.1\|WP_045087947.1\|1316635_1317208_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293792	cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.	3.94868e-49
NZ_LN824141.1\|WP_045087946.1\|1314846_1316601_+\|M3-family-oligoendopeptidase	gnl\|CDD\|341073	cd09610, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid.	0
NZ_LN824141.1\|WP_045087955.1\|1328654_1329197_+\|folate-family-ECF-transporter-S-component	gnl\|CDD\|275311	TIGR04518, conserved_hypothetical_protein, ECF transporter S component, folate family. Members of this model are the multiple membrane-spanning S (specificity) component of ECF (energy coupling factor) type uptake transporters. All seed members were found in the vicinity of the bifunctional enzyme folC, involved in making active cofactor from imported folate. However, some species have multiple members of this family, suggesting some diversity of function. [Transport and binding proteins, Unknown substrate].	1.07994e-24
NZ_LN824141.1\|WP_045087944.1\|1307225_1308683_-\|alpha-glucosidase/alpha-galactosidase	gnl\|CDD\|133433	cd05297, GH4_alpha_glucosidase_galactosidase, Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.	0
NZ_LN824141.1\|WP_171820596.1\|1318758_1319628_+\|hypothetical-protein	gnl\|CDD\|197215	cd09116, PLDc_Nuc_like, Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins. Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.	1.00384e-26
NZ_LN824141.1\|WP_045087950.1\|1319772_1321500_+\|NAD+-synthase	gnl\|CDD\|237577	PRK13981, PRK13981, NAD synthetase; Provisional.	0
NZ_LN824141.1\|WP_084217212.1\|1317572_1318742_+\|sulfate-adenylyltransferase	gnl\|CDD\|235227	PRK04149, sat, sulfate adenylyltransferase; Reviewed.	0

>NZ_LN824141.1|WP_045087947.1|1316635_1317208_+|MBL-fold-metallo-hydrolase
MEIQKLVTSKGFQTNTYIINNEIIIDPGEGVGQFVSKDHEFIVLLTHGHFDHILGLSEIKVKELYVHPLDVNLLQNPKENLSFLLDKPFSWLKPWKNISENYRVIHTPGHTPGSCVIHIGDYLFTGDTLFFDSIGRTDLPNSSTDDMKNSLKILKQYFKSLPRNTFIAPGHMRTGTLEEVLENNPFLKEI
>NZ_LN824141.1|WP_045087946.1|1314846_1316601_+|M3-family-oligoendopeptidase
MPIWDLTFFYKSPHDDKIKKDLEEGLNKAEQLRQKYHNKLSDPTLSSSQLKNFFVECEELFNKVWLTIQYASLNYAADTSNELYQKLAAICDDYESKIEMELSFWKPAILKQSDSKLKEFMESEELKDYKHVIENLLKSKKHVLSADAEKVLAAMYNSSRGGFQDLYQRLTSSYIFEIEIDGMIKTLTEPQMRSLRMHPDKDVRRRAMKILFDRYEKDQLVIEKTYNSIVKNYDTEASLRNFQEPISMRNLENEVDDKIVSTVIEVTTENTPLVHQYYNWKTKKMGIPLTLADIYAPLEKEQKEYSFEEAKNLVLEAYYHFDEEFGEIVDSFFTEKRIDSDIRKGKRGGAFTSYVVPNKKPFILMNFTGNMNDVMTLAHELGHGIHGVLASKQNVWNYHPPLVMAEVASVFGEMLVMDAVLPTLSEEERIAFIASKIEDTFATMFRQNMFARFEISSHKMISDNGSATWKELSNLYSQELKIMFGDSVIIPDEYHFEWSSISHMFHTPFYVYAYNFANLLVLALYEQYKQEGRSFVPKYKELLSSGANDSPDRLLKKVGIDINQKAFWKRGFEFIEREFLNKLD
>NZ_LN824141.1|WP_045087945.1|1313650_1314628_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MKALYITEPHHIELIEKDDPEIRENESLLKILGCGVCGTDLKIYKGETLATYPIIPGHEIVGEIINSSKYEKGTKVTVDPNKPCGYCKYCREGKPHLCDDLKAVGVNRNGGFAELLSVPNDLIYPLNENIDVKSALFAEPLSCIIHGIDLSNFSFTDDIAIIGGGAIGLIFAMLFNKFSVGIKLIFEISQDKITYIEKEFGFDIVHPQEYKKFKEFDLVIECSGSISGLELAYTLVKKGGKIIVFGVTPKGLTTTELEPFQIYSEEITLTGSYINPFTMQKAVKIINSKEFPFHKLLTDQASLQDINEYISGNKHPFLKAAYINK
>NZ_LN824141.1|WP_045087944.1|1307225_1308683_-|alpha-glucosidase/alpha-galactosidase
MPGVKISIIGAGSASFSLRLVGDLCKTKGLSGSLVSLMDIDKNRLNAVHTLAKKYAEELGSDLRFETTMNLEDSIKDASFVVNTALVGGHSYFEKVRQISEKYGYYRGIDAQEFNMVSDYYTISNFNQIKFMFDVAKLIEKLSPKAWLLQAANPVFELTTLISRVVPINMVGICHGHHGVDYIIEKMGLEKQKVDWQVAGVNHGIWLTRFKYEGKDAHHLIDELLEKELKNFKPTNPFDDQISLVAKDMYEFYGRMPIGDTVRNGSWKYHYNLETKKKWFGEPWGGVDSELGWKWYQERQAERAIITQQVAKYFKENPKAKLLSKETQQAIISTAKDDLKKEYTKEVYELLDPEKKSGEQHILLANALLNDEKVDLVLNILNKGTIPGIADDVAVEIPVYADKNGIHPYKIDPDIPERIKKMYLMPRILRMEWALEAFLTGDRRVLEEFLIRDPRTRSYEQVVKVIDEILALPENEEMRKHYSKK
>NZ_LN824141.1|WP_045087943.1|1306428_1307178_+|DeoR/GlpR-transcriptional-regulator
MNKIMRQDKILEILQNRNSVNLDDLAKELKVSMVTIRRDVAELYERGLIEKFYGGIRKRNHFTEALFFERVKINQDKKEKIAELALRFISRDSTVFLDASSTCYLLARKLAERYEFLNIVTNNLYTALALAENTTHNIIVIGGTLDNKNGVTMGVIPENMMKEIRVEKAFFSCSAFSVDEGAFENLPQSASIKKIVGENCDEIYMLVDSSKFDKRSIMKTFSIEEIDKFVSDSFDEKIYKVFKDNFIYQ
>NZ_LN824141.1|WP_045087942.1|1302778_1305892_-|hypothetical-protein
MLYPKNKRDISQELFKNPTSEYRGAPFWAWNSSLNKEDLLEQIDNFKIMGIGGFHIHSRTGLAVDYLSDEFMSLVKLCNEKAKEEDMLCWLYDEDRWPSGFAGGYVTKDDQYRQRFLVFTPIYYNDSEIVVEHLRANKRVEQGKKRKLLARYEIVLENGYLTRYKRLKDNEKSKDNSKIWYAYLEIAADDPWFNNQAYVDTLNKRAIETFVEITHEKYFQELGEDFGKSIPAIFTDEPQFTRKSYLQFSEDESEIILPFTDDFEESYFNSYNQSILDHLPELIWELPNDQISLVRYRYHDHLTERFTQAFADTIGDWCENHGILLTGHLMEEPTLESQTACVGEAMRSYRSFQLPGIDMLCDRREFTTAKQAQSAAHQYAREGVLSELYGVTNWDFDFRGYKLAGDWQAALGVTVRVHHLTWVSMQGEAKRDYPPSIGYQIPWYKEYSLIEDHFARLNTVLTRGTPEVKVGVIHPIESYWLYWGPQDKTAIKREELEDNFKNITEWLLFGLIDFDYIAESLLPSLSKIQENKTFQVGAMNYDVIIVPGCETLRSTTLDRLEAFQKTGGKIIFLGELPRFVDAVESNKAKKLAEKSTVIPFSKGKLMQELNQYRDIEIIKQDGSPSDNLFYQMRKDANNKWLFISHVYKMKNPDIAEKERIKIIIKGECNPVIYDTINGSIKETEAKIINGETIVDYEFYPHDSLLLKLESSNFTESEKKKENLSIVEKETKEIRLEDPVNYSLSEPNVLLLDMAEYSFDGRGWQQVDEILRIDNKFRELLNYPLRMNKLAQPWTIKKEEPFEHVLKLKFSIESDIELKNPCLALENVENTKIFVNKKHVEPEVVGWFVDKSIKKVKIPNLRLGISEIILEIPFNSKTNVEWCYLLGDFGVKVSGKHKKIVEPQKALTFGNWVNQGLPFYAGNVTYHCTIECNEGNLTIEVPQFRNPLLSISVDGQEKGKIAFAPYTLELGKVNKGKHDIDITAYGNRINAFGTVHNCDDTYFWFGPDAWRTTGSRWSYEYRLKPMGILVSPKIYLKQ
>NZ_LN824141.1|WP_045088653.1|1301578_1302214_-|class-II-aldolase/adducin-family-protein
MNEKQRLINICLSMEKNGLVKGTWGNASIKDGDKIFITPSGYPYDKMNEDDVMVIDIDGNILEGFRKPSSEYQLHLEIYKNRKDVNAIIHSHPIYSSVVSLVKEYIPPLIEDGVMICGERINVAKYGEPGTKDLALKAVEALEMNYAVILKNHGLVTIGENEIEALTTSIIAEKTAQIYIEALKIGEISELSPQDAKKLREKYLSSYRQKG
>NZ_LN824141.1|WP_045087941.1|1300784_1301495_-|hypothetical-protein
MKNLSRTLVSLIVIIVASLSFSQGFSGGEFGGLGGGDFGAKWMDLGELNKTLNDNNLPTFSNPAFYTGGGGYALIGKTLYGGEGYGITLSEKADDYTVELDVGYGLFDIGYLIYAKQSLRVYGMGGVGFGGMTFKVSEFPDSKKFEDLLTDYHENLFISGPIPIFKIGFGADYILTFKASSSTGGFAIGISAGYVFAPFDPIGGWKLSDTSVSNVPKFGPTGPYITIKIGGGGFAF
>NZ_LN824141.1|WP_045087940.1|1300268_1300757_-|peroxiredoxin
MKYFRLEEGDRLPTFSLKDANGELININDFLGKWLVIYFYPKDGSKGCLLEALDFSNKLSEFKKYNCEIIGISPDSEESHKKFIEKNDLKILLLSDPDHVVLEKLGVWQLKKMYGREHWGVIRTTILVDPDGFVRKIWENVKVKDHASNVLHSLIELIRSNK
>NZ_LN824141.1|WP_045087939.1|1297817_1300142_-|methyl-accepting-chemotaxis-protein
MKPRDRENMNIKWFNKFSNKISIILLVLGLLPCIFLVIYITLSIQNKTLENEANISYVVEDLNNEYLKQINEYNDAVQEQLNSYNNYLKSQITLIEEEVSKQMKEMYTQSFDNSLKTLGTIFSNFLDSEKRTLEKTGKLIASDTILKEKTASKSISLMERYSILEPFVTTQEYNGMQLWILYPPNTAGTGVEVTSKNQTYKLQKKAETYSKGYEYTKQLNLDDFLKEIFTNILEIGYLTPVVKTKSFNSIPYFIGVFPIVDPIATNTVNGFLVIIEEFENQKLLEISKLLDASVTLYDKNYNFIYSNFPKDEIYIDENKLNAKFVTEEILNKPKRSYYFQTEEFDGLYIQISKDYQDFDASINIPLETSFDLPTLTAKEVTFEIDLGLNKIIRNTIIILIILILIIIFVSYLLSRRFGTQIRNFTKNLQRLSEGDLTVEISHVTQIKDEFDQMNKELNKTISSLKMMIKNLLEDSEQIIVSSKNVDEKSKLLKNTQQNLNSLLEQIKDLGDTVSKISSRFSEKIDELISNSRKVKNATENISKISNETITFANEGKKFVGSVLNVSNSVEELVKNSSVSVDNFSKEVEKINEFVKNISDIAKQTNLLALNASIEAARAGEAGKGFAVVAEEIRNLSEETSMTAMGISDKMINILNSLKTLAQGIQETNKKTNDLGNTIKVFEEGFNNLENSSKSLTSVVNDLTQSVREQNQTIEEFKNEIQGIESQTNTTISKLNIVEEGIKADSDAINSLLEQVEILNKIAHNLKEETSRFKI
>NZ_LN824141.1|WP_084217212.1|1317572_1318742_+|sulfate-adenylyltransferase
MIEPHGGKLINRIVSEQEKDEWLKKSKELKSITVSYYDLSELENISTGLFSPLEGFMNKNDYDSVLNNMRLESGIVWSIPIVLSVKKQIADNLKVGEDIIIKSEEDGKTYAVLHLEDKFIRRKEEEAKKVYKTNEDKHPGVKFLYEQGEVALGGKITLLSRINHENFQEYRFDPVETRRIFSENGWKTIVAFQTRNPIHRAHEYLQKTALEIVDGLFINPLVGKTQEEDIPSDVRMHSYEVILDKYYPKNRVCLGVFPVNMRYAGPREAVFHAICRKNYGCSHIIIGRDHAGVGNYYGTYEAQEIFDQFKPEEIGIIPLKFEHAFYCKRCENMATSKTCPHGNEEHVFLSGTKVREMLSRGEKPPKEFTRPEVAEILMKFYQEKNNVEK
>NZ_LN824141.1|WP_171820596.1|1318758_1319628_+|hypothetical-protein
MILLLAINIFSYEIFFSGEELVRFLKEKILESNSLRLVSFSLDDTISNELLKVKSEIFLEYEGGYSGVLFLPIIYDKNIEGYLHEKFIVFDDNSVLFGTGNFTKSGLLTDFNVFIYTDDQKIVNVFLQEISNFKKGKYANDKSKIKVNLKKTDLNNVKIVTGPSDQITKEILNNIKKAKKSIKVFSYSFTDPYFVEALERMSSKGVDVQILSDDWNKLYDSPIKYLSNINVRYNDKIHAKTIIIDEKKSIIGSYNLTYRAREKNDEIIMIIDNESVANILTKKFDLLFQ
>NZ_LN824141.1|WP_045087950.1|1319772_1321500_+|NAD+-synthase
MEIRVAIAQMNSIVGDYYGNINKIKNNIRQACNDHADIIVFPELCLNGYPPEDLLLKTQFLNDSLKSIKDVKDFTEDKDIVIILGAVECDEYYNIYNSAQIIFKGNLLGKYKKRLLSSFSFFDERRYFNPSDILTLIELNGSKIGITIGNEICFPNSSLYSAVNNETDLILNLSASVFYKNKINSIHNILKARALELSSWVVYCNMVGGQDELVFDGGSMVIDPYGVIEMNAPLFEEGIYFIDIDAEEAKRAKLKNSKSSSLCQVKNNVEIININKIVSKKRKIKSITSKIPDENELLYSAIKLGLRDYLVKNGFSSVVLGLSGGVDSALVASIAADSIGNKNVLALIMPSEFTSKKSVEDAVELSLNLGIEYKIISISELYNTYLDTLKESFKGKTFDETEENLQARIRGNIIMAFSNKFGHLALVCGNKSEVATGYSTLYGDTAGGFAPIKDLYKTELYKVAKKYNEIHNKEIITKSILEKPPSAELRPNQKDEDKLPPYDILDKILFNYIERGKSYNELLEMGLNEEIVKNVINMVEKSEWKRRQLPAGIKLSELSFGKERKMPITKKYRFW
>NZ_LN824141.1|WP_045087951.1|1321549_1322323_+|hypothetical-protein
MKENKIEEILEQKLKETEKEEFGSWKNLLIIIIAMGLIYAVALLLWNMYSGYLENRHYYPYIKLKDTGYEKISKYPYNAKDTNIIINKTDYSNIYSVKTPFGAFSVQTFDNRFFFFENSETAVISYPSYDFRGLEYSVINKNGDFFRFVIVPSEEVIPDIFDFVENLSEIKILDSSELIKYEFLSENDEAYIVKTKYEELDLPKNLIESVGESEKFVYLVSKKYGLFNKIYYIEKDTSKLRELIIISETSFPIRTIE
>NZ_LN824141.1|WP_045087952.1|1322353_1324921_+|alpha-glucan-family-phosphorylase
MNFINKITVVPKLPEEIVGLKELSENMWWTWNYKAQQLFKKIDENLWNSVQRNPVVFLKKVEQKKLNSAVASNDFMSLYQEVMNNFHNYMNEDQKTWFKKTHSHTNYGEIAYFCMEYGMHESFPMYSGGLGILAGDHIKSASDLGIPLVAVGLLYRKGYFIQKINSEGWQESIYLDYDFSDFPIHPAVDQNGEEVYVSITLPERTVYIKVWEIKVGRVKLYLLDTDLLQNDPEDRKITSTLYGGDLEMRIKQEMVIGIAGVRALRKLGYKPSVWHMNEGHSAFLGLERIREFVQEYNLSFSEAVQAVRAGNIFTTHTPVPAGNDLFPIYLIDKYFGDYWPQLKATRQDFLDLGLEKQKSGESLFSMAILALKLSGRANGVSKLHGTVSKKLWNHVWPGIEWVEVPITYVTNGVHINSWLNPLLQESFKKYLGEDWMLKIDDPDLWTKINDIPNEELWKIHMLLKKELIKFVRESIKAQRMRHGETVEQLEEVENIGNEEALTIGFARRFATYKRADLIFKDPERLKKILNNPERPVELIFAGKAHPADKPGQELMKKIYEYSRDPEFKNKIIILENYDMNMARFLVSGVDIWLNNPRRPLEASGTSGQKAGMNGAINFSVLDGWWNEGYNGKNGWTIGDDRDYENHELQDKIDSVSIYNQLEKQIVPLYYERGNGNIPQEWIEKMKESLKSVTSFFNTYRMLKEYTQKLYMPASEQHRNFCSNDFKVVKDFTKWLNLLKENWNSIKIHVMFDYEKSQIINAEEEIEIQAEIYMPGIGPDSIIAEIVVASLQNGKIEQLKTYDMKLVKEIQKDAYLYTGKIKIEDRGEYGINVRVTPNHPYMPHKNYLMGLVKYPE
>NZ_LN824141.1|WP_045087953.1|1325028_1327542_+|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase
MRVIDDWLNKEISQNAMAILQDRYFLKDADGNYIENTWDEVAKRVARHVASAEINFSQDVKEIQKAETIFYKLIRSRIFIPNSPTLFNAGKTIDKQFFNKAIEDMTIDDYKQIFNLRTKHNMLSACFVVPMEDSLASIFDAVKNAALIMKYGGGVGYDFSVLRPKGSSIAGTGGKSSGPVSFMHVFNVAASTIEQGGSRRAAQMAVLRYDHPDVFEFINSKKDNKGNNVLNYFNISINIDNPSTFKRLIENDEELLLKHPDSKIQKKVKARELIDKMAENAWKTGDPGVLFLGRHNEYYAMSEYTPVTATNPCGEEPLPPFGSCNLGSLDISKLVEKIDLGNPTSSTGEEFKEIVYWAVRFLDDVVEANVFPLKEIEEITRRQRFVGLGIMGLADALYKKEIPYNSEDGRKFMAKVTAQLAYYSHLASTGLAKERGNFPDFEKSKYPNGFIPFAMLDDQIDKDIKIWNDKIREHFYGEAKQYKRNVQTNTVAPTGSISNLADTSSGIEPNFLLSYIRYMTNKEGERVPLTYINPVLIEKVGALITDEIKEEIVKKGSIQHIKSIPDDIKKIFVTAVDISPEDHLLAQHVIQSYLDASCSKTINMPNTATIDDVKSMYLKALDLNVKGLTIYRDGSLETQVLTTTSENDKKNVRQNVTFFVLDEKHKLRARPRKETLRSVTRKFRYNGNTVYVTVSFDDLGEAIEIFLSDGTETAEVIGRLSSIALRAGVSTEEIIEQLKKVKGQYCKGLAEEITKALNDFKELWGKSIGEYELIRTGVPKTKEEVEKFVFANDLKYEDGYYIDLEGNRYCPNCLSKNSLINESGCVSCTTCGWSKCS
>NZ_LN824141.1|WP_045087954.1|1328167_1328599_+|hypothetical-protein
MWINFTEESKTAFLSEINGYDEELSKEMNDFLSTYDIDNQIVPIHFPLEFESDEDIDNFLLFIDNIKTIVEIKAYSILSEISLFDEESSEVDDGFPALFSEEKNGECYLTVFDWNIQELDDYSNKYDKNDETITPLRLSIFSD
>NZ_LN824141.1|WP_045087955.1|1328654_1329197_+|folate-family-ECF-transporter-S-component
MPARKSYKLILNSLFIVLSMILTRVLSIRIPIGNVEVIRFGFGTIPVYLSSYLFGPLSGMLVGSFEDLLGYWINPVGPFLPQFTLTKALYGLLPGLVFKYGFKKKINYWSLAFSCVAGEIVGITLTPFFIHQAFGVPYVVLMPPRIGGFVALFFLNPLIIQLILTRVPQLNRLIKENSDG
>NZ_LN824141.1|WP_171820597.1|1329207_1330044_+|50S-ribosomal-protein-L11-methyltransferase
MIYKLKDKEAESLIIEDLNMIDFSKFFIEEDAERSINLLKLYFNLKDEYEKEVLSRLAKYNLELVADQILEEKNWLDEWIKSVKVFEFIDGVWINPYLDKKVEKPGLVLNIVPGSAFGTGTHTTTKLAAKLLSEIGCEGKYVLDVGTGSGILAVYAKKMGARYVKAVDNDIFAVEKAQEAAKLNKVDIDIQKSDLLKDINTDIKYDILVSNIIAEVLIELIEDPKFHIILNNKANIVFSGIIKEKEDIMLTEAKKYGLELKKRMEDVGWVALWFQKVI
>NZ_LN824141.1|WP_052670406.1|1330010_1330544_+|DUF501-domain-containing-protein
MGCSLVSKSDLDIIYNQLNRKVDNILSITLRCKYNYPQVIQCYPLKDNKPFPTLYWVTCPYLVEVVSKLESESLIATLEKKVFENSELKEQLFQAHLEEIKKRVIILGDQLEQLPRNIKKKIEESGIGGTADFNKIKCLHMHLASFLSKEPNPIGQIVSNMISEKNCLDERCKSFIS

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Crispr_ID: NZ_LN824141_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_16

1736260-1736390

Unclear

Consensus_repeat	Method
AATTCAAAAACAGTAATTAATAATTACAACTTTTCGGTACTTGTACCA	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_LN824141_16

>merge|NZ_LN824141|16|1736260-1736390|CRISPRCasFinder
AATTCAAAAACAGTAATTAATAATTACAACTTTTCGGTACTTGTACCAGCGAGGGATGAGGGCTTTGCCCTAGACCCGCTATGAATTCAAAAACAGTAATTAATAATTACAACTTTACGGTACTTGTACCA

>NZ_LN824141|16|15|1736260-1736390|CRISPRCasFinder
AATTCAAAAACAGTAATTAATAATTACAACTTTTCGGTACTTGTACCA	GCGAGGGATGAGGGCTTTGCCCTAGACCCGCTATG
AATTCAAAAACAGTAATTAATAATTACAACTTTACGGTACTTGTACCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045088245.1\|1733279_1734146_+\|polyamine-aminopropyltransferase	unknown	unknown	gnl\|CDD\|234843
NZ_LN824141.1\|WP_045088255.1\|1743713_1744337_-\|chemotaxis-protein-CheC	unknown	unknown	gnl\|CDD\|381737
NZ_LN824141.1\|WP_045088242.1\|1728870_1729737_+\|polyamine-aminopropyltransferase	unknown	unknown	gnl\|CDD\|234843
NZ_LN824141.1\|WP_045088248.1\|1736576_1737932_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	unknown	unknown	gnl\|CDD\|235392
NZ_LN824141.1\|WP_045088243.1\|1730757_1731591_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|350159
NZ_LN824141.1\|WP_045088252.1\|1742198_1742504_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088241.1\|1728472_1728871_+\|S-adenosylmethionine-decarboxylase-proenzyme	unknown	unknown	gnl\|CDD\|235105
NZ_LN824141.1\|WP_045088257.1\|1745122_1745980_-\|P-loop-NTPase	unknown	unknown	gnl\|CDD\|349758
NZ_LN824141.1\|WP_045088254.1\|1743227_1743713_-\|chemotaxis-protein-CheD	unknown	unknown	gnl\|CDD\|184088
NZ_LN824141.1\|WP_045088256.1\|1744394_1745099_-\|PilZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|227868
NZ_LN824141.1\|WP_045088253.1\|1742524_1743214_-\|FliA/WhiG-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274153
NZ_LN824141.1\|WP_045088244.1\|1731603_1733025_-\|DNA-polymerase-III-subunit-gamma/tau	unknown	unknown	gnl\|CDD\|274111
NZ_LN824141.1\|WP_045088247.1\|1734893_1736069_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|378925
NZ_LN824141.1\|WP_045088251.1\|1741682_1742180_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088240.1\|1727921_1728458_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380339
NZ_LN824141.1\|WP_045088711.1\|1726665_1727661_-\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|237562
NZ_LN824141.1\|WP_045088246.1\|1734173_1734791_-\|YigZ-family-protein	unknown	unknown	gnl\|CDD\|376491
NZ_LN824141.1\|WP_045088250.1\|1741323_1741704_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_052670440.1\|1729772_1730789_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|213890
NZ_LN824141.1\|WP_045088249.1\|1737947_1740872_-\|transcription-repair-coupling-factor	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|224118

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045088245.1\|1733279_1734146_+\|polyamine-aminopropyltransferase	gnl\|CDD\|234843	PRK00811, PRK00811, polyamine aminopropyltransferase.	1.82251e-145
NZ_LN824141.1\|WP_045088255.1\|1743713_1744337_-\|chemotaxis-protein-CheC	gnl\|CDD\|381737	cd17909, CheC_ClassI, chemotaxis protein CheC, Class I. This subfamily contains Class I CheC proteins with phosphatase activity. The Class I cheC genes are generally found in firmicute and archaeal chemotaxis operons with cheD, usually translationally coupled. Class I CheCs interact with the CheD protein which is responsible for deamidation of certain glutamine residues to glutamates on the chemotaxis receptor proteins. This family contains two active sites with the consensus sequence ([DS]xxxExxNx(22)P), with four conserved residues thought to form the phosphatase active site. The C-terminal helix of CheC acts as a mimic of the natural enzymatic target of CheD, the alpha-helical receptors, and serves as the binding site for CheD. The CheC/CheD heterodimerization increases CheY-P phosphatase activity five-fold. Class I CheCs are involved in adaptation of the chemotaxis system.	2.11587e-64
NZ_LN824141.1\|WP_045088242.1\|1728870_1729737_+\|polyamine-aminopropyltransferase	gnl\|CDD\|234843	PRK00811, PRK00811, polyamine aminopropyltransferase.	6.46209e-147
NZ_LN824141.1\|WP_045088248.1\|1736576_1737932_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	gnl\|CDD\|235392	PRK05291, trmE, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE.	0
NZ_LN824141.1\|WP_045088243.1\|1730757_1731591_-\|hypothetical-protein	gnl\|CDD\|350159	cd09008, MTAN, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	1.92979e-14
NZ_LN824141.1\|WP_045088256.1\|1744394_1745099_-\|PilZ-domain-containing-protein	gnl\|CDD\|227868	COG5581, COG5581, c-di-GMP-binding protein [Signal transduction mechanisms].	4.13104e-18
NZ_LN824141.1\|WP_045088241.1\|1728472_1728871_+\|S-adenosylmethionine-decarboxylase-proenzyme	gnl\|CDD\|235105	PRK03124, PRK03124, S-adenosylmethionine decarboxylase proenzyme; Provisional.	3.0193e-62
NZ_LN824141.1\|WP_045088257.1\|1745122_1745980_-\|P-loop-NTPase	gnl\|CDD\|349758	cd02038, FlhG-like, MinD-like ATPase FlhG. FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.	9.26765e-66
NZ_LN824141.1\|WP_045088254.1\|1743227_1743713_-\|chemotaxis-protein-CheD	gnl\|CDD\|184088	PRK13495, PRK13495, chemoreceptor glutamine deamidase CheD; Provisional.	3.25207e-67
NZ_LN824141.1\|WP_045088253.1\|1742524_1743214_-\|FliA/WhiG-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274153	TIGR02479, RNA_polymerase_sigma_factor_WhiG, RNA polymerase sigma factor, FliA/WhiG family. Most members of this family are the flagellar operon sigma factor FliA, controlling transcription of bacterial flagellar genes by RNA polymerase. An exception is the sigma factor WhiG in the genus Streptomyces, involved in the production of sporulating aerial mycelium.	1.43153e-69
NZ_LN824141.1\|WP_045088244.1\|1731603_1733025_-\|DNA-polymerase-III-subunit-gamma/tau	gnl\|CDD\|274111	TIGR02397, DNA_polymerase_III_subunit_gamma, DNA polymerase III, subunit gamma and tau. This model represents the well-conserved first ~ 365 amino acids of the translation of the dnaX gene. The full-length product of the dnaX gene in the model bacterium E. coli is the DNA polymerase III tau subunit. A translational frameshift leads to early termination and a truncated protein subunit gamma, about 1/3 shorter than tau and present in roughly equal amounts. This frameshift mechanism is not necessarily universal for species with DNA polymerase III but appears conserved in the exterme thermophile Thermus thermophilis. [DNA metabolism, DNA replication, recombination, and repair].	2.55575e-151
NZ_LN824141.1\|WP_045088247.1\|1734893_1736069_-\|ABC-transporter-permease	gnl\|CDD\|378925	pfam12698, ABC2_membrane_3, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family pfam01061.	2.93463e-18
NZ_LN824141.1\|WP_045088240.1\|1727921_1728458_+\|cupin-domain-containing-protein	gnl\|CDD\|380339	cd02209, cupin_XRE_C, XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain. This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	6.5103e-22
NZ_LN824141.1\|WP_045088711.1\|1726665_1727661_-\|rod-shape-determining-protein	gnl\|CDD\|237562	PRK13927, PRK13927, rod shape-determining protein MreB; Provisional.	1.69698e-172
NZ_LN824141.1\|WP_045088246.1\|1734173_1734791_-\|YigZ-family-protein	gnl\|CDD\|376491	pfam01205, UPF0029, Uncharacterized protein family UPF0029.	1.10229e-50
NZ_LN824141.1\|WP_052670440.1\|1729772_1730789_-\|hypothetical-protein	gnl\|CDD\|213890	TIGR04070, photo_TT_lyase, spore photoproduct lyase. DNA damage to bacterial spores from ultraviolet light accumulates in the form of 5-thyminyl-5,6-dihydrothymine, spore photoproduct. The damage is repaired by spore photoproduct lyase, a member of the radical SAM family of enzymes. The score of this model is set to restrict itself to spore-forming members of the Firmicutes, but additional homologs scoring below the trusted cutoff tend to occur in radioresistant organisms (e.g. Kineococcus radiotolerans) and may be functionally equivalent. A related family in the Mycobacterium lineage is described by family TIGR03886, and may or may not be equivalent in function. [DNA metabolism, DNA replication, recombination, and repair, Cellular processes, Sporulation and germination].	0.000550979
NZ_LN824141.1\|WP_045088249.1\|1737947_1740872_-\|transcription-repair-coupling-factor	gnl\|CDD\|224118	COG1197, Mfd, Transcription-repair coupling factor (superfamily II helicase) [DNA replication, recombination, and repair / Transcription].	0

>NZ_LN824141.1|WP_045088247.1|1734893_1736069_-|ABC-transporter-permease
MKSLKMVKYEIKKILRSRAVLILSIIVPVILAFFGSSFYPKNISQNFNLVIYNQDKSFLGNFTFLLIKQFLNFENTVEISNESEFNRLIELGNYDSIIIIPKGFTNDLVNKLQTSLYIVPNPHNIQNSLMIYTAFKAVFDELAGIPEIKVGSTTDFLLSGGIGIDETRPKPEIKMLIPNAKEKMLFESESNDFGINDMFAPIVAVVTILISSMIGISYSVGQARESKLLDLYISNGLSIRVFAFSKLIAYLLVGFVMGLFSWGMFRLFGVQSQAISWHLFLLIFVSVFTFTSFGLVLSSFLKSSKAASFLVTAVIGLMFVFGNVLIPVPKGGFLEKFSYIFPVKYSLDAWRKLTVLGYGLSDIYKEIVILTIFGIFCFYLAIFLMRVTQET
>NZ_LN824141.1|WP_045088246.1|1734173_1734791_-|YigZ-family-protein
MKYLSIKDSKEISINIERSIFIGNAQKVNTIEEAQNYIKYITQKYNNATHNCWAYKVGDGNQEFFHYSDNGEPSGTAGKPIYGIIEKYNLFNVAIVVTRYFGGVKLGIRGLIDAYSSCAEEVVKNSRLTKFETTFIFEVRCSYSNYSQILRLISQESGIYLLFQEFLEDVFFRIEIIESIKERVLPIIENNSQEITFIGTSEREL
>NZ_LN824141.1|WP_045088245.1|1733279_1734146_+|polyamine-aminopropyltransferase
MLEKVYPPFIFNEFDRKNKFGLFMDVEKVIYSGVTKFQRIDIFETKAFGKVFTLDGVPMTCELDEFVYHEMISHVPLFLHENPKKVLVIGGGDGGTVREVLKHPSIEKVIMCELDEEVVEATKKYLPNLSYELNNPKVHLVFEDGSKFIKNFNNEFDVIIIDSTDPTEGGGGALYTESFYQDCFKALTENGVFTAQTEEPFIEKEWMIRAYKRISSVFNVAKLYLGFVPEYTPGTWSWTFASKNIDPIKDFNPEKVRNFDKELKYYNEEMHVASFALPNFVKKMIKDI
>NZ_LN824141.1|WP_045088244.1|1731603_1733025_-|DNA-polymerase-III-subunit-gamma/tau
MNSNLYRKYRPRNFEDIIGQPHVVKYFYNALKKGEISHAYIFSGPRGTGKTTTARILAKALNCKNPLDFNPCNECENCVSINKNSFIDVIELDAASNRGIDEIRNIRDSTNYLPVYGNYKVYIIDEFHMLTREAFNALLKTLEEPPAHVIFVLATTNLEKVPDTIISRAQIINFKNLSMKDILLGLKKIADLEGIKYDEKALEIIAKKAKGSMRDAISMFEQVEKFGDDKVFLEDVMDILGLFDESFVSKFINNVSDSNIDGFLSQSEELFKQGKDPEILLEESIEYIFDRIKEKEDPFFDIEMMKEFNVILKDLKYSENKRLTFDVEVLGFITRGLKSTTLNSSFKDVPEGGTIKEINKNDTDFNTEYFNNPIIVKIMNFFRDPRSKKTNLAIYYSLLASKIEIRNNRIIFNFSENELLEYEILKKYIDELKVNISLLINESYEVSLLFSGKENETFNLSEKAPTYQEKRLF
>NZ_LN824141.1|WP_045088243.1|1730757_1731591_-|hypothetical-protein
MINILCALRAEAEEIIKKYRLKKIHDKPFEIFISNDVRLIISGIGKVNAAGATAFILSDLDIDFNSTDIFINFGICGALQKEYVVGELILCNKVLDYEMRKSFFTDILIDYGLYEASIQTINNLDEQYDFLEDLVDMEASAAFKMASKFLYTHQIYVLKIVSDLVYEKSNERISRGFVKNLVKNKIETIINFVDVTESFLKNNPPFFQREDLELIEEVSNSLKLTFSQQEQLKNAYCFYKSHNRCEPAFLKDYLIIKPENSKERNVIFDQIKHQLYS
>NZ_LN824141.1|WP_052670440.1|1729772_1730789_-|hypothetical-protein
MIKSNTNYIANSFSHIYIENSVFDFPITQYIIDRFPRSKIVRIENYNEVFSRKNQNPYLQKLSPSLIVGEKKEGFFYKGSRLCHNFEEEHFYYTNFILNCLFDCDYCYLKGMNLSSNIVFFVNLNDYFNEIARLLNTKNKLYLSISYDSDILIFDEIYPFLNEWYNFVEKNPKITVEIRTKSVLWKKFIKYKSLDNLILSWSLAPSDIIVQYEKKTPSLEARLNAISQLLKRDWKINLALDPLIYTGKPWKIIYKEFLEYLVTKIDINLINSITVGVFRIPINYLRRMKSFSNSPISFFPYETVEGVASYPKDLKEEMLNYVVLFLERYFNRDKIYIK
>NZ_LN824141.1|WP_045088242.1|1728870_1729737_+|polyamine-aminopropyltransferase
MSEKVYPPFIFNEFDRINKFGLFMDVEKVIYSGVTKFQRIDIFETKAFGKVFTLDGVTMTRDSDEFVYHEMISHVPLFLHENPKKVLVIGGGDGGTVREVLKHPSIEKVIMCELDEEVVEATKKYLPNLSYELNNPKVHLVFEDGSKFIKNFNNEFDVIIIDSTDPTEGGGGALYTESFYQDCFKALTENGVFTAQTEDPFLKKEWMVRAYKSISSVFNVAKLYLGFVPQYPPGTWSWTFASKNIDPIKDFNPEKVRNFDKELKYYNEEMHVASFALPNFVKKMIKDI
>NZ_LN824141.1|WP_045088241.1|1728472_1728871_+|S-adenosylmethionine-decarboxylase-proenzyme
MAKFLGRHLIAELYDCDEEILNNVTEIEYQMTKAAIECGATIVTSTFHRFLPHGVSGAIIISESHLAIHTWPEYKYASLDIYTCGDSVDPWVAFNYLKDAFKSGRQEVIENKRGMFETIGVPNDSLHKVEVK
>NZ_LN824141.1|WP_045088240.1|1727921_1728458_+|cupin-domain-containing-protein
MKIGEKIKSLRIMRNMTQEELAVRSDLTKGFISQVERDLTSPTIESLEMILRALGTDLKEFFSNLENKEKVVYTKEDRIPIYDTPEGVYEELLLTASDPKNIEPSFIILDPNKATEIEKPHEGVEFGFVIEGTIELHLNKETYIIDTGECFFFTPNKKHYIKNKSKNQKAKFIWIEIF
>NZ_LN824141.1|WP_045088711.1|1726665_1727661_-|rod-shape-determining-protein
MRSYLGIDLGTANTIVYMKGKGVILNEPSVIALNRDNGEIICVGIEAKKMIGKTPANIFAIRPLKEGVIADYNVAVAMLKYYINAAVGNFVILKPVVVVGVPTGATEVEKSALREAALDAGASKAFLIEEAMATAIGAGLDVEEPSGNMIVDIGGGTTEIAVISLGNIVLSKSLRVAGDQMDQEIMDYIKTRYNIVIGEKTAERIKMEIGNVYDSDENNKLSMEIVGLDVLSGLPKTIQVSGYEVRQAIKNSVGKIIENIKSAIEETPPELLYDIVNKGIFLAGGGAMIKGMKELIEKETFIRVIVADDPITCVARGAGLVIDKINILRTL
>NZ_LN824141.1|WP_045088248.1|1736576_1737932_-|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE
MYDTIVAISTPIGMGAIGAVRVSGGDVDKIIRNCLKKHKYESKKMYYGWMYDEDSPVDEVTWVYHSKPNSYTGEDMLEIFCHGGKLVTYNILKTIIKLGARQALPGEFSKRAVLNGKIDLIKAEAINSLIKAETPFSLDASLKLLKKNRLSETIQELKHEMINIAAEIEVELDYPDEVEIDSLNLKEKISDILKTVDKILKEADNGIIAVEGVKTAIVGKPNSGKSTLLNALLKKDRAIVTEIPGTTRDTIEESLNINGILLKLIDTAGIRPTEDKIEKIGIEKTLNAMEESNLILFILDGTTPYDYEDEMIFSRIKELNNKSVIIVLNKSDSEHFKLSNCPTKLFDQKFDIVTISAKNKEIKSLEDKIYEIYFEKINIEEPTLTNMRQKNSLESSRKYLLNALNSLNMGFSNDVVMIDVRKALEKIYELTGENYTEELLNTIFSNFCVGK
>NZ_LN824141.1|WP_045088249.1|1737947_1740872_-|transcription-repair-coupling-factor
MVSNELLSFLKSLKKENKQHIIIIPDNYYNWFDEYEDYFMFYPDFDIFPFENLDVSPNIKAQRIKVLYSLIKKEQISILTTLSSLCRFTIPMKDFLIKKYKVNDDLDLFTDELYKFGYLLTEEVNSPGEYAKRGFVRDIFIPIYEEPIRIELFDTQIDRITLFDTFSQRSINKLEEFEIVPGSEIQKFNNNIDIFQERIMRFFSDTNEFDISIDIFNSIPGIFYKDKNTILSYLNRDCDIYIVNKQEVIKSFVEKERENLEMCDNDLKKRIYKAYSGHTLEILNKIEYKEIDLKLEKVYFKKSKKEDNRIDFIPLLDWEDLKEGDLVVHEDYGVGIYLGVNKVETNLGLREYITLEYANNAKVYVPVGRLDKLSKYIGDSTTVTISSLNGKKWKATKKKVNEEIRKKIKELLQIYVLRENQQGIQLFGDKELEDKFRESFPYIETPDQERSIREILEDLESPKPMDRLLAGDSGFGKTEVAMRAAFRTVVSNYQVLLLAPTTILASQHYESFKERMEPFGVKIELLTRHKTSKEKEIIFEKIKNGEIDIIIGTHALLSDLLQIRRLGLVIIDEEQRFGVMQKEKFKKLGEGINFLMMSATPIPRTLYMSISGLREISTISTPPLGRLPIQTFVGKYSDKLVRTAVLREKARGGQIIYIHNRIQELENIYKKLQNLIPEVKIGLVHGNSHKNDFIKTMNDFYAGKIDLLFSTTILENGIDIPNANTLIVDDAERYGIAQLYQLKGRVGRSNKRAFAYFLYKKELTPEAKKRLEAIKQYNEPGSGLKLSLRDMEIRGYGDLLGIEQKGHINSVGLHLYKEMLNKALVEYGIKEIEEHTRPLSYTEIKGIKGSIVIPEEYVPNSIERMRIYRRIAVSRTPEEVEDIKKEVRDRYGKLPQEVERLFKYAIIRVKANMEGIKEIEIGDSFITFKFSDDVKPSIDKFNKYSRRAFYYPNSQELIAYGPKDDIEYMENIFS
>NZ_LN824141.1|WP_045088250.1|1741323_1741704_-|hypothetical-protein
MLEERRLNLEVVDASIKIKINEICLDHLNMDESKFIINRIETGNIPKIQEITPLTKEIFFGHYDLCSLITQNVKRNITENSILFDININSKRMVNASLLVCIEKIKVSPLINTTKMIEIKIHEINY
>NZ_LN824141.1|WP_045088251.1|1741682_1742180_-|hypothetical-protein
MIAYFSLYKSDDEKYAGGLLIINENGIPVSFKYTEPVTPSEIQKIIYGDNIKNYLAYEILRNEDLFKPYDVDIVFVDDNDLLNYVVTDKILVYISELSLSRSFEIKENEGVIPLHDNKSLKFYASKVVDSNILKRIKYIIDKYDIFEPFGRLKEALIYICSKRED
>NZ_LN824141.1|WP_045088252.1|1742198_1742504_-|hypothetical-protein
MPSTHEIQIMLTKSVNVAENVQAVTQAHDSAKNILLVKQAAEYAQNLHRKVKNKDRTEKKSLDNDLLGRTAYYQGQVEEETYSESNFKIDDYRGKILDLRL
>NZ_LN824141.1|WP_045088253.1|1742524_1743214_-|FliA/WhiG-family-RNA-polymerase-sigma-factor
MKYNIDEEQLVLDYLPKIKYIALNLKSTLPKNVELDDLIQEGIIGLLQSYRKYDPEKGASFNTFAMKRIKGSMLDYLRKIDWLPKETRSLIKKYEDLVYEVGEEEYLDDKLIAERLNIEENDVDKIKFSISKRQILQLDSYFFDSEEVNWSIEEDDSNDPEVIAYKEIFKDKLKDCIEKLSQREQLILSLYYDNNLTFREIGEILDLSESRISQVHSQILIKLKKMVDE
>NZ_LN824141.1|WP_045088254.1|1743227_1743713_-|chemotaxis-protein-CheD
MENKKIVGIGEYLVDKNPGILITLGLGSCVAVCIRDKVKGIGGLVHVMLPDSRRDKDRPGKYADTGITAVVDEIIKIGGDIKNLEAKIAGGASMFKNTNKTFEIGAKNVEAVKKILKNLGIKLVAEDTGGSRARSVEFHIASGELRIRKVGGGEKVEIVVI
>NZ_LN824141.1|WP_045088255.1|1743713_1744337_-|chemotaxis-protein-CheC
MSVFDNIDDQKLDVLKELGNIGAGNAATSISLMLGKTIKITVPSAEIIPVSELWKKFTDPEEVTSGAMVEIEGEIEGALLFLLGAEETKSLIELLMLPRPDDLTNMDELTSSAIGEIANIMCSSYIIALSNFTGINIHSMPPKVVVDMLSAIVSEVSLIITNGGDYVILIQTDILLEELEDKVKGYLIYISDEKNTQKILESLGMKF
>NZ_LN824141.1|WP_045088256.1|1744394_1745099_-|PilZ-domain-containing-protein
MSEFIEKVLAKNVLFTNMPLDIEIKEKGFKGIYKSILYEYNIDLNLAKIGMPIHKGAYIKIPREVTLSVKAYSKNNLYLFNSLVYGIGKESSVRFLIITVPDEIYRVQRRNYVRIPLCEEGFFSIKREFNLKNNENLEQNEKYRFVTKDFSAGGAAIVTKKQLSIGDKILINMKLKDEVVLENIEAEVVREIGQTQFEDNIYGIKFIGITGNLEKELVRFVFKWEIGNVKNNNS
>NZ_LN824141.1|WP_045088257.1|1745122_1745980_-|P-loop-NTPase
MSYLFNDQASRLREEFASNDTKIISVVSGKGGVGKSIFSVNIAALLASYDKRVLVFDSDAGFANASILLGSSIKHTLSDYMKGIVTFKECIQETRYGVKIVSTGFDYTDWKIFQNNFDGSILNEFLSVTREIDYLIIDVGAGYSEKLNNFYLNSDKIFIVTAPEPTAVVNAYSLLKALSYLGVGSEIEIVLNMTKNKEELDNIKYALENTVKKFLNKDINSFYELSYDPNVPLSVKAQTPIVILKKDSKFSKDMKKIVEDILNLNNSGKEESFANRIKRLFGLEH

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Crispr_ID: NZ_LN824141_17

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_17

1824144-1824238

Orphan

Consensus_repeat	Method
GTTTCCATTCCTCATAGGTAGGATAAGAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_17

>merge|NZ_LN824141|17|1824144-1824238|CRISPRCasFinder
GTTTCCATTCCTCATAGGTAGGATAAGAACAAGGGTCTCCATTTGGATTTGCATCTTTTACTGAAGTTTCCATTCCTCATAGGTAGGATAAGAAC

>NZ_LN824141|17|16|1824144-1824238|CRISPRCasFinder
GTTTCCATTCCTCATAGGTAGGATAAGAAC	AAGGGTCTCCATTTGGATTTGCATCTTTTACTGAA
GTTTCCATTCCTCATAGGTAGGATAAGAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045088307.1\|1823065_1823320_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|350690
NZ_LN824141.1\|WP_045088314.1\|1836180_1837566_+\|tryptophanase	unknown	unknown	gnl\|CDD\|237314
NZ_LN824141.1\|WP_045088305.1\|1821391_1821637_-\|HU-family-DNA-binding-protein	unknown	unknown	gnl\|CDD\|365952
NZ_LN824141.1\|WP_045088308.1\|1823495_1824062_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|224116
NZ_LN824141.1\|WP_045088303.1\|1819192_1819891_-\|restriction-endonuclease-subunit-M	unknown	unknown	gnl\|CDD\|376069
NZ_LN824141.1\|WP_084217265.1\|1818089_1819073_+\|DNA-polymerase-III-subunit-beta	unknown	unknown	gnl\|CDD\|238082
NZ_LN824141.1\|WP_171820610.1\|1824322_1824475_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088313.1\|1833806_1836137_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|227061
NZ_LN824141.1\|WP_052670450.1\|1829519_1832402_-\|PolC-type-DNA-polymerase-III	unknown	unknown	gnl\|CDD\|234767
NZ_LN824141.1\|WP_171820607.1\|1815755_1815920_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088310.1\|1826214_1827522_+\|histone-deacetylase	unknown	unknown	gnl\|CDD\|212518
NZ_LN824141.1\|WP_045088306.1\|1821646_1823056_-\|UvrD-helicase-domain-containing-protein	unknown	unknown	gnl\|CDD\|350690
NZ_LN824141.1\|WP_045088309.1\|1824548_1826228_+\|hydantoinase/oxoprolinase-family-protein	unknown	unknown	gnl\|CDD\|223223
NZ_LN824141.1\|WP_045088316.1\|1838155_1838749_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088301.1\|1817129_1817345_+\|DUF3006-domain-containing-protein	unknown	unknown	gnl\|CDD\|378598
NZ_LN824141.1\|WP_171820608.1\|1816061_1817111_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|225212
NZ_LN824141.1\|WP_045088312.1\|1832745_1833807_+\|DNA-repair-exonuclease	unknown	unknown	gnl\|CDD\|277319
NZ_LN824141.1\|WP_045088304.1\|1819896_1821255_-\|site-specific-DNA-methyltransferase	unknown	unknown	gnl\|CDD\|223931
NZ_LN824141.1\|WP_045088311.1\|1827571_1828945_-\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|240545
NZ_LN824141.1\|WP_045088315.1\|1837624_1838083_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045088307.1\|1823065_1823320_-\|AAA-family-ATPase	gnl\|CDD\|350690	cd17932, DEXQc_UvrD, DEXQD-box helicase domain of UvrD. UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	2.89352e-10
NZ_LN824141.1\|WP_045088314.1\|1836180_1837566_+\|tryptophanase	gnl\|CDD\|237314	PRK13238, tnaA, tryptophanase.	0
NZ_LN824141.1\|WP_045088305.1\|1821391_1821637_-\|HU-family-DNA-binding-protein	gnl\|CDD\|365952	pfam00216, Bac_DNA_binding, Bacterial DNA-binding protein.	1.69285e-14
NZ_LN824141.1\|WP_045088308.1\|1823495_1824062_+\|AAA-family-ATPase	gnl\|CDD\|224116	COG1195, RecF, Recombinational DNA repair ATPase (RecF pathway) [DNA replication, recombination, and repair].	8.51438e-09
NZ_LN824141.1\|WP_045088303.1\|1819192_1819891_-\|restriction-endonuclease-subunit-M	gnl\|CDD\|376069	pfam18643, RE_BsaWI, BsaWI restriction endonuclease type 2. Type II restriction endonucleases recognize short 4-8 bp nucleotide sequences and cleave phosphodiester bonds within or close to their target site. BsaWI restriction endonuclease from the thermophilic bacterium Bacillus stearothermophilus W1718 belongs to a group of restriction endonucleases that share CCGG motif within their target sites, termed 'CCGG-family'. However, the R-(D/E)R motif residues, which are supposed to recognize CCGG from the major groove side, are poorly ordered and located far away from the DNA bases. BsaWI contacts with the CCGG tetranucleotide from the minor groove side. It is folded into two domains an N-terminal helical domain and a C-terminal catalytic domain. Furthermore, it carries a PDXKXE motif at the putative active site.	8.73705e-40
NZ_LN824141.1\|WP_084217265.1\|1818089_1819073_+\|DNA-polymerase-III-subunit-beta	gnl\|CDD\|238082	cd00140, beta_clamp, Beta clamp domain. The beta subunit (processivity factor) of DNA polymerase III holoenzyme, refered to as the beta clamp, forms a ring shaped dimer that encircles dsDNA (sliding clamp) in bacteria. The beta-clamp is structurally similar to the trimeric ring formed by PCNA (found in eukaryotes and archaea) and the processivity factor (found in bacteriophages T4 and RB69). This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds. .	3.83916e-64
NZ_LN824141.1\|WP_045088313.1\|1833806_1836137_+\|AAA-family-ATPase	gnl\|CDD\|227061	COG4717, COG4717, Uncharacterized conserved protein [Function unknown].	7.99464e-14
NZ_LN824141.1\|WP_052670450.1\|1829519_1832402_-\|PolC-type-DNA-polymerase-III	gnl\|CDD\|234767	PRK00448, polC, DNA polymerase III PolC; Validated.	0
NZ_LN824141.1\|WP_045088301.1\|1817129_1817345_+\|DUF3006-domain-containing-protein	gnl\|CDD\|378598	pfam11213, DUF3006, Protein of unknown function (DUF3006). This family of proteins has no known function.	9.65832e-23
NZ_LN824141.1\|WP_045088310.1\|1826214_1827522_+\|histone-deacetylase	gnl\|CDD\|212518	cd09992, HDAC_classII, Histone deacetylases and histone-like deacetylases, classII. Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation.	1.37129e-105
NZ_LN824141.1\|WP_045088306.1\|1821646_1823056_-\|UvrD-helicase-domain-containing-protein	gnl\|CDD\|350690	cd17932, DEXQc_UvrD, DEXQD-box helicase domain of UvrD. UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	2.66361e-07
NZ_LN824141.1\|WP_045088309.1\|1824548_1826228_+\|hydantoinase/oxoprolinase-family-protein	gnl\|CDD\|223223	COG0145, HyuA, N-methylhydantoinase A/acetone carboxylase, beta subunit [Amino acid transport and metabolism / Secondary metabolites biosynthesis, transport, and catabolism].	1.91621e-76
NZ_LN824141.1\|WP_171820608.1\|1816061_1817111_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|225212	COG2333, ComEC, Predicted hydrolase (metallo-beta-lactamase superfamily) [General function prediction only].	3.98717e-83
NZ_LN824141.1\|WP_045088312.1\|1832745_1833807_+\|DNA-repair-exonuclease	gnl\|CDD\|277319	cd00840, MPP_Mre11_N, Mre11 nuclease, N-terminal metallophosphatase domain. Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	1.13188e-24
NZ_LN824141.1\|WP_045088304.1\|1819896_1821255_-\|site-specific-DNA-methyltransferase	gnl\|CDD\|223931	COG0863, COG0863, DNA modification methylase [DNA replication, recombination, and repair].	0.000174798
NZ_LN824141.1\|WP_045088311.1\|1827571_1828945_-\|MATE-family-efflux-transporter	gnl\|CDD\|240545	cd13140, MATE_like_1, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	0

>NZ_LN824141.1|WP_045088308.1|1823495_1824062_+|AAA-family-ATPase
MRTELFESIHIKNFRSIDDCQLNELGKINFLLGENSVGKTSILEAIIMHANKFNIASILRTLSVSRYVQRKECNQNISELFNSKRKENIEVVAVLGEDKIITTFEPDLLEKSKDKLEVNNEVNQEEEPIKQNKFIVPDVLDCLSEFSSDNYYLVIKSMQRTFSEIKNISVKKQIMGHLKSLILLITLS
>NZ_LN824141.1|WP_045088307.1|1823065_1823320_-|AAA-family-ATPase
MLTDEQKTIIDSDEDRMMVKAVAGSGKTTTILKKVESIDENKTILYLAFNKSIERGIQPIAAKRKNFLPKTFHALAYRYVGYKY
>NZ_LN824141.1|WP_045088306.1|1821646_1823056_-|UvrD-helicase-domain-containing-protein
MDTYRVNDVITDLGLRRNELNIIYATTLLNVFNFYLHSEYMRIDDMPLSTLFKSWSHFGKDMPADLNRLFKLQKNVNNHVGVSHDLYMKLFQLSKPKLDYDYIFVDEAQDLNGAIIDVIQNQDAKLMLVGDSYQQIYGFRLSIDALNQFDGFKNYALTNSFRFGPETAELAKKVLSIGYRTPQIFGLNKQQNIDKITKYPYAYLCRSNAGIFDILIQFMSKGTKIAFEGGKNSYNFSLIRDVYALYNDEPQLVKNPQLKMFRDWYELETFLNTSGDRELSAAVNIVDKYKDDIPKYLHEIHKLPDIPKENAEIILSTVHKAKGMEYDQVKLHNDFAEIGYLNKVISETEGDYIAGQTLEEINLLYVAATRSKHKLELNEDLEKLRSKEYQIIDNTTNFKRRNVVEEINEVELAKYHFLKQKHSKTSNIKNKNNVKITTVDNKIKINNPTVVPNNRMSSYDFIKQYIKNN
>NZ_LN824141.1|WP_045088305.1|1821391_1821637_-|HU-family-DNA-binding-protein
MDEQKRVCRSFIEKKTGTPKKLIEQIVAVYSETVIEEDVKSNLVSLRNFGTFKPVEFKPQKGVNPQTLEEIHIPAKRTLKF
>NZ_LN824141.1|WP_045088304.1|1819896_1821255_-|site-specific-DNA-methyltransferase
MAMEKVVDDATTSTTKSPEEIINLFKTKKIDKDWSFAECKPSDTGKWTHNYHRYPAKFIPQLVEKLIDDYISQEEAHINDPFMGCGTTIVTAISRGFKVSGTDINKIAYLITKVKSTPIDPKYLNKKIEQLLNRLKFLKESQAILFDDKIEPLIPQKHIDRINYWFTEENKNELGIILRVIYNEEDETIRNFFLVAFSHVLKNCSIWLQGSTKPTRDLKKNAAKPYDALQRQLRKMQKGNEAFYKVVPTKVRENLNQYLKIEVGDARNQPVSDETADLVITSSPYVTSYEYADLHQLSTIWLDLADDLTEYKKEFIGTSYKKYENKRLRSLIAKDIVSKMSKKSKKIAKEIEAFFIDMEEVFDESYRILKQGGRCCYVIGNTKLKGVDILNAEVFAESLQYSGFKFDRLIKREIPSKILPQRRDEKTGRFANNHEANSEAYPIEYIVVGLKE
>NZ_LN824141.1|WP_045088303.1|1819192_1819891_-|restriction-endonuclease-subunit-M
MNFKDLEKLYLEKKQQFGTEAYKHISELLEEAKEIHKADWQNNKTPKGDHEQSWRAFKGKNLERLVQYIITDEVEKMGLKVVNGNRLERSTKLSKELSQVKRNLAIDYGKFGLHLPDVDVVIYNPRNCKVLAVISIKVTLRERIAQTGYWKLKLLQDKLTKHIKVFFITPDEDGVLTSKKPAKKGRAIVEVDLDGSYVLTKDKIEESNKVKLFEHFIDDLKQLLKNEAYDND
>NZ_LN824141.1|WP_084217265.1|1818089_1819073_+|DNA-polymerase-III-subunit-beta
MYATDLQQAFHKVITINALFPEQFATVIDQRILLEVVSNINDETIKLSYNNNVLVISGDRMEFKLPTMELKEFPVINFSIVGNDFSLDKNELLKCIDKVMFCALKDAEYLTMRFNAVYWEFEPNKLCLVASDSFRLALATMNTNTNVFTTFLLSLKSMEELKSVLSSCTTKTVAITEISSQILFKFPEDDIEIVFNVLEQSFPEYEQIVPDSFNTFVVANTEALLSAIKRVSIASNKDNSISCTFSNNNLNIYASSPDIGEAQENMGIKLSGQDLNVLYTPKYLKEALEKIETVETEMKIVGDSEPAVLKPLNDNTYFYVIMPQRKV
>NZ_LN824141.1|WP_045088301.1|1817129_1817345_+|DUF3006-domain-containing-protein
MKLIVDRFEGNYAVCEKEDGTIMNLGKDRLPKGVKEGDVLILEGKSIVIDNNATLERKKYIEELMKDMWDE
>NZ_LN824141.1|WP_171820608.1|1816061_1817111_+|MBL-fold-metallo-hydrolase
MIFLLSLSLILTGFTTSTTQTPAPESLEVYYIDVGQGDSIFIISPTGKTILIDGGEKDSGVTDFLESKKIKTIDVVIATHPHSDHIGGLVDVIKNYDVKSVYMPKATHTTKIFENLILAIKEKGLKINPVYEGVTLPFEDINAVFVAPEKDIINDNLNEYSAVLKLTYKDTSFLFTGDAESGSEQRMLFSKQNIKADVLKAGHHGSKYSTSTTFLDEVNPKYVIISCGAGNKYGYPHDETIKKLTDRKIKTYRTDEDGTIHAISDGKTIKFETIKSDKKTDVTVNSTKTTTTVGNNTKSEDKKEEVVYITKSGKKYHRAGCRYLKSSQIKISKEEAIKKGYTPCSICNP
>NZ_LN824141.1|WP_171820607.1|1815755_1815920_+|hypothetical-protein
MDILFTSIILTLISIVVVFYIIIPQKSLETAITFSSIVAIYNLLYVDKSDISRH
>NZ_LN824141.1|WP_171820610.1|1824322_1824475_+|hypothetical-protein
MLINHSCDEKNKSVDPLGFLAYWGSTDFFGIIDIVRKMFSAYFFILNLEI
>NZ_LN824141.1|WP_045088309.1|1824548_1826228_+|hydantoinase/oxoprolinase-family-protein
MIVGLDMGGTNIDAVLIDNGKIINSVKNPTDRNDLFQSIWTTLTELLQDFDTSKIQRINLSTTVCTNAIVENTTSPVGLIIQSGPGLPHDFLAFGDENVFISGYIDHRGTEVEPWKKEEIDNAVRIFRKKNLDCCAVVTKFSPRNPKHETDIQDILEKEGFSTVTMGHTVSGKLNFPRRVATSFLNSAVFKTFEEFSSNIKKSLEQENIKAPVYILKADGGTMNIKSAKEKPVETILSGPAASCTGINALLETNQDAILLDVGGTTTDIFFLADGIPLFEPLGIKIENYNTLVRSIYSVSIGLGGDSSISVNDGKLKIGPRREGPAYSYGGPKPTPTDAMIVLGIIQGDKQKAIEAMETLGKKLNLSSIDAAKLVLETMAEMIKVKVDELLTEINSKPVYTIKELLYGKKIEPKVINIIGAPAKALAPTLEKKFNLPCYYPKNYAVANAIGAALAKPTTEINMLVDTAKGIMTVPELEIYQNVDRKFSLELARKKAIELLKESARSLGAKEDEIEAEIVEESCFNMVRGFYTSGQNIRIKAQIKPGLIYNLRGDNIDQG
>NZ_LN824141.1|WP_045088310.1|1826214_1827522_+|histone-deacetylase
MIKAKNKLGLVFFPAFDWAISPTHPEREERLLYTQDQIFEEGIQDIEGITFYNPIVAEEKDVQRVHFCVPNVKSRVTQSHLISAGGAIVSLKKVLEKEVDKSFALVRPPGHHAQRVVYGDRGFCIINIEAVMLERIRQEFGNLRVAIVDTDCHHGDGTQDIYWNDKDTLFISFHQDGRTLFPGTGFVDEFGGPGAYGYNINIPLPPGTGEEGFLYVLENVVMPILEEYKPDIIVNSAGQDNHYTDPITNMNFTAQGYAKLNDRLNPDIAVLEGGYSIEGALPYINLGIILAMAGIDYSNVREPDYDAHELKQPEKITNYIKGLSELVYQRWKNKEDLWLNDFKGMEKVERTRRIYYDTDGILEQQTQTFKICKKCSGVNTIRSRSDTGYNVFAITIPRDACSDCIDEGYKMYKNASNEFTNVYLQDRVNDEYLAK
>NZ_LN824141.1|WP_045088311.1|1827571_1828945_-|MATE-family-efflux-transporter
MKNNYLTNGPITKALVKLALPIMATSFVQMTYTMMDMIWLGRIGSNAVAASGTVGFFTWIGSALFILSKIAVEVGVAQSLGKDDIHAAREYVRHSIQLDIIIALVYTAILIIFRNSMIGFFRIDDQEVVQMALDYLVIISIGLIFYFINPVLSGVFNGVGDSVTPFKVNVVGLIVNMVLDPLMILGIGPFPYMGIKGAAWATVIAQATVTFLFIFECRKLTSLFSGLNIFKLPKKEYLKSIVKLGVPVSIQNVIFATISMFLARIIAQWGYQAIAVQNVGSQIESISWMTAGGFSTAISTFVGQNYGAGKWDRIREGYKKGLMIVGIIGLIATFLFFFVPEPIIKIFIPTDREAIEIGINYLKILSLSQFFMVVEIATQGAFNGLGKTLPPSLVGIILNALRIPGALILSSTVLGLNGVWWSICISSILKGVILFIWLAIVLKSFPKSSLNEAYEEC
>NZ_LN824141.1|WP_052670450.1|1829519_1832402_-|PolC-type-DNA-polymerase-III
MYFFEKLSKLVGNEINFVNKEISVKGKVFRVEENKDSFYVYISDYECSFLCQTQDKIKKGEWFRFEGILEYDSVMASYYINVFQVKKAVPIETCDLAVNKRVELHAHSKMSSKSSILDMKELVDTALIYGHRAVAITDNENVHIIPAFYQYAKQKNIKPIFGCELNVFDESKGIMKNVNVLVKNQKGLKNLYKIITISHMNVVNKKAVITLTDLIKHRDGLLLGSSLDSFLLYYYLKGSSEDRLSELISFYDYIELFPLDCYIDSNIETSKLVDYSKTIYNLSKKLNKIVVMSGDVRYLRKGEQDYLNVMILGTSTKSKPRKQTNNVNYFRNTQEMYDEAYKIFKKIGIAKEITVKNTSKIAESIEEVVPFDLKLKVPKFESADENLRKYAYENARKIYGKELHPQIIERMEKELNNIINNGYAVIFLISTEMVKESLRFGYPIGSRGSVGSSLIAFLLGITEVNPLAPHYFCKHCGYVEFSENLNLCGFDLEKKSCPRCGKILSSDGHNIRFEVFMGYSGEKIPDIDVNFSADIFNDIQRYLEKRFGRDYCYKAGTISTISRYNAMKMVNKYYKNKEVRNVNYAHSVYISEKIKGTKLNTGQHPSAMIIIPREYDVHDFTPYQYSANSPEIGIITTHYDFKALENDLLKIDVLSHDGPTFLKMLKDLTGFDYNDIPMDDERVLSLFSSTKELGVDLSEIETEIGTLGVPEVWTPFSHKMLIETRPKTFYDLCRTNSLAHGTNIWFNNAREIVLKNTADINQIVSCRDDILIMLEYYGVDSKLSFRIMEKVRKGKDLTDEEISAIKDSNAPEWYLDSLRKIHYLFPKAHAVAYMIMAYKIAYYKLYYPLEFYSVYFTVRAKCFDIGIVMSEELTLKLIKILSKNEFQHNYEQSNVYSTLKTVYEMRKRGYDFLGPDKDKSEAHVFKIEGDYLRIPLTKMKNIGNKKANKIIRQRQQQKII
>NZ_LN824141.1|WP_045088312.1|1832745_1833807_+|DNA-repair-exonuclease
MKILHTADVHLCDYEDERWKSLEHIIDIGKSENIDLFVISGDLFDEDVKSEVLRSKIRGLFSNNEFITVIIPGNHDSKSFSEDLYFGEDVVILTDLNKPYEYNDVCVWGFPFEPISGEEFFRKIKSISSKLDTAKTNILLFHGELVDTFYSPSDFGDEGEVRYMPAKLSYFKNLGFDYILSGHFHSKFDLYEFEDNKYFVYPGSPVSITKKETGQRKVNLFEIGNAPSEYLLDTPHFIELQIKINPFEKMNPIEHIKKELQKVHPQAKVILKVTGYINSKLIGITEKELANQLKDALNDKVIERHFEVRDISRVLEDELFKSFLKKLQEKNYSQEKKNELIDLTIKAMMEVVK
>NZ_LN824141.1|WP_045088313.1|1833806_1836137_+|AAA-family-ATPase
MKLKEFSIIRYGPLENLNKIKLNDFNLIWGKNECGKTLTIDGLVKLLFNKTGKDFENLERVQEVPEGYVVLVDEKGNEYKIPEKGDLPKISGLSATECNNIFIVRNSNLSVAHDLSKESMFYESITDKLTGLETERIAKISEKIKEIARLTDKSLEFQDVKDEKLKTRINEANKLIEEIDQLIQEVKEKGLDELEEKKVELKEQLETIEEEIKKLEALRKREKYEKGDEALTILKKLMDEIKELDVYNENDAKLWNDLEKELDMYSSQKQKKEKELEVKVKELEKADEKYKELSEEFKSYEEKKKKIDEEIKPEMSRFNSSRDVNKLEKKNKVFTVSMIISIVILAISVVGIVFNKSLLFYVLTAVSSIAVAAFGGLKYKVIKDQDQVINKFEEFKAKLQTLGLMADTLGEIYENIKNYEVWYETKLKEFNRAFLDKEKIKLQINDLKNKEIAEIEQHIKNIQEKIEKLKEKSKETSLESYNEKLKLKNEIKNTIGKQETILKSHFGYVGKSLEEAIPYWENEIKKLEIYKDNFPEDKFSEDLLTNLKYNENKYKNEYEEVHNNTKLIQKMFEDIEGRVNKILLPDEHLFCETSTDLEAIKKLLSDFVNTHENNRNNALVVLSIFEELEREEKGKISSLFGQNSLVTKYFKEITDGLYDEVTFDSNENKIKVRRKDKVVLDAYQLSGGAYDQLYFSIRLALGRTLLKDRFGFFIMDDPFVKSDFERLNRQMNLLKKIANSGWQIIYFSSKDEIKDLLKEEIANKTINYVELSPLFS
>NZ_LN824141.1|WP_045088314.1|1836180_1837566_+|tryptophanase
MGKVSKPEPFKIKMVEPIKLISRQEREEALKRAGYNVFALRADEVYIDLLTDSGTGAMSDNQWAGIMLGDESYAGSKNYYNLIDTCKEIFNYEYFIPTHQGRGAEKVLFPLLISKPGQYVLSNMHFDTTKAHVELANARAVDLVIQEAFDTSSFHPFKGNIDIEKLEKFIREKGSENIAFIVITVTCNSAGGQPVSMQNIRETSQLAKKYGIHVFLDAARYAENAYFIKYREKGYADKSIKDIVQEMFSYADGFTMSAKKDAIVNMGGLIGIKDDEELYNQARANLVPLEGFPTYGGLSGRDIEAMARGLKEGIELDYLEYRIGQVEYLGNKLRAADIPIQYPVGGHAVFVDAKKMLPHIPYYQFPAQALANALYLESGVRAVEIGSLMLGRDPDTGEQLESPLELLRLTIPRRVYTNNHMDYVAESLIEVNKIAHTLKGLEFVYEPKILRHFTAKLKPIE
>NZ_LN824141.1|WP_045088315.1|1837624_1838083_-|hypothetical-protein
MKKKLSLIIISLLLLTSFIFADKFILVSDSSFKVYRLEAYDSFELTGDALTLKKADTLWSGSDVSVKINLVTELELQKYQQLEQMLKEGRTIPAPTKPGERSTGKIITVEWLKEDKKEKLTEEMKKFLVDANQTMFDLTKWLNDWANWIPVK
>NZ_LN824141.1|WP_045088316.1|1838155_1838749_-|hypothetical-protein
MKKASFFIVLGLAVLLLFGCAGDGGPLGGVSKEPEGIWLISTYTDPDGDEVYQEFDSFFYVKISVNDDKNGYDAIALNEDGDPDETIEETTFELENIDVMLTILNMAQPFGLGEFDYELDGTFYDVSKDEDDLMFGNFLEDVSNDEGIWFAVRYTFPAPAASLEVDNPLIGREDEIEKIIEARTGYKVEIDFSEIIK

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Crispr_ID: NZ_LN824141_18

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN824141_18

1839012-1839154

Orphan

Consensus_repeat	Method
TTTATACTTTTTGGTACTTGTACTAAAGGAAGGGCTTCTCCCTGGTACCCTTTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN824141_18

>merge|NZ_LN824141|18|1839012-1839154|CRISPRCasFinder
TTTATACTTTTTGGTACTTGTACTAAAGGAAGGGCTTCTCCCTGGTACCCTTTTCAATTCAAAAAGCTTTTTTACAAAATTTTCATTTCTTTATACTTTTTGGTACTTGTACTAAAGGAAGGGCTTCTCCCTGGTACCCTTTT

>NZ_LN824141|18|17|1839012-1839154|CRISPRCasFinder
TTTATACTTTTTGGTACTTGTACTAAAGGAAGGGCTTCTCCCTGGTACCCTTTT	CAATTCAAAAAGCTTTTTTACAAAATTTTCATTTC
TTTATACTTTTTGGTACTTGTACTAAAGGAAGGGCTTCTCCCTGGTACCCTTTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN824141.1\|WP_045088321.1\|1844207_1846502_+\|primosomal-protein-N'	unknown	unknown	gnl\|CDD\|235514
NZ_LN824141.1\|WP_045088317.1\|1839533_1840508_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187539
NZ_LN824141.1\|WP_045088323.1\|1847224_1847467_-\|glutathione-S-transferase-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|239274
NZ_LN824141.1\|WP_052670531.1\|1847807_1848647_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|366166
NZ_LN824141.1\|WP_045088325.1\|1849207_1850455_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088320.1\|1842192_1844190_+\|alpha-glucosidase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|200477
NZ_LN824141.1\|WP_045088314.1\|1836180_1837566_+\|tryptophanase	unknown	unknown	gnl\|CDD\|237314
NZ_LN824141.1\|WP_045088313.1\|1833806_1836137_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|227061
NZ_LN824141.1\|WP_045088311.1\|1827571_1828945_-\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|240545
NZ_LN824141.1\|WP_045088324.1\|1848654_1849179_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088309.1\|1824548_1826228_+\|hydantoinase/oxoprolinase-family-protein	unknown	unknown	gnl\|CDD\|223223
NZ_LN824141.1\|WP_045088315.1\|1837624_1838083_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088318.1\|1840841_1841258_+\|OsmC-family-protein	unknown	unknown	gnl\|CDD\|224679
NZ_LN824141.1\|WP_171820610.1\|1824322_1824475_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088316.1\|1838155_1838749_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN824141.1\|WP_045088312.1\|1832745_1833807_+\|DNA-repair-exonuclease	unknown	unknown	gnl\|CDD\|277319
NZ_LN824141.1\|WP_045088322.1\|1846587_1847178_+\|ribosome-associated-translation-inhibitor-RaiA	unknown	unknown	gnl\|CDD\|379821
NZ_LN824141.1\|WP_052670450.1\|1829519_1832402_-\|PolC-type-DNA-polymerase-III	unknown	unknown	gnl\|CDD\|234767
NZ_LN824141.1\|WP_045088319.1\|1841348_1842152_+\|Mrp/NBP35-family-ATP-binding-protein	unknown	unknown	gnl\|CDD\|378455
NZ_LN824141.1\|WP_045088310.1\|1826214_1827522_+\|histone-deacetylase	unknown	unknown	gnl\|CDD\|212518

Protein	Function_ID	Function_description	E-value
NZ_LN824141.1\|WP_045088314.1\|1836180_1837566_+\|tryptophanase	gnl\|CDD\|237314	PRK13238, tnaA, tryptophanase.	0
NZ_LN824141.1\|WP_045088323.1\|1847224_1847467_-\|glutathione-S-transferase-N-terminal-domain-containing-protein	gnl\|CDD\|239274	cd02976, NrdH, NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.	1.07765e-30
NZ_LN824141.1\|WP_052670531.1\|1847807_1848647_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	1.26093e-07
NZ_LN824141.1\|WP_045088311.1\|1827571_1828945_-\|MATE-family-efflux-transporter	gnl\|CDD\|240545	cd13140, MATE_like_1, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	0
NZ_LN824141.1\|WP_045088322.1\|1846587_1847178_+\|ribosome-associated-translation-inhibitor-RaiA	gnl\|CDD\|379821	pfam16321, Ribosom_S30AE_C, Sigma 54 modulation/S30EA ribosomal protein C-terminus. This domain often occurs at the C-terminus of proteins containing pfam02482.	1.15235e-22
NZ_LN824141.1\|WP_045088313.1\|1833806_1836137_+\|AAA-family-ATPase	gnl\|CDD\|227061	COG4717, COG4717, Uncharacterized conserved protein [Function unknown].	7.99464e-14
NZ_LN824141.1\|WP_052670450.1\|1829519_1832402_-\|PolC-type-DNA-polymerase-III	gnl\|CDD\|234767	PRK00448, polC, DNA polymerase III PolC; Validated.	0
NZ_LN824141.1\|WP_045088321.1\|1844207_1846502_+\|primosomal-protein-N'	gnl\|CDD\|235514	PRK05580, PRK05580, primosome assembly protein PriA; Validated.	0
NZ_LN824141.1\|WP_045088310.1\|1826214_1827522_+\|histone-deacetylase	gnl\|CDD\|212518	cd09992, HDAC_classII, Histone deacetylases and histone-like deacetylases, classII. Class II histone deacetylases are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. This group includes animal HDAC4,5,6,7,8,9,10, fungal HOS3 and HDA1, plant HDA5 and HDA15 as well as other eukaryotes, archaeal and bacterial histone-like deacetylases. Eukaryotic deacetylases mostly use histones (H2, H3, H4) as substrates for deacetylation; however, non-histone substrates are known (for example, tubulin). Substrates for prokaryotic histone-like deacetylases are not known. Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. Histone deacetylases usually act via association with DNA binding proteins to target specific chromatin regions. Interaction partners of class II deacetylases include 14-3-3 proteins, MEF2 family of transcriptional factors, CtBP, calmodulin (CaM), SMRT, N-CoR, BCL6, HP1alpha and SUMO. Histone deacetylases play a role in the regulation of cell cycle, cell differentiation and survival. Class II mammalian HDACs are differentially inhibited by structurally diverse compounds with known antitumor activities, thus presenting them as potential drug targets for human diseases resulting from aberrant acetylation.	1.37129e-105
NZ_LN824141.1\|WP_045088318.1\|1840841_1841258_+\|OsmC-family-protein	gnl\|CDD\|224679	COG1765, COG1765, Predicted redox protein, regulator of disulfide bond formation [Posttranslational modification, protein turnover, chaperones].	1.20066e-35
NZ_LN824141.1\|WP_045088309.1\|1824548_1826228_+\|hydantoinase/oxoprolinase-family-protein	gnl\|CDD\|223223	COG0145, HyuA, N-methylhydantoinase A/acetone carboxylase, beta subunit [Amino acid transport and metabolism / Secondary metabolites biosynthesis, transport, and catabolism].	1.91621e-76
NZ_LN824141.1\|WP_045088312.1\|1832745_1833807_+\|DNA-repair-exonuclease	gnl\|CDD\|277319	cd00840, MPP_Mre11_N, Mre11 nuclease, N-terminal metallophosphatase domain. Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	1.13188e-24
NZ_LN824141.1\|WP_045088317.1\|1839533_1840508_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187539	cd05228, AR_FR_like_1_SDR_e, uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs. This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.14955e-83
NZ_LN824141.1\|WP_045088320.1\|1842192_1844190_+\|alpha-glucosidase-C-terminal-domain-containing-protein	gnl\|CDD\|200477	cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	1.29868e-172
NZ_LN824141.1\|WP_045088319.1\|1841348_1842152_+\|Mrp/NBP35-family-ATP-binding-protein	gnl\|CDD\|378455	pfam10609, ParA, NUBPL iron-transfer P-loop NTPase. This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.	5.20298e-129

>NZ_LN824141.1|WP_045088316.1|1838155_1838749_-|hypothetical-protein
MKKASFFIVLGLAVLLLFGCAGDGGPLGGVSKEPEGIWLISTYTDPDGDEVYQEFDSFFYVKISVNDDKNGYDAIALNEDGDPDETIEETTFELENIDVMLTILNMAQPFGLGEFDYELDGTFYDVSKDEDDLMFGNFLEDVSNDEGIWFAVRYTFPAPAASLEVDNPLIGREDEIEKIIEARTGYKVEIDFSEIIK
>NZ_LN824141.1|WP_045088315.1|1837624_1838083_-|hypothetical-protein
MKKKLSLIIISLLLLTSFIFADKFILVSDSSFKVYRLEAYDSFELTGDALTLKKADTLWSGSDVSVKINLVTELELQKYQQLEQMLKEGRTIPAPTKPGERSTGKIITVEWLKEDKKEKLTEEMKKFLVDANQTMFDLTKWLNDWANWIPVK
>NZ_LN824141.1|WP_045088314.1|1836180_1837566_+|tryptophanase
MGKVSKPEPFKIKMVEPIKLISRQEREEALKRAGYNVFALRADEVYIDLLTDSGTGAMSDNQWAGIMLGDESYAGSKNYYNLIDTCKEIFNYEYFIPTHQGRGAEKVLFPLLISKPGQYVLSNMHFDTTKAHVELANARAVDLVIQEAFDTSSFHPFKGNIDIEKLEKFIREKGSENIAFIVITVTCNSAGGQPVSMQNIRETSQLAKKYGIHVFLDAARYAENAYFIKYREKGYADKSIKDIVQEMFSYADGFTMSAKKDAIVNMGGLIGIKDDEELYNQARANLVPLEGFPTYGGLSGRDIEAMARGLKEGIELDYLEYRIGQVEYLGNKLRAADIPIQYPVGGHAVFVDAKKMLPHIPYYQFPAQALANALYLESGVRAVEIGSLMLGRDPDTGEQLESPLELLRLTIPRRVYTNNHMDYVAESLIEVNKIAHTLKGLEFVYEPKILRHFTAKLKPIE
>NZ_LN824141.1|WP_045088313.1|1833806_1836137_+|AAA-family-ATPase
MKLKEFSIIRYGPLENLNKIKLNDFNLIWGKNECGKTLTIDGLVKLLFNKTGKDFENLERVQEVPEGYVVLVDEKGNEYKIPEKGDLPKISGLSATECNNIFIVRNSNLSVAHDLSKESMFYESITDKLTGLETERIAKISEKIKEIARLTDKSLEFQDVKDEKLKTRINEANKLIEEIDQLIQEVKEKGLDELEEKKVELKEQLETIEEEIKKLEALRKREKYEKGDEALTILKKLMDEIKELDVYNENDAKLWNDLEKELDMYSSQKQKKEKELEVKVKELEKADEKYKELSEEFKSYEEKKKKIDEEIKPEMSRFNSSRDVNKLEKKNKVFTVSMIISIVILAISVVGIVFNKSLLFYVLTAVSSIAVAAFGGLKYKVIKDQDQVINKFEEFKAKLQTLGLMADTLGEIYENIKNYEVWYETKLKEFNRAFLDKEKIKLQINDLKNKEIAEIEQHIKNIQEKIEKLKEKSKETSLESYNEKLKLKNEIKNTIGKQETILKSHFGYVGKSLEEAIPYWENEIKKLEIYKDNFPEDKFSEDLLTNLKYNENKYKNEYEEVHNNTKLIQKMFEDIEGRVNKILLPDEHLFCETSTDLEAIKKLLSDFVNTHENNRNNALVVLSIFEELEREEKGKISSLFGQNSLVTKYFKEITDGLYDEVTFDSNENKIKVRRKDKVVLDAYQLSGGAYDQLYFSIRLALGRTLLKDRFGFFIMDDPFVKSDFERLNRQMNLLKKIANSGWQIIYFSSKDEIKDLLKEEIANKTINYVELSPLFS
>NZ_LN824141.1|WP_045088312.1|1832745_1833807_+|DNA-repair-exonuclease
MKILHTADVHLCDYEDERWKSLEHIIDIGKSENIDLFVISGDLFDEDVKSEVLRSKIRGLFSNNEFITVIIPGNHDSKSFSEDLYFGEDVVILTDLNKPYEYNDVCVWGFPFEPISGEEFFRKIKSISSKLDTAKTNILLFHGELVDTFYSPSDFGDEGEVRYMPAKLSYFKNLGFDYILSGHFHSKFDLYEFEDNKYFVYPGSPVSITKKETGQRKVNLFEIGNAPSEYLLDTPHFIELQIKINPFEKMNPIEHIKKELQKVHPQAKVILKVTGYINSKLIGITEKELANQLKDALNDKVIERHFEVRDISRVLEDELFKSFLKKLQEKNYSQEKKNELIDLTIKAMMEVVK
>NZ_LN824141.1|WP_052670450.1|1829519_1832402_-|PolC-type-DNA-polymerase-III
MYFFEKLSKLVGNEINFVNKEISVKGKVFRVEENKDSFYVYISDYECSFLCQTQDKIKKGEWFRFEGILEYDSVMASYYINVFQVKKAVPIETCDLAVNKRVELHAHSKMSSKSSILDMKELVDTALIYGHRAVAITDNENVHIIPAFYQYAKQKNIKPIFGCELNVFDESKGIMKNVNVLVKNQKGLKNLYKIITISHMNVVNKKAVITLTDLIKHRDGLLLGSSLDSFLLYYYLKGSSEDRLSELISFYDYIELFPLDCYIDSNIETSKLVDYSKTIYNLSKKLNKIVVMSGDVRYLRKGEQDYLNVMILGTSTKSKPRKQTNNVNYFRNTQEMYDEAYKIFKKIGIAKEITVKNTSKIAESIEEVVPFDLKLKVPKFESADENLRKYAYENARKIYGKELHPQIIERMEKELNNIINNGYAVIFLISTEMVKESLRFGYPIGSRGSVGSSLIAFLLGITEVNPLAPHYFCKHCGYVEFSENLNLCGFDLEKKSCPRCGKILSSDGHNIRFEVFMGYSGEKIPDIDVNFSADIFNDIQRYLEKRFGRDYCYKAGTISTISRYNAMKMVNKYYKNKEVRNVNYAHSVYISEKIKGTKLNTGQHPSAMIIIPREYDVHDFTPYQYSANSPEIGIITTHYDFKALENDLLKIDVLSHDGPTFLKMLKDLTGFDYNDIPMDDERVLSLFSSTKELGVDLSEIETEIGTLGVPEVWTPFSHKMLIETRPKTFYDLCRTNSLAHGTNIWFNNAREIVLKNTADINQIVSCRDDILIMLEYYGVDSKLSFRIMEKVRKGKDLTDEEISAIKDSNAPEWYLDSLRKIHYLFPKAHAVAYMIMAYKIAYYKLYYPLEFYSVYFTVRAKCFDIGIVMSEELTLKLIKILSKNEFQHNYEQSNVYSTLKTVYEMRKRGYDFLGPDKDKSEAHVFKIEGDYLRIPLTKMKNIGNKKANKIIRQRQQQKII
>NZ_LN824141.1|WP_045088311.1|1827571_1828945_-|MATE-family-efflux-transporter
MKNNYLTNGPITKALVKLALPIMATSFVQMTYTMMDMIWLGRIGSNAVAASGTVGFFTWIGSALFILSKIAVEVGVAQSLGKDDIHAAREYVRHSIQLDIIIALVYTAILIIFRNSMIGFFRIDDQEVVQMALDYLVIISIGLIFYFINPVLSGVFNGVGDSVTPFKVNVVGLIVNMVLDPLMILGIGPFPYMGIKGAAWATVIAQATVTFLFIFECRKLTSLFSGLNIFKLPKKEYLKSIVKLGVPVSIQNVIFATISMFLARIIAQWGYQAIAVQNVGSQIESISWMTAGGFSTAISTFVGQNYGAGKWDRIREGYKKGLMIVGIIGLIATFLFFFVPEPIIKIFIPTDREAIEIGINYLKILSLSQFFMVVEIATQGAFNGLGKTLPPSLVGIILNALRIPGALILSSTVLGLNGVWWSICISSILKGVILFIWLAIVLKSFPKSSLNEAYEEC
>NZ_LN824141.1|WP_045088310.1|1826214_1827522_+|histone-deacetylase
MIKAKNKLGLVFFPAFDWAISPTHPEREERLLYTQDQIFEEGIQDIEGITFYNPIVAEEKDVQRVHFCVPNVKSRVTQSHLISAGGAIVSLKKVLEKEVDKSFALVRPPGHHAQRVVYGDRGFCIINIEAVMLERIRQEFGNLRVAIVDTDCHHGDGTQDIYWNDKDTLFISFHQDGRTLFPGTGFVDEFGGPGAYGYNINIPLPPGTGEEGFLYVLENVVMPILEEYKPDIIVNSAGQDNHYTDPITNMNFTAQGYAKLNDRLNPDIAVLEGGYSIEGALPYINLGIILAMAGIDYSNVREPDYDAHELKQPEKITNYIKGLSELVYQRWKNKEDLWLNDFKGMEKVERTRRIYYDTDGILEQQTQTFKICKKCSGVNTIRSRSDTGYNVFAITIPRDACSDCIDEGYKMYKNASNEFTNVYLQDRVNDEYLAK
>NZ_LN824141.1|WP_045088309.1|1824548_1826228_+|hydantoinase/oxoprolinase-family-protein
MIVGLDMGGTNIDAVLIDNGKIINSVKNPTDRNDLFQSIWTTLTELLQDFDTSKIQRINLSTTVCTNAIVENTTSPVGLIIQSGPGLPHDFLAFGDENVFISGYIDHRGTEVEPWKKEEIDNAVRIFRKKNLDCCAVVTKFSPRNPKHETDIQDILEKEGFSTVTMGHTVSGKLNFPRRVATSFLNSAVFKTFEEFSSNIKKSLEQENIKAPVYILKADGGTMNIKSAKEKPVETILSGPAASCTGINALLETNQDAILLDVGGTTTDIFFLADGIPLFEPLGIKIENYNTLVRSIYSVSIGLGGDSSISVNDGKLKIGPRREGPAYSYGGPKPTPTDAMIVLGIIQGDKQKAIEAMETLGKKLNLSSIDAAKLVLETMAEMIKVKVDELLTEINSKPVYTIKELLYGKKIEPKVINIIGAPAKALAPTLEKKFNLPCYYPKNYAVANAIGAALAKPTTEINMLVDTAKGIMTVPELEIYQNVDRKFSLELARKKAIELLKESARSLGAKEDEIEAEIVEESCFNMVRGFYTSGQNIRIKAQIKPGLIYNLRGDNIDQG
>NZ_LN824141.1|WP_171820610.1|1824322_1824475_+|hypothetical-protein
MLINHSCDEKNKSVDPLGFLAYWGSTDFFGIIDIVRKMFSAYFFILNLEI
>NZ_LN824141.1|WP_045088317.1|1839533_1840508_+|NAD-dependent-epimerase/dehydratase-family-protein
MILITGGTGHLGNVLVKQFINLGEKPVVYTHPSDTCKSLNNVDVEIVKADIRDKNVLEKYIKESEAVFHLAAVISILPWKSKAIEDVNVGGTKNVADLCMKYNKKLIYVSSVHAFSEKEEGDVIDEKTPILPELTTGAYGKSKAKAALLIMNYAKAGLNVITICPTGIIGPFDYKPSEMGNMFLSYLKGELNTIIEGAFDFVDVRDVSDGIIKAYEKGNKGEFYILGNENIEVFELINMVNTIKNKDFKPKILGKNTAYFVSILLLLKNLISKEKLLLTPYSVHTLQTNTLFSHEKAARELGYNPRPLEETVKDTVTWLENNLM
>NZ_LN824141.1|WP_045088318.1|1840841_1841258_+|OsmC-family-protein
MTEFLVKNLHGSHFYMKTPSGHDVHIDAGVDNNGYDSAPRPMEYLIAGLAGCTGMDVVSILKKMRVDFEEFNLRVLTERNEDHPKKYNKIHVIYEFKGDNLPIDKLERAAKLSQEKYCGAIASFRGSVDITYEVKIVD
>NZ_LN824141.1|WP_045088319.1|1841348_1842152_+|Mrp/NBP35-family-ATP-binding-protein
MSNIQEVKEKVNKKLEDIENVILVMSGKGGVGKTTVAVNLAVSLALLGKKVGLLDVDLHGPDVVRMLGGEEYPLTQVGDEIVPPEVHGIRVISISQFLNEGNVAVIWRGPLKTGAILQFIGDVAWGNLDYLVVDAPPGTGDEPLTVIQNISKLRGALLVTSPSVVSQDDVERAIDFVKKMNVDILGIVENMSYFICPNCKSKHFIFGEGGGKSLSERFNLDLLAQIPLDSSIRENMDKGRPVAYFGLPEISDAYMNLAQKLIEKIEQ
>NZ_LN824141.1|WP_045088320.1|1842192_1844190_+|alpha-glucosidase-C-terminal-domain-containing-protein
MNKYSFIFLLFILLSLGSVFAINSSFLLSKDASSVYLVASFNNFEPVEMERGFGELWRYSIDLEPGEYLYKYIIDGEEILDFQNSNITVFNGEVFNVRVVKEPYSFPKTGDGRVKEIYFRNERRYINPVKPGEIYLAIEFEKNDIEDVNLQSNAKLVSKEVIESGNNVIYRFHVFTEAPVLKYRFAIDDSQEIIYGYNGTENFFEFDFSKPIIPYFDTPEWAKGRVYYQIFPDRFRNGDPHNDPKGTYNWYGPHNQSSLGSSFYGGDLQGVIDSVDYLEYLGVEAIYFNPIFEALSTHKYDTKNYLKIDPSFGDEEIFLDMLDILHEYDMKVILDGVFNHTGTEFFAMQENFAKQEESRYLDWYYIKSFPIRKSTSSYEGWHGYADLPQLNNNNPKVKAYINHVIGKWMSLGIDGWRLDAVDQLPVSYWASLYENFKNIDENTFIVGEFWRDATSYFEDPAFDSVMNYIFRDAVISYARGGSANNFVKTTNAYLDKYPPQVLHSLWNLLGSHDTERILTALDENVDKMKLAAVLHITFIGSPLIYYGDEIGMTGTTDPFCRVPFYWDEDMWNMNIFDLYQALIQLRKDSLAIRQGDYNVLYSKGNVLIYERSYKSEKVIVALNSKNASVNVNYKLDGEYVDYFSKEKVNVIESIPANGFYILFSE
>NZ_LN824141.1|WP_045088321.1|1844207_1846502_+|primosomal-protein-N'
MYYYDVVPLGQRLFKPYTYKYEQKLEVGQRVVIDLRGKFVQGLVYRESNTPEILKIKDIEFPLDEKSYLNNSHIKLLERVCNYFLAPMGEIAKLFFPPASSDVYKLKIVPLNELAPFEKPIFYKDFLSLYKDNSTANKKLKELLSTNVVKLDLHKRSIRENKDYFVSLSMDLSEIWNFNLSKGARNVINYLSINGETLESELYEKGIINRGTTVLKTLHKKGIINITEDFLINSDEEKVDLTDEQKTAVDFIRTHDDKPHLLYGVTGSGKTEVFFEVGESVLEKGGKLLILVPEISLTSEIMSRLKKRFSKYKAAFYHSSLTSSERVDTWYKAVEGEIDIVIGTRSAVWIPIKDLKMIIIDEEHDQSFYQIENVTYDAIEVALFRKELENIQLILSSATPRVVDIKKAKDDEMYLETISSRYFSEMPDVEIIDMKKEEKYNWIFSKKVISSIKNVVAKNKKVIVFTPTRGYANYIVCSECGYIFKCENCDVSLTFHKKERKLVCHYCGNEQPLSNFCPRCGGFKLQSRGYGTERVLTELTKLFPSEPIVRVDRTVIKSFEDLKNTFSFMKEPGRKIIVGTKMITKGLDIKDLDLVVILDSDRYTHLPDYNAKESTASLIMQVAGRSGRKEKGKVLIQTFDSDNEIYQAAINHDYTLIAEKELEQRSIYKYPPFTKLFLIMINNNKMDKVKSISQDIINELEKVIEKQQVELLGPVTPIISKLRGNYRLQIILKVYQHDTNFLLPIVEKFDKDIKVYFNPPTTIL
>NZ_LN824141.1|WP_045088322.1|1846587_1847178_+|ribosome-associated-translation-inhibitor-RaiA
MEYKVFTKSVELSEANKNYLAKRMSKPDHLLKKQKDLVSPADVRITKERGIYKVEITTHVKALSKIIKVEERSNDLYEAIDKVTDALERKIREIKTRLHPKNLSDKGIPVNPKEAVLTRTDNLDYEDEDEFSEKPVAPKIARVKHHDLTIMNVEEAILQMQLLGHSFFVFRDSTNDAVSVLYERKDGNLGLLVFNE
>NZ_LN824141.1|WP_045088323.1|1847224_1847467_-|glutathione-S-transferase-N-terminal-domain-containing-protein
MNDVKVIIYTTPTCPWCRKAKAYLNEKGVNFKEIDVSKDQKAAEELVRKTHQMGVPVIQIGNEYVIGFDKKRIDKLLGIN
>NZ_LN824141.1|WP_052670531.1|1847807_1848647_+|alpha/beta-fold-hydrolase
MFVPEGKIKGDIVFLHGIGPNNIPYLEWYGRYFSKIGYRTSVVIFPYHLERAPKGLQDGDPFYSSEPDECVVLFHNAVKDVRRTIDLLESFDDYSEDNLYLMGVSFGGIIGTMALALDKRIKKGILMITGGNWRWINFYSPFTQKVRDAYATQKNAYGCDSEEYCIKFRENAFDFVKDNINSIDDIFQKTPIPCYHYDPISYAKFVNQPVLFIKGTFDKIIPHRATNELIKLLPNKKVKYILAGHKSSYLWKSVVGRWVISFIEQGKLKEAEKKLQKTM
>NZ_LN824141.1|WP_045088324.1|1848654_1849179_-|hypothetical-protein
MVNAVNPDVYNPYIGYKLDPGEPGLSNSVPASLSILRVAAHEAGNINQFKSQAIKNGGVVIYTDIDLHFQKRGGFLAAVAGKSKAVILYKKENVISKPQENELPIPENEQEIENKIQQNVEKEIEKIKMQIMQETDPEKITKLLQKLQTLELLRNNASSLNAEFFLGLELDLSA
>NZ_LN824141.1|WP_045088325.1|1849207_1850455_-|hypothetical-protein
MNKKILISMIFVVLGIITFTQTYTFLFRDAQLYYVPTDQTTFQVPSGFEVLWVSGANTWRLEKNYQQFSFKIVSLEDYKNKLIQQIDENIFKIDGTNDILFYNSQINHWCITNEKNKDKITAATVKVVLEKPKNSKTSIIALKTSGTWKTVYEMKKDGTFKKNVEIEGKAVGTTNLYLVNEYLNLSTRDYVGNTKALALGSDRTTDFQSVVEEAILTQTYTINLGSIKFVSDTMNFSISENRVLSYEDRNVITFNLYTNLQDFTKTRLVRYIENTTYNGLGIDLPYGEVWIYEQYNDKNFPTKKSNIFDTPVGDMVKIDLGESWDVQYKIEKLSDVEVKTSDSRMIDFLITIKNFSDKIRVVQISATSPNIEIDQMTMDGGYRGLKDYSQTGKIDMSFEITDEVKIRMTVKTTLN

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	NC_014838	Pantoea sp. At-9b plasmid pPAT9B01, complete sequence	745589-745616	5	0.821
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	NZ_KY290886	Enterococcus faecalis strain Transconjugant T4 plasmid pJH-T4, complete sequence	69819-69846	6	0.786
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	NZ_CP027515	Enterococcus faecium strain AUSMDU00004028 plasmid unnamed3, complete sequence	26684-26711	6	0.786
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	NC_007594	Enterococcus faecium plasmid pHT beta, complete sequence	30483-30510	6	0.786
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	MN693111	Marine virus AFVG_25M354, complete genome	32667-32694	6	0.786
NZ_LN824141_12	12.28\|1136677\|37\|NZ_LN824141\|CRISPRCasFinder,CRT	1136677-1136713	37	NC_010371	Finegoldia magna ATCC 29328 plasmid pFMC, complete sequence	168591-168627	6	0.838
NZ_LN824141_12	12.79\|1136678\|37\|NZ_LN824141\|PILER-CR	1136678-1136714	37	NC_010371	Finegoldia magna ATCC 29328 plasmid pFMC, complete sequence	168591-168627	6	0.838
NZ_LN824141_15	15.1\|1317373\|31\|NZ_LN824141\|CRISPRCasFinder	1317373-1317403	31	NZ_AP019717	Clostridium butyricum strain NBRC 13949 plasmid pCBU1, complete sequence	535388-535418	6	0.806
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	MN693482	Marine virus AFVG_25M316, complete genome	9418-9447	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	MN693224	Marine virus AFVG_25M317, complete genome	9516-9545	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	MN693583	Marine virus AFVG_25M274, complete genome	9498-9527	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	NZ_CP013982	Staphylococcus equorum strain KM1031 plasmid unnamed2, complete sequence	2362-2391	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	NZ_CP013982	Staphylococcus equorum strain KM1031 plasmid unnamed2, complete sequence	27457-27486	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	NZ_MG205641	Paeniclostridium sordellii strain 7508-A plasmid pCS1-7, complete sequence	66118-66147	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	NZ_MG205642	Paeniclostridium sordellii strain 7543-A plasmid pCS1-6, complete sequence	66118-66147	7	0.767
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	MN693253	Marine virus AFVG_25M311, complete genome	15053-15082	7	0.767
NZ_LN824141_9	9.3\|1059657\|28\|NZ_LN824141\|CRISPRCasFinder	1059657-1059684	28	NZ_LR134399	Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence	208664-208691	7	0.75
NZ_LN824141_15	15.1\|1317373\|31\|NZ_LN824141\|CRISPRCasFinder	1317373-1317403	31	NZ_CP036489	Rahnella aquatilis strain MEM40 plasmid pMEM40-2, complete sequence	5514-5544	7	0.774
NZ_LN824141_9	9.2\|1059589\|30\|NZ_LN824141\|CRISPRCasFinder	1059589-1059618	30	MN065183	Bacillus phage vB_BthS-HD29phi, complete genome	11010-11039	8	0.733
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019135	Synechococcus phage ACG-2014a isolate Syn7803C101, complete genome	170734-170768	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019114	Synechococcus phage ACG-2014a isolate Syn7803US60, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019138	Synechococcus phage ACG-2014a isolate Syn7803C107, complete genome	170755-170789	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019122	Synechococcus phage ACG-2014a isolate Syn7803US79, complete genome	170745-170779	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019055	Synechococcus phage ACG-2014a isolate Syn7803C86, complete genome	170754-170788	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019038	Synechococcus phage ACG-2014a isolate Syn7803C59, complete genome	170533-170567	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019068	Synechococcus phage ACG-2014a isolate Syn7803US102, complete genome	170691-170725	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019137	Synechococcus phage ACG-2014a isolate Syn7803C104, complete genome	170749-170783	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019157	Synechococcus phage ACG-2014a isolate Syn7803C31, complete genome	170752-170786	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019087	Synechococcus phage ACG-2014a isolate Syn7803US19, complete genome	170698-170732	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019076	Synechococcus phage ACG-2014a isolate Syn7803US112, complete genome	171832-171866	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019065	Synechococcus phage ACG-2014a isolate Syn7803C99, complete genome	170639-170673	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019026	Synechococcus phage ACG-2014a isolate Syn7803C42, complete genome	170742-170776	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019081	Synechococcus phage ACG-2014a isolate Syn7803US117, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019033	Synechococcus phage ACG-2014a isolate Syn7803C53, complete genome	170495-170529	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019153	Synechococcus phage ACG-2014a isolate Syn7803C26, complete genome	170626-170660	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019158	Synechococcus phage ACG-2014a isolate Syn7803C33, complete genome	170752-170786	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019067	Synechococcus phage ACG-2014a isolate Syn7803US101, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019039	Synechococcus phage ACG-2014a isolate Syn7803C60, complete genome	170756-170790	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019030	Synechococcus phage ACG-2014a isolate Syn7803C47, complete genome	170739-170773	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019163	Synechococcus phage ACG-2014a isolate Syn7803C38, complete genome	170639-170673	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019116	Synechococcus phage ACG-2014a isolate Syn7803US62, complete genome	169863-169897	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019088	Synechococcus phage ACG-2014a isolate Syn7803US1, complete genome	170736-170770	8	0.771
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	KJ019084	Synechococcus phage ACG-2014a isolate Syn7803US123, complete genome	170643-170677	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019135	Synechococcus phage ACG-2014a isolate Syn7803C101, complete genome	170734-170768	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019114	Synechococcus phage ACG-2014a isolate Syn7803US60, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019138	Synechococcus phage ACG-2014a isolate Syn7803C107, complete genome	170755-170789	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019122	Synechococcus phage ACG-2014a isolate Syn7803US79, complete genome	170745-170779	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019055	Synechococcus phage ACG-2014a isolate Syn7803C86, complete genome	170754-170788	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019038	Synechococcus phage ACG-2014a isolate Syn7803C59, complete genome	170533-170567	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019068	Synechococcus phage ACG-2014a isolate Syn7803US102, complete genome	170691-170725	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019137	Synechococcus phage ACG-2014a isolate Syn7803C104, complete genome	170749-170783	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019157	Synechococcus phage ACG-2014a isolate Syn7803C31, complete genome	170752-170786	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019087	Synechococcus phage ACG-2014a isolate Syn7803US19, complete genome	170698-170732	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019076	Synechococcus phage ACG-2014a isolate Syn7803US112, complete genome	171832-171866	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019065	Synechococcus phage ACG-2014a isolate Syn7803C99, complete genome	170639-170673	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019026	Synechococcus phage ACG-2014a isolate Syn7803C42, complete genome	170742-170776	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019081	Synechococcus phage ACG-2014a isolate Syn7803US117, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019033	Synechococcus phage ACG-2014a isolate Syn7803C53, complete genome	170495-170529	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019153	Synechococcus phage ACG-2014a isolate Syn7803C26, complete genome	170626-170660	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019158	Synechococcus phage ACG-2014a isolate Syn7803C33, complete genome	170752-170786	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019067	Synechococcus phage ACG-2014a isolate Syn7803US101, complete genome	170652-170686	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019039	Synechococcus phage ACG-2014a isolate Syn7803C60, complete genome	170756-170790	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019030	Synechococcus phage ACG-2014a isolate Syn7803C47, complete genome	170739-170773	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019163	Synechococcus phage ACG-2014a isolate Syn7803C38, complete genome	170639-170673	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019116	Synechococcus phage ACG-2014a isolate Syn7803US62, complete genome	169863-169897	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019088	Synechococcus phage ACG-2014a isolate Syn7803US1, complete genome	170736-170770	8	0.771
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	KJ019084	Synechococcus phage ACG-2014a isolate Syn7803US123, complete genome	170643-170677	8	0.771
NZ_LN824141_15	15.1\|1317373\|31\|NZ_LN824141\|CRISPRCasFinder	1317373-1317403	31	NC_015386	Treponema succinifaciens DSM 2489 plasmid pTRESU01, complete sequence	78606-78636	8	0.742
NZ_LN824141_15	15.1\|1317373\|31\|NZ_LN824141\|CRISPRCasFinder	1317373-1317403	31	NZ_CP031220	Arcobacter mytili LMG 24559 plasmid pAMYT, complete sequence	23225-23255	8	0.742
NZ_LN824141_17	17.1\|1824174\|35\|NZ_LN824141\|CRISPRCasFinder	1824174-1824208	35	MN693413	Marine virus AFVG_25M209, complete genome	19322-19356	8	0.771
NZ_LN824141_18	18.1\|1839066\|35\|NZ_LN824141\|CRISPRCasFinder	1839066-1839100	35	MK817115	Escherichia phage vB_EcoM_phAPEC6, complete genome	182743-182777	8	0.771
NZ_LN824141_18	18.1\|1839066\|35\|NZ_LN824141\|CRISPRCasFinder	1839066-1839100	35	LC494302	Escherichia phage SP27 DNA, complete genome	293791-293825	8	0.771
NZ_LN824141_18	18.1\|1839066\|35\|NZ_LN824141\|CRISPRCasFinder	1839066-1839100	35	LT603033	Escherichia phage vB_Eco_slurp01 genome assembly, chromosome: I	235301-235335	8	0.771
NZ_LN824141_12	12.41\|1137543\|38\|NZ_LN824141\|CRISPRCasFinder,CRT	1137543-1137580	38	NZ_CP007625	Bacillus pseudomycoides strain 219298 plasmid unnamed, complete sequence	24519-24556	9	0.763
NZ_LN824141_12	12.41\|1137543\|38\|NZ_LN824141\|CRISPRCasFinder,CRT	1137543-1137580	38	NZ_CP009650	Bacillus pseudomycoides strain BTZ plasmid pBTZ_1, complete sequence	203241-203278	9	0.763
NZ_LN824141_12	12.41\|1137543\|38\|NZ_LN824141\|CRISPRCasFinder,CRT	1137543-1137580	38	MN812239	Flavobacterium phage vB_FspS_tant8-1, complete genome	3228-3265	9	0.763
NZ_LN824141_12	12.92\|1137544\|38\|NZ_LN824141\|PILER-CR	1137544-1137581	38	NZ_CP007625	Bacillus pseudomycoides strain 219298 plasmid unnamed, complete sequence	24519-24556	9	0.763
NZ_LN824141_12	12.92\|1137544\|38\|NZ_LN824141\|PILER-CR	1137544-1137581	38	NZ_CP009650	Bacillus pseudomycoides strain BTZ plasmid pBTZ_1, complete sequence	203241-203278	9	0.763
NZ_LN824141_12	12.92\|1137544\|38\|NZ_LN824141\|PILER-CR	1137544-1137581	38	MN812239	Flavobacterium phage vB_FspS_tant8-1, complete genome	3228-3265	9	0.763
NZ_LN824141_12	12.14\|1135741\|37\|NZ_LN824141\|CRISPRCasFinder,CRT	1135741-1135777	37	NZ_LR134399	Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence	165100-165136	10	0.73
NZ_LN824141_12	12.43\|1137679\|35\|NZ_LN824141\|CRISPRCasFinder,CRT	1137679-1137713	35	NZ_CP033462	Brevibacillus laterosporus strain 1821L plasmid p1821L02, complete sequence	31874-31908	10	0.714
NZ_LN824141_12	12.65\|1135742\|37\|NZ_LN824141\|PILER-CR	1135742-1135778	37	NZ_LR134399	Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence	165100-165136	10	0.73
NZ_LN824141_12	12.94\|1137680\|35\|NZ_LN824141\|PILER-CR	1137680-1137714	35	NZ_CP033462	Brevibacillus laterosporus strain 1821L plasmid p1821L02, complete sequence	31874-31908	10	0.714
NZ_LN824141_14	14.1\|1306043\|33\|NZ_LN824141\|CRISPRCasFinder	1306043-1306075	33	CP015514	Vibrio vulnificus strain FORC_036 plasmid unnamed, complete sequence	305222-305254	10	0.697

1. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to NC_014838 (Pantoea sp. At-9b plasmid pPAT9B01, complete sequence) position: , mismatch: 5, identity: 0.821

aaaaaatcaattcacatttttt-gctacg	CRISPR spacer
aaaaaatcaattcaccttttttaaatat-	Protospacer
*************** ****** . **.

2. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to NZ_KY290886 (Enterococcus faecalis strain Transconjugant T4 plasmid pJH-T4, complete sequence) position: , mismatch: 6, identity: 0.786

aaaaaatcaattcacattttttgctacg	CRISPR spacer
tcaaaatcacttcatattttttgctatc	Protospacer
  ******* ****.***********.

3. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to NZ_CP027515 (Enterococcus faecium strain AUSMDU00004028 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.786

aaaaaatcaattcacattttttgctacg	CRISPR spacer
tcaaaatcacttcatattttttgctatc	Protospacer
  ******* ****.***********.

4. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to NC_007594 (Enterococcus faecium plasmid pHT beta, complete sequence) position: , mismatch: 6, identity: 0.786

aaaaaatcaattcacattttttgctacg	CRISPR spacer
tcaaaatcacttcatattttttgctatc	Protospacer
  ******* ****.***********.

5. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to MN693111 (Marine virus AFVG_25M354, complete genome) position: , mismatch: 6, identity: 0.786

aaaaaatcaattcacattttttgctacg	CRISPR spacer
aaaaaatcaattcacttttttttatgtc	Protospacer
*************** ******  *..

6. spacer 12.28|1136677|37|NZ_LN824141|CRISPRCasFinder,CRT matches to NC_010371 (Finegoldia magna ATCC 29328 plasmid pFMC, complete sequence) position: , mismatch: 6, identity: 0.838

-atattttagctttgtgtatttgtctgttatgctttct	CRISPR spacer
gataattt-gctttgtgtatttgtctattatggcatct	Protospacer
 *** *** *****************.***** . ***

7. spacer 12.79|1136678|37|NZ_LN824141|PILER-CR matches to NC_010371 (Finegoldia magna ATCC 29328 plasmid pFMC, complete sequence) position: , mismatch: 6, identity: 0.838

-atattttagctttgtgtatttgtctgttatgctttct	CRISPR spacer
gataattt-gctttgtgtatttgtctattatggcatct	Protospacer
 *** *** *****************.***** . ***

8. spacer 15.1|1317373|31|NZ_LN824141|CRISPRCasFinder matches to NZ_AP019717 (Clostridium butyricum strain NBRC 13949 plasmid pCBU1, complete sequence) position: , mismatch: 6, identity: 0.806

actttgagaaaagtttcagatattaaaaaat	CRISPR spacer
aattatggaaaagtttaagatattacaaaat	Protospacer
* **  .********* ******** *****

9. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to MN693482 (Marine virus AFVG_25M316, complete genome) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
tcctcataaattcataaaatggttttttat	Protospacer
     **************** *** ****

10. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to MN693224 (Marine virus AFVG_25M317, complete genome) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
tcctcataaattcataaaatggttttttat	Protospacer
     **************** *** ****

11. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to MN693583 (Marine virus AFVG_25M274, complete genome) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
tcctcataaattcataaaatggttttttat	Protospacer
     **************** *** ****

12. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to NZ_CP013982 (Staphylococcus equorum strain KM1031 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
taccagtaaattcagaaaatgttttattat	Protospacer
 *  ..******** **********.****

13. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to NZ_CP013982 (Staphylococcus equorum strain KM1031 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
taccagtaaattcagaaaatgttttattat	Protospacer
 *  ..******** **********.****

14. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to NZ_MG205641 (Paeniclostridium sordellii strain 7508-A plasmid pCS1-7, complete sequence) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
aggttataaattcaaataatgttttgtttt	Protospacer
*..  ********* * *********** *

15. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to NZ_MG205642 (Paeniclostridium sordellii strain 7543-A plasmid pCS1-6, complete sequence) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
aggttataaattcaaataatgttttgtttt	Protospacer
*..  ********* * *********** *

16. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to MN693253 (Marine virus AFVG_25M311, complete genome) position: , mismatch: 7, identity: 0.767

aaaagataaattcataaaatgttttgttat	CRISPR spacer
aaaagataaatttataaaatattataatga	Protospacer
************.*******.** *. *.

17. spacer 9.3|1059657|28|NZ_LN824141|CRISPRCasFinder matches to NZ_LR134399 (Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence) position: , mismatch: 7, identity: 0.75

aaaaaatcaattcacattttttgctacg	CRISPR spacer
ccgcaatcaattcacattttttattacc	Protospacer
  . ******************..***

18. spacer 15.1|1317373|31|NZ_LN824141|CRISPRCasFinder matches to NZ_CP036489 (Rahnella aquatilis strain MEM40 plasmid pMEM40-2, complete sequence) position: , mismatch: 7, identity: 0.774

actttgagaaaagtttcagatattaaaaaat	CRISPR spacer
tttttttaaaaagtttaagacattaaaaaat	Protospacer
 .***  .******** ***.**********

19. spacer 9.2|1059589|30|NZ_LN824141|CRISPRCasFinder matches to MN065183 (Bacillus phage vB_BthS-HD29phi, complete genome) position: , mismatch: 8, identity: 0.733

aaaagataaattcataaaatgttttgttat	CRISPR spacer
catttatcaattcatcaaatgttttgttca	Protospacer
 *   ** ******* ************

20. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019135 (Synechococcus phage ACG-2014a isolate Syn7803C101, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

21. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019114 (Synechococcus phage ACG-2014a isolate Syn7803US60, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

22. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019138 (Synechococcus phage ACG-2014a isolate Syn7803C107, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

23. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019122 (Synechococcus phage ACG-2014a isolate Syn7803US79, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

24. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019055 (Synechococcus phage ACG-2014a isolate Syn7803C86, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

25. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019038 (Synechococcus phage ACG-2014a isolate Syn7803C59, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

26. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019068 (Synechococcus phage ACG-2014a isolate Syn7803US102, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

27. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019137 (Synechococcus phage ACG-2014a isolate Syn7803C104, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

28. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019157 (Synechococcus phage ACG-2014a isolate Syn7803C31, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

29. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019087 (Synechococcus phage ACG-2014a isolate Syn7803US19, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

30. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019076 (Synechococcus phage ACG-2014a isolate Syn7803US112, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

31. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019065 (Synechococcus phage ACG-2014a isolate Syn7803C99, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

32. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019026 (Synechococcus phage ACG-2014a isolate Syn7803C42, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

33. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019081 (Synechococcus phage ACG-2014a isolate Syn7803US117, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

34. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019033 (Synechococcus phage ACG-2014a isolate Syn7803C53, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

35. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019153 (Synechococcus phage ACG-2014a isolate Syn7803C26, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

36. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019158 (Synechococcus phage ACG-2014a isolate Syn7803C33, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

37. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019067 (Synechococcus phage ACG-2014a isolate Syn7803US101, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

38. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019039 (Synechococcus phage ACG-2014a isolate Syn7803C60, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

39. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019030 (Synechococcus phage ACG-2014a isolate Syn7803C47, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

40. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019163 (Synechococcus phage ACG-2014a isolate Syn7803C38, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

41. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019116 (Synechococcus phage ACG-2014a isolate Syn7803US62, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

42. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019088 (Synechococcus phage ACG-2014a isolate Syn7803US1, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

43. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to KJ019084 (Synechococcus phage ACG-2014a isolate Syn7803US123, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

44. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019135 (Synechococcus phage ACG-2014a isolate Syn7803C101, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

45. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019114 (Synechococcus phage ACG-2014a isolate Syn7803US60, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

46. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019138 (Synechococcus phage ACG-2014a isolate Syn7803C107, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

47. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019122 (Synechococcus phage ACG-2014a isolate Syn7803US79, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

48. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019055 (Synechococcus phage ACG-2014a isolate Syn7803C86, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

49. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019038 (Synechococcus phage ACG-2014a isolate Syn7803C59, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

50. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019068 (Synechococcus phage ACG-2014a isolate Syn7803US102, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

51. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019137 (Synechococcus phage ACG-2014a isolate Syn7803C104, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

52. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019157 (Synechococcus phage ACG-2014a isolate Syn7803C31, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

53. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019087 (Synechococcus phage ACG-2014a isolate Syn7803US19, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

54. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019076 (Synechococcus phage ACG-2014a isolate Syn7803US112, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

55. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019065 (Synechococcus phage ACG-2014a isolate Syn7803C99, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

56. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019026 (Synechococcus phage ACG-2014a isolate Syn7803C42, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

57. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019081 (Synechococcus phage ACG-2014a isolate Syn7803US117, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

58. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019033 (Synechococcus phage ACG-2014a isolate Syn7803C53, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

59. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019153 (Synechococcus phage ACG-2014a isolate Syn7803C26, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

60. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019158 (Synechococcus phage ACG-2014a isolate Syn7803C33, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

61. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019067 (Synechococcus phage ACG-2014a isolate Syn7803US101, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

62. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019039 (Synechococcus phage ACG-2014a isolate Syn7803C60, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

63. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019030 (Synechococcus phage ACG-2014a isolate Syn7803C47, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

64. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019163 (Synechococcus phage ACG-2014a isolate Syn7803C38, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

65. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019116 (Synechococcus phage ACG-2014a isolate Syn7803US62, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

66. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019088 (Synechococcus phage ACG-2014a isolate Syn7803US1, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

67. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to KJ019084 (Synechococcus phage ACG-2014a isolate Syn7803US123, complete genome) position: , mismatch: 8, identity: 0.771

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ggatatgtcaaagcattcgataaaaatttaaaaga	Protospacer
  ***.   ***.******* **************

68. spacer 15.1|1317373|31|NZ_LN824141|CRISPRCasFinder matches to NC_015386 (Treponema succinifaciens DSM 2489 plasmid pTRESU01, complete sequence) position: , mismatch: 8, identity: 0.742

actttgagaaaagtttcagatattaaaaaat	CRISPR spacer
gcagctaaaaaagtttcagatattagaatat	Protospacer
.*  . *.*****************.** **

69. spacer 15.1|1317373|31|NZ_LN824141|CRISPRCasFinder matches to NZ_CP031220 (Arcobacter mytili LMG 24559 plasmid pAMYT, complete sequence) position: , mismatch: 8, identity: 0.742

actttgagaaaagtttcagatattaaaaaat	CRISPR spacer
tgttattcaaaagtttaagaaattaaaaaat	Protospacer
  **    ******** *** **********

70. spacer 17.1|1824174|35|NZ_LN824141|CRISPRCasFinder matches to MN693413 (Marine virus AFVG_25M209, complete genome) position: , mismatch: 8, identity: 0.771

aagggtc---tccatttggatttgcatcttttactgaa	CRISPR spacer
---ggtttaatccatttggctttgcatcttctactcca	Protospacer
   ***.   ********* **********.****  *

71. spacer 18.1|1839066|35|NZ_LN824141|CRISPRCasFinder matches to MK817115 (Escherichia phage vB_EcoM_phAPEC6, complete genome) position: , mismatch: 8, identity: 0.771

caattcaaaaagcttttttacaaaattttcatttc	CRISPR spacer
caattcaaaaaccttttttataaaagggcaatttt	Protospacer
*********** ********.****   . ****.

72. spacer 18.1|1839066|35|NZ_LN824141|CRISPRCasFinder matches to LC494302 (Escherichia phage SP27 DNA, complete genome) position: , mismatch: 8, identity: 0.771

caattcaaaaagcttttttacaaaattttcatttc	CRISPR spacer
caattcaaaaaccttttttataaaagggcaatttt	Protospacer
*********** ********.****   . ****.

73. spacer 18.1|1839066|35|NZ_LN824141|CRISPRCasFinder matches to LT603033 (Escherichia phage vB_Eco_slurp01 genome assembly, chromosome: I) position: , mismatch: 8, identity: 0.771

caattcaaaaagcttttttacaaaattttcatttc	CRISPR spacer
caattcaaaaaccttttttataaaagggcaatttt	Protospacer
*********** ********.****   . ****.

74. spacer 12.41|1137543|38|NZ_LN824141|CRISPRCasFinder,CRT matches to NZ_CP007625 (Bacillus pseudomycoides strain 219298 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagatttcaagaaagtaattgatataaaagcttc	Protospacer
***********.********.*******  *.**..

75. spacer 12.41|1137543|38|NZ_LN824141|CRISPRCasFinder,CRT matches to NZ_CP009650 (Bacillus pseudomycoides strain BTZ plasmid pBTZ_1, complete sequence) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagatttcaagaaagtaattgatataaaagcttc	Protospacer
***********.********.*******  *.**..

76. spacer 12.41|1137543|38|NZ_LN824141|CRISPRCasFinder,CRT matches to MN812239 (Flavobacterium phage vB_FspS_tant8-1, complete genome) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagattttaaaaacgtgattgatttcaaggttgc	Protospacer
**************.** *********  .*..**.*

77. spacer 12.92|1137544|38|NZ_LN824141|PILER-CR matches to NZ_CP007625 (Bacillus pseudomycoides strain 219298 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagatttcaagaaagtaattgatataaaagcttc	Protospacer
***********.********.*******  *.**..

78. spacer 12.92|1137544|38|NZ_LN824141|PILER-CR matches to NZ_CP009650 (Bacillus pseudomycoides strain BTZ plasmid pBTZ_1, complete sequence) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagatttcaagaaagtaattgatataaaagcttc	Protospacer
***********.********.*******  *.**..

79. spacer 12.92|1137544|38|NZ_LN824141|PILER-CR matches to MN812239 (Flavobacterium phage vB_FspS_tant8-1, complete genome) position: , mismatch: 9, identity: 0.763

atagaagattttaagaaagtgattgataatagagtcga	CRISPR spacer
atagaagattttaaaaacgtgattgatttcaaggttgc	Protospacer
**************.** *********  .*..**.*

80. spacer 12.14|1135741|37|NZ_LN824141|CRISPRCasFinder,CRT matches to NZ_LR134399 (Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence) position: , mismatch: 10, identity: 0.73

agatgctatttcaaaatcatgtgcattaggtttgatg	CRISPR spacer
aggagtaatttcaaaatcatatgcaataggttttgaa	Protospacer
**. *. *************.**** ******* . .

81. spacer 12.43|1137679|35|NZ_LN824141|CRISPRCasFinder,CRT matches to NZ_CP033462 (Brevibacillus laterosporus strain 1821L plasmid p1821L02, complete sequence) position: , mismatch: 10, identity: 0.714

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ttagaccagaaaccattcgaaaaaaacacatgtcc	Protospacer
*** ******** *************. .* .

82. spacer 12.65|1135742|37|NZ_LN824141|PILER-CR matches to NZ_LR134399 (Listeria monocytogenes strain NCTC7974 plasmid 2, complete sequence) position: , mismatch: 10, identity: 0.73

agatgctatttcaaaatcatgtgcattaggtttgatg	CRISPR spacer
aggagtaatttcaaaatcatatgcaataggttttgaa	Protospacer
**. *. *************.**** ******* . .

83. spacer 12.94|1137680|35|NZ_LN824141|PILER-CR matches to NZ_CP033462 (Brevibacillus laterosporus strain 1821L plasmid p1821L02, complete sequence) position: , mismatch: 10, identity: 0.714

ttataccagaaaacattcgaaaaaaatttaaaaga	CRISPR spacer
ttagaccagaaaccattcgaaaaaaacacatgtcc	Protospacer
*** ******** *************. .* .

84. spacer 14.1|1306043|33|NZ_LN824141|CRISPRCasFinder matches to CP015514 (Vibrio vulnificus strain FORC_036 plasmid unnamed, complete sequence) position: , mismatch: 10, identity: 0.697

acaataattaaattatggctttttaatacttgc	CRISPR spacer
ttaataattaaattattgcattttaaccttatt	Protospacer
 .************** ** ******. .*  .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

294314 : 303212

Indivirus(16.67%)

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_045087206.1\|294314_296768_-	DNA mismatch repair protein MutS	A0A1V0SDQ0	Indivirus	3.1e-45	26.4
WP_045087207.1\|296855_297470_-	ATP-dependent Clp endopeptidase proteolytic subunit ClpP	A0A223W000	Agrobacterium_phage	1.8e-50	52.6
WP_045087208.1\|297471_297762_-	DUF370 domain-containing protein	NA	NA	NA	NA
WP_045087209.1\|297885_298143_-	hypothetical protein	NA	NA	NA	NA
WP_052670238.1\|298195_299599_-	exodeoxyribonuclease VII large subunit	G5CRZ1	Megavirus	1.8e-21	27.5
WP_045087210.1\|299576_300257_-	16S rRNA (cytidine(1402)-2'-O)-methyltransferase	M1PLC5	Streptococcus_phage	4.7e-36	40.7
WP_045087211.1\|300296_300857_-	hypothetical protein	NA	NA	NA	NA
WP_045087212.1\|301136_301394_+	acyl carrier protein	A0A1P8VVJ5	Erythrobacter_phage	3.6e-05	35.9
WP_045087213.1\|301613_303212_+	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	1.1e-112	42.1

DBSCAN-SWA_2

884741 : 893171

Bacillus_phage(33.33%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_052670356.1\|884741_885368_-	hypothetical protein	Q331Y3	Clostridium_botulinum_C_phage	4.5e-49	57.3
WP_045087653.1\|886308_887262_+\|tRNA	tRNA lysidine(34) synthetase TilS	A0A0U2S5Z2	Escherichia_phage	1.0e-07	22.5
WP_084217307.1\|887345_889229_+	ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein	H8ZJI5	Ostreococcus_tauri_virus	8.1e-110	42.5
WP_045087654.1\|889188_889626_+	hypothetical protein	NA	NA	NA	NA
WP_045087655.1\|889710_890439_+	response regulator transcription factor	W8CYM9	Bacillus_phage	5.8e-40	40.1
WP_045087656.1\|890571_891858_+	two-component sensor histidine kinase	W8CYF6	Bacillus_phage	5.5e-25	31.8
WP_045087657.1\|891860_893171_+	thymidine phosphorylase	A0A0H3UZD4	Geobacillus_virus	2.4e-105	52.1

DBSCAN-SWA_3

1162713 : 1240219

Erysipelothrix_phage(64.1%)

head,portal,terminase,capsid,tail,transposase,tRNA,holin,protease

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_045087853.1\|1162713_1164636_-\|tRNA	threonine--tRNA ligase	A0A2K9L297	Tupanvirus	1.1e-143	41.2
WP_045088638.1\|1164659_1165724_-	peptide chain release factor 1	W8EDB3	Pseudomonas_phage	4.7e-06	48.2
WP_045087854.1\|1166031_1166907_-	DegV family protein	NA	NA	NA	NA
WP_045087855.1\|1167063_1169064_-	methyl-accepting chemotaxis protein	A0A2H4J162	uncultured_Caudovirales_phage	1.8e-11	42.0
WP_045087856.1\|1169121_1169610_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_045087857.1\|1169781_1170969_-	glycoside hydrolase family 18 protein	A0A2K9KZQ8	Tupanvirus	4.9e-36	31.1
WP_045088639.1\|1170975_1172229_-	carbohydrate ABC transporter permease	NA	NA	NA	NA
WP_045087858.1\|1172234_1173107_-	sugar ABC transporter permease	NA	NA	NA	NA
WP_045087859.1\|1173223_1174429_-	extracellular solute-binding protein	NA	NA	NA	NA
WP_052670397.1\|1174532_1175954_-	hypothetical protein	NA	NA	NA	NA
WP_045087861.1\|1175968_1177054_-	ROK family transcriptional regulator	NA	NA	NA	NA
WP_084217196.1\|1177378_1177843_+	purine-binding chemotaxis protein CheW	NA	NA	NA	NA
WP_045087862.1\|1177905_1178181_-	carbon storage regulator CsrA	NA	NA	NA	NA
WP_045087863.1\|1178183_1178657_-	flagellar assembly protein FliW	NA	NA	NA	NA
WP_045087864.1\|1178674_1179559_-	flagellar hook-associated protein FlgL	NA	NA	NA	NA
WP_171820594.1\|1179577_1181983_-	flagellar hook-associated protein FlgK	NA	NA	NA	NA
WP_144403486.1\|1181993_1182488_-	hypothetical protein	NA	NA	NA	NA
WP_045087867.1\|1182492_1182762_-	flagellar biosynthesis anti-sigma factor FlgM	NA	NA	NA	NA
WP_045087868.1\|1183043_1183694_+	peroxiredoxin	NA	NA	NA	NA
WP_045087869.1\|1183762_1185106_-	magnesium transporter	NA	NA	NA	NA
WP_045087870.1\|1186331_1187405_+	aminopeptidase P family protein	NA	NA	NA	NA
WP_045087871.1\|1187521_1188103_+	cyclodeaminase/cyclohydrolase family protein	NA	NA	NA	NA
WP_045087872.1\|1188103_1189231_+\|tRNA	tRNA guanosine(34) transglycosylase Tgt	A0A1B1IVQ4	uncultured_Mediterranean_phage	5.0e-83	44.8
WP_045087873.1\|1189249_1189606_+	hypothetical protein	NA	NA	NA	NA
WP_045087874.1\|1189701_1190094_+	VanZ family protein	NA	NA	NA	NA
WP_171820595.1\|1190161_1191934_+	hypothetical protein	NA	NA	NA	NA
WP_045087875.1\|1191944_1194806_+	hypothetical protein	NA	NA	NA	NA
WP_144403488.1\|1195165_1195726_+	hypothetical protein	Q331Y3	Clostridium_botulinum_C_phage	9.9e-48	56.3
WP_045087876.1\|1195937_1197095_+	23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD	A0A2K5B251	Erysipelothrix_phage	1.3e-46	34.6
WP_045087878.1\|1197615_1200507_+	DEAD/DEAH box helicase family protein	NA	NA	NA	NA
WP_045087879.1\|1200507_1202451_+	site-specific DNA-methyltransferase	A0A0H3UZ66	Geobacillus_virus	1.9e-29	34.6
WP_045087880.1\|1202651_1204124_+\|transposase	IS21 family transposase	A0A2L1IVA1	Escherichia_phage	1.4e-16	26.3
WP_012032690.1\|1204116_1204803_+	ATP-binding protein	A0A2L1IVB6	Escherichia_phage	3.2e-08	22.5
WP_003515999.1\|1205067_1205619_+\|terminase	P27 family phage terminase small subunit	A0A2K5B277	Erysipelothrix_phage	3.1e-70	68.1
WP_045087881.1\|1205775_1207074_+	DNA modification methylase	A0A2I4R670	Erysipelothrix_phage	3.6e-77	40.5
WP_045087882.1\|1207079_1208333_+	DNA modification methylase	A0A2I4R670	Erysipelothrix_phage	1.3e-100	46.5
WP_045087883.1\|1208449_1209142_+	virulence factor	A0A2K5B280	Erysipelothrix_phage	1.1e-27	34.8
WP_045087884.1\|1209134_1209470_+	hypothetical protein	NA	NA	NA	NA
WP_045088643.1\|1209840_1210740_+	amidoligase family protein	A0A2K9V489	Faecalibacterium_phage	2.8e-52	40.8
WP_013782360.1\|1210801_1211269_+	gamma-glutamylcyclotransferase	NA	NA	NA	NA
WP_004464027.1\|1211272_1211467_+	DUF5049 domain-containing protein	NA	NA	NA	NA
WP_045087885.1\|1211521_1213171_+\|terminase	terminase large subunit	A0A2K5B285	Erysipelothrix_phage	1.3e-249	77.5
WP_008409535.1\|1213167_1213572_-	hypothetical protein	NA	NA	NA	NA
WP_045087886.1\|1213679_1214945_+\|portal	phage portal protein	A0A2K5B287	Erysipelothrix_phage	2.6e-189	76.1
WP_045087887.1\|1214941_1215670_+\|protease	Clp protease ClpP	A0A2K5B288	Erysipelothrix_phage	9.5e-75	64.4
WP_023062540.1\|1215720_1216923_+\|capsid	phage major capsid protein	A0A2I4R671	Erysipelothrix_phage	4.9e-177	78.2
WP_045087888.1\|1216943_1217252_+\|head,tail	phage gp6-like head-tail connector protein	A0A2K5B290	Erysipelothrix_phage	2.3e-38	74.5
WP_045087889.1\|1217359_1217695_+\|head,tail	head-tail adaptor protein	A0A2K5B291	Erysipelothrix_phage	2.1e-29	58.7
WP_045087890.1\|1217711_1218143_+	HK97 gp10 family phage protein	A0A2K5B292	Erysipelothrix_phage	1.2e-45	62.2
WP_045087891.1\|1218139_1218484_+	hypothetical protein	A0A2K5B293	Erysipelothrix_phage	7.5e-30	55.0
WP_004464008.1\|1218489_1219089_+\|tail	phage tail protein	A0A2K5B294	Erysipelothrix_phage	3.1e-79	74.2
WP_014256679.1\|1219088_1219472_+	hypothetical protein	A0A2K5B295	Erysipelothrix_phage	5.7e-39	68.0
WP_045087892.1\|1219468_1219660_+	hypothetical protein	A0A2K5B296	Erysipelothrix_phage	1.9e-11	73.2
WP_045087893.1\|1219687_1221874_+\|tail	phage tail protein	A0A2K5B297	Erysipelothrix_phage	1.8e-12	38.3
WP_045087894.1\|1221887_1222661_+\|tail	phage tail family protein	A0A2I4R672	Erysipelothrix_phage	3.2e-73	51.6
WP_045087895.1\|1222665_1225188_+\|tail	phage tail protein	A0A2K5B298	Erysipelothrix_phage	0.0e+00	63.2
WP_045087896.1\|1225406_1226195_-	23S ribosomal RNA methyltransferase Erm	E4ZFQ0	Streptococcus_phage	8.8e-34	35.6
WP_045087897.1\|1226406_1226982_+	hypothetical protein	A0A2K5B2A0	Erysipelothrix_phage	2.1e-53	52.9
WP_045087898.1\|1226978_1229447_+	glycosyl hydrolase	A0A2K5B2A1	Erysipelothrix_phage	0.0e+00	68.3
WP_045087899.1\|1229533_1229953_+\|holin	phage holin family protein	A0A2K5B2A2	Erysipelothrix_phage	4.6e-50	67.6
WP_028992648.1\|1231007_1231226_+	hypothetical protein	NA	NA	NA	NA
WP_045087900.1\|1231287_1232856_+	recombinase family protein	A0A2K5B2B2	Erysipelothrix_phage	6.2e-148	52.3
WP_084217198.1\|1232819_1233311_+	recombinase	A0A2K5B2B3	Erysipelothrix_phage	1.1e-21	43.1
WP_045087902.1\|1233273_1234842_+	recombinase family protein	A0A2K5B2B4	Erysipelothrix_phage	1.1e-171	57.9
WP_004103228.1\|1235341_1235716_+	winged helix-turn-helix transcriptional regulator	E4ZFI8	Streptococcus_phage	5.1e-16	41.1
WP_045087903.1\|1235729_1238090_+	cadmium-translocating P-type ATPase	E4ZFI9	Streptococcus_phage	1.2e-113	34.9
WP_004103231.1\|1238176_1238641_+	signal peptidase II	NA	NA	NA	NA
WP_045087904.1\|1238798_1239284_+	copper chaperone Copz family protein	NA	NA	NA	NA
WP_045087905.1\|1239706_1240219_+	helix-turn-helix domain-containing protein	A5GZ65	Lactococcus_phage	1.7e-06	35.4

DBSCAN-SWA_4

1538077 : 1545321

Prochlorococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_045088099.1\|1538077_1538494_+	AIR carboxylase family protein	A0A2P0VNU7	Tetraselmis_virus	1.5e-13	42.9
WP_045088100.1\|1538493_1539210_+	phosphoribosylaminoimidazolesuccinocarboxamide synthase	E3SPA9	Prochlorococcus_phage	8.8e-41	40.9
WP_045088101.1\|1539206_1539479_+	phosphoribosylformylglycinamidine synthase subunit PurS	NA	NA	NA	NA
WP_052670428.1\|1539485_1540154_+	phosphoribosylformylglycinamidine synthase I	NA	NA	NA	NA
WP_045088102.1\|1540146_1542342_+	phosphoribosylformylglycinamidine synthase subunit PurL	A6N228	Microbacterium_phage	1.3e-122	36.2
WP_045088103.1\|1542335_1543700_+	amidophosphoribosyltransferase	A0A1B1ISH6	uncultured_Mediterranean_phage	6.6e-53	31.2
WP_045088104.1\|1543722_1544700_+	phosphoribosylformylglycinamidine cyclo-ligase	A0A0E3FZ01	Synechococcus_phage	2.1e-53	42.0
WP_045088105.1\|1544751_1545321_+	phosphoribosylglycinamide formyltransferase	E3SNR5	Prochlorococcus_phage	2.0e-24	39.1

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_LN824141

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection