CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Prophage number
NZ_CP043960	Streptomyces tendae strain 139 plasmid unnamed1, complete sequence	0 crisprs	NA	2
NZ_CP043961	Streptomyces tendae strain 139 plasmid unnamed2, complete sequence	0 crisprs	NA	0
NZ_CP043959	Streptomyces tendae strain 139 chromosome, complete genome	16 crisprs	csa3,DinG,DEDDh,cas4,WYL,casR,Cas9_archaeal,cas3	2

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP043959_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_1

33767-33873

Orphan

Consensus_repeat	Method
GCGGCCGGCGGGTAGCCGTAACCGCCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_1

>merge|NZ_CP043959|1|33767-33873|CRISPRCasFinder
GCGGCCGGCGGGTAGCCGTAACCGCCGGGACGTCCGCCGGGCGGCGGCGCGGCCGGCATGGGCGGGGCGCCCGCGGGGGCGGCCGGCGGGTAGCCGTAGCCGCCGGG

>NZ_CP043959|1|1|33767-33873|CRISPRCasFinder
GCGGCCGGCGGGTAGCCGTAACCGCCGGG	ACGTCCGCCGGGCGGCGGCGCGGCCGGCATGGGCGGGGCGCCCGCGGGG
GCGGCCGGCGGGTAGCCGTAGCCGCCGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_145829410.1\|37371_38211_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|99751
NZ_CP043959.1\|WP_150150814.1\|32927_33434_-\|FHA-domain-containing-protein	unknown	unknown	gnl\|CDD\|366133
NZ_CP043959.1\|WP_150150820.1\|40243_40981_-\|phenylacetate-CoA-oxygenase-subunit-PaaC	unknown	unknown	gnl\|CDD\|368300
NZ_CP043959.1\|WP_150157162.1\|38264_38594_+\|rhodanese-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|238089
NZ_CP043959.1\|WP_150157160.1\|31256_32795_-\|Stp1/IreP-family-PP2C-type-Ser/Thr-phosphatase	unknown	unknown	gnl\|CDD\|223704
NZ_CP043959.1\|WP_150150822.1\|40977_41265_-\|1,2-phenylacetyl-CoA-epoxidase-subunit-B	unknown	unknown	gnl\|CDD\|237504
NZ_CP043959.1\|WP_150150808.1\|25318_26083_+\|class-E-sortase	unknown	unknown	gnl\|CDD\|320679
NZ_CP043959.1\|WP_145829412.1\|29792_31229_-\|FtsW/RodA/SpoVE-family-cell-cycle-protein	unknown	unknown	gnl\|CDD\|223843
NZ_CP043959.1\|WP_167534426.1\|35428_36958_+\|DUF2252-family-protein	unknown	unknown	gnl\|CDD\|313268
NZ_CP043959.1\|WP_145829417.1\|23515_24154_+\|aminodeoxychorismate/anthranilate-synthase-component-II	unknown	unknown	gnl\|CDD\|181107
NZ_CP043959.1\|WP_145829406.1\|41261_42278_-\|1,2-phenylacetyl-CoA-epoxidase-subunit-A	unknown	unknown	gnl\|CDD\|184320
NZ_CP043959.1\|WP_150150812.1\|28320_29796_-\|penicillin-binding-protein-2	unknown	unknown	gnl\|CDD\|223839
NZ_CP043959.1\|WP_150150806.1\|24150_25305_+\|class-E-sortase	unknown	unknown	gnl\|CDD\|320679
NZ_CP043959.1\|WP_150150818.1\|39710_40250_-\|phenylacetate-CoA-oxygenase-subunit-PaaJ	unknown	unknown	gnl\|CDD\|131214
NZ_CP043959.1\|WP_150150826.1\|43701_44946_+\|HTTM-domain-containing-protein	unknown	unknown	gnl\|CDD\|214802
NZ_CP043959.1\|WP_150150824.1\|42592_43705_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236090
NZ_CP043959.1\|WP_019526631.1\|23309_23519_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150150810.1\|26180_28151_-\|Stk1-family-PASTA-domain-containing-Ser/Thr-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP043959.1\|WP_150150804.1\|22352_23135_+\|DUF881-domain-containing-protein	unknown	unknown	gnl\|CDD\|377575
NZ_CP043959.1\|WP_150150816.1\|38652_39711_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|131215

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150150814.1\|32927_33434_-\|FHA-domain-containing-protein	gnl\|CDD\|366133	pfam00498, FHA, FHA domain. The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.	1.6551e-18
NZ_CP043959.1\|WP_150150820.1\|40243_40981_-\|phenylacetate-CoA-oxygenase-subunit-PaaC	gnl\|CDD\|368300	pfam05138, PaaA_PaaC, Phenylacetic acid catabolic protein. This family includes proteins such as PaaA and PaaC that are part of a catabolic pathway of phenylacetic acid. These proteins may form part of a dioxygenase complex.	1.56241e-93
NZ_CP043959.1\|WP_150157162.1\|38264_38594_+\|rhodanese-like-domain-containing-protein	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	6.32764e-25
NZ_CP043959.1\|WP_150157160.1\|31256_32795_-\|Stp1/IreP-family-PP2C-type-Ser/Thr-phosphatase	gnl\|CDD\|223704	COG0631, PTC1, Serine/threonine protein phosphatase [Signal transduction mechanisms].	1.58731e-79
NZ_CP043959.1\|WP_150150822.1\|40977_41265_-\|1,2-phenylacetyl-CoA-epoxidase-subunit-B	gnl\|CDD\|237504	PRK13781, paaB, phenylacetate-CoA oxygenase subunit PaaB; Provisional.	5.93152e-66
NZ_CP043959.1\|WP_145829410.1\|37371_38211_+\|hypothetical-protein	gnl\|CDD\|99751	cd06257, DnaJ, DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.	0.000433799
NZ_CP043959.1\|WP_145829412.1\|29792_31229_-\|FtsW/RodA/SpoVE-family-cell-cycle-protein	gnl\|CDD\|223843	COG0772, FtsW, Bacterial cell division membrane protein [Cell division and chromosome partitioning].	3.59331e-82
NZ_CP043959.1\|WP_167534426.1\|35428_36958_+\|DUF2252-family-protein	gnl\|CDD\|313268	pfam10009, DUF2252, Uncharacterized protein conserved in bacteria (DUF2252). This domain, found in various hypothetical bacterial proteins, has no known function.	2.11925e-164
NZ_CP043959.1\|WP_145829417.1\|23515_24154_+\|aminodeoxychorismate/anthranilate-synthase-component-II	gnl\|CDD\|181107	PRK07765, PRK07765, aminodeoxychorismate/anthranilate synthase component II.	5.49405e-142
NZ_CP043959.1\|WP_145829406.1\|41261_42278_-\|1,2-phenylacetyl-CoA-epoxidase-subunit-A	gnl\|CDD\|184320	PRK13778, paaA, phenylacetate-CoA oxygenase subunit PaaA; Provisional.	0
NZ_CP043959.1\|WP_150150812.1\|28320_29796_-\|penicillin-binding-protein-2	gnl\|CDD\|223839	COG0768, FtsI, Cell division protein FtsI/penicillin-binding protein 2 [Cell envelope biogenesis, outer membrane].	7.12795e-89
NZ_CP043959.1\|WP_150150806.1\|24150_25305_+\|class-E-sortase	gnl\|CDD\|320679	cd05830, Sortase_E, Sortase domain found in the class E family of sortases. Class E sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Actinobacteria). Genes encoding class A and E sortases are never found in the same organism, and similar to class A sortases, the genes encoding class E sortases are not positioned adjacent to genes encoding potential protein substrates, suggesting a housekeeping sortase function of class E sortases in some high G + C Gram-positive bacteria. Similar to class A sortase, class E sortases are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They recognize an LAXTG sorting signal, instead of the canonical LPXTG motif processed by class A sortases. The prototypical class E sortase from Corynebacterium diphtheria (named Cd-SrtF) is a non-polymerization sortase that is not required for pilus polymerization, and proceeds to complete the assembly process by anchoring the polymer to the cell wall peptidoglycan. Moreover, in Streptomyces coelicolor, one or both of Staphylococcus aureus SrtA homologs may function as class E sortase responsible for the cell wall anchoring of the long chaplin proteins (ChpA-C) containing an LAXTG sorting signal, which presumably mediate aerial hyphae formation. The family also includes some class E sortase homologs from Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown.	4.11114e-50
NZ_CP043959.1\|WP_150150818.1\|39710_40250_-\|phenylacetate-CoA-oxygenase-subunit-PaaJ	gnl\|CDD\|131214	TIGR02159, Putative_12-phenylacetyl-CoA_epoxidase_subunit_D, phenylacetate-CoA oxygenase, PaaJ subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other].	1.9129e-52
NZ_CP043959.1\|WP_150150808.1\|25318_26083_+\|class-E-sortase	gnl\|CDD\|320679	cd05830, Sortase_E, Sortase domain found in the class E family of sortases. Class E sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Actinobacteria). Genes encoding class A and E sortases are never found in the same organism, and similar to class A sortases, the genes encoding class E sortases are not positioned adjacent to genes encoding potential protein substrates, suggesting a housekeeping sortase function of class E sortases in some high G + C Gram-positive bacteria. Similar to class A sortase, class E sortases are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They recognize an LAXTG sorting signal, instead of the canonical LPXTG motif processed by class A sortases. The prototypical class E sortase from Corynebacterium diphtheria (named Cd-SrtF) is a non-polymerization sortase that is not required for pilus polymerization, and proceeds to complete the assembly process by anchoring the polymer to the cell wall peptidoglycan. Moreover, in Streptomyces coelicolor, one or both of Staphylococcus aureus SrtA homologs may function as class E sortase responsible for the cell wall anchoring of the long chaplin proteins (ChpA-C) containing an LAXTG sorting signal, which presumably mediate aerial hyphae formation. The family also includes some class E sortase homologs from Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown.	1.61212e-41
NZ_CP043959.1\|WP_150150824.1\|42592_43705_+\|hypothetical-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	1.02567e-08
NZ_CP043959.1\|WP_150150826.1\|43701_44946_+\|HTTM-domain-containing-protein	gnl\|CDD\|214802	smart00752, HTTM, Horizontally Transferred TransMembrane Domain. Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane) in its N-terminus. In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal gene transfer than by early invention. The conservation of VKGC catalytic sites indicates an enzymatic function also for the other family members.	2.33002e-30
NZ_CP043959.1\|WP_150150810.1\|26180_28151_-\|Stk1-family-PASTA-domain-containing-Ser/Thr-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.61168e-127
NZ_CP043959.1\|WP_150150804.1\|22352_23135_+\|DUF881-domain-containing-protein	gnl\|CDD\|377575	pfam05949, DUF881, Bacterial protein of unknown function (DUF881). This family consists of a series of hypothetical bacterial proteins. One of the family members YlxW from Bacillus subtilis is thought to be involved in cell division and sporulation.	5.69626e-53
NZ_CP043959.1\|WP_150150816.1\|38652_39711_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	gnl\|CDD\|131215	TIGR02160, 12-phenylacetyl-CoA_epoxidase_subunit_E, phenylacetate-CoA oxygenase/reductase, PaaK subunit. Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other].	8.94398e-138

>NZ_CP043959.1|WP_150150814.1|32927_33434_-|FHA-domain-containing-protein
MSELTLTVMRLGFLAVLWLFVIVAVQVIRSDLFGTRVTQRGARREAGRQQANRQAPPQQRQQSGGGRRGRNTPTKLVVTEGTLTGTTVALQGQTITLGRAHDSTIVLDDDYASSRHARIYPDRDGQWIVEDLGSTNGTYLDRTRLTTPTPISLGAPIRIGKTVIELRK
>NZ_CP043959.1|WP_150157160.1|31256_32795_-|Stp1/IreP-family-PP2C-type-Ser/Thr-phosphatase
MSLSLRFAAGSHKGMIREGNEDSGYAGPRLLAIADGMGGAAAGEVASSEAISTIVALDDDVPGSDLLTSLGTAVQRANDQLRMMVEEDPQLEGMGTTLTALLWTGQRLGMVHVGDSRAYLLRDGVLTQITQDHTWVQRLVDEGRITEEEATTHPQRSLLMRALGSGEHVEPDLSIREVRAGDRYLICSDGLSGVVSHQTLEEALASYQGPEETVQNLIELALRGGGPDNITVIVADVLDLDTGDTLAGQLSDTPVVVGAVAENQNQPHDNGIMQTPAGRAAGLGRRRGGGGGEFGPPGSGDVTGFIQTDGFDYGDDDFVKPAKNRRWLKRSVYSLLALAVIGGGLYGGWRWTQTQYFVGAKGEHVALYRGINQDLAWVSLSKVEKDHPEIELKYLPPYQRKQVEATIVEGDLYGAREKIEELAVQASACKKQAERRASDSETNARTGAGEAGGTTGTTPASFSSKASPTPNPSDSAKAPEQSTTPSTTAPTTSPGPSLSEEEQKVVSLCGKQ
>NZ_CP043959.1|WP_145829412.1|29792_31229_-|FtsW/RodA/SpoVE-family-cell-cycle-protein
MSSTTNPSTQHTSTIGAIGAPSRRNTELALLVFAVVIPVFAYANVGLAINGDVPAGLLSYGLGLGLLAGVGHLVVRKFAPYADPLLLPLATLLNGLGLVAIWRLDQSELLQQIKQAGTAAPRQLMYTAMGIALFVAVLVFLKDHRVLQRYTYISMVGALFLLLLPLVPGLGQNIYGAKIWIKVGGFSIQPGEFAKIVLAVFFAGYLMVKRDALALASRRFMGLYLPRGRDLGPILVVWMVSILILVFETDLGTSLLFFGMFVIMLYVATERTSWIVFGLLMSAVGAVGVASFEPHIQQRVDAWLDPMKEYTLSRAGVGGHSEQAMQALWAFGSGGTLGTGWGQGHSELIRFAANSDFILATFGEELGLTGLMALLLLYALIVERGVRTALAARDPFGKLLAIGLSGAFALQVFVVAGGVMGLIPLTGMTMPFLAYGGSSVIANWALIGILLRISDTARRPAPAPATNPDAEMTQVVRP
>NZ_CP043959.1|WP_150150812.1|28320_29796_-|penicillin-binding-protein-2
MNKPLRRIAIFCGLLVLTLLIRDNWLQYVQADELRTDENNRRVAIERYASPRGDIIVEGEPITGHTTTKGDFKYKRTYKDGPMWAPVTGFVSQAYGANQLEAIEDGILTGNDDRLFFRNTLDMLTGKKKEGGNVVTTLNAAAQKAAYKGLKKQGGKGSVVAIEPSTGKILAMASYPSYDPSTIAGSSLDTDAEAWSKLQKKNNPDDPMLNRALREVYPPGSTFKVVTAAAALEHGLVEDADQKTETPLPWIMTGTRTELKNEGDLPCEDATLREALRVSCNTVFGKAGADLGNDKMLETAKKFGFTEEQFTPVRATASVFSDNMDPSQVALSSIGQFNTAATPLQMAMVASAVANNGSLMKPYMVDELQAPSLDVIEKTDPEEMSRPMSAKNAQILQSMMETVVEDGTGTNAKIPGVTVGGKTGTAQHGVDNSENPYAWFISYAKGEDGSSPVAVAVVIEDENAVRDDISGGGLAAPIAKSVMEAVLKGKQ
>NZ_CP043959.1|WP_150150810.1|26180_28151_-|Stk1-family-PASTA-domain-containing-Ser/Thr-kinase
MEEPRRLGGRYELGPVLGRGGMAEVYHAHDTRLGRQVAVKTLRADLARDPSFQARFRREAQSAASLNHPAIVAVYDTGEDYIDGVSIPYIVMEYVDGSTLRELLHSGRKLLPERTLEMTIGILQALEYSHRAGIVHRDIKPANVMLTRNGQVKVMDFGIARAMGDSGMTMTQTAAVIGTAQYLSPEQAKGEQVDARSDLYSTGCLLYELLTVRPPFVGDSPVAVAYQHVREEPQPPSVFDPEITPEMDAIVLKALVKDPDYRYQSADEMRADIEACLDGQPVAATAAMGSVGYGGYPDDQPTTALRADAGGATSMLPPMNPDDGGYGYDERQSRRRPPKKNNTSTILLVVAGVLVLIGAILIGRWAINGSGGVGNGTVAAPNFVGETKANAQKLADNSDLTLAFTEKPCENQAKGNVCDQDPAAGTKVDKESTVTLTVSTGAPKVAVPSVIGDDIDDAKAELEGDKYQFVVEVEEKISGEEPGTVIEQKPDLGEEVEKGTTVTLTVAKAEDKATVPDVLTKSCEEAKAQMTASTLTGNCVEEETDDPNLVGKVIRTSPDANTQVSKNSQVTIFIGKAKAAEKVAVPEINGKKLEEAQRLLGEAGLSVTGVTGPNDPNARVFGSNPPQGTPVDKGTGVTLFTVGGGGGGDGGFFGGG
>NZ_CP043959.1|WP_150150808.1|25318_26083_+|class-E-sortase
MAATADDTAQHSDAPASPPPRARRRMGPVAMVISFFGEMLITAGVLLGLFVVYSLWWTNVVADRAADRQADKVRDSWAQESGGGDKSAPAVYDSKNGIGFLHVPAMSGDDILVEKGTSMKVLNDGVAGYYTDPVKATLPTSGKKGNFSLAAHRDGHGAKFHGIHKIRKGDPIVFETKDTWYVYKVFGILPETSKYNVDVLAKVPAESGRKKAGHYITLTTCTPIYTSTYRYIVWGELVRKEKVDENRTPPQELN
>NZ_CP043959.1|WP_150150806.1|24150_25305_+|class-E-sortase
MTALRPERESGAHGYGAGDQGTSYGGQPYGVQGAYGDGWYGGAATPDPYGGTADDATTRLPPIDEETVALRIPDPPERAVREEPPAPGGRAARRKAAKKRQGRRGGSHKAADGSSAGRGPDDASEGASRASAGRGPDDASEGASRAPLSRVEARRQARARKASPAVVASRAIGEVFITTGVLMLLFVTYQLWWTNVRAHAQAGKEASDLQQDWANGERKPGAFEPGQGFALLHIPKLDVVVPIAEGISSKKVLDRGMVGHYAEGALKTAMPDAKTGNFGLAGHRNTHGEPFRYINRLQPGDPIVVETQDTYFVYKTASTLPVTPPSNVSVLEPVPKGSGFTGPGRYITLTTCTPEFTSKYRLIVWGQMVEERPRSKGKPDALVS
>NZ_CP043959.1|WP_145829417.1|23515_24154_+|aminodeoxychorismate/anthranilate-synthase-component-II
MSARILVVDNYDSFVFNLVQYLYQLGAECEVLRNDEVSTGHAQDGFDGVLLSPGPGTPEEAGVCVDMVRHCAATGVPVFGVCLGMQSMQVAYGGVVDRAPELLHGKTSPVTHEGKGVFAGLPSPFTATRYHSLAAEPATVPAELEVTARTADGIVMGLRHRELLVEGVQFHPESVLTEHGHRMLANWLAECGDTEAVARSAGLAPVVGRSSA
>NZ_CP043959.1|WP_019526631.1|23309_23519_+|hypothetical-protein
MAYGVGLVPWYDGRDGMYSWIWRHLPGNGWVRALISLVLITVVVYVLFQYVFPWAEPLLPFNDVTVDNQ
>NZ_CP043959.1|WP_150150804.1|22352_23135_+|DUF881-domain-containing-protein
MSNSADFPGTESSPAPRPRRVRPVRVLTAGIFALAGLLFFISFDTAKGTNIRTDASLLKLSDLIHERSRKNGELDESNGALRKDVEALAERDDGSTEAEDAKLADLEERAGTQELKGKAITVTLNDAPPDATAKLPGYPEPQPDYLVIHQQDLQAVVNAMWQGGAEGIQVMDQRLISTSAVRCVGNTLILQGRVYSPPYTITAVGEPEKLKKALAASPAIQNYMVYVNVYGLGWKVEDEGTKTLPGYSGTVDLHYAEPVD
>NZ_CP043959.1|WP_167534426.1|35428_36958_+|DUF2252-family-protein
MCTAYTCRGEAVVVSDAGAGGAEVVAGTAGAGKADAGTAGAATVDAGQERRLPQVAGFGRWPAAGTPKQEGKALRERVPRSAHAAFGLDASRPDAVTAVEQSGHGRLPELTPLRVGRMAATPFAFLRGSAGLMAHDLARTPITRIGAQICGDAHAANFGLYGDARGRLVIDLNDFDETVHGPWEWDLKRLAASLVLAGREAGADEDTCRAAAHDAVGAYRRTMRLLAKLPALDAWNAIADEELVSHTDAHDLVGTLERVAEKARANTSGRFAAKSTERTEDGGRRFVDAPPVLRRIPDAEAAAVAASLEQYLGTLPSDRHPLLARHAVHDVAFRVVGTGSVGTRSYVVLLLDHRGEPLVLQVKEARPSALVPHLPTAGFDAPRAEHEGRRVVEGQKRMQVISDSLLGWTTVDGRPYQVRQFRNRKGSVDPAALAADQVDDYARMTGALLARAHSHSADPRLIAGYCGKNDELDEAVATFAVAYADRTEADHTDLVGAVRTGRIAAEMGV
>NZ_CP043959.1|WP_145829410.1|37371_38211_+|hypothetical-protein
MTTSEGEQGGGAGAQRTPAGGGAARPEERLEQAVRAAEQALIEFEIAVETFRVEVENFSRLHEQKLGPLYARIEELDARILEAKASRSDDPEDRRRADEARARLLPIPGVEELMNGWMDGDGLFPEATAMLTDQPVRPPQRVRPSEEARKLYRDLARKAHPDLAQEDEERARREEFITRVNAAYARGSETELRELAEEWAAGPELKRVPSAADELYARLEWLSRRKELLTVVAKNLEDSAIASMLRLAPDDPDRLLEDIAAQLQADVAEREAQLAALRD
>NZ_CP043959.1|WP_150157162.1|38264_38594_+|rhodanese-like-domain-containing-protein
MPTVQVGDLKDGDFLLDVREDDEWKAGHAEGALHIPISEFVARYGELTEDAPQDGRIHVICRSGGRSAQVTMYLAQQGIDAVNVDGGMQVWEAAGRPVVTDEGQPGHVL
>NZ_CP043959.1|WP_150150816.1|38652_39711_-|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein
MARFHRLQVAAVDRLTDDSVALTLTVPPQLREEFRYVPGQHLALRRTADGQEIRRTYSICSPAPDGEAPGTLRVGVRLVEGGAFSTYALKEIDLGDELEVMTPAGRFTLPPAPGLYAAVVGGSGITPVLSIVSTLLAREPRARFCLIRSDRTTASTMFLEEVADLKDRYPDRFQLVTALSREEQQAGLPSGRLDQERLAGLLPALLPVDQVDGWFLCGPYGLVEGAERALRGLGVARSRIHQEIFHVDSGATAPATATAPAHSTVTARLDGRGGTWPVQTGESLLDTVLRNRPDAPYACKGGVCGTCRAFLVSGEVRMDRNFALESEETEAGYVLACQSHPVTEQVELDFDR
>NZ_CP043959.1|WP_150150818.1|39710_40250_-|phenylacetate-CoA-oxygenase-subunit-PaaJ
MVTVTPLEAELLELAGSVPDPELPVLTLRELGVVRAVRAHGTDSVEVDLTPTYTGCPAVEVMSLDIERVLRDHGVREVTVRTVLAPAWSTDDITDEGRRKLREFGIAPPRAGVASGPVRVQLGPTRTGAGGPADEPEPVRCPHCGSAETELLSRFSSTACKALRRCLACREPFDHFKEL
>NZ_CP043959.1|WP_150150820.1|40243_40981_-|phenylacetate-CoA-oxygenase-subunit-PaaC
MTTTPAAETVPTAAALALGDDALVLSHRLGEWAGHAPVLEEEVALANIALDLLGQARVLLSTAGDEDELAFRREERAFRNCQLVEQPNGDFAHTIARQLFFSTYQHLLHDRLASGDGPFAPLAGKAVKEAAYHRDHAEQWTLRLGDGTDESHSRTQRAVDALWRYTGELFQPVEGLDEVDWAGLERTWLELVTDVLGRATLTVPEGPRTGAWSAGAGRQGLHTEPFGRMLAEMQHLHRSHPGATW
>NZ_CP043959.1|WP_150150822.1|40977_41265_-|1,2-phenylacetyl-CoA-epoxidase-subunit-B
MTHTDWPLWEVFVRSRRGLSHTHAGSLHAPDAELALRNARDLYTRRGEGISIWVVPSSAVTASSPDEKDPFFEPAADKPYRHPTFYEIPEGVQHL
>NZ_CP043959.1|WP_145829406.1|41261_42278_-|1,2-phenylacetyl-CoA-epoxidase-subunit-A
MATAAARDTAGSPTAQEAPAGLGDPAEFQRAFDAAVAADERIEPRDWMPDAYRATLVRQIAQHAHSEIIGMQPEANWITRAPSLRRKAILMAKVQDEAGHGLYLYSAAETLGVGRDELLDKLHSGRQKYSSIFNYPTLTWADVGAIGWLVDGAAITNQVPLCRCSYGPYARAMVRVCKEESFHQRQGYELLLALSKGTPEQHAMAQDAVDRWWWPSLMMFGPPDDESQHSAQSMAWKIKRHSNDELRQRFVDICVPQAESLGLTLPDPDLRWNEERGHYDFGAIDWSEFWEVLKGNGPCNEERLSRRRKAHEEGAWVREAAAAHAAKHRNDETGATRA
>NZ_CP043959.1|WP_150150824.1|42592_43705_+|hypothetical-protein
MNAYDKGSDARHGPARPAVPGPRAPLPGPPPPSDAPGPAASDVPTPDAPESDAAPGLTSPAPETPGADVSPALASDASEAPASDVPEPHKAPGPGLPAPGSEGPDSGTSDAAPETPEPSAVPPDSRETPSRTPSGLQNPAPPGAEEAWGGPLAEARTGVAALSLRYQIGAALALAVVAVAVCVHLGMTFLHVAPANTVSKKHSETIADWIYPEFEQNWKLFAPNPLQQNVSVQVRAEIRTPDGGSRTTGWYDLSAQDGRAIDGNLAPSHTQQNELRRAWDFFVATHDDDNRPVGMRGALSETYLRRIMAMRLDRADAAGPDGELARVQVRSRTTDVPPPSWSKEKVSGKPVYRVLPWWTLPEKEIRGGIG
>NZ_CP043959.1|WP_150150826.1|43701_44946_+|HTTM-domain-containing-protein
MNRVSLAVSRAIARVTDSPLGPHQTAVLRIGLALTWLLFLLREYPHRQELYGPDGPWDWDLAAQLVSTNQAFTVLLWSDSRLWFEAVYALAVLAGLLLLLGWRTRTMSVLFMVGVLALQNRSVFMGDGGDNVLHIMAIYLVFTRCGRVWSLDARRARRADEARARGELPRDRVGPALWAVLGSVLLLAFLAGRTDGDWFIPAVLWGVWLALAVWWLVGRLARSGQPRILLDVVANVVHNGALLVIMAEACLIYATAGWYKVQGSRWQDGTAVHYPLHLEYFSPWQGLADLLSANGTMVMLVTYVTVVVQVAFPFTLFNRRVKNVLLTFMIMEHAVIAVVLGLPFFSLAMIAADAVFLPTSFLRRIGALAARAQGRLRSPASRSPAPPPRRPAGLPPGGPAGPAPVTGGVPGART

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Crispr_ID: NZ_CP043959_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_2

101387-101576

Orphan

Consensus_repeat	Method
GGGTGCGGGTCGGTGGGGGCTTGTCGCGCAGTTCCCCGCGCCCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_2

>merge|NZ_CP043959|2|101387-101576|CRISPRCasFinder
GGGTGCCGGTGCGTTGGGGCCTGTCGCGCAGTTCCCCGCGCCCCTTGGGGGTGGGGCGGTTCGTGGGGTGGGTGCGGGTCGGTGGGGGCTTGTCGCGCAGTTCCCCGCGCCCCTGAAGGTGCGGGGCAGTTCCCCATGCGCCTGAGGGTGCGGGTCGGTGGGGGCTTGTCGCGCAGTTCCCCGCGCCCCT

>NZ_CP043959|2|2|101387-101576|CRISPRCasFinder
GGGTGCCGGTGCGTTGGGGCCTGTCGCGCAGTTCCCCGCGCCCCT	TGGGGGTGGGGCGGTTCGTGGGGTGGGTGCGGGTCGGTGGGGGCTTGTCGCGCAGTTCCCCGCGCCCCTGAAGGTGCGGGGCAGTTCCCCATGCGCCTGA
GGGTGCGGGTCGGTGGGGGCTTGTCGCGCAGTTCCCCGCGCCCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150157168.1\|100378_101296_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150150905.1\|98242_99160_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176106
NZ_CP043959.1\|WP_150150908.1\|99384_100065_+\|snapalysin	unknown	unknown	gnl\|CDD\|280248
NZ_CP043959.1\|WP_150150902.1\|96123_98190_+\|DUF839-domain-containing-protein	unknown	unknown	gnl\|CDD\|253386
NZ_CP043959.1\|WP_150150924.1\|110860_111610_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|198080
NZ_CP043959.1\|WP_145829129.1\|109352_110696_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|238045
NZ_CP043959.1\|WP_150157167.1\|91697_92144_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150150927.1\|111655_111931_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|180688
NZ_CP043959.1\|WP_150150918.1\|103487_104627_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150150899.1\|92381_93998_-\|methionine--tRNA-ligase	unknown	unknown	gnl\|CDD\|237012
NZ_CP043959.1\|WP_150150921.1\|107645_109016_+\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270453
NZ_CP043959.1\|WP_145829348.1\|104654_105014_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_167534427.1\|95098_95836_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235906
NZ_CP043959.1\|WP_150150915.1\|102154_103423_+\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP043959.1\|WP_150150896.1\|88997_91688_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340404
NZ_CP043959.1\|WP_167534428.1\|109090_109255_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150150893.1\|87148_87460_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|375180
NZ_CP043959.1\|WP_150150912.1\|101584_102025_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376764
NZ_CP043959.1\|WP_048457137.1\|88503_88869_-\|PH-domain-containing-protein	unknown	unknown	gnl\|CDD\|377953
NZ_CP043959.1\|WP_150157169.1\|105045_107646_+\|solute-binding-protein	unknown	unknown	gnl\|CDD\|238119

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150150905.1\|98242_99160_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176106	cd08414, PBP2_LTTR_aromatics_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of aromatic compounds and that of other related regulators, contains type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LTTRs involved in degradation of aromatic compounds, such as CbnR, BenM, CatM, ClcR and TfdR, as well as that of other transcriptional regulators clustered together in phylogenetic trees, including XapR, HcaR, MprR, IlvR, BudR, AlsR, LysR, and OccR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	6.78328e-23
NZ_CP043959.1\|WP_150150908.1\|99384_100065_+\|snapalysin	gnl\|CDD\|280248	pfam02031, Peptidase_M7, Streptomyces extracellular neutral proteinase (M7) family.	2.15804e-73
NZ_CP043959.1\|WP_150150902.1\|96123_98190_+\|DUF839-domain-containing-protein	gnl\|CDD\|253386	pfam05787, DUF839, Bacterial protein of unknown function (DUF839). This family consists of several bacterial proteins of unknown function that contain a predicted beta-propeller repeats.	0
NZ_CP043959.1\|WP_150150924.1\|110860_111610_+\|GAF-domain-containing-protein	gnl\|CDD\|198080	smart01012, ANTAR, ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.	4.8153e-07
NZ_CP043959.1\|WP_145829129.1\|109352_110696_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	1.67207e-09
NZ_CP043959.1\|WP_150150927.1\|111655_111931_+\|hypothetical-protein	gnl\|CDD\|180688	PRK06771, PRK06771, hypothetical protein; Provisional.	5.16703e-14
NZ_CP043959.1\|WP_150150893.1\|87148_87460_-\|hypothetical-protein	gnl\|CDD\|375180	pfam17410, Stevor, Subtelomeric Variable Open Reading frame. The parasite protein STEVOR (Subtelomeric Variable Open Reading frame) is an erythrocyte-binding protein recognizing Glycophorin C on the red blood cell (RBC) surface. The cytoplasmic domain of STEVOR is shown to interact with ankyrin complex at the erythrocyte skeleton. It is phosphorylated by protein kinase A (PKA) at a specific serine residue (S324). The N-terminal semi-conserved region of Stevor that is present in this domain is shown to specifically bind to to a chymotrypsin-resistant RBC receptor. The expression of STEVOR in multiple parasite stages including merozoites suggests that STEVOR mediates multiple distinct functions in parasitic infectious cycle.	0.00354837
NZ_CP043959.1\|WP_150150921.1\|107645_109016_+\|extracellular-solute-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.	1.54356e-61
NZ_CP043959.1\|WP_150157169.1\|105045_107646_+\|solute-binding-protein	gnl\|CDD\|238119	cd00198, vWFA, Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.	5.37771e-07
NZ_CP043959.1\|WP_150150915.1\|102154_103423_+\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	2.02156e-31
NZ_CP043959.1\|WP_150150896.1\|88997_91688_-\|hypothetical-protein	gnl\|CDD\|340404	cd16927, HATPase_Hsp90-like, Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including Escherichia coli HtpG, and related domains. This family includes the histidine kinase-like ATPase (HATPase) domains of 90 kilodalton heat-shock protein (Hsp90) eukaryotic homologs including cytosolic Hsp90, mitochondrial TRAP1 (tumor necrosis factor receptor-associated protein 1), GRP94 (94 kDa glucose-regulated protein) of the endoplasmic reticulum (ER), and chloroplast Hsp90C. It also includes the bacterial homologs of Hsp90, known as HtpG (High temperature protein G). Hsp90 family of chaperones assist other proteins to fold correctly, stabilizes them against heat stress, and aids in protein degradation.	1.63559e-20
NZ_CP043959.1\|WP_150150899.1\|92381_93998_-\|methionine--tRNA-ligase	gnl\|CDD\|237012	PRK11893, PRK11893, methionyl-tRNA synthetase; Reviewed.	0
NZ_CP043959.1\|WP_150150912.1\|101584_102025_-\|hypothetical-protein	gnl\|CDD\|376764	pfam02322, Cyt_bd_oxida_II, Cytochrome bd terminal oxidase subunit II. This family consists of cytochrome bd type terminal oxidases that catalyze quinol-dependent, Na+-independent oxygen uptake. Members of this family are integral membrane proteins and contain a protohaem IX centre B558. One member of the family, Klebsiella pneumoniae CydB, is implicated in having an important role in micro-aerobic nitrogen fixation in the enteric bacterium Klebsiella pneumoniae. The family forms an integral functional unit with subunit I, family Bac_Ubq_Cox, pfam01654.	0.0074123
NZ_CP043959.1\|WP_048457137.1\|88503_88869_-\|PH-domain-containing-protein	gnl\|CDD\|377953	pfam08000, bPH_1, Bacterial PH domain. This family contains many bacterial hypothetical proteins. The structures of Structure 3hsa and Structure 3dcx show similarities to the PH or pleckstrin homology domain. First evidence of PH-like domains in bacteria suggests role in cell envelope stress response.	3.47264e-64
NZ_CP043959.1\|WP_167534427.1\|95098_95836_-\|hypothetical-protein	gnl\|CDD\|235906	PRK07003, PRK07003, DNA polymerase III subunit gamma/tau.	5.77511e-08

>NZ_CP043959.1|WP_150157168.1|100378_101296_-|hypothetical-protein
MPHRTRNALAAALLALACLLTPCAVLAAWAAHDLADTTRYVRTVAPLATDPNVRDAVADAVGDQVVRELDARTTDSAAPLGPFARDAIHSFTRTDAFRTAWEAGNRAVHAALLHALRDDVSARGPVTVDLAPVTAQVKQRLEADRMPYAHRIPVQHTEVPVVPADEVAGLRRGYRLLEAAALWLPLTAVTLAVTGVALAAARRRVLTAAGLGTALGGALLALAVTVGRRLTLADLPDAVHRPAAAAVYDALTATLRTASWLLLAVGAAAALLTWLSGVPARRRDRLRTAGTPDPAPAPAPTGART
>NZ_CP043959.1|WP_150150908.1|99384_100065_+|snapalysin
MRLRMPLSVLSAAGLSLTALGLGAAPAGAAPAPVAPTGSYAAYDGSSEEAAATRAFFEAVLKSVAEKRAADPTGAAAVTVVYNASQAPTFATQIARSAQIWNSSVSNVRLQSGTSGADFSYREGNDSRGSYASTDGHGRGYVFLDYAQNQTYDSTRVTTHETGHVLGLPDNYSGPCSELMSGGGPGPSCTNAIPNSAERSRVDQLWANGFAAALDQAEKALEKSAR
>NZ_CP043959.1|WP_150150905.1|98242_99160_-|LysR-family-transcriptional-regulator
MELEVRHLRALCAIADTGSLHRAARQLGVAQPSLSTQLRRIEQELGGALFVRARTGCRPTPLGRLVLSRARPLVTELRSLVTEARAAAVGGRQLRIGSTASRALAGWLRRLRRHWQEPTLHMDVSANALLRMVADGQLDVAFVHEVEGCPLRVPENLRTRVLIAREPQFVSLPADHPAAARPVVRLSELAHDRWMIDPAVDGEWAAVRRMLDGAGIDPPVLHGDYHTAASLVAIGEVVTVCQPTSPSRPETAVRRIDGDPLGVRLLLAARTETELEGVYPHLAEAYREVARQASAYREWLEELVL
>NZ_CP043959.1|WP_150150902.1|96123_98190_+|DUF839-domain-containing-protein
MRKLLPLIGTPSRSHPGGRSALTCRFRCGDACFHEVPNTSANAYVGDVVAGALSRRSVMRAAAVVTVAAAGAGAVGVAAAPEAGAAGAAKGHRPPKGARGLRFTPVAPNTRDAVTVPEGYRQNVVIRWGEPILRGAPAFDPERQSARAQAGQFGYNCDFLALLPLKGERDRQLLVANHEYTDEILMFRDYDPQNPTREQVEIAWAAHGLAVVAVEEDRGSGRLTAVGRHHLNRRLTATSEFRLTGPVAGSDLVKTSADPSGTRVRGTLNNCSGGTTPWGTTLHGEENFNQYFANGSSATDKRYGIGTGATERKWERFDKRFDLAQEPNEVHRFGYVVELDPYDPDSTPRKHTALGRFKHEAATVRLTHDGRPVVYSGDDERFDYFYKFVSSKRMRHGDSRAARAHNLTLLDEGTLYVARLTGDSPAIEIDGTGKLPGDGEFDGSGEWIPLATATARGAVSHVEGMTAEEVFVFTRLAGDKVGATKMDRPEDIEPNPVTGKVYVALTNNSNRGTGANPKADEANPRHANKHGHVLELTERFNRPESTRFAWSLFLVAGDPDDPATYFAGFPKDAVSPISCPDNVAFDAHGNLWISTDGSALGSHDGLFGVATRGERRGELKQFLTVPTGAETCGPVVQDRRVLVAVQHPGEVDGATVERPASTWPDGPGTYVRPAVVAVWRADGRDIGV
>NZ_CP043959.1|WP_167534427.1|95098_95836_-|hypothetical-protein
MGILTLLRNAFGRSRKARPAEAEGAAPAAEATETAAPTTPEPSPEPTIPSPSPEPGPATPTVPEQRERDEHDLVSAAFDKITVPRPTPSTDPEPAPKQAAATDPEPKTETEAAPEPKASTAPNPRRSRPRGDPEPEAKSDAAQEPEAKTEAAPEPEPEAKPATEPEAKPAIEPEAEAETASEPEAKAETDPATEDKGSLEAEAEATPPPEPEPEAKAEPKAEAKAEPKAEAKAEAEGGGQGRGRA
>NZ_CP043959.1|WP_150150899.1|92381_93998_-|methionine--tRNA-ligase
MAATGSEKQGAKAYYVSTPIYYVNDAPHLGHAYTTVAGDVLTRWHRQRGEKVWYLTGTDEHGQKIMRTAEANGVTPQAWADKLVTEAWKPLWEHLDIANDDFIRTTQKRHTDRVQEFVQDLYDKGEIYKGGYEGPYCVGCEEYKLPGELLDGEGDYAGQKLCPIHKKPVEILSEENYFFKLSEYSEKLLAHYEANPGFIQPESARNEVVNFVRQGLQDLSISRSTFDWGVKVPWDDKHVIYVWVDALLNYATAVGYNENPEKFESTFPADVHLVGKDILRFHAIIWPAMLMAQGLPLPGKIAANGWLMVGGEKMSKSNLTGIKPQDLTSHFGVDAYRWYFLRAIAFGQDGSFSWEDFSARYTSELANDYGNLASRVAAMVGKYFGGELPAATADGDAEKAIHDGLAKAVTEADRKIGEELDFQGGILAVFDFVKQVNGYITEQEPWKVAKDDSPESKARLATILYTAAESLRAVAVLLNPIMPETSQKLWESLGAEPSLGALADQRVQESAAWGLLPAGSTVTKGAVLFPRLEEKPTA
>NZ_CP043959.1|WP_150157167.1|91697_92144_-|hypothetical-protein
MRRELALERYRYVLQQIQTVNENAHRFLAIYQTLATTLVAAALALFVGYRKWELAADTARGGVIGLLTLTTVVAAFTGTLIVVGALAWLDYRHEECDVTDELVGPGFRKRPRPGNFLRWYETYVVLFILVSVITMWVLAGLFLLPAMR
>NZ_CP043959.1|WP_150150896.1|88997_91688_-|hypothetical-protein
MTEHVHTNTSLWKNTLAARPGPEADPHAEQRGQLRASYRELRRKAAVLLEENARSMPDFTVHDISHVDALWETADLVCGDTVTLNPAEAYVLGCAFVLHDAAMGTAAYGTTVPEALGEKRWRDLVSLAYYEREGCWPERNELEDPPAEIAEACVATAIRETHAEQAKRLVDQPWRSSTGNEIHLIDEVQLREWYGPLFGDLAASHWWPVDRLAREFRHSIGSLPWQPSEWVIEPLKLACILRLADATQIDSRRAPSFLFSLRRPRGVSREHWRFQEHISRPYRNGDRVTYSSLRPFPPRDAASWWLALDYLRGIDRELKAVDALLHDLGRKRLAARAVAGVDSPERFAELFRVQDWRPIDATVKVSDIPSLVGTLGGRQLYGDEPEVALRELIQNAQDAVLARQTLQPDFPLGQVEIRLTRTDDDWYLEVRDSGTGMDEETLVHGLLDFGTSGWSSTSVRNRLPGLADGGFRPSGRFGIGFFSVFLLGDEVELITRRYDASLADARRLTFDGPSHRPLLTPVPGQGWVPEGTTVRVKLRKSPYATQGLFSRTYDERLAELARRLVLENAVPIHTWEPGAAVPQVLRPFSLASGAREEVFDRLYPPQAAKGRAGEEKLRLQMRDDFVDRATEVRDDKGQRVGLAMLWSSWAHQGQRDYPGIVTVNGFLADTSVSFAGYLMGQPSRASRDKAALVATRDEMRQWIDTQEQRLRHAGLFDDSLQLEIALTLHTASAPLSDDVAFALTAQGVLSLSEVREWVVQRNQIFVGLGWPLSWRTRPPEIGHPVSGEPIQLPDDCVFICQYGTTPPLTEVFPYAANRDSAYEFARDHPTLTWQKHWWRMSDDLYGLFVRTLCDVWNCSLESLLAPLEQRDWSDCIHVDESLGPVPGYHFRRPSGT
>NZ_CP043959.1|WP_048457137.1|88503_88869_-|PH-domain-containing-protein
MALFGNAHTVDPAKAQQDYARLLGHGEQVHAAFLLIRDTILFTDRRLILVDKQGITGKKTEYHSIPYRSISHFAVETAGHFDLDAELKIWISGAPTPIQKTFTKGVDIYEVQAILTQFVAR
>NZ_CP043959.1|WP_150150893.1|87148_87460_-|hypothetical-protein
MRSEHCLTRNHIEVFHNRVLSSGPQRIRFRTLVYGSTLPLLVWTGIAGFLHHVFNPIAPMVLCGLFVTLIALGFALRRRRKHSVRCSFYGALGAVLAGSMDGF
>NZ_CP043959.1|WP_150150912.1|101584_102025_-|hypothetical-protein
MAHAAPRTRGMIEQARTPDVFDARTHRMARVVLPVLTALVYGFWAAANRRYGGPITGWNLLFGFLTALVFAALFITLLTVGPKLRRAAHALAWAAFAGCAVGFLFSQSNGSIYRSVAVGVGIMAGVFLIMFYRYYTQQDAEGHPRE
>NZ_CP043959.1|WP_150150915.1|102154_103423_+|SpoIIE-family-protein-phosphatase
MSPASTGHALPDRYPAAGRADVVQRQQMLRVRGRSVAWLPPLLLLLAIAVADYNTTGEFRIISWIVLVPGIAAALCGVWGTALFAALSMGTYTLVDNAWPHQFQAGLPDFILVALGGALATLACGVRVRGERRALHMRDVTDTVRRTVLRPLPPGWGGLEHAGVYLTADAQARVGGDFYDIQPGPHGTRVFVGDVQGKGLGAVETAAVLLGTFREAGFHERDLAAVADRLEARMVRHRAYTTALGRADGDRFATAVLLDFPADGTDVVDAVVFGHEPPLAVGPSGVRHLPTAGGLPLGYRDLAPGPPVVRRVHLGADETLLLVTDGVTEARDVHGHFYAVADDVRRSVAADPRLTAPAPLVMLVRDGTVRHCRGHLTDDTTVFAVRRTRVTRSGRPAGATALPTGADPAAGVERREGGRSPL
>NZ_CP043959.1|WP_150150918.1|103487_104627_+|hypothetical-protein
MPGTVLLLAASPLGRGRLVDAASVLPVLAAVPPAVLSGTDTANVVELADPLEPQAVLTRLRAAAAAPGPLTVYAAGELRLDRRQRLPHLALARTTPATVRYTALPWHWFRDELRLRPAGATTLFLDLHADADTWQALCAPPAPGRPFLMDCGRDAAVYGRIAPPPSRRGVVAPSYMKALATVLRSGRRPAAEDLHQQVLARIAPESAGTDLVLAQRGPLPGDPHAAVTDAVRAGRHAEADALAARLEQAAGFAHGPVSEEALHWTEVRADLAMLAGDAVRSCQAWMALAGTRLAAGQPADAPAVEAAVDRAHHQWGLVDDPVRVRELGLTLVDLRGRVPGRRDGAAEHVRRRLRAVQASVGVPAGQLRTDPPQGATAVP
>NZ_CP043959.1|WP_145829348.1|104654_105014_+|hypothetical-protein
MADQDICIRLDGTATEGDISALRNWLEREKPLDDLLGDGRVRMRVRPATDVGAADRSGAPMGTSTEIVIAVTSAGATVVFQELLEQVKRGVLAWQANRRRVENGEPPQGRVEPVNRDDR
>NZ_CP043959.1|WP_150157169.1|105045_107646_+|solute-binding-protein
MDRALLIGVSEYDFTEPPDGVPNDLPAVRHNLTALREALVRGRVFAEQEIRTLPSPYLADTGRVLQRAAKEARGLLLVYFAGHGAIPSGGDELYLQMRDARVIAGEHTVFSGAEKFGDLMATVLATSAARRIVVVLDCCFAGNAARVWEHFEDKRRVAVLMSVQANHRIDAGDRHTPTPFTAELAALLGEGGGIELPDLLAALRRRMAERGHRTLREDRWEPQLRADAGLKVRLGKGEEPQGAQHPDPLVPRPVPPGQVSGGPDRPPRPPRGGRPAVLAAWRRTRAEPRERPGPEEPPPVRRPVLRFALPVLLALGLLGFGLYGPPGLAGGDGTHCVPPLELRVLTDPDLEPTVRAAADAYLTSEGNTTDAGCRRTGVTVYSAGSSDVVGALRGHTGDWQEPRDDDVNPQRDVGPQPDVWIPASRADVDRVLDEQDTDAVAALEREASPFAYSPVVLAVPQQIAVDSLEGRTAQSLTEMVRDLTARAPDAAVRRPDPEFTDSGLLATVGLYGAEGRAVARGERLLDQDGPPSPTAGELLCALPDDDAVDDRTAALVPEFLMRSGVGCDSTTRNRRMAHYPDDVPGMEPVFVRVRWSGGDRDEADRDASVAAFHDWLSGEGGRAVFARYGFRSADTRELLQPEGASDLGMMYAPAPLDESAGRDAMDRALRDYQAYGGPGRVLFLLDSSGSMADLWQGPSGGPGLLRQSLGGLGTADEYGVWAVADTGDGPYETLLGFGTHRTHDAQRAVDTRARVRDAAADPHAALLAAFEEMERRGSDGRPQLIVHITDGEHGERLTGGRLTEVLDGAGAGGVPVTVAVLGSGGCDTGRPDRRIADASGGRCLDAGDDVGAALHDEIARTGTGEG
>NZ_CP043959.1|WP_150150921.1|107645_109016_+|extracellular-solute-binding-protein
MPRRFAVLPALLLLLAACTGGGDGERPPDAAVTEEVPGTIVVASGRDVTGTNGVRQQLIDAWNRREQRTGSQYRARLVELPGSADEQRSQLLGALQSRSAEYDVVNLDVTWVPEFAEAGLVRALPDDVVDEDVIASVAETARWDGKVYAVPFNSDVGLLYYRRDLMRRAGVEEPYVPEGFTWDRLRGHVETLHAKLPGAFANGWTTQLAAYEGRTVNAVEAFASAVPGLELVDGKGRYTGDVEELTRGVAELRRRTEPAYTLPDAAGSDEAAATSDFVKGRTVFLRAWPSAYPTLYQVFGDELGVARLPGRAVLGGQNLAVSRTSQRSGKATELIRYLTGRESERCLLEAGFAATRDSAYDGLVRCPPAVSAVPSPSPTGEGADGAPRRDGGRPGFADEMLRDALSEAVHRPRTPLYGAFTQTFITELGPLFGEGPPGDEELARRLDQALRRALPG
>NZ_CP043959.1|WP_167534428.1|109090_109255_-|hypothetical-protein
MLDRTRPTERYARGLVAALAAVAALVLAANVGPAKAVGHESDQVTTAPVEAAER
>NZ_CP043959.1|WP_145829129.1|109352_110696_+|tetratricopeptide-repeat-protein
MGERDEPGTIGRRVQRLRVARGLTQKQLAEPVYTPAYISTLEAGRVRPSDDALRHLAERLEVEFDELATGRSARRVTELRLGLTEAQRSLALGEAEAAVERYTALLAEADAQGLPEEQAAALLGLGECALDTGELESGRRYFERAEERLAEAPLPARVPALRGRAVAHYLAGELRYAVYLLETAIDELNRGGLHDPDALLLLYASVIGPYMDMGAHARAAQAAEFALTLAPQSGDPALVARMHRSVARTLLAEGRLAEADASLAKAAELYRRLQLRTELANCHWMRGYVYAQNGDLEQAEGEMREALRMLSATRAFLYSSQLTVELADVLHRRGRSEEAADLLRDVLGGLSPERGAVHAAAAHRLLGIIAEDARDTEQAEEHYVRALSLLERAGAAGDLADLCRLLGDLLRRTGRVEAALDAYRTGLGHRTAPGTTTLGPAPAQPPV
>NZ_CP043959.1|WP_150150924.1|110860_111610_+|GAF-domain-containing-protein
MRPGDDPGGGQDRGAGTGGYARAVGAIAAGLRDAEPAQVPERLCAVAVDLLPVDGASVSLRGDSMPLQLAASGARAARLAQLQATLGDGPCHHVLKTGAPVLARDLADDDCADRWPVFVQQALGTGVRAVYALPLGSTAVCVGTLDLYSGSPGVLSAHQMHVALLLAGVMTGALMDLPHDARDADKGWLSGLAADHDRVHQAVGMIMAQLGVGADEALARLRGDAFAQGVTVLEAAVDVVSHRRRFDSR
>NZ_CP043959.1|WP_150150927.1|111655_111931_+|hypothetical-protein
MDTAILFLTCVVILGVASIQTRQARSDRRVARVERKLDQVMRHLGLDEEMPREDEIRALVRDGKQVQAIRLYREATGADLVEAKQAVDRLS

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Crispr_ID: NZ_CP043959_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_3

1813630-1813745

Orphan

Consensus_repeat	Method
TCACCGGACGGGAGTGAAGTCCCGCGCTCCGATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_3

>merge|NZ_CP043959|3|1813630-1813745|CRISPRCasFinder
TCACCGGACGGGAGTGAAGTCCCGCGCTCCGATGCTGTGTCTTTCGGGGGACAACCCCCGAACCCCCGGCAAGGGGACGGACTCACCGGACGGGAGTGAAGTCCCGCGCCCCGATG

>NZ_CP043959|3|3|1813630-1813745|CRISPRCasFinder
TCACCGGACGGGAGTGAAGTCCCGCGCTCCGATG	CTGTGTCTTTCGGGGGACAACCCCCGAACCCCCGGCAAGGGGACGGAC
TCACCGGACGGGAGTGAAGTCCCGCGCCCCGATG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150153506.1\|1808326_1810057_-\|two-component-sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP043959.1\|WP_150153500.1\|1804645_1805119_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NZ_CP043959.1\|WP_004932953.1\|1814614_1815013_-\|ectoine-synthase	unknown	unknown	gnl\|CDD\|183953
NZ_CP043959.1\|WP_167534492.1\|1823021_1823975_+\|LPXTG-cell-wall-anchor-domain-containing-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150153508.1\|1810289_1810886_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227231
NZ_CP043959.1\|WP_145825107.1\|1816388_1816895_-\|diaminobutyrate-acetyltransferase	unknown	unknown	gnl\|CDD\|131459
NZ_CP043959.1\|WP_145825104.1\|1819249_1820101_+\|transporter-substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|270342
NZ_CP043959.1\|WP_150153504.1\|1807573_1808236_-\|response-regulator	unknown	unknown	gnl\|CDD\|225107
NZ_CP043959.1\|WP_004989734.1\|1805122_1805896_-\|IclR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224332
NZ_CP043959.1\|WP_150153522.1\|1817956_1819057_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|223153
NZ_CP043959.1\|WP_150153510.1\|1810933_1811542_+\|DUF1349-domain-containing-protein	unknown	unknown	gnl\|CDD\|377771
NZ_CP043959.1\|WP_150153502.1\|1806037_1807567_+\|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|143447
NZ_CP043959.1\|WP_150153512.1\|1811635_1812379_+\|DsbA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|239322
NZ_CP043959.1\|WP_150153514.1\|1812448_1813501_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|223594
NZ_CP043959.1\|WP_150153498.1\|1802933_1804391_-\|penicillin-binding-protein-2	unknown	unknown	gnl\|CDD\|274573
NZ_CP043959.1\|WP_150153524.1\|1820105_1820942_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223836
NZ_CP043959.1\|WP_145825102.1\|1820938_1821730_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224051
NZ_CP043959.1\|WP_150153520.1\|1817248_1817788_-\|DUF664-domain-containing-protein	unknown	unknown	gnl\|CDD\|368218
NZ_CP043959.1\|WP_150153526.1\|1821751_1822843_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238624
NZ_CP043959.1\|WP_150153518.1\|1815049_1816321_-\|diaminobutyrate--2-oxoglutarate-transaminase	unknown	unknown	gnl\|CDD\|236437

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150153506.1\|1808326_1810057_-\|two-component-sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.6038e-34
NZ_CP043959.1\|WP_150153500.1\|1804645_1805119_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	1.12287e-24
NZ_CP043959.1\|WP_004932953.1\|1814614_1815013_-\|ectoine-synthase	gnl\|CDD\|183953	PRK13290, ectC, L-ectoine synthase; Reviewed.	6.15171e-78
NZ_CP043959.1\|WP_150153508.1\|1810289_1810886_+\|hypothetical-protein	gnl\|CDD\|227231	COG4894, COG4894, Uncharacterized conserved protein [Function unknown].	9.88938e-05
NZ_CP043959.1\|WP_145825107.1\|1816388_1816895_-\|diaminobutyrate-acetyltransferase	gnl\|CDD\|131459	TIGR02406, L-24-diaminobutyric_acid_acetyltransferase, diaminobutyrate acetyltransferase. This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analagous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase. [Cellular processes, Adaptations to atypical conditions].	2.30364e-70
NZ_CP043959.1\|WP_145825104.1\|1819249_1820101_+\|transporter-substrate-binding-domain-containing-protein	gnl\|CDD\|270342	cd13624, PBP2_Arg_Lys_His, Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold. This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.60207e-67
NZ_CP043959.1\|WP_150153504.1\|1807573_1808236_-\|response-regulator	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	2.34494e-67
NZ_CP043959.1\|WP_004989734.1\|1805122_1805896_-\|IclR-family-transcriptional-regulator	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	1.43824e-63
NZ_CP043959.1\|WP_150153522.1\|1817956_1819057_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|223153	COG0075, COG0075, Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase [Amino acid transport and metabolism].	3.89423e-80
NZ_CP043959.1\|WP_150153510.1\|1810933_1811542_+\|DUF1349-domain-containing-protein	gnl\|CDD\|377771	pfam07081, DUF1349, Protein of unknown function (DUF1349). This family consists of several hypothetical bacterial proteins but contains one sequence from Saccharomyces cerevisiae. Members of this family are typically around 200 residues in length. The function of this family is unknown.	9.0437e-57
NZ_CP043959.1\|WP_150153502.1\|1806037_1807567_+\|aldehyde-dehydrogenase-family-protein	gnl\|CDD\|143447	cd07129, ALDH_KGSADH, Alpha-Ketoglutaric Semialdehyde Dehydrogenase. Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.	0
NZ_CP043959.1\|WP_150153512.1\|1811635_1812379_+\|DsbA-family-oxidoreductase	gnl\|CDD\|239322	cd03024, DsbA_FrnE, DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.	3.3651e-80
NZ_CP043959.1\|WP_150153514.1\|1812448_1813501_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|223594	COG0520, csdA, Selenocysteine lyase/Cysteine desulfurase [Posttranslational modification, protein turnover, chaperones].	8.18857e-43
NZ_CP043959.1\|WP_150153498.1\|1802933_1804391_-\|penicillin-binding-protein-2	gnl\|CDD\|274573	TIGR03423, pbp2_mrdA, penicillin-binding protein 2. Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	3.44051e-83
NZ_CP043959.1\|WP_150153524.1\|1820105_1820942_+\|ABC-transporter-permease-subunit	gnl\|CDD\|223836	COG0765, HisM, ABC-type amino acid transport system, permease component [Amino acid transport and metabolism].	2.3626e-59
NZ_CP043959.1\|WP_145825102.1\|1820938_1821730_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224051	COG1126, GlnQ, ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism].	8.33487e-156
NZ_CP043959.1\|WP_150153520.1\|1817248_1817788_-\|DUF664-domain-containing-protein	gnl\|CDD\|368218	pfam04978, DUF664, Protein of unknown function (DUF664). This family is commonly found in Streptomyces coelicolor and is of unknown function. These proteins contain several conserved histidines at their N-terminus that may form a metal binding site.	3.13157e-44
NZ_CP043959.1\|WP_150153526.1\|1821751_1822843_+\|amidohydrolase-family-protein	gnl\|CDD\|238624	cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.	4.50585e-68
NZ_CP043959.1\|WP_150153518.1\|1815049_1816321_-\|diaminobutyrate--2-oxoglutarate-transaminase	gnl\|CDD\|236437	PRK09264, PRK09264, diaminobutyrate--2-oxoglutarate transaminase.	0

>NZ_CP043959.1|WP_150153514.1|1812448_1813501_+|aminotransferase-class-V-fold-PLP-dependent-enzyme
METFESLVRAEFTPKNTYLNTASSALLPARTVSALDAAARLRAEGRPLDPLFADVEVCRAAYARLAGVPVERVAAGATVALYSSLVAASLPPGAEVLTAEDDFTSVLNPFHARGDLKVRAAPLERLADAVRPGTALVAVSAAQSADGRIADLPALREAARSHGARTYVDFSQAAGWLPVGAGAYDYSVSITFKWLLGPHGAAFLVVPEDFGDLIPVQAGWVAGEDPWSSCYGPVAELASSARRFDTTPALFSYAGLRASLELVEEIGVDTVRTHDLALADRFRAGLVSLGREPLPAPGSPIVSVPGLGGLQPELAEAGIQVSNRAGNLRASFHLYNTADDVDRLLDALSG
>NZ_CP043959.1|WP_150153512.1|1811635_1812379_+|DsbA-family-oxidoreductase
MRVEIWSDIACPWCYVGKARFEKALASFPHRDGVEVVHRSFELDPHRAKDDIEPVLTMLTRKYGMSEAQAEAGEDNLGAQAAAEGLPYRARGRDHGGTFDMHRLLHFAREHGRQEQLLDLLYRANFAEERSVFGDDERLVELAGAAGLDTDAARTVLADPEAYAAEVRADESEAAQLGARGVPFFVLDRKYGVSGAQPVEVFTQALTQAWGERSPLTLVTGGTDAEACGPDGCEVPPRRNPQAGADV
>NZ_CP043959.1|WP_150153510.1|1810933_1811542_+|DUF1349-domain-containing-protein
MDLDIPELPFPLRTYGPEGSWAYEDGVLTGWAGPRQDRFVPPTGESLESAADAPRLLGAPEGDFQLIARVTVGFGAAFDAGVLYVHVGEQAWAKLCLEYSPKVPTICTVVTRGHSDDANSFTVEGSSFWLRVSRTGRAFAFHASRDGKQWTFVRLFTLGDEKETGAALVGFATQSPTGEGCVVTFDHIEYRLHWPPDLRDGS
>NZ_CP043959.1|WP_150153508.1|1810289_1810886_+|hypothetical-protein
MDATGPWKSRRFTVTQRATLKADRYVVTETLRDGSAGRVLAHAEQKRFSLKEELTFYGDASRQQVLFTVKERTLLDPGEGFDVLDAEGKPLGAFHERFFTSLVRSTWVLEQPGAPDAVGRERNRFVAVLRRAWGWLPLDLVPFAWPYHFDFTTDGKPVMTVDRKTGLRDRYLVDVVAPDLDLRLAVAQAVALDTFQGR
>NZ_CP043959.1|WP_150153506.1|1808326_1810057_-|two-component-sensor-histidine-kinase
MAQTSRTARPLLSRLAAASPWSRGRIAGETALVLVLAGTAGTAYSLESGSAARSWALAVAVGVLTLVRRSLPATVLVLSSALAGSVLGTGPLLIYASWSAGSRIGRPWHAVGAYATGLVLYAAGALLGDGGEEALEFSLLLTAALSAGPYLVMAVVPGLASRYRAQRRDLLDALRRHNVQLVREQAMVARQARLLERQRIAQDMHDSLGHQLALIAVHAGALEVDPELGDRHREGVGILREAARAGMRELREAVGILRDDADEPPASGPGPGPEAAGAPPARGAAGLDALVASSRGAGVPVELRRSGTARPLAPAADHAVYRIVQEGLTNAHKHAPGAPITVELRHEPDSLVVEVANGPVPAGVPAAPPAISGGQGLAGLRERARLVGGMVHSGPAPDGGFRVAGVLPYGDGSAPAGRKDATSVAPAGDFRGQSGRGAAGDGGADIDRFDPQKEYAAIMSTKKNVALGCALVAVVLVAGTAALLVWGVGKLIDEVEKGVIPASVYDSARIGDAEADLREEFPDGDSLLTDGVEKQGPPLPEDAVCEHFVDEDEDIVYRFCFRDGKLVAKESYPHEI
>NZ_CP043959.1|WP_150153504.1|1807573_1808236_-|response-regulator
MIRVLVADDEPLIRAGIRMILTSADDIDVVAEARDGREAVETARATAVDVALLDIQMPVMDGLTALAEMGRAAPGVRVLILTTFGERENVLRALGHGGAGFLLKDSAPQELIHAVRAAAAGNAYLSPAATRHVVDTLASPAATARGEEARRRLTGLTERERQVLALLGEGLSNADAGARLHMSEATVKTYVSRILTKLDCDNRVQAALLARDAGLEPTGG
>NZ_CP043959.1|WP_150153502.1|1806037_1807567_+|aldehyde-dehydrogenase-family-protein
MAAAPVWSVDPRTGKQREQVAVEATAQEVDAAVRAAEEAREALTDRTVRAAFLRSAADELEAARDRLVEAADAETALGPVRLTGELARTCYQLRAFAGIVEEGAFLDVVIDHPDDTATPPIPDLRRYKIPLGVVAVYSASNFPFAFSVAGGDTASALAAGCPVVVKAHPDHPALSELVARVIRRAAARHAVPDGVLGLVHGFEAGLELIRHPRVAAAGFTGSVRGGRALFDAAAARPVPIPFHGELGSLNPVVVTEAAAAERGEAIGAGLAGSMTLGVGQFCVKPGLVLAPASAAGDALLKSLTDAVSDTDPGVLLDHRMRDNFLAGVTERAQLPDVESPVTAGAGGDHTVSAGFLTVPAERLTREGDHDLLIEECFGPVTVVARYTDEAEVRAVLTRLPGNLTATVQLSSEEAAGHGSGAELVRELTPLAGRVLVNGWPTGVAVAPAQHHGGPYPATTSTSTSVGGTAIERWLRPVVYQGTPEALLPPELRDDNPLGLPRRFNGRLER
>NZ_CP043959.1|WP_004989734.1|1805122_1805896_-|IclR-family-transcriptional-regulator
MSAGETGGGAQVKSAVRTVELLEYFAGRPGMHSLAAVQEAVGYPKSSLYMLLRTLVDLGWVETDATGTRYGIGVRALLVGTSYIDGDEVVAAARPTLDRLSDDTTETIHLARLDGTNVVYLATRQSQHYLRPFTRVGRRLPAHSTSLGKALLSTYTDEQVRKMLPETLPALTENTITDREKLIEELHQVREQGFAVDREENTLGLRCFGVAIPYRTPARDAISCSVPVARLTPAHEQMVKDALFDARDRLTLATRRL
>NZ_CP043959.1|WP_150153500.1|1804645_1805119_-|GNAT-family-N-acetyltransferase
MDVALRPVHDSDLPVFYRQMNDPEALRMAAFTPEDPADRDRFDAHWAHIRSSPGIVARTVLADGDVVGTASVYGEAGEREVTYWIDRACWGKGIATAALRALLAEVTDRPLYARVAEDNAGSLRVLRKCGFEVTGKARAYAPGRGAETDELVLGLER
>NZ_CP043959.1|WP_150153498.1|1802933_1804391_-|penicillin-binding-protein-2
MNRTIRRASVFTLLLVLALLVRATWVQFYEGRALADDKDNRRNAIETYAEPLGNIVVGGEAITGSARTKGGDLAYKRTYTNGPLYAAVTGYASQAYAPTQLEGIYADLLNGTDTRLKTVMDTVTDRRAGPGNVVTTIDPAVQKAAYEALGDKKGAAVAIDPETGRILAAVSTPSYDPTALTDANTAGEAWTRLNADKDKPLTNRALRQPLPPGSTFKLVVAAAALEDGLYASVDAPTDSPDPYPLPGTSRDLGNENPSAPCENASIRVGLQYSCNNVFGKMAVDLGQDKVRAMAEKFGFNDEKQDVPVRAYPSVYPSDMDKAQTALSGIGQFDVTATPLQIAMVSAALANGGELMSPHMVSRVTDSGGDVLEDHDEDASARRIVSGSTAEQLRSAMETVVSEGTGTNAQISGATVGGKTGTAQHGENNSKTPYAWFTSYGESDSNGRKVAVAVLVEQSDAARSEVSGNGLAAPIARATMKAALHD
>NZ_CP043959.1|WP_004932953.1|1814614_1815013_-|ectoine-synthase
MIVRSFKEIEGTDRHVKSASGTWESKRIVLAKEKVGFSVHETILYAGTETDMWYANHIEAVVCTKGDAELTDRETGKTYHITPGTMYLLDGHERHTLKVKEDFHCICVFNPPVTGREDHDENGVYPLLTEEV
>NZ_CP043959.1|WP_150153518.1|1815049_1816321_-|diaminobutyrate--2-oxoglutarate-transaminase
MTITQPDLSVFETLESEVRSYCRGWPAVFDRAHGSRMYDEDGHEYLDFFAGAGSLNYGHNNPVLKRALIDYLERDGVTHGLDMSTTAKRAFLESFQNYVLRPRDLPYKVMFPGPTGTNAVESALKLARKVKGREAIVSFTNAFHGMSLGSLAVTGNAFKRAGAGIPLVHGTPMPFDNYFDGQVPDFLWFERLLEDQGSGLNKPAAVIVETVQGEGGINVARPEWLRALAELCERQDMLLIVDDIQMGCGRTGAFFSFEEAGITPDIVTVSKSISGYGLPMALTLFKPELDIWEPGEHNGTFRGNNPAFVTATAALEAYWADGSAMEKQTRGRGEQVEQAMIAITEENLADVKEYRGRGLVWGLEFHDKERAGRVARRAFELGLLIETSGPESEVVKLLPALTVTPDELDEGLTVLARAVRETA
>NZ_CP043959.1|WP_145825107.1|1816388_1816895_-|diaminobutyrate-acetyltransferase
MTAAQADLQIDRPTVADGAVLWRIARDSKVLDLNSSYSYLLWCRDFAATSAVARDERGAPVGFITGYLRPDSPRTLLVWQVAVDETHRGRGLAAAMLDGLAARTAAEHGVDTVETTVAPGNTASERLFTAFAERHDALLEREVLFDAGQFPDGPHDPEVLYRIGPFAL
>NZ_CP043959.1|WP_150153520.1|1817248_1817788_-|DUF664-domain-containing-protein
MGDDVSSSGPITLPDGRPVPRFRGDERAMLESWLEYHRATLALKCAGLDDAQVRLASAEPSALTLLGLVQHLAEVERNWFQRIVAGRDVPPVFDDVTGFALDPARGIDEALAAWHREIARGQELTEGLPLDGTGLITDGPMAGVEVSLRWVLIHLIEEYARHNGHADLLRERIDGVTGS
>NZ_CP043959.1|WP_150153522.1|1817956_1819057_-|aminotransferase-class-V-fold-PLP-dependent-enzyme
MTNLLLDLPPLSAARFASVEDRVARLLGTGQDVVITQGEALLPLEGAIRAAAGPGTTALNVITGPYGQTFGDWLRDCGATVIDLTVPFHTAVTAGQIQDAFAEHPEIDFVSLVHAEAATGNTNPVAGIGEVVRSHGALFYLDAVASVGAEPVLPDAWGVDLCVIGAQKAMGGPAGVSAVSVSERAWARMAANPHAPRRSYLSLLDWKERWIDGGRKALLHAPAQLEMLALEACVERIEAEGLETVMARHASAAAATRAGALALGGGIAPYVHDAADAAPVATTLRAPSGTTASELVARALAADPDLPLAAGGGALAREMIRVNHYGPDATRGTVRACLTALATALTDAGLPTDLPAALAAAEEAWQ
>NZ_CP043959.1|WP_145825104.1|1819249_1820101_+|transporter-substrate-binding-domain-containing-protein
MKTLLGRRTRVLAATTATAGMVLLAACTSTDDGGSGSTTAAGGVELVKAGQLTTCTHLPYPPFQSEIDGKVQGFDVALIDLVADDLGVKQQILDTPFENFKTGAFLNSGECDLAAAGMTITDERKKNVDFSDPYFNATQAVLVDKDSGVTSLADVKSENVKLGAQAQTTGEDYVKGQGFDPVSFESSDAVLNGLRTGQVKAVVIDYPVVQGWLKDKANADAFTVAEQIDTGEEYGFTVKKGNTALQKAVNKALADAKADGTYKKLYEQWIGPYDESAASPAAS
>NZ_CP043959.1|WP_150153524.1|1820105_1820942_+|ABC-transporter-permease-subunit
MADTEKTPLQPKRKGLTRRQKRSVSRGIQYAVFVAAVIAFAVTADWGRLQNQFAQVDIAERMFPDVITLALKNTVLYTVTGFAVGLALGMLIALMRLSSVGPYRWLAGVYIEIFRGLPALLIFIFIGVAVPLAFPGTEIIGGTYGKVALALGLVAAAYMAETIRAGIQAVPKGQMEAARSLGFSPARAMVSVIIPQAFRIILPPLTNELVLLFKDSSLVLFLGVTLEERELSKYGRDLASQTANSTPILVAGLCYLLITIPLGFVVRRMEAKAQEAVK
>NZ_CP043959.1|WP_145825102.1|1820938_1821730_+|ATP-binding-cassette-domain-containing-protein
MSRPEIRVSALHKSFGDNHVLRGIDLEIGQGEVVCVIGPSGSGKSTLLRCVNLLEEPTEGQVFVGGTELTDPDVDIDAVRRRIGMVFQQFNLFPHLTVTENLTLPQRRVLRRGKAEAAKVAAENLERVGLAEKADAYPSSLSGGQQQRVAIARALAMGPEVMLFDEPTSALDPELVGDVLAVMRMLADEGMTMMVVTHEMTFAREVADRVVFMDGGVIVEDGSPAQVIGAPRHERTRHFLSRLLDPAMAEVEEETSDQVGKSG
>NZ_CP043959.1|WP_150153526.1|1821751_1822843_+|amidohydrolase-family-protein
MSERAVLHLKGRILVGPHEVRDELWVVDGRISYDRPAGARDVCTLDGWVLPGLVDAHCHVGLDRHGAVPEDVAEKQALTDRDAGALLLRDAGSPSDTRWTDAREDLPKIIRAGRHIARTRRYIRGYAWEVEPGDLVAYVAQEARRGDGWVKLVGDWIDRDLGDLSACWPRGAVEAAIAEAHRLGARVTAHCFAEDSLRDLVEAGIDCVEHATGLTDDTIPLFAERGVAIVPTLVNIATFPALADGGEGKFPRWSAHMRRLHERRYDTVRSAYDAGIPVFVGTDAGGTLPHGLAAEEVAELAKAGLPAVEALAAGTWKAREWLGRPGLEEGAPADLVVYDADPRADLRVLTDPRRVVLNGRVVA
>NZ_CP043959.1|WP_167534492.1|1823021_1823975_+|LPXTG-cell-wall-anchor-domain-containing-protein
MYTINFPAPARRWTASAAACALVAGPVVLTGAGAAYATEGHGSASAAVLRTGLDVSLLNKTVQVPLTVSLNAVQAPRSAQKTALTATLDGVNHGKPFSVLRAEVADAEATVEGERAEASTTLADARLHVPGLPLLSVVEIEAVSSKAVCEAGKNPHASVTLPAAVTVLGKRVSLSAGGPTHVEVPGVGSVRLDLSKTETTSSTAVATALKLEVSVNPAKLNVAEVEGSLTLAESRCEAPAAGEEPQTAAPEEAGDAPAQEEAAVEAQGARAEQAASTETNLAETGGDSATPYVAGGAVALLAAGGGAVLLSRRGRRN

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Crispr_ID: NZ_CP043959_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_4

2143517-2143616

Orphan

Consensus_repeat	Method
CCCCTCCAGGGGCGCGGGGAACTGCGCGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_4

>merge|NZ_CP043959|4|2143517-2143616|CRISPRCasFinder
CCCCTCCAGGGGCGCGGGGAACTGCGCGAACAATCACAACGCCCCCGCACGAACCGTGCCACGGAGACCACCCCTCCCAGGGGCGCGGGGAACTGCGCGA

>NZ_CP043959|4|4|2143517-2143616|CRISPRCasFinder
CCCCTCCAGGGGCGCGGGGAACTGCGCGA	ACAATCACAACGCCCCCGCACGAACCGTGCCACGGAGACCAC
CCCTCCCAGGGGCGCGGGGAACTGCGCGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150153939.1\|2142016_2143447_+\|argininosuccinate-lyase	unknown	unknown	gnl\|CDD\|179143
NZ_CP043959.1\|WP_150153933.1\|2136345_2137098_-\|FMN-binding-protein	unknown	unknown	gnl\|CDD\|226484
NZ_CP043959.1\|WP_024885111.1\|2139328_2139916_-\|pyridoxamine-5'-phosphate-oxidase-family-protein	unknown	unknown	gnl\|CDD\|334450
NZ_CP043959.1\|WP_150153929.1\|2132680_2133583_+\|acetylglutamate-kinase	unknown	unknown	gnl\|CDD\|234869
NZ_CP043959.1\|WP_145827960.1\|2147115_2147790_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153251
NZ_CP043959.1\|WP_145827957.1\|2150611_2151040_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_167534499.1\|2144831_2145401_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP043959.1\|WP_167534498.1\|2137151_2138534_-\|ferredoxin-reductase-family-protein	unknown	unknown	gnl\|CDD\|99795
NZ_CP043959.1\|WP_145827956.1\|2151041_2151401_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150153937.1\|2140697_2141912_+\|argininosuccinate-synthase	unknown	unknown	gnl\|CDD\|234785
NZ_CP043959.1\|WP_150153949.1\|2151495_2152146_+\|HAD-IA-family-hydrolase	unknown	unknown	gnl\|CDD\|319829
NZ_CP043959.1\|WP_167534500.1\|2152536_2153574_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|236863
NZ_CP043959.1\|WP_150157280.1\|2135549_2136287_-\|FAD:protein-FMN-transferase	unknown	unknown	gnl\|CDD\|376782
NZ_CP043959.1\|WP_150153935.1\|2140056_2140503_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_145827969.1\|2134792_2135359_+\|arginine-repressor	unknown	unknown	gnl\|CDD\|235116
NZ_CP043959.1\|WP_150153943.1\|2145397_2146918_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|184957
NZ_CP043959.1\|WP_150153947.1\|2149481_2150009_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357
NZ_CP043959.1\|WP_150153931.1\|2133579_2134785_+\|acetylornithine-transaminase	unknown	unknown	gnl\|CDD\|235112
NZ_CP043959.1\|WP_150157282.1\|2150066_2150564_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379228
NZ_CP043959.1\|WP_150153945.1\|2148236_2149406_+\|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl\|CDD\|176544

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150153939.1\|2142016_2143447_+\|argininosuccinate-lyase	gnl\|CDD\|179143	PRK00855, PRK00855, argininosuccinate lyase; Provisional.	0
NZ_CP043959.1\|WP_150153933.1\|2136345_2137098_-\|FMN-binding-protein	gnl\|CDD\|226484	COG3976, COG3976, Uncharacterized protein conserved in bacteria [Function unknown].	2.23064e-09
NZ_CP043959.1\|WP_024885111.1\|2139328_2139916_-\|pyridoxamine-5'-phosphate-oxidase-family-protein	gnl\|CDD\|334450	pfam01243, Putative_PNPOx, Pyridoxamine 5'-phosphate oxidase. Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as yeast YLR456W and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.	1.39551e-11
NZ_CP043959.1\|WP_150153929.1\|2132680_2133583_+\|acetylglutamate-kinase	gnl\|CDD\|234869	PRK00942, PRK00942, acetylglutamate kinase; Provisional.	2.8461e-150
NZ_CP043959.1\|WP_145827960.1\|2147115_2147790_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153251	cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.	1.38898e-52
NZ_CP043959.1\|WP_167534500.1\|2152536_2153574_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|236863	PRK11153, metN, DL-methionine transporter ATP-binding subunit; Provisional.	6.91695e-169
NZ_CP043959.1\|WP_167534499.1\|2144831_2145401_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	3.36559e-05
NZ_CP043959.1\|WP_167534498.1\|2137151_2138534_-\|ferredoxin-reductase-family-protein	gnl\|CDD\|99795	cd06198, FNR_like_3, NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.	1.18486e-66
NZ_CP043959.1\|WP_150153937.1\|2140697_2141912_+\|argininosuccinate-synthase	gnl\|CDD\|234785	PRK00509, PRK00509, argininosuccinate synthase; Provisional.	0
NZ_CP043959.1\|WP_150153949.1\|2151495_2152146_+\|HAD-IA-family-hydrolase	gnl\|CDD\|319829	cd07527, HAD_ScGPP-like, subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.12279e-73
NZ_CP043959.1\|WP_150157280.1\|2135549_2136287_-\|FAD:protein-FMN-transferase	gnl\|CDD\|376782	pfam02424, ApbE, ApbE family. This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalyzing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.	1.12509e-56
NZ_CP043959.1\|WP_145827969.1\|2134792_2135359_+\|arginine-repressor	gnl\|CDD\|235116	PRK03341, PRK03341, arginine repressor; Provisional.	7.4068e-88
NZ_CP043959.1\|WP_150153943.1\|2145397_2146918_+\|MFS-transporter	gnl\|CDD\|184957	PRK14995, PRK14995, SmvA family efflux MFS transporter.	1.85366e-101
NZ_CP043959.1\|WP_150153947.1\|2149481_2150009_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	1.0453e-12
NZ_CP043959.1\|WP_150153931.1\|2133579_2134785_+\|acetylornithine-transaminase	gnl\|CDD\|235112	PRK03244, argD, acetylornithine transaminase.	0
NZ_CP043959.1\|WP_150157282.1\|2150066_2150564_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379228	pfam13508, Acetyltransf_7, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	2.53338e-12
NZ_CP043959.1\|WP_150153945.1\|2148236_2149406_+\|glycerophosphodiester-phosphodiesterase	gnl\|CDD\|176544	cd08602, GDPD_ScGlpQ1_like, Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.	1.15366e-169

>NZ_CP043959.1|WP_150153939.1|2142016_2143447_+|argininosuccinate-lyase
MSSNSGDVRLWGGRFADGPAEALAKLSASVHFDWRLAPYDVAGSRAHARVLHTAGLLTEDELTRMIEGLDQLEADVASGAFTGTIADEDVHTALERGLLERLGPDLGGKLRAGRSRNDQVATLFRMYLRDHARVIGGLIAELQDALVGLAEAHPDVAMPGRTHLQHAQPVLFAHHVLAHVQSLSRDAERLRQWDERTAVSPYGSGALAGSSLGLDPEAVAEDLGFEHGSAANSIDGTASRDFVAEFAFITAMIGVNLSRIAEEVIIWNTKEFSFVTLHDAFSTGSSIMPQKKNPDIAELARGKSGRLIGNLTGLMATLKALPLAYNRDLQEDKEPVFDSIDQLEILLPAFTGMMATLTVHRERMEELAPAGFSLATDIAEWLVRQGVPFRVAHEVAGECVKVAEAEGKELDELTDEQFAKISAHLTPEVRSVLDVPGALASRNGRGGTAPSAVAIQLAEIKQDVAAQHQWATAKKQ
>NZ_CP043959.1|WP_150153937.1|2140697_2141912_+|argininosuccinate-synthase
MHCEEKPVTERVVLAYSGGLDTSVAIGWIAEETGAEVIAVAVDVGQGGEDLDVIRKRALACGAVEAEVADAKDEFAEEYCLPAIKANALYMDRYPLVSALSRPTIVKHLVAAAQKHGATTVAHGCTGKGNDQVRFEAGIVALAPDLKCIAPVRDYAMTRDKAIAFCEAKGLPIATTKKSPYSIDQNVFGRAVETGFLEDIWNAPIEDVYEYTQNPAVVREPDEVVITFKEGVPVAIDGKPVTVLQAIQQLNERAGAQGIGRIDMVEDRLVGIKSREVYEAPGAIALITAHQELENVTVERELARYKRQVEQRWGELVYDGQWFSPLKRALDGFIAEANQHVNGDIRMTLHGGRAVVTGRRSESSLYDFNLATYDTGDTFDQAAAKGFIDIYSLSSKIAAKRDLA
>NZ_CP043959.1|WP_150153935.1|2140056_2140503_-|hypothetical-protein
MSRALPKYNKRRVGLAGGAAAVALTGAVIAGTALAGEPSDGGGADARTLAGPGTVSCPDVASRLPAIPASAQAEVTRNLGQLDQQTVEANQRLVDTVGQGGPNFARNAILGPLKDKRAAAIDRIALSIGRTTDRPAELDSLAACTLTK
>NZ_CP043959.1|WP_024885111.1|2139328_2139916_-|pyridoxamine-5'-phosphate-oxidase-family-protein
MGKTYERIDGRLRTFIEDQPVFFTATAPLSADGTVNLSPKGLKGSFAVLDELTVAYLDFAGSNAETVAHLRENGRITLMWCAFQGPPNIVRVHGRGEPVFRDDPRFAELLAHFPDIDPWTHGLRAIVVVRAELIRDTCGYAVPFMAYESERDLHEKRFAREDDASLDAYFTKKEHIATSMDGLPGLPLPLPPSSV
>NZ_CP043959.1|WP_167534498.1|2137151_2138534_-|ferredoxin-reductase-family-protein
MTTTLAGGRAARRQTMRRIRPRRSPAVPLLFAVGAGAVAVLWLWWTSTPSIADTTGKIIAAGRITGLLAGYLMALVVLQMARVPALERRVGSDRVARWHAMSGRYTVSLVLAHVFLIMWGYARQAGRTLADIVSQTVTSVTTLPDMGKAAIGTGLLFVIAFLSVGPVRRRLPYDGWYHVHLLTYAAVFLTFWHQISTGNEFAVTPSAKTFWYGLYGTVTALVLWYRIITPVRLNLRHQMRVQAVIEETPGVVSVLISGRRLHRMGAEAGQFFRWRFLAPGMRFSSHPYSLSAAPRPDMLRITVKAIGDHSSRLRELEPGTRVWAEGPYGALTAQRRSRGKVLLVAGGVGITPMRALFETLPGASGDITLLYRANSTQDLALWGELAKIADERGARLMYAVNSPDGERPDISAESLRRKMPDIDRHDVFMCGPPGFAQQVYAALRDAGVPARRIHHESFEM
>NZ_CP043959.1|WP_150153933.1|2136345_2137098_-|FMN-binding-protein
MRKSHPLRRAVLATAATVSGIVLLLSLKPGSDPGSAAAAGGAPPAAESVQGGARPIGDGTVTGDAAQTQYGAVQVRLTVSGGKITKAEAVQAPKGGQSDQVTSTSVPRLNQAAVAAQSAEIDAVSGATYTSNGYKQSLQSALDKARAAAPAGTGGGAAAEARTVTGEVAQTQYGPVQVRITVDGGKITKAEAVQAPKGGQSDQVTSTSVPKLNEAAVQAGSADIDAVSGATYTSNGYKESLQSALDEAGG
>NZ_CP043959.1|WP_150157280.1|2135549_2136287_-|FAD:protein-FMN-transferase
MGTVFSLDVRGGEPGAVRAALEEAVAGLRRVDEVFSTYREDSQISRLARGELDVGACDREVAEVLELAAEAERVSEGWFSTRYRGELDPTGIVKGWATERAARRLLAAGASGVSVNGGGDVQLLGSPGTGRPWRVGVSDPLRPGGLAAVVSAAGARDLAVATSGTAERGDHIVDPRTGLSAVTDLVAVTVVAPRLTWADCWATAAFAMGSREALRWLESLPDTEALLITAGDEVRCTGNLAAWLG
>NZ_CP043959.1|WP_145827969.1|2134792_2135359_+|arginine-repressor
MSQEQDQGRTAGGAGQAGPAVPQTRTARHRRIVDILNRQPVRSQSQLAKLLADDGLSVTQATLSRDLDELNAVKIRNNDGDLIYAVPSEGGFRTPRAPLGESAKEERMRRLSAELLISAEASANLVVLRTPPGAAQFLASAIDQAELQDILGTIAGDDTLLLISREPTGGQALADHLLRLAQNGHNGH
>NZ_CP043959.1|WP_150153931.1|2133579_2134785_+|acetylornithine-transaminase
MSNAELTARWQGALMNNYGTPRLPLVRGEGQRLWDADGKEYLDFVGGIATNALGHAHPAVVEAVTLQISSLGHISNLFLAEPTVALAERLLQHFGRDGRVFFCNSGAEANEAAFKIGRLTGRTHVVATEGAFHGRTMGALALTGQAGKREPFLPLPGDVTHVPFGDAQVLDAAVTEDTAAVVLEPIQGELGVVVPPPGYLKAARAITAAKGALLVLDEVQTGIGRTGNWFEYQAHEGVLPDVVTLAKQLGGGLPLGATVAFGRAAHLLGPGHHGTTFGGNPVACSAGLAVLDTIADEGLLENVKRQGAKLRDGIEGSGHALIDHVRGAGLLLGIVLTEPLAPQAQQAAQDAGFLVNAPAPDVVRLMPPLNLGDDAVDAFLGALPGILDAAGQAGGEGRSGE
>NZ_CP043959.1|WP_150153929.1|2132680_2133583_+|acetylglutamate-kinase
MTVTRKHTALPKAQILIEALPWLTRHHGRTVVIKFGGNAMVDEDLKAAFAQDVVFLRHAGLKPVVVHGGGPQISRALETHGIVSEFKAGLRVTTEDAMDVVRMVLAGQVQRELVGLLNRHGPLAVGLTGEDAHTLTAVKHQPEIDGELVDIGRVGEITEIDTGAIEALLADGRIPVVSSIARSQDDHHVYNVNADTAAAALAAALGAETLMVLTDVEGLYEDWPNSDEVISRLTASQLEKLLPDLSSGMVPKMEGCLHAVRNGVNTARVIDGRVQHSILLEIFTDEGIGTMVVPDEQGES
>NZ_CP043959.1|WP_167534499.1|2144831_2145401_+|TetR-family-transcriptional-regulator
MAVDRDHVLRSAAGLLTRKSTATMDEVARAAGISRATLHRQFAGRDALVRALEALGIAECEAALTAARTDEGPATDAVRRLVAEIEPHAGLLAFLYSENQLFEGEEQNEGWARIDEGVADLFRRGQSSGEFRIDLTPAWLTEALYGLLASAAWAVAEGRVAPNDFTHMIVELLLGGVRRPAEPARRKQS
>NZ_CP043959.1|WP_150153943.1|2145397_2146918_+|MFS-transporter
MTSAIRPHTTTEETPRPGRWLALSVLVLAVLLVAVDATVLGLATPYISEDLAPTGTQLLWIGDVYSFVIAGLLVSMGSLGDRIGRKRILLYGAAAFGAVSVLNAYAHTPEVMILARALLGVAGATLMPATLALIRNLFHDPRERSLAIGIWGATASAGTAVGPILGGLLLEHFWWGSVFLINLPVMAVLVVVGIKFLPESRTPQPGPWDLTSVVLSLAGMIGVVYAVKETASHGPAPSALAAGLLGAAALYLFVRRQLTLPVPLLDVRLFRHPGFSGAVLADLLAVLGLSGLVFFLSQYLQLVQGRRPFEAGLAELPAAIGAVVAGLIAGRAARRFSVRSVVAGGLAAIGLALASLTVIGQSTGYPLLGAALLVVGAGAGFSFTVTADVILSSVPKEQAGAASAVSETAYELGAALGIAVLGSIVTGVYRGFPGPPGTPAAAHESLGGAVEAATHLPAATAAPMLDAAREAFVNGLTLAAGTGAIVLLTAAAAAWYMLRDQHLDNT
>NZ_CP043959.1|WP_145827960.1|2147115_2147790_-|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MSRFALIKAVLGPIMRLMFRPRVEGAEHIPGDGPVILAGNHLTFIDSMILPLVCDRQVFFIGKDEYVTGKGFKGRLMAWFFTGVGMIPVDRDGGRGGVAALMTGRRVLEEGNVFGIYPEGTRSPDGRLYRGRTGIARLTLMTGAPVVPFAMIGTDKLQPGGAGLPRPGRVTVRFGEAMEFSRYEGMDRDRYVLRAVTDSVMTEVMRLSGQEYVDMYASKAKEAA
>NZ_CP043959.1|WP_150153945.1|2148236_2149406_+|glycerophosphodiester-phosphodiesterase
MAAPESNEQVGGTGRRALLGAAVLGAGGTVLGLGGTARAAGAGHGGGRGLDSLPVPTVIGHRGASGYRPEHTLGSYQLALDMGADIVEAGDLVPTKDGHLVCRHEPEIGGTTDVADHPEFAGRRTTKTLDGVQVTGWFTEDFTLAELKRLRAVERVPANRPHNTLYDGRWEIPTFEEVLRWQDEQTRRRGKQVWIYPELKHPTYFRKLGLGLEERVAKVLRRHGKDRKNSPVILQSFESTAVERMNELVGNPLVVLLDAAGTRPWDFTETGDPRTVDDLITPKGLKEIASYAQGIGPTLNLIIPRDASGRLTEPTTLVRDAHRAGLVLHPYTMRNENPFLPAEFRKGSDPDAYGDVFGAYRAYFATGIDGVFTDNPDTGLLAREDFVNR
>NZ_CP043959.1|WP_150153947.1|2149481_2150009_+|sigma-70-family-RNA-polymerase-sigma-factor
MTTDPLSTYDAPAHDLIALLRPLLAAEAAAEAFGSGAEPGDLEQAVWLRLLERLRRDGPPPDPPLWLRRAVRAEARRARRTARRETSLTCEPADADRPDPERLALAAARRRVLRDAVRRLPGRCPRLLAALLSPLDPTYREIAGELGISQGSLGPERSRCLGCLRRLLAAEVAAR
>NZ_CP043959.1|WP_150157282.1|2150066_2150564_+|GNAT-family-N-acetyltransferase
MGMSVTISAAAEQDAEQIFRLQYLCFQSEAALYGNYRIDPLIQSLDSVREEVAGDCVFVARLGDEIVGSVHGRITEDGAAAIGKLCVHPRLQGHGIGARLLKAAESALAGERGARTFRLQAGHRSESNLRLYSKVGYQRVGTSRGADGVPMIVLEKKAEAYATTA
>NZ_CP043959.1|WP_145827957.1|2150611_2151040_-|hypothetical-protein
MTATQERPNRTRLTGGPGVLLVWLYGVMVVGAVSRSVYQIATEFDRAPLAYSLSALAGVVYGFITYTLVRGGEKARKAALVCCAAELVGVLTVGTWTWVEPSAFPDATVWSDYGMGYLFIPVLLPLTAVYWLRRARPQEPAA
>NZ_CP043959.1|WP_145827956.1|2151041_2151401_-|hypothetical-protein
MLDVLTVVTAVAALLLAAWCGWAAYRDQPTKDWHFIGMAVVTLLALVQLVVGIVQLARGEKPEQGTTVFVAYLLGSFACVPAAGFLSLGERTRWGSLTVAASGVVLAVLEVRLFDIWGG
>NZ_CP043959.1|WP_150153949.1|2151495_2152146_+|HAD-IA-family-hydrolase
MTIHARALLFDNDGTLVSSLDSVNRCWTRWAVEYGLTAEDFARVELHGRPAAEIAADLLPAHVVPEAVARIEDLEVADVPNGGVRLLPGTKEFLAALPAERWAVVTSATRRLAEARLGAVGILPKTLIAADDITRGKPDPEPYLLAARTLGVDPAHCVVFEDAPAGLQAGRAAGMTTVALATTHRAEELTADLVVDNLSTLSALVTDAGVEISVRP
>NZ_CP043959.1|WP_167534500.1|2152536_2153574_+|ATP-binding-cassette-domain-containing-protein
MITTSGLTKVYRSRGREVTALDGVDLHVREGEVYGVIGQSGAGKSSLIRCVNLLERPTAGTVTVAGQDLTALAGRGPRAGRELRQARSRIGMVFQHFNLLSSRTVQDNVELPLEILGTSGKERSRKALELLDLVGLADKAKAYPAQLSGGQKQRVGIARALAGDPKVLLSDEATSALDPETTRSILQLLRDLNRQLGLTVLLITHEMDVVKSICDSAALMERGRIVESGTVTDLLATPGSELAAALFPVGGEATGEDRTVVDVTFHGESATQPVISQLSRTYNIDISILGAAIDTVAGLQVGRMRIELPGRYEDNVVPIGFLREQGLQIDVVDHDEPTLVKEGAK

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Crispr_ID: NZ_CP043959_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_5

2146947-2147041

Orphan

Consensus_repeat	Method
GCGACAAGCCCCGCCCACCCGCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_5

>merge|NZ_CP043959|5|2146947-2147041|CRISPRCasFinder
GCGACAAGCCCCGCCCACCCGCACCAGCCGCCAAGGCGACGGAGCCGCCCCCTAGGGGCGCGGGGAACTGCGCGACAAGCCCCGCCCACCCGCAC

>NZ_CP043959|5|5|2146947-2147041|CRISPRCasFinder
GCGACAAGCCCCGCCCACCCGCAC	CAGCCGCCAAGGCGACGGAGCCGCCCCCTAGGGGCGCGGGGAACTGC
GCGACAAGCCCCGCCCACCCGCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150153939.1\|2142016_2143447_+\|argininosuccinate-lyase	unknown	unknown	gnl\|CDD\|179143
NZ_CP043959.1\|WP_150153933.1\|2136345_2137098_-\|FMN-binding-protein	unknown	unknown	gnl\|CDD\|226484
NZ_CP043959.1\|WP_024885096.1\|2154382_2155210_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270315
NZ_CP043959.1\|WP_024885111.1\|2139328_2139916_-\|pyridoxamine-5'-phosphate-oxidase-family-protein	unknown	unknown	gnl\|CDD\|334450
NZ_CP043959.1\|WP_167534501.1\|2153570_2154308_+\|methionine-ABC-transporter-permease-MetI	unknown	unknown	gnl\|CDD\|224922
NZ_CP043959.1\|WP_145827960.1\|2147115_2147790_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153251
NZ_CP043959.1\|WP_145827957.1\|2150611_2151040_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_167534499.1\|2144831_2145401_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP043959.1\|WP_167534498.1\|2137151_2138534_-\|ferredoxin-reductase-family-protein	unknown	unknown	gnl\|CDD\|99795
NZ_CP043959.1\|WP_145827956.1\|2151041_2151401_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150153937.1\|2140697_2141912_+\|argininosuccinate-synthase	unknown	unknown	gnl\|CDD\|234785
NZ_CP043959.1\|WP_150153949.1\|2151495_2152146_+\|HAD-IA-family-hydrolase	unknown	unknown	gnl\|CDD\|319829
NZ_CP043959.1\|WP_150157280.1\|2135549_2136287_-\|FAD:protein-FMN-transferase	unknown	unknown	gnl\|CDD\|376782
NZ_CP043959.1\|WP_150153935.1\|2140056_2140503_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_145827969.1\|2134792_2135359_+\|arginine-repressor	unknown	unknown	gnl\|CDD\|235116
NZ_CP043959.1\|WP_150153943.1\|2145397_2146918_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|184957
NZ_CP043959.1\|WP_150153947.1\|2149481_2150009_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357
NZ_CP043959.1\|WP_167534500.1\|2152536_2153574_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|236863
NZ_CP043959.1\|WP_150157282.1\|2150066_2150564_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379228
NZ_CP043959.1\|WP_150153945.1\|2148236_2149406_+\|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl\|CDD\|176544

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150153939.1\|2142016_2143447_+\|argininosuccinate-lyase	gnl\|CDD\|179143	PRK00855, PRK00855, argininosuccinate lyase; Provisional.	0
NZ_CP043959.1\|WP_150153933.1\|2136345_2137098_-\|FMN-binding-protein	gnl\|CDD\|226484	COG3976, COG3976, Uncharacterized protein conserved in bacteria [Function unknown].	2.23064e-09
NZ_CP043959.1\|WP_024885111.1\|2139328_2139916_-\|pyridoxamine-5'-phosphate-oxidase-family-protein	gnl\|CDD\|334450	pfam01243, Putative_PNPOx, Pyridoxamine 5'-phosphate oxidase. Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as yeast YLR456W and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.	1.39551e-11
NZ_CP043959.1\|WP_167534501.1\|2153570_2154308_+\|methionine-ABC-transporter-permease-MetI	gnl\|CDD\|224922	COG2011, AbcD, ABC-type metal ion transport system, permease component [Inorganic ion transport and metabolism].	1.13079e-99
NZ_CP043959.1\|WP_145827960.1\|2147115_2147790_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153251	cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.	1.38898e-52
NZ_CP043959.1\|WP_024885096.1\|2154382_2155210_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270315	cd13597, PBP2_lipoprotein_Tp32, The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum binds L-methionine; the type 2 periplasmic-binding protein fold. This group includes the lipoprotein Tp32, a periplasmic component of a methionine uptake transporter system, and its closely related homologs. The Tp32 has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus it belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.	9.93925e-128
NZ_CP043959.1\|WP_167534499.1\|2144831_2145401_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	3.36559e-05
NZ_CP043959.1\|WP_167534498.1\|2137151_2138534_-\|ferredoxin-reductase-family-protein	gnl\|CDD\|99795	cd06198, FNR_like_3, NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.	1.18486e-66
NZ_CP043959.1\|WP_150153937.1\|2140697_2141912_+\|argininosuccinate-synthase	gnl\|CDD\|234785	PRK00509, PRK00509, argininosuccinate synthase; Provisional.	0
NZ_CP043959.1\|WP_150153949.1\|2151495_2152146_+\|HAD-IA-family-hydrolase	gnl\|CDD\|319829	cd07527, HAD_ScGPP-like, subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.12279e-73
NZ_CP043959.1\|WP_150157280.1\|2135549_2136287_-\|FAD:protein-FMN-transferase	gnl\|CDD\|376782	pfam02424, ApbE, ApbE family. This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalyzing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.	1.12509e-56
NZ_CP043959.1\|WP_145827969.1\|2134792_2135359_+\|arginine-repressor	gnl\|CDD\|235116	PRK03341, PRK03341, arginine repressor; Provisional.	7.4068e-88
NZ_CP043959.1\|WP_150153943.1\|2145397_2146918_+\|MFS-transporter	gnl\|CDD\|184957	PRK14995, PRK14995, SmvA family efflux MFS transporter.	1.85366e-101
NZ_CP043959.1\|WP_150153947.1\|2149481_2150009_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	1.0453e-12
NZ_CP043959.1\|WP_167534500.1\|2152536_2153574_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|236863	PRK11153, metN, DL-methionine transporter ATP-binding subunit; Provisional.	6.91695e-169
NZ_CP043959.1\|WP_150157282.1\|2150066_2150564_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379228	pfam13508, Acetyltransf_7, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	2.53338e-12
NZ_CP043959.1\|WP_150153945.1\|2148236_2149406_+\|glycerophosphodiester-phosphodiesterase	gnl\|CDD\|176544	cd08602, GDPD_ScGlpQ1_like, Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.	1.15366e-169

>NZ_CP043959.1|WP_150153943.1|2145397_2146918_+|MFS-transporter
MTSAIRPHTTTEETPRPGRWLALSVLVLAVLLVAVDATVLGLATPYISEDLAPTGTQLLWIGDVYSFVIAGLLVSMGSLGDRIGRKRILLYGAAAFGAVSVLNAYAHTPEVMILARALLGVAGATLMPATLALIRNLFHDPRERSLAIGIWGATASAGTAVGPILGGLLLEHFWWGSVFLINLPVMAVLVVVGIKFLPESRTPQPGPWDLTSVVLSLAGMIGVVYAVKETASHGPAPSALAAGLLGAAALYLFVRRQLTLPVPLLDVRLFRHPGFSGAVLADLLAVLGLSGLVFFLSQYLQLVQGRRPFEAGLAELPAAIGAVVAGLIAGRAARRFSVRSVVAGGLAAIGLALASLTVIGQSTGYPLLGAALLVVGAGAGFSFTVTADVILSSVPKEQAGAASAVSETAYELGAALGIAVLGSIVTGVYRGFPGPPGTPAAAHESLGGAVEAATHLPAATAAPMLDAAREAFVNGLTLAAGTGAIVLLTAAAAAWYMLRDQHLDNT
>NZ_CP043959.1|WP_167534499.1|2144831_2145401_+|TetR-family-transcriptional-regulator
MAVDRDHVLRSAAGLLTRKSTATMDEVARAAGISRATLHRQFAGRDALVRALEALGIAECEAALTAARTDEGPATDAVRRLVAEIEPHAGLLAFLYSENQLFEGEEQNEGWARIDEGVADLFRRGQSSGEFRIDLTPAWLTEALYGLLASAAWAVAEGRVAPNDFTHMIVELLLGGVRRPAEPARRKQS
>NZ_CP043959.1|WP_150153939.1|2142016_2143447_+|argininosuccinate-lyase
MSSNSGDVRLWGGRFADGPAEALAKLSASVHFDWRLAPYDVAGSRAHARVLHTAGLLTEDELTRMIEGLDQLEADVASGAFTGTIADEDVHTALERGLLERLGPDLGGKLRAGRSRNDQVATLFRMYLRDHARVIGGLIAELQDALVGLAEAHPDVAMPGRTHLQHAQPVLFAHHVLAHVQSLSRDAERLRQWDERTAVSPYGSGALAGSSLGLDPEAVAEDLGFEHGSAANSIDGTASRDFVAEFAFITAMIGVNLSRIAEEVIIWNTKEFSFVTLHDAFSTGSSIMPQKKNPDIAELARGKSGRLIGNLTGLMATLKALPLAYNRDLQEDKEPVFDSIDQLEILLPAFTGMMATLTVHRERMEELAPAGFSLATDIAEWLVRQGVPFRVAHEVAGECVKVAEAEGKELDELTDEQFAKISAHLTPEVRSVLDVPGALASRNGRGGTAPSAVAIQLAEIKQDVAAQHQWATAKKQ
>NZ_CP043959.1|WP_150153937.1|2140697_2141912_+|argininosuccinate-synthase
MHCEEKPVTERVVLAYSGGLDTSVAIGWIAEETGAEVIAVAVDVGQGGEDLDVIRKRALACGAVEAEVADAKDEFAEEYCLPAIKANALYMDRYPLVSALSRPTIVKHLVAAAQKHGATTVAHGCTGKGNDQVRFEAGIVALAPDLKCIAPVRDYAMTRDKAIAFCEAKGLPIATTKKSPYSIDQNVFGRAVETGFLEDIWNAPIEDVYEYTQNPAVVREPDEVVITFKEGVPVAIDGKPVTVLQAIQQLNERAGAQGIGRIDMVEDRLVGIKSREVYEAPGAIALITAHQELENVTVERELARYKRQVEQRWGELVYDGQWFSPLKRALDGFIAEANQHVNGDIRMTLHGGRAVVTGRRSESSLYDFNLATYDTGDTFDQAAAKGFIDIYSLSSKIAAKRDLA
>NZ_CP043959.1|WP_150153935.1|2140056_2140503_-|hypothetical-protein
MSRALPKYNKRRVGLAGGAAAVALTGAVIAGTALAGEPSDGGGADARTLAGPGTVSCPDVASRLPAIPASAQAEVTRNLGQLDQQTVEANQRLVDTVGQGGPNFARNAILGPLKDKRAAAIDRIALSIGRTTDRPAELDSLAACTLTK
>NZ_CP043959.1|WP_024885111.1|2139328_2139916_-|pyridoxamine-5'-phosphate-oxidase-family-protein
MGKTYERIDGRLRTFIEDQPVFFTATAPLSADGTVNLSPKGLKGSFAVLDELTVAYLDFAGSNAETVAHLRENGRITLMWCAFQGPPNIVRVHGRGEPVFRDDPRFAELLAHFPDIDPWTHGLRAIVVVRAELIRDTCGYAVPFMAYESERDLHEKRFAREDDASLDAYFTKKEHIATSMDGLPGLPLPLPPSSV
>NZ_CP043959.1|WP_167534498.1|2137151_2138534_-|ferredoxin-reductase-family-protein
MTTTLAGGRAARRQTMRRIRPRRSPAVPLLFAVGAGAVAVLWLWWTSTPSIADTTGKIIAAGRITGLLAGYLMALVVLQMARVPALERRVGSDRVARWHAMSGRYTVSLVLAHVFLIMWGYARQAGRTLADIVSQTVTSVTTLPDMGKAAIGTGLLFVIAFLSVGPVRRRLPYDGWYHVHLLTYAAVFLTFWHQISTGNEFAVTPSAKTFWYGLYGTVTALVLWYRIITPVRLNLRHQMRVQAVIEETPGVVSVLISGRRLHRMGAEAGQFFRWRFLAPGMRFSSHPYSLSAAPRPDMLRITVKAIGDHSSRLRELEPGTRVWAEGPYGALTAQRRSRGKVLLVAGGVGITPMRALFETLPGASGDITLLYRANSTQDLALWGELAKIADERGARLMYAVNSPDGERPDISAESLRRKMPDIDRHDVFMCGPPGFAQQVYAALRDAGVPARRIHHESFEM
>NZ_CP043959.1|WP_150153933.1|2136345_2137098_-|FMN-binding-protein
MRKSHPLRRAVLATAATVSGIVLLLSLKPGSDPGSAAAAGGAPPAAESVQGGARPIGDGTVTGDAAQTQYGAVQVRLTVSGGKITKAEAVQAPKGGQSDQVTSTSVPRLNQAAVAAQSAEIDAVSGATYTSNGYKQSLQSALDKARAAAPAGTGGGAAAEARTVTGEVAQTQYGPVQVRITVDGGKITKAEAVQAPKGGQSDQVTSTSVPKLNEAAVQAGSADIDAVSGATYTSNGYKESLQSALDEAGG
>NZ_CP043959.1|WP_150157280.1|2135549_2136287_-|FAD:protein-FMN-transferase
MGTVFSLDVRGGEPGAVRAALEEAVAGLRRVDEVFSTYREDSQISRLARGELDVGACDREVAEVLELAAEAERVSEGWFSTRYRGELDPTGIVKGWATERAARRLLAAGASGVSVNGGGDVQLLGSPGTGRPWRVGVSDPLRPGGLAAVVSAAGARDLAVATSGTAERGDHIVDPRTGLSAVTDLVAVTVVAPRLTWADCWATAAFAMGSREALRWLESLPDTEALLITAGDEVRCTGNLAAWLG
>NZ_CP043959.1|WP_145827969.1|2134792_2135359_+|arginine-repressor
MSQEQDQGRTAGGAGQAGPAVPQTRTARHRRIVDILNRQPVRSQSQLAKLLADDGLSVTQATLSRDLDELNAVKIRNNDGDLIYAVPSEGGFRTPRAPLGESAKEERMRRLSAELLISAEASANLVVLRTPPGAAQFLASAIDQAELQDILGTIAGDDTLLLISREPTGGQALADHLLRLAQNGHNGH
>NZ_CP043959.1|WP_145827960.1|2147115_2147790_-|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MSRFALIKAVLGPIMRLMFRPRVEGAEHIPGDGPVILAGNHLTFIDSMILPLVCDRQVFFIGKDEYVTGKGFKGRLMAWFFTGVGMIPVDRDGGRGGVAALMTGRRVLEEGNVFGIYPEGTRSPDGRLYRGRTGIARLTLMTGAPVVPFAMIGTDKLQPGGAGLPRPGRVTVRFGEAMEFSRYEGMDRDRYVLRAVTDSVMTEVMRLSGQEYVDMYASKAKEAA
>NZ_CP043959.1|WP_150153945.1|2148236_2149406_+|glycerophosphodiester-phosphodiesterase
MAAPESNEQVGGTGRRALLGAAVLGAGGTVLGLGGTARAAGAGHGGGRGLDSLPVPTVIGHRGASGYRPEHTLGSYQLALDMGADIVEAGDLVPTKDGHLVCRHEPEIGGTTDVADHPEFAGRRTTKTLDGVQVTGWFTEDFTLAELKRLRAVERVPANRPHNTLYDGRWEIPTFEEVLRWQDEQTRRRGKQVWIYPELKHPTYFRKLGLGLEERVAKVLRRHGKDRKNSPVILQSFESTAVERMNELVGNPLVVLLDAAGTRPWDFTETGDPRTVDDLITPKGLKEIASYAQGIGPTLNLIIPRDASGRLTEPTTLVRDAHRAGLVLHPYTMRNENPFLPAEFRKGSDPDAYGDVFGAYRAYFATGIDGVFTDNPDTGLLAREDFVNR
>NZ_CP043959.1|WP_150153947.1|2149481_2150009_+|sigma-70-family-RNA-polymerase-sigma-factor
MTTDPLSTYDAPAHDLIALLRPLLAAEAAAEAFGSGAEPGDLEQAVWLRLLERLRRDGPPPDPPLWLRRAVRAEARRARRTARRETSLTCEPADADRPDPERLALAAARRRVLRDAVRRLPGRCPRLLAALLSPLDPTYREIAGELGISQGSLGPERSRCLGCLRRLLAAEVAAR
>NZ_CP043959.1|WP_150157282.1|2150066_2150564_+|GNAT-family-N-acetyltransferase
MGMSVTISAAAEQDAEQIFRLQYLCFQSEAALYGNYRIDPLIQSLDSVREEVAGDCVFVARLGDEIVGSVHGRITEDGAAAIGKLCVHPRLQGHGIGARLLKAAESALAGERGARTFRLQAGHRSESNLRLYSKVGYQRVGTSRGADGVPMIVLEKKAEAYATTA
>NZ_CP043959.1|WP_145827957.1|2150611_2151040_-|hypothetical-protein
MTATQERPNRTRLTGGPGVLLVWLYGVMVVGAVSRSVYQIATEFDRAPLAYSLSALAGVVYGFITYTLVRGGEKARKAALVCCAAELVGVLTVGTWTWVEPSAFPDATVWSDYGMGYLFIPVLLPLTAVYWLRRARPQEPAA
>NZ_CP043959.1|WP_145827956.1|2151041_2151401_-|hypothetical-protein
MLDVLTVVTAVAALLLAAWCGWAAYRDQPTKDWHFIGMAVVTLLALVQLVVGIVQLARGEKPEQGTTVFVAYLLGSFACVPAAGFLSLGERTRWGSLTVAASGVVLAVLEVRLFDIWGG
>NZ_CP043959.1|WP_150153949.1|2151495_2152146_+|HAD-IA-family-hydrolase
MTIHARALLFDNDGTLVSSLDSVNRCWTRWAVEYGLTAEDFARVELHGRPAAEIAADLLPAHVVPEAVARIEDLEVADVPNGGVRLLPGTKEFLAALPAERWAVVTSATRRLAEARLGAVGILPKTLIAADDITRGKPDPEPYLLAARTLGVDPAHCVVFEDAPAGLQAGRAAGMTTVALATTHRAEELTADLVVDNLSTLSALVTDAGVEISVRP
>NZ_CP043959.1|WP_167534500.1|2152536_2153574_+|ATP-binding-cassette-domain-containing-protein
MITTSGLTKVYRSRGREVTALDGVDLHVREGEVYGVIGQSGAGKSSLIRCVNLLERPTAGTVTVAGQDLTALAGRGPRAGRELRQARSRIGMVFQHFNLLSSRTVQDNVELPLEILGTSGKERSRKALELLDLVGLADKAKAYPAQLSGGQKQRVGIARALAGDPKVLLSDEATSALDPETTRSILQLLRDLNRQLGLTVLLITHEMDVVKSICDSAALMERGRIVESGTVTDLLATPGSELAAALFPVGGEATGEDRTVVDVTFHGESATQPVISQLSRTYNIDISILGAAIDTVAGLQVGRMRIELPGRYEDNVVPIGFLREQGLQIDVVDHDEPTLVKEGAK
>NZ_CP043959.1|WP_167534501.1|2153570_2154308_+|methionine-ABC-transporter-permease-MetI
MTWSEMQPLLEQACTETLVMVGWSTLIAVVGGLPLGILLVLTDKGGLLQNTVVNKVVGQIVNIGRSLPFIILMVALMNFTRWVTGTTIGSEAAIVPLAIGGIPFFARLVETAVREVDHGLVEAVQAMGGNTWTIVRKILVPEALPSLIASTTTTVIALIGYSAMAGTVGGGGLGDLAVRYGYQRFETGLMWITVAILAVVISLIQFAGDSAARALHRRGARSGPGPKLRLLKGDEPAAAEVGKVA
>NZ_CP043959.1|WP_024885096.1|2154382_2155210_+|ABC-transporter-substrate-binding-protein
MRNTAKITTAVLAAGALTLGLSACGSDKDAASDTSGPLVVAASPVPHAEILNFVKDNLAEKAGLDLEVKEFTDYVTPNTATEDGSVGANFFQTQPYLDDFNKKNGTHIVSVVDVHLEPLGLYSHKVKKADELKSGATIAIPNDTVNEGRALQLLAANGLLTLKDGVGTSATPADITDNPKKLTFKELEAAQTPRSLDDVDAAVVNGNYAIEADLKPAKDALVLEEAKDNPNSNLLAVKEGQEDDPRVKKLADLLTSPEVKKYIEDTYAGSVLPSF

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Crispr_ID: NZ_CP043959_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_6

2435578-2435684

Orphan

Consensus_repeat	Method
CGTCCGGTGATGCGTCGCCCGGCTGTCCGGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_6

>merge|NZ_CP043959|6|2435578-2435684|CRISPRCasFinder
CGTCCGGTCGCCCGTCGTCCGGTGATGCGTCGCCCGGCTGTCCGGCGCGGGAGGGCGCGGCCCCCGGCCCCCCTCCGTCCGGTGATGCGTCGCCCGGCTGTCCGGCG

>NZ_CP043959|6|6|2435578-2435684|CRISPRCasFinder
CGTCCGGTCGCCCGTCGTCCGGTGATGCGTCG	CCCGGCTGTCCGGCGCGGGAGGGCGCGGCCCCCGGCCCCCCTC
CGTCCGGTGATGCGTCGCCCGGCTGTCCGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150154133.1\|2423771_2424533_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225099
NZ_CP043959.1\|WP_150154147.1\|2444137_2444614_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|340413
NZ_CP043959.1\|WP_150154137.1\|2429742_2430756_-\|DUF21-domain-containing-protein	unknown	unknown	gnl\|CDD\|224173
NZ_CP043959.1\|WP_024884898.1\|2436733_2436973_+\|toxin-antitoxin-system-antitoxin-component	unknown	unknown	unknown
NZ_CP043959.1\|WP_024884885.1\|2424578_2425736_-\|ROK-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224851
NZ_CP043959.1\|WP_150154141.1\|2436976_2437351_+\|fic-family-toxin-antitoxin-system,-toxin-component	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154146.1\|2441500_2442628_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|235655
NZ_CP043959.1\|WP_150154136.1\|2428879_2429671_-\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238870
NZ_CP043959.1\|WP_150154143.1\|2438130_2438847_-\|ATP-dependent-dethiobiotin-synthetase-BioD	unknown	unknown	gnl\|CDD\|234625
NZ_CP043959.1\|WP_150154138.1\|2430752_2432135_-\|DUF21-domain-containing-protein	unknown	unknown	gnl\|CDD\|224173
NZ_CP043959.1\|WP_150154140.1\|2432795_2435363_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|223650
NZ_CP043959.1\|WP_150154145.1\|2440121_2441354_-\|biotin-synthase-BioB	unknown	unknown	gnl\|CDD\|235755
NZ_CP043959.1\|WP_145826061.1\|2442830_2443055_-\|DUF397-domain-containing-protein	unknown	unknown	gnl\|CDD\|377231
NZ_CP043959.1\|WP_150154134.1\|2426818_2427319_-\|G/U-mismatch-specific-DNA-glycosylase	unknown	unknown	gnl\|CDD\|381679
NZ_CP043959.1\|WP_150154135.1\|2427363_2428806_-\|adenylosuccinate-lyase	unknown	unknown	gnl\|CDD\|176471
NZ_CP043959.1\|WP_145826073.1\|2426323_2426758_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154139.1\|2432292_2432718_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|235142
NZ_CP043959.1\|WP_150154142.1\|2437351_2438062_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_CP043959.1\|WP_150154144.1\|2438848_2440129_-\|adenosylmethionine--8-amino-7-oxononanoate-transaminase	unknown	unknown	gnl\|CDD\|235656
NZ_CP043959.1\|WP_145826060.1\|2443064_2443925_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379262

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150154133.1\|2423771_2424533_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	4.27759e-35
NZ_CP043959.1\|WP_150154137.1\|2429742_2430756_-\|DUF21-domain-containing-protein	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	4.96557e-80
NZ_CP043959.1\|WP_150154147.1\|2444137_2444614_+\|ATP-binding-protein	gnl\|CDD\|340413	cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.	7.53431e-14
NZ_CP043959.1\|WP_024884885.1\|2424578_2425736_-\|ROK-family-transcriptional-regulator	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	1.67138e-47
NZ_CP043959.1\|WP_150154146.1\|2441500_2442628_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|235655	PRK05958, PRK05958, 8-amino-7-oxononanoate synthase; Reviewed.	1.62708e-164
NZ_CP043959.1\|WP_150154143.1\|2438130_2438847_-\|ATP-dependent-dethiobiotin-synthetase-BioD	gnl\|CDD\|234625	PRK00090, bioD, ATP-dependent dethiobiotin synthetase BioD.	5.59787e-65
NZ_CP043959.1\|WP_150154138.1\|2430752_2432135_-\|DUF21-domain-containing-protein	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	1.41811e-111
NZ_CP043959.1\|WP_150154140.1\|2432795_2435363_-\|FtsX-like-permease-family-protein	gnl\|CDD\|223650	COG0577, SalY, ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms].	6.43072e-27
NZ_CP043959.1\|WP_150154145.1\|2440121_2441354_-\|biotin-synthase-BioB	gnl\|CDD\|235755	PRK06256, PRK06256, biotin synthase; Validated.	0
NZ_CP043959.1\|WP_145826061.1\|2442830_2443055_-\|DUF397-domain-containing-protein	gnl\|CDD\|377231	pfam04149, DUF397, Domain of unknown function (DUF397). The function of this family is unknown.	1.22549e-17
NZ_CP043959.1\|WP_150154134.1\|2426818_2427319_-\|G/U-mismatch-specific-DNA-glycosylase	gnl\|CDD\|381679	cd10028, UDG-F2_TDG_MUG, Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins. Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..	2.8598e-80
NZ_CP043959.1\|WP_150154135.1\|2427363_2428806_-\|adenylosuccinate-lyase	gnl\|CDD\|176471	cd03302, Adenylsuccinate_lyase_2, Adenylsuccinate lyase (ASL)_subgroup 2. This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.	5.49069e-180
NZ_CP043959.1\|WP_150154136.1\|2428879_2429671_-\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238870	cd01832, SGNH_hydrolase_like_1, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.	2.59801e-63
NZ_CP043959.1\|WP_150154139.1\|2432292_2432718_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|235142	PRK03624, PRK03624, putative acetyltransferase; Provisional.	7.14018e-25
NZ_CP043959.1\|WP_150154142.1\|2437351_2438062_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	2.57018e-17
NZ_CP043959.1\|WP_150154144.1\|2438848_2440129_-\|adenosylmethionine--8-amino-7-oxononanoate-transaminase	gnl\|CDD\|235656	PRK05964, PRK05964, adenosylmethionine--8-amino-7-oxononanoate transaminase; Provisional.	0
NZ_CP043959.1\|WP_145826060.1\|2443064_2443925_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379262	pfam13560, HTH_31, Helix-turn-helix domain. This domain is a helix-turn-helix domain that probably binds to DNA.	8.33457e-13

>NZ_CP043959.1|WP_150154140.1|2432795_2435363_-|FtsX-like-permease-family-protein
MLKATLRSFLAHKGRLLLSALAVVLSVAFVAGSLIFSDTVTRTFDRLFASSSADVTVQPRDDLESAVPTGAVATVPAALARQLSGVEGVASAHPDVEVENVTVVDARNESVGPTTGAPTLAVDWHVTERSVVELTSGRTPRGDGEAVLDADTADAKGVEIGDTLTVQAQPGSFRVEIVGIATFTTTNPGAALVFLDPQVAAARLLGSADSATSVSVEAAPGVADADLKRRITAELGAGAYEVRTAGELAETASDELGAFLDVIKYAMLGFAGIAVLVGVFLIVNTFSMLIAQRTRELGLLRALGADRRQVRRSVLTEAVLLGLAGSTVGLAAGVGLAFGLIRLMGAFGMNLKTTEMVVGWATPVTAYVVGVGVTFVAAYLPARRAAAVSPMAALADAEVAGVGRPLRTRAVAGSVVGALGAAALLGCVLSGDTASASSLLGLGVLLTLVATVVAGPLLVRPVIRVLGAAFPAVFGAVGRMSQRNALRNPRRTGATAAALMVGLALVGGLSVASASMSRSFDDQIDKTLGADFIVQNGNFMPFPREITDRVRDTEGVGLVVRQRFAPVAVRLPDGERIETTASGYDDGVDDVARVTYAEGGTAAALAEGGLAMDAGFAAEHGVRRGDTVPVEFPGSRSAEFTVAALTDMAGGEGFGMSGGLFLGIAAVEEYVPGGQDSALYVNAAAGTSPDDLRDRLEAALEPFPQVQARDQADYKELVHDQIAVLLYLVYALLGLAIVIAVLGVVNTLALSVVERTREIGLLRAIGLGRRQLRRMIRLESVVIAVFGAVLGLGLGLVWGVCIQQVLALEGLTAFAVPWGTVVAVVVGSAVVGIAAALLPALRASRMNVLEAIAHE
>NZ_CP043959.1|WP_150154139.1|2432292_2432718_-|GNAT-family-N-acetyltransferase
MSELRTRAAGPEDLDDVLAFWKSAAEGTSISDDREGVERLVARDPEALILAERDGELVGTVIAGFDGWRCHLYRLAVRPDRRRQGIATALLTAAEDRFVRLGGRRADAMVLQRNATAHHAWDAAGYAPEERWRRWVKPLTG
>NZ_CP043959.1|WP_150154138.1|2430752_2432135_-|DUF21-domain-containing-protein
MTEVLLLLAAILLSLLCGAFVAAEFSLTTVERAELERAVERGERGAAGALQAVRSLTFQLSGAQLGITVTNLVVGMLSEPSIAALIRGPLRDIGASEPVARSLALVIGTGLSTVFLMVVGELVPKNWAISSPLAVAKRVGNAQRWFSAAFRPFITHLNNQANRMVRRIGLEPAEELESARGPQELAALARHSAKEGALEPDTAELFVRTLNLADLTAENVMTPRVQVIALEVRATCEDVANVTRATGLSRFPVYRETLDAVVGTAHVKDVLGVPAERRPEVPVSELMREPLLVPGSLTVDRLLDRLSGRRTMAVVIDEYGGTAGVATLEDIVEEVVGEVRDEHDPHETPDLARAGTDEEGRTLFSADGSARLDQLARVGLRAPEGPYETLAGLVAAQLGRIPEEGDVLEVAGWRLEVADASGRRAARVLLRAPRDDGQLTRHEAGASAAGDTEDDRGARR
>NZ_CP043959.1|WP_150154137.1|2429742_2430756_-|DUF21-domain-containing-protein
MTAVQLLIGLATLVANAFFVGAEFALISVRRSQVEPHADQGDRRAKSVLWGLEHVSVLLAAAQLGITLCTLILGIVAEPAIAHLLEPVFHAVGVPDGAGHAVSFVIALTLATYLHMLLGEMVPKNIALAEPVRSALMLGPPLVALSRALRPVIFTVNAFANTLLKLLRVETRDEVVASFSDAELAQIVKDSGQAGLIDDRALERLNDALELGRRPVRDVVMPLERVVYARVGVTPEGLERLSAESGFSRFPVVDEQRRIVGYLHIKDALDASPRDMPFRLRDMRSIARVRESTPLDDVLTAMRGSRTHLAAVSGTDGRLAGLVTMEDVLRELFGQRA
>NZ_CP043959.1|WP_150154136.1|2428879_2429671_-|SGNH/GDSL-hydrolase-family-protein
MQTNPASSSPAHTSLVALGDSFTEGMSDLLPDGTYRGWADLLAARMAAVAPGFRYANLAVRGKLIQQIVDEQVETAAAMGADVITLVGGLNDTLRPKCDMVRVQDLLTEAVERLAPRCERLVLMHSPGRRGPVLERFRPRMEALFACIDELAAKHDALVVDLYGAPALGDPRLWDVDRLHLTGEGHRRVAEAVWQALGHPAEDPEWHLPPEATLPPHWVARRVEDARFARRHLLPWIGRRLTGRSSGDGLPPKRPELLPYETA
>NZ_CP043959.1|WP_150154135.1|2427363_2428806_-|adenylosuccinate-lyase
MTAAPAKPRIPNVLAGRYASAELATLWSPEQKVRLERQLWLAVLRAQKDLGIEVPDAAIADYERVLDTVDLASIAEREKVTRHDVKARIEEFNDLAGHEHVHKGMTSRDLTENVEQLQVRLSLELMRDRTVAVLARLGKLAGEYGELVMAGRSHNVAAQATTLGKRFATAADELLVAYGRLEELLGRYPLRGIKGPVGTAQDMLDLLGGDAAKLADLERRIAGHLGFSQAFTSVGQVYPRSLDYEVVTALVQLAAAPSSLARTIRLMAGHELVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAGDQWNEGDVSCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGREVAHEAIKENAVATALAMREQGAERNDLLDKLAADERLPLGRAELEALMADKLSFTGAASDQVATVTGRIDEIVKQHPEAAGYTPGAIL
>NZ_CP043959.1|WP_150154134.1|2426818_2427319_-|G/U-mismatch-specific-DNA-glycosylase
MPDVVADGLRVLFCGINPGLMTAATGHHFARPGNRFWPALHRSGFTPRQLAPSEQHELLSYGLGITNVVARATARADELSAEEYRQGGRELAVKVGRLRPRLLAVLGVTAYRAAFDDRTAKVGPQVRTIGESRVWVLPNPSGLNAHWTPTTLAEEFARLREAAEQD
>NZ_CP043959.1|WP_145826073.1|2426323_2426758_+|hypothetical-protein
MNLARHIALIDELCFRPFPAEHGPSDVGFSGPGHHVAVLESGGPDLDPAHWAATVDQFEKQRDAVYELLASRWGDVDPWNLQTVLLRTEREDVPQPWAWLSHEAGVAWLWEVQGTGRWAAVALADRDAGGAVQLLAVVTETAPP
>NZ_CP043959.1|WP_024884885.1|2424578_2425736_-|ROK-family-transcriptional-regulator
MGRLTGGDPSLLRRINSAVVLHALRATDCATLTEVTRVTGLSRPTVEGVVEGLIEAGLVVEAAADEGTARRQGRPARRFRFRAEAGHLLGLEIGVHRVAALLADLDGRVIGAQVRDVDETVDADERLDRLRAAVAELLRRAGVPRGSLRAVGVGTPGIVDADGTVRLGTALPGWTGLGLGERLSRSFKCPVLVENDANAAVVAEHWKGSAKETDDVVFVLAGLSPGAGSLIGGRLHRGYGGAAGEIGALHLLGREATPETLLSTTDEPLHPLDEQAVAAVFAQAREGDQRALAAMDRFIQRLVHDVAALVLALDPELVVIGGWAAGLDGVLEPLRRELSRYCLRPPEVTLSLLGEAAVATGAVRLALDHVEEQLFAVEGTVTARR
>NZ_CP043959.1|WP_150154133.1|2423771_2424533_+|GntR-family-transcriptional-regulator
MGTTQLESVPEPKYWHLKTVLSEALDSEFSVGEILPNERDLAARFGVARATLRQALEQLELEGRLQRRRGVGTTVAPPRMGVSVGSEQHAWPGGPHDAWHSVDCRLDVPSAALAEVLVTGSDEPVHIVRRSRVSRGQPVASELLYIPAASVPDLSGIDAPSGAARARAVLRELQRLELERQENAVELGSAGADEAKELDRLPGAPVLVVTTRYIARGRTAALSVATYRADTCRLTFGDSGGVEIHHGPERQAS
>NZ_CP043959.1|WP_024884898.1|2436733_2436973_+|toxin-antitoxin-system-antitoxin-component
MAKTQLNVRVDEGTARAARERALARGISVNRYIEELVRQDTGESGRAFVEAAADFMKQYESVFAEEFGRDREGAREGHR
>NZ_CP043959.1|WP_150154141.1|2436976_2437351_+|fic-family-toxin-antitoxin-system,-toxin-component
MDHVRIDLAWLLMLAEQQTPGDPQVTDWGALVAAVARHDAGIFDVPVYDTPHSRAAALLQLLIHVPALERSNALFASAVAYAYLVASGLKVVTSPEQVRDLAHLVKRDGADVDTIAAELRRWCA
>NZ_CP043959.1|WP_150154142.1|2437351_2438062_-|methyltransferase-domain-containing-protein
MQLRSPRSAQAARDPVHHPVFARWYARCSVAAESRAGMADVRRRLLGGLSGRVIEIGAGNGLNFAHYPRTVAEVVAMEPERALRTLAVEAALRAEMPVDVAPGVAEALPVKSEAFDAAVLSLVLCSVRDVERALAEVRRVLRPGGEVRFFEHGAGGGRVMHLTQRALDRTVWPPLAGGCHLARNPVGALRAAGFELGPYRRMTVPENGPALPQSFCVIGTAWRPVGDAESTEAAGR
>NZ_CP043959.1|WP_150154143.1|2438130_2438847_-|ATP-dependent-dethiobiotin-synthetase-BioD
MPVLVVTGTNTEVGKTVVTAAVAATASAGGRSVAVLKAAQTGVGPGEPGDAAEVERLAGPVTSAELARYPEPLAPATAARRAGRAPVHPHEIAERAAKLATEHDLVLVEGAGGLLVRFDAAGGTLADAAALLRAPVLVVASAGLGTLNATELTVRELRGRGLDPVGVVIGSWPADPGLAERCNLLDLPDVTGVPLLGAVPEGAGRLGPDRFRTAAPDWLAPRLEGTWDADVFRAREAA
>NZ_CP043959.1|WP_150154144.1|2438848_2440129_-|adenosylmethionine--8-amino-7-oxononanoate-transaminase
MPEQSVAALLELDRRHVWHPYGPMPGRQEPLVVASASGVRLTLADGSGELVDGMSSWWSAIHGYNHPVLNEAAHDQLGRMSHVMFGGLTHEPAVRLAKLLVDMSPDGLEHVFLADSGSVSVEVAVKMCLQYWRSLGRPEKSRLLTWRGGYHGDTWHPMSVCDPEGGMHELWSGVLPRQVFADAPPGPYEEAYADHLREMIERHAGELAAVIVEPVVQGAGGMRFHSPAYLRVLREACDAHDVLLVLDEIATGFGRTGALFAAEHAAVSPDVMCVGKALTGGYLTMAATLCTARVAEGISRGEVPVLAHGPTFMGNPLATAVACASVELLLGQDWRAEVKRIESGLREGLAPAARLPGVRDVRVLGAIGVVQLDHDVDMTAATRAAVREGVWLRPFRDLVYTMPPYVTGDEDVARIARAVCAAAKEG
>NZ_CP043959.1|WP_150154145.1|2440121_2441354_-|biotin-synthase-BioB
MDLLNTLVDKGLRRETPTRAEALAVLATSDEELLDVVAAAGKVRRHWFGRRVKLNYLVNLKSGLCPEDCSYCSQRLGSKADILKYTWLKPDEASRAAAAGLAGGAKRVCLVASGRGPTDRDVDRVSDTIRTIKEQNEDVEVCACLGLLSDGQAERLREAGADAYNHNLNTSESTYGEITTTHTYADRVDTVRKAHAAGLSACSGLIAGMGETDEDLVDVVFSLRELDPDSVPVNFLIPFEGTPLAKEWNLTPQRCLRILAMVRFVCPDAEVRIAGGREVHLRTMQPLALHLANSIFLGDYLTSEGQAGKADLEMIADAGFEVEGAGEVTLPEHRAGGGCGSHASGGACGSQGDPGCGSHDGAEGGCGSHEGGGVCGTAPAAAPAASADEPRPDLVAVRRRGAGTDLAPNA
>NZ_CP043959.1|WP_150154146.1|2441500_2442628_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MAFGWIDEQAEQRRSAGLVRTLRPRPADTPLLDLASNDYLGLARHPEVTEGAARAARTWGGGATGSRLVTGTTELHAELEHELADFCGFEAALVFSSGYAANLAAVTALAPHGSLVVSDAGNHASLIDGCRLARGVTQVVAHRDPDSVRKALDGHEGPAVAVSDTVFSVDGDAAPLVALAEACREHGAGLVLDDAHGLGVLGDGGRGAPHAAGVAGADDVVVTVTLSKSLGSQGGAVLGPARVIGHLVNAARTFIFDTGLAPAAAGAALAALRLLRREPGRAARAGAVARELHTRLTAAGLEAVRPDAAVVSVRAPSPEQAVRWAADCRAAGLSVGCFRPPSVPDGISRLRLTARADLSGAEIERAVRVIGDTRP
>NZ_CP043959.1|WP_145826061.1|2442830_2443055_-|DUF397-domain-containing-protein
MPAPPRTIPSSLALRDVRWLRSSYSTGANNCVETARPATGPLAGLLAVRDSKAPDGPALLFSPDSWAEFVTAVR
>NZ_CP043959.1|WP_145826060.1|2443064_2443925_-|helix-turn-helix-domain-containing-protein
MQHGPAVRRRKLGAELRALRTAAGLTSGDAARLAGWHQSKVSRIETGTSGVKPADVRLLLDVYGVDEPQLRELLLVLSGSGKGDGRDHWWHAYRGVLPPTYRDFISLESQASAMRTLETTVIPGLLQTPEYARAVTEAALEGASEERLDALVEVRLARQDVLRADPPLELNAVLDEAVLRREVGGPEVMSRQLDRLIEAARLPQVRLQVLPFSAGAHIGVTGPFVIFSFSRTSDLDVVVLDHLTSSHYLERKEDLRAYSEAFDALSTHALSPEESLDFIAGAAAGA
>NZ_CP043959.1|WP_150154147.1|2444137_2444614_+|ATP-binding-protein
MADHLEASVTLPSDPASVAAARAHVAGALAEWGLPPDAELYDTVRLIVSELATNAVQHTFGQSPTFTVDVVLVREERVHIGVTDSHPRLPKRLPAAVQQDNGRGLVIIRWLTVEYGGRLRVRPTRQGGKTVAVELPWPGTTVTAQPTEAVTAAVQPEL

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Crispr_ID: NZ_CP043959_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_7

2698239-2698337

Orphan

Consensus_repeat	Method
GGTGCGCAGTTCCCCGCGCCCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_7

>merge|NZ_CP043959|7|2698239-2698337|CRISPRCasFinder
GGTGCGCAGTTCCCCGCGCCCCTGGAGGGCGTGTGCCCGTTGGGCTTGTTCGCCCGCGAGCGGGTGGGGCTGGCTTGGCGCGCAGTTCCCCGCGCCCCT

>NZ_CP043959|7|7|2698239-2698337|CRISPRCasFinder
GGTGCGCAGTTCCCCGCGCCCCT	GGAGGGCGTGTGCCCGTTGGGCTTGTTCGCCCGCGAGCGGGTGGGGCTGGCTT
GGCGCGCAGTTCCCCGCGCCCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150154404.1\|2696399_2697119_+\|response-regulator	unknown	unknown	gnl\|CDD\|223816
NZ_CP043959.1\|WP_150154396.1\|2692442_2692910_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154423.1\|2706435_2706867_-\|roadblock/LC7-domain-containing-protein	unknown	unknown	gnl\|CDD\|367422
NZ_CP043959.1\|WP_145828753.1\|2700904_2701594_-\|response-regulator	unknown	unknown	gnl\|CDD\|223816
NZ_CP043959.1\|WP_150154410.1\|2701884_2703042_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224050
NZ_CP043959.1\|WP_150154402.1\|2695569_2696295_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133022
NZ_CP043959.1\|WP_150154391.1\|2689650_2691027_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_167534685.1\|2694194_2695211_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_CP043959.1\|WP_150157311.1\|2693118_2694198_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154412.1\|2703038_2703731_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224095
NZ_CP043959.1\|WP_150157312.1\|2699459_2700866_-\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|223715
NZ_CP043959.1\|WP_145828742.1\|2689227_2689635_+\|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl\|CDD\|376583
NZ_CP043959.1\|WP_150154421.1\|2706080_2706434_-\|DUF742-domain-containing-protein	unknown	unknown	gnl\|CDD\|283084
NZ_CP043959.1\|WP_150154408.1\|2698354_2699356_-\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187566
NZ_CP043959.1\|WP_150154394.1\|2691142_2692429_+\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|238198
NZ_CP043959.1\|WP_150154414.1\|2703727_2704393_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224095
NZ_CP043959.1\|WP_150154419.1\|2705497_2706094_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|225138
NZ_CP043959.1\|WP_150154389.1\|2687824_2689213_+\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_CP043959.1\|WP_150154406.1\|2697121_2698234_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP043959.1\|WP_150154417.1\|2704468_2705425_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270324

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150154404.1\|2696399_2697119_+\|response-regulator	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].	2.22395e-91
NZ_CP043959.1\|WP_150157312.1\|2699459_2700866_-\|HAMP-domain-containing-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	7.51217e-59
NZ_CP043959.1\|WP_150154402.1\|2695569_2696295_-\|glycosyltransferase	gnl\|CDD\|133022	cd04179, DPM_DPG-synthase_like, DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.	1.00227e-40
NZ_CP043959.1\|WP_150154408.1\|2698354_2699356_-\|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.	4.87031e-67
NZ_CP043959.1\|WP_145828753.1\|2700904_2701594_-\|response-regulator	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].	1.19011e-74
NZ_CP043959.1\|WP_150154423.1\|2706435_2706867_-\|roadblock/LC7-domain-containing-protein	gnl\|CDD\|367422	pfam03259, Robl_LC7, Roadblock/LC7 domain. This family includes proteins that are about 100 amino acids long and have been shown to be related. Members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. It is proposed that roadblock/LC7 family members may modulate specific dynein functions. This family also includes Golgi-associated MP1 adapter protein and MglB from Myxococcus xanthus, a protein involved in gliding motility. However the family also includes members from non-motile bacteria such as Streptomyces coelicolor, suggesting that the protein may play a structural or regulatory role.	2.82766e-24
NZ_CP043959.1\|WP_167534685.1\|2694194_2695211_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	4.77648e-08
NZ_CP043959.1\|WP_150154419.1\|2705497_2706094_-\|ATP-binding-protein	gnl\|CDD\|225138	COG2229, COG2229, Predicted GTPase [General function prediction only].	8.32853e-45
NZ_CP043959.1\|WP_150154412.1\|2703038_2703731_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	5.23163e-36
NZ_CP043959.1\|WP_150154414.1\|2703727_2704393_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	1.10644e-48
NZ_CP043959.1\|WP_145828742.1\|2689227_2689635_+\|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl\|CDD\|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	9.38688e-78
NZ_CP043959.1\|WP_150154410.1\|2701884_2703042_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224050	COG1125, OpuBA, ABC-type proline/glycine betaine transport systems, ATPase components [Amino acid transport and metabolism].	2.05574e-142
NZ_CP043959.1\|WP_150154394.1\|2691142_2692429_+\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|238198	cd00321, SO_family_Moco, Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.	8.23935e-32
NZ_CP043959.1\|WP_150154421.1\|2706080_2706434_-\|DUF742-domain-containing-protein	gnl\|CDD\|283084	pfam05331, DUF742, Protein of unknown function (DUF742). This family consists of several uncharacterized Streptomyces proteins as well as one from Mycobacterium tuberculosis. The function of these proteins is unknown.	2.90506e-36
NZ_CP043959.1\|WP_150154389.1\|2687824_2689213_+\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	0
NZ_CP043959.1\|WP_150154406.1\|2697121_2698234_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.19606e-49
NZ_CP043959.1\|WP_150154417.1\|2704468_2705425_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270324	cd13606, PBP2_ProX_like, Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold. This group includes periplasmic substrate-binding component of ABC transport systems from gram-negative and -positive bacteria that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.	1.70232e-112

>NZ_CP043959.1|WP_150154406.1|2697121_2698234_+|HAMP-domain-containing-histidine-kinase
MRDTLLIALFAFLGATSAGVLGAGVLLLIRRRSLTAHLAVVAAVAVAAMLAGTLAVARAMFLSSHDLSVVTTVVAMAAVVSLVTALLLGRWVVARSRELALAARSFGDGGEFAAPDGPATAELAALSRELEATSVRLAQSRDRERALESSRRELVAWISHDLRTPLAGLRAMAEALEDGVAAEPDRYLRQIRTEVERLNDMVGDLFELSRIHAGTLKLSPARISLYDLVGDALAGADPLAREHGVRLVGHGVEPVPVEVDGREMSRVLGNLLVNAIRRTPADGTVAVAARRSSEGAVVVSVTDGCGGIPEEDLPRVFDTGWRGTHARTPPAGAGLGLAIVRGIVEAHRGTASVRNVRGGCRFEVTLPAEV
>NZ_CP043959.1|WP_150154404.1|2696399_2697119_+|response-regulator
MDQPPPSGEAGARVLVVDDDPTVAEIVTGYLDRAGYVVDRAGDGPDALARAAAHWPDLVVLDLMLPGMDGLEVCRRMRGQGPVPVIMLTARGDEDDRILGLEVGADDYVTKPFSPRELVLRVESVLRRTRPGPAAAGLLGAVGLTVDPAARRATKRGAELALTIREFDLLAFLLAHPGRAFAREELMREVWGWDFGDLSTVTVHVRRLRGKVEDDPARPRLIQTVWGVGYRFDPATGEA
>NZ_CP043959.1|WP_150154402.1|2695569_2696295_-|glycosyltransferase
MRAVTSSPSSPEPPGPASVDVVLPCLDEAAALPWVLRRIPPGWRALVVDNGSTDGSDRVARELGATVVHEARRGFGAACHTGLSAATADIVCFCDCDASLDPADLVPFVHEVASGTADLVLGRRRPRGRGAWPLHARAGNVALARLLRRRTGLRLRDLGPLRAARREELLALDLTDRRSGYPLQMVVRAADAGWRVIEHDVPYTPRTGASKVTGTWRGTFQAVRDMSRVLQEPAAREGVAS
>NZ_CP043959.1|WP_167534685.1|2694194_2695211_-|methyltransferase-domain-containing-protein
MVRPGRGRRLLGAGPGRTRPRAAARGAHVTAGHRGRAAAAAGRPTGTGPAVAAGRRHGPGRGGRRRCGAGRPVRHGAGRADGGPPVSGARVATTPRLGPRRTTGRAVPAADRAWSADPYADALRAGRGPLFLRRSDGRLLPLDVERWCAEPDAADLEVLERCEGAVLDVGCGPGRLVAALGARGRRVLGIDVSEAAVAHTVRRGGQAVPASVFGPLPGTGCWDTALLMDGNIGIGGDPAALLDRLARVLTAGGLLIAETVPDPEVDERILVQVTDAHGSPGELFPWARLGTPALLRHARARGWHPEDQWSTPTRTFAALRPPAPAPADTTRGGPRRTA
>NZ_CP043959.1|WP_150157311.1|2693118_2694198_+|hypothetical-protein
MPDEEWERFLRESVDGAGDAPVEPSARAREVQARLRKGGGRPEGWRTYTPATRGRRTGWYVTGLVAAVALVLVALFPQQIVGWFGGDGGDPAGAPVAAESERPTAAPGPERALRPTPDEPFRGSPAARWADGADGITVPAARATGWMDAAQVERALRRSKEFMVAAGLDSGVLRGKRPERATALLNPHQRDVREYLRAALSSATPTEETDPLLLFSRFRPDQAELVGDVVKTRGRLTYREGERGAVEVTADVTFVYPVTPAAGDGGADAEVVRTIVRREVVMSWDDPSKVITEPDTMSLVSYSLDLTNGGCSGPTGYFDPPFGRADEQPADEALLDPYDRSEPVGTATGADGCVTATRS
>NZ_CP043959.1|WP_150154396.1|2692442_2692910_+|hypothetical-protein
MRRSPLNRVPRPVLGSPFHLLVLLCSFALCAYAGVRLLDGDWLMITVWFVGAALIHDLVLLPLYAAADRALITATGRRAAWVNHVRVPAALSGLLLLVWFPLITGRVSERYAAVTALSADGFAARWLLVTAALFGGSAVLFAVRTGRRRPATEDQ
>NZ_CP043959.1|WP_150154394.1|2691142_2692429_+|molybdopterin-dependent-oxidoreductase
MARSSLLGRLPRGPFAPDFWRSPLRGPRFTSVLGVVLLAGITVMFVTGLVSYAAYNPDLSPVNDRTPGKGILGFYLFSWPTDPPWLYRLTQGVHVTLGLALVPVLLAKLWSVVPRLFTLPPARSVTHALERISLLLLVGGALFEFTTGILNVQLDYIFPGSFYPLHFYGAWVFFGAFLAHTVLKAPAAFRNLRRMRQGAGEAGDEDPVEAPVEDLAAPRPDPPTVSRRGALGLVGGGSLLLVATSAGRSFDGPLRETAVLAPHGGPEPGSGPGAFQVNKTAEYAGIRPDDTTEEAWRLTVTGRTGTVRLSRAELLTLPQHDVALPIACVEGWSTSDQDWRGVRLRDLAALAGHDDPVDVFVESLQLRGTWRHAALSADQVADGRSLLALFVNGAELTPDHGHPARVIVPAAPGVLNTKWVDRLTFGEL
>NZ_CP043959.1|WP_150154391.1|2689650_2691027_-|hypothetical-protein
MKRTSPRTDPRDPVRGSRGTLLDGYAVAAAAALVLAAALVGTRIQDRYGTLRVGWPPLVGNWMPHVGPGTPAAIAVAVAVVAYGPALAARLPWRRLLLTVWGGALAWTWSLALADGWSRGVAGRLTTRHEYLQVVDRWQDIPATLRDFHAHILIGTPDNWPAHVAGHPPGATLTFVLLDRIGLSGGGWAGAFVITAGTTAAVAVLVTVRRLADEGLARRAAPFLVLAPAAVWVGTSADGWFAAVAAWALALLALAVTGCRPAWTGLGSGLLFGLTLYLSYGLTLVAVIAAAVLLLGTRRLRPLPYVAAGFLVVPAVFTALGFDWWEAYRLLVTRYYQGAGGVRPYGYWIWANLACAVLVVGPATVAGLRRGGGVLLGTARAALLRGPAPRLALLVGSALLALLIADLSGMSKAETERIWLPFTLWLLPAGSFLPGPRGWLAGQAASALLLNHLVLTGW
>NZ_CP043959.1|WP_145828742.1|2689227_2689635_+|peptide-methionine-(R)-S-oxide-reductase-MsrB
MPYDVEKPDEQWRAELSPSEYAVLRQAATEPAFTGEYTDTKTEGVYSCRACGAELFTSDTKFESHCGWPSFFDPKDTDAVELVQDRSHGMVRTEVRCARCGSHLGHVFEGEGYPTPTDQRYCINSISLSLQPADS
>NZ_CP043959.1|WP_150154389.1|2687824_2689213_+|UDP-N-acetylmuramate--L-alanine-ligase
MAPGLPTAMDRPHFIGIGGAGMSGIAKILAQRGAAVAGSDAKDSATAEALRGLGATVHIGHAAGHLADDASCVVVSSAIREDNPELLRAAELGIPVVHRSDALAALMDGLRPIAVAGTHGKTTTTSMLAVSLTELGREPSYAIGGDLDAPGSNALHGAGDIFVAEADESDRSFHKYAPEVAIILNVELDHHANYASMEEIHESFETFVGRIVPGGTLVISADHEGARELTRRLDGSVRTVTYGESADADVKVLSVVPQGLKSEVTVELDGAPLTFTVSVPGRHYAHNAVAALAAGVALGIPAAELAPALAAYTGVKRRLQLKGEAAGVQVIDSYAHHPTEMTADLEAMRAAAGDARILVVFQPHLFSRTRELGKEMGIALALADASLVLDVYPAREDPIPGVTSELIIEAARAAGADVTAVHDAAEIPGAVAGMAKPGDLVLTMGAGDVTDLGPRILDRLSN
>NZ_CP043959.1|WP_150154408.1|2698354_2699356_-|NAD-dependent-epimerase/dehydratase-family-protein
MRVLVTGGAGFIGSTVVTALRERGHEPVVFDVRTDPGADVRSPGAVRAALDGVDAVCHQAAMVGLGTGFGDAPEYVSRNDLGTAVLLAATADAGVRRLVLAGSMVVYGEGRYVCAGHGVVRPGPRAEEDLAAGRFEPRCPVCGAALEPGLVGEDAPVDPRNVYATTKLAQEHLAAAWARATGGSAVSLRYHNVYGPGMPRDTPYAGVASFFRSALARGEAPRVFEDGGQRRDFVHVRDVASANVTALEADAAAGALTAYNTGSGTPHTVGEMARALADACGGPEPVVTGEYRLGDVRHITADSTRLRTDLGWTPHITFEHGMREFAQAPLQET
>NZ_CP043959.1|WP_150157312.1|2699459_2700866_-|HAMP-domain-containing-protein
MRLGTRLALGLGVLSLAVFAVVGTALTAYMRDYLERQLGDQLKLIQTVQAKDAAAHGTVRRKPYYGWYTAVYDVTGDAVRLRRPADVPADTGPLADLARAMAHSDTELMRTARIDGEGTYRLRGCEVEPGVVLVSAAPVEDVEKTVERLVTVQVVVFALALAALVVFGRRMLRRGLKPLSDMAHTAHGIASHDLTESAARLPLRADGRDGGREVAELRTAFNTMLEHIDDSLAVRAEAEQRLRRFVADASHELRTPLMSVRGYADLFQYAAANEPAERERHLARLRAEAARMGVLLDDLLLLARLDAAEAEAPLRTADTDLTELVQQAADAFRAARPTHPLTVTARAPGPPVLRLDPQRVRQVLDNLLANAAVHTPAGTPVSVEVSVSGDTALVRVTDAGPGIPAEDRERVFDRFHRVDKARSRDRGGSGLGLSVARSLVRAHGGDITLTAGPGATVFTVRLPLRGVC
>NZ_CP043959.1|WP_145828753.1|2700904_2701594_-|response-regulator
MDRVRVLVVDDDPPIADLVATVARYEGWEAVTAHSGEEALRRAAAFRPDIVVLDLMLPDVDGFGVLDGLRSSGRMVPVVFLTARDGVADRVAGLTRGGDDYLVKPFAVEELMARLRTVLRRSAGPDFRRSVLRVGDLSLDEDTREVRRGEHLLALTPTEYEVLRYLMRRSPTVLTKAQILDHVWEYGFGGRANVVELVVSRLRRKLDATGAPLIRTVRGFGYVIRQAAE
>NZ_CP043959.1|WP_150154410.1|2701884_2703042_+|ATP-binding-cassette-domain-containing-protein
MIRIDSVTKRYPDGTVAVDRLSLEIPDRSITVLVGPSGCGKTTTLRMINRMVEPTEGTILLDGEDVQRQPVTTLRRSMGYVIQNAGLFQHRTIVDNIATVPRMLGWGKQRARERAAELMERVGLDTSLAKRYPYQLSGGQQQRVGVARALAADPPVLLMDEPFSAVDPVVRKGLQDELLRIQDELGKTIVFVTHDIDEAIKLGTMVAVLREGGRLAQYAPPAELLSNPADGFVEDFLGADRGIRRLSFFTSEALELTTDAVVPADAPAARLTAARTPYVLVTDADGRPLGWRERGSTGDSGQLLPYGRPFRPGTDSLRVALDCAVLSPTGWAVAVDGDGRATGVVSQQTIGEAIRAAHTAAGTAPAGASADAPASARGEDEKVAG
>NZ_CP043959.1|WP_150154412.1|2703038_2703731_+|ABC-transporter-permease-subunit
MSGFFDIPSDLQHSWAGLVGLHLREALLPVAAGLLLALPLALLCGRFRWLYPPVLGVTTVLYAVPSLAFFVVLIDYTGQTELTVMIPLALYSLVVLVPAIVDGVRSVPDETLAAATAMGFGPVRRYAQVQLPIAAPAIIAGLRVATASSISLVSVGALIGNQGALGNLLAAAQKYDRPELAMNAVLTTAALAILCDVALVALRRVLTPWMPGRKQAASPREELLAKGAAR
>NZ_CP043959.1|WP_150154414.1|2703727_2704393_+|ABC-transporter-permease-subunit
MNVLNFVQAFFSDNAHWHGYDGIPTRFVEHVQYSLLALAIAAAIGLPVGLLTGHTGRGGNVIAFVANAARALPSFGLLVLAVLLIGFGLLPVMIPLVVLAVPPILVTTYEAVRTVDPAPVDAARGMGMHESRILFRVEVPVALPLILGGLRSAAIQIVSTATIAAYVSLGGLGRYIIDGLYQRDYEKVVGGATLVAVLALVTLALFWAAGRLAVSPGVRRR
>NZ_CP043959.1|WP_150154417.1|2704468_2705425_+|ABC-transporter-substrate-binding-protein
MISTAKSCRPTKRHTGAAAVALAAAAALLAGCSSGDTSENPLDGEKADAGTVVVGSNNFAESTLLADIYGEALRAKGLKVTYKHNIGSRETTYGLMRNGSVTVLPEYNGSLLAYLDADAEQTSADAVNEAAKAKLDKQLTLLESSPAEDKDSVSVNAATAKKYGLTAESTLADLKDIAPELAIGGSPEFQTRQQGLKGLEAVYGLKFKTFKALDAGGPLTQAALAQNEVQAADVFTTDPTIVKEKFVVLKDPENLFGFANVTPLVRKDGLSKEGVEALNAVSAKLDTKTLLDLDAQVQLEKKDPLDVAKAWLKSAGLA
>NZ_CP043959.1|WP_150154419.1|2705497_2706094_-|ATP-binding-protein
MAGSDTTARASADRGAPDTVKILIAGGFGVGKTTMVGSVSEIRPLRTEESLTMAGLDVDDLDGVEEKRVTTVAMDFGRITVSDDLVLYLFGTPGQQRFWFMWNDLALGALGAVVLVDVRRPKSSFAAIDFFERRGIPFVVAVNGFHGEHPYPVEDIREALTLPAAVPVLLCDARERESSRDVLIALIDLLIAQAAAVG
>NZ_CP043959.1|WP_150154421.1|2706080_2706434_-|DUF742-domain-containing-protein
MGGSDSAGRLVRPFTLTGGRTRPSRADFTLITTVTAADPQPETAARPQPEHTRILRLCAEPVAVAELAARLDLPVSVVVIMLSDLLEAGRITVRAPRSVTTPDPDLLQKVREGLGRL
>NZ_CP043959.1|WP_150154423.1|2706435_2706867_-|roadblock/LC7-domain-containing-protein
MTRPLPATHTQLDQLLTGLVERVADVNQAVVLSEDGLVVSKSTGFLRDDAERLAATASGLMSLSKGVSMDFRGGPVRQALIEMAQSYLILTSAGPGAHLVVLTGPKADVGVVAYQMNMLVKKIGEHLSAAPRDAGGPAVDPGV

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Crispr_ID: NZ_CP043959_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_8

2761706-2761817

Orphan

Consensus_repeat	Method
GCCGCCCCCGTGACGGCGCCCGCCGCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_8

>merge|NZ_CP043959|8|2761706-2761817|CRISPRCasFinder
GCCGCCCGTGTAACGGCACCAGGCGCAGCCGCCCCCGTGACGGCGCCCGCCGCAGCCGCCCCCCGTCACGGGGGCGTCCGCCTCGGCCGCCCCCGTGACGGCGCCCGGCGCA

>NZ_CP043959|8|8|2761706-2761817|CRISPRCasFinder
GCCGCCCGTGTAACGGCACCAGGCGCA	GCCGCCCCCGTGACGGCGCCCGCCGCAGCCGCCCCCCGTCACGGGGGCGTCCGCCTCG
GCCGCCCCCGTGACGGCGCCCGGCGCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150154486.1\|2759862_2760630_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|180604
NZ_CP043959.1\|WP_150154479.1\|2752531_2754166_-\|DNA-alkylation-response-protein	unknown	unknown	gnl\|CDD\|183199
NZ_CP043959.1\|WP_150154489.1\|2762859_2764410_+\|carboxylesterase-family-protein	unknown	unknown	gnl\|CDD\|365897
NZ_CP043959.1\|WP_150154480.1\|2754277_2755426_+\|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl\|CDD\|377085
NZ_CP043959.1\|WP_150154481.1\|2755486_2756326_-\|NAD(P)H-binding-protein	unknown	unknown	gnl\|CDD\|187578
NZ_CP043959.1\|WP_150157315.1\|2773822_2774299_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154484.1\|2758578_2759082_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154488.1\|2761838_2762486_+\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643
NZ_CP043959.1\|WP_150154482.1\|2756407_2757346_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378976
NZ_CP043959.1\|WP_150154494.1\|2769951_2770866_-\|homocysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|181899
NZ_CP043959.1\|WP_150157313.1\|2758237_2758516_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154493.1\|2768435_2769590_-\|transcription-termination-factor-Rho	unknown	unknown	gnl\|CDD\|237150
NZ_CP043959.1\|WP_150154483.1\|2757356_2758052_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|197666
NZ_CP043959.1\|WP_150154492.1\|2767351_2767762_+\|NAD(+)--rifampin-ADP-ribosyltransferase	unknown	unknown	gnl\|CDD\|378815
NZ_CP043959.1\|WP_167534518.1\|2759259_2759730_-\|glyoxalase	unknown	unknown	gnl\|CDD\|319901
NZ_CP043959.1\|WP_150154495.1\|2770962_2773677_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225461
NZ_CP043959.1\|WP_150154491.1\|2766536_2767070_+\|2'-5'-RNA-ligase-family-protein	unknown	unknown	gnl\|CDD\|379265
NZ_CP043959.1\|WP_150157314.1\|2767912_2768395_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150154490.1\|2764426_2765887_-\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP043959.1\|WP_150154487.1\|2760692_2761601_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150154486.1\|2759862_2760630_+\|SDR-family-oxidoreductase	gnl\|CDD\|180604	PRK06523, PRK06523, short chain dehydrogenase; Provisional.	4.05636e-101
NZ_CP043959.1\|WP_150154479.1\|2752531_2754166_-\|DNA-alkylation-response-protein	gnl\|CDD\|183199	PRK11561, PRK11561, isovaleryl CoA dehydrogenase; Provisional.	3.13905e-172
NZ_CP043959.1\|WP_150154489.1\|2762859_2764410_+\|carboxylesterase-family-protein	gnl\|CDD\|365897	pfam00135, COesterase, Carboxylesterase family.	5.58678e-107
NZ_CP043959.1\|WP_150154480.1\|2754277_2755426_+\|YihY/virulence-factor-BrkB-family-protein	gnl\|CDD\|377085	pfam03631, Virul_fac_BrkB, Virulence factor BrkB. This family acts as a virulence factor. In Bordetella pertussis, BrkB is essential for resistance to complement-dependent killing by serum. This family was originally predicted to be ribonuclease BN, but this prediction has since been shown to be incorrect.	9.43873e-46
NZ_CP043959.1\|WP_150154481.1\|2755486_2756326_-\|NAD(P)H-binding-protein	gnl\|CDD\|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. 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.	2.76763e-47
NZ_CP043959.1\|WP_150154494.1\|2769951_2770866_-\|homocysteine-S-methyltransferase	gnl\|CDD\|181899	PRK09485, mmuM, homocysteine methyltransferase; Provisional.	4.61679e-143
NZ_CP043959.1\|WP_150154488.1\|2761838_2762486_+\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	8.07613e-103
NZ_CP043959.1\|WP_150154482.1\|2756407_2757346_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378976	pfam12852, Cupin_6, Cupin. This is a family of bacterial and eukaryotic proteins that belong to the Cupin superfamily. Some of the proteins in this family are annotated as being members of the AraC family of transcription factors, in which case this domain corresponds to the ligand binding domain.	3.04086e-44
NZ_CP043959.1\|WP_150154495.1\|2770962_2773677_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225461	COG2909, MalT, ATP-dependent transcriptional regulator [Transcription].	3.10517e-73
NZ_CP043959.1\|WP_150154493.1\|2768435_2769590_-\|transcription-termination-factor-Rho	gnl\|CDD\|237150	PRK12608, PRK12608, transcription termination factor Rho; Provisional.	0
NZ_CP043959.1\|WP_150154483.1\|2757356_2758052_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	9.32012e-13
NZ_CP043959.1\|WP_150154492.1\|2767351_2767762_+\|NAD(+)--rifampin-ADP-ribosyltransferase	gnl\|CDD\|378815	pfam12120, Arr-ms, Rifampin ADP-ribosyl transferase. This protein is found in bacteria. Proteins in this family are typically between 136 to 150 amino acids in length. The opportunistic pathogen Mycobacterium smegmatis is resistant to rifampin because of the presence of a chromosomally encoded rifampin ADP-ribosyltransferase (Arr-ms). Arr-ms is a small enzyme whose activity thus renders rifamycin antibiotics ineffective.	6.65047e-71
NZ_CP043959.1\|WP_167534518.1\|2759259_2759730_-\|glyoxalase	gnl\|CDD\|319901	cd07235, MRD, Mitomycin C resistance protein (MRD). Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.	2.98213e-53
NZ_CP043959.1\|WP_150154491.1\|2766536_2767070_+\|2'-5'-RNA-ligase-family-protein	gnl\|CDD\|379265	pfam13563, 2_5_RNA_ligase2, 2'-5' RNA ligase superfamily. This family contains proteins related to pfam02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity.	8.28135e-08
NZ_CP043959.1\|WP_150154490.1\|2764426_2765887_-\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	1.84329e-40
NZ_CP043959.1\|WP_150154487.1\|2760692_2761601_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	6.48012e-39

>NZ_CP043959.1|WP_150154487.1|2760692_2761601_-|LysR-family-transcriptional-regulator
MSLRQYEYALAVAEEGSVTAAAERLHVAQPSVSQQIRGLERELGVKLFARTPTGLVPTTVGRAFLREAEIAVSASRRARATARAGAEDLVGELVVAVQMGFGTRQLPRALGELRRRFPRLEITVFEEPSATELDRLCRRGALDFALMAACDRTPSDAHHLGDEELVVVLGEGHPRLGSERVELRDLESEPWVRFDRDSTLDAVLLEVLRDDGLAPATAARVSQAATAVRWAAQGLGVTLLPASAVPPEHEHLARPVSPALSRPVIAVVRQDGGPAETALLDLLRHENWPGSVRERLTLSRVS
>NZ_CP043959.1|WP_150154486.1|2759862_2760630_+|SDR-family-oxidoreductase
MSTAHNENSATGELTGKRALVTGGTKGIGAAVVRQLLDAGAEVLTTARSASGTVPEGARFVAADVRTRAGAEALAEAVADTLGGVDIVVHNAGGAGPHRSALAIPDEEWQDALDLNYLSAVRLDALLAPGMRDRRAGAIVHVSSAVVPVPGPLFLHYTAAKAALENYSRGLATELAPAGVRVNTVTPGRTATPGGEETRRQWAALSDTTGATSTPPLGREGLPDDIAYAVLYLVSDRASWVTGTNLVVDGGEFPR
>NZ_CP043959.1|WP_167534518.1|2759259_2759730_-|glyoxalase
MASRAPVSDSFKTPGAGLPTVGGMSARFDAIGMVVSDMAASVAFYRRLGLVFPDGAETQGHVEAELRGGLRLLLDSEEVVRSFHPRWRAPSGEGRTSLAVRCDSPAEVDALFAGMVESGARAELKPWDAEWGQRYAVVLDPDGNGVDLFAPLSTGE
>NZ_CP043959.1|WP_150154484.1|2758578_2759082_-|hypothetical-protein
MGYKLRDPYRDVWVRFHSLPESKRYPEDEGEYDIVLGRYNTVLDELFAGEDVYVITPVRTAEAKVPPFQPEAGYWQSLLVNDDPDPEFRTYCHLFAARRPWQHGCLDGPLRDIADDRVAGVLITDTQVRRIHHPYDGGADVFLATPGERDRMRQRHADWLSSHPLGL
>NZ_CP043959.1|WP_150157313.1|2758237_2758516_+|hypothetical-protein
MRGDEFVGLLTVHGIDMPVYLCDFGPGPGWEPVRPLFEAWAAVQGPDPDGSRTTAALKPILDLGLTLVPVAGGETINRFFLRIDGDKASLRY
>NZ_CP043959.1|WP_150154483.1|2757356_2758052_+|helix-turn-helix-domain-containing-protein
MYRERASRLPGAVVWTSNPSGDGGSGRVLPDGCMDLLWHDGRLLVAGPDTRAHPVGEPSAWAGVRFRPGTAPPLLGVPAHELRDSRVDLADLWPTADVRRASARVHAADHPAQGLEEVALRLAAEAAPPDPVLGRLVTALAAGRPVAAAADELGLGARQLHRRSLTAFGYGPKTLARILRLRRALALARAGVPFAETAARAGYADQPHLSREVRSLTGVPLRELVPPAPHA
>NZ_CP043959.1|WP_150154482.1|2756407_2757346_+|helix-turn-helix-domain-containing-protein
MDALTGLLEGPRARGAFMIRACFDPPWAVRVEDRAPLTVMLLVRGEAWLLPDQGERVRLRAGDLAVARGPDPYTCADHPDTAPQALILPGGACHYPDGRPLNGVMDLGVRTWGDRPDGETVLLIGTYQMRGEIGGRLLEALPPLLSLGADVWECPFTPFLMHEVTREAPGQEVVLDRLLDLLVIAALRAWFARPEAEPPAWYEALSDPVVGPVLRRVQDDPARPWTVAGLAAEAGVSRAALARRFTRLVGEPPMTYLTGWRLALAADRLRDTDDTIGAIARHVGYGSAFALSTAFKRAFGVSPQEWRGRAAA
>NZ_CP043959.1|WP_150154481.1|2755486_2756326_-|NAD(P)H-binding-protein
MDEKTDTKDMTLVVTGASGRTGRRVARAAEAAGTTVRPASRATGFDWEDRSTWADTLRGADAAYLVHPADVGAPGTAEAVGALADVAVRLGVRRLVLLSARGEDQALATEEALRASGADWTVVRAAWFAQNFSEGPLAQELRRGELVFPAGEVAEPFVDVRDIAEVVVAALADGNRYAGRTLSVTGPRLLTWAEAVAEIAAATGRPLTFRAVPADAYREALEGFGLPGEEAAFLTDVFATLLDGRNARVEDGVRQVLGREPRDFAGFVREEAAAGTWTA
>NZ_CP043959.1|WP_150154480.1|2754277_2755426_+|YihY/virulence-factor-BrkB-family-protein
MQPASESPDAPSGRLHRARALYRNVSKRRTAWLLLKDTVNSCMEYRILGLAAEAAFFTLLSVPPLLLSLIGLLGYVDAWTGADTIQSVQRNLLDASRTVLSDRGVKEVAEPILRDVTKGGRPDVISLGFLIAVWSGSRAVNVFIETITVMYGLDGVRGIVKTRLLAFLLFIVALLIGSVALPLMVAGPDAVVDVVPWSTTVVQILYWPVVILLSVAFLTTLYHVSVPVRSPWIEDVPGALVALAMWVLGSFLLRIYLTSTVEGPTIYGSLAAPVAVLLWIGVSAFAVLVGAAVNAAIDRVWPAAATAAAREANERQRQAQVAEYVARTSASGEADPDMPSEFPERWSRFLPPEDVTARLRAHTKPSHPRGGNGPGHDDKRGD
>NZ_CP043959.1|WP_150154479.1|2752531_2754166_-|DNA-alkylation-response-protein
MAGITHSVTNQAPPLVQYDVFGSDRALVEAVERHLAPEVRDDGLAELSALGHTAGSAQVQEWGVQANENPPRLRTHDRYGRRIDEVEFHPAWHRLLGKGVSAGLTAAWGRPGGHVRRAAAFLMWTQVEAGNGCPLSMTHASVPALRTDPALAAEWEPRLTSVIYDRALRPPGQKPGALFGMGMTEKQGGSDVRANTTAARPLAEDGTYALTGHKWFCSAPMSDAFLVLAQAPGGLTCFLVPRVLEDGSRNVFLLQRLKDKLGNRSNASAEVEFDGTWARRVGEEGQGVRTIIGMVAATRLDCALGSAGLMRQAVAQAVHHCAYREAFGGKLADKPLMRNVLADLALESEAATTLALRLAAAYDDGGEQERALLRIAVPAAKYWVTKRCAPVAVEAAECLGGNGYVEESGMPRLVRESPLNSIWEGAGNVQALDVLRALRREPAALDAYLREVGKARGADHRLDAAIKDLLTDLADLEGVEGRARRLTERLALVLQGSLLVRHAPPEVADAFCAGRLGGDAGSAFGTLPYTLNLASVVERARPLS
>NZ_CP043959.1|WP_150154488.1|2761838_2762486_+|ThuA-domain-containing-protein
MSDPALLVYTRTTDYRHDSIPAGVAALRALGGFDVHAHEDPAVFEEPLDRYAAVVFLSTSGDVLTPAGRERLAAHVEAGGGFVGVHAAACTEYDWPYYGELLGARFDRHPPLQPGRAVVEDHGHPATRHLPAVWELTDEWYDFRTNPRPAVRVLVSADESSYDGGTMGADHPLAWCREQGAGRVFYTSLGHTSEIYDDPDFRAHLRGGISWAAAR
>NZ_CP043959.1|WP_150154489.1|2762859_2764410_+|carboxylesterase-family-protein
MTADRENPVATTAYGAVRGRREQGVAVFRGIPYAAPPFGPRRFRPPVPPEPWDGVRDAGAFGPTAPKPPYSPAFAEYLSDPDIAGDDCLNLNVWTPDPSPDARLPVLVWLHGGALTRGSSAVPVYDGSTFARDGVVFVSLNYRLGVEGYGRFPDAPANAGLRDQLAALQWVHESIAAFGGDPGRITLAGQSAGAISAGALVAAPQAQGLVRQAVLQSGPPESTDRDKVRRMVRRMAGRLKVPATAEAFAGVDREQLLRAQAEVGRLGGPVLGGPAFGIVVDGDLVPRDPLEALTDGAAPGVTLLTGWTRDEYRLWLVPGGLTERVDRLGAVALAGAMARCRCGSEVPRGYRALHPDAGTTETVGQMVTDHLLRNPLHRLSDGRTEPSYVFEFAWPSNRPGMGACHALELGFVFDSGDSPDARKLAGEGAPQDLADAMHGAWVRFVTDGTPGWERWGPDHPVRVFGDGAPRTVHGPRDRELALWTTPAAERSAHTPQSPELRSVVRRLRRGGALRRT
>NZ_CP043959.1|WP_150154490.1|2764426_2765887_-|SpoIIE-family-protein-phosphatase
MAGRAEPPCPAGDGLRGTGVCPLSEQQEPGPQDGRADSQQPQVPDLRPHLDAELERIGTQLRALADAKDRLQGLLDAVLSISGELDLSSVLRRIVTTAMDLVGARYGALGVLHESGEYLKEFITAGLDEAERAALSGIPFPHGRGVLGLLIHNPEPLRVESIPSHPSSAGFPPGHPPMRTLLGVAISVRGEIYGDLYLSERSDGRPFAPEDEDIVVALAGAAGIAIENARLFGQVRDSAERFQRLLLPALPGLSPFEAATVYRPANRPNQLGGDWYDAVVLPDDAVGVMIGDVAGHDLYAAAAMARINSMLRALLYDLRNPPSQVLGQLDRTLLTTTDIPVTTVCLARIEPQETGWVLRWSTAGHFPPLLIGPDLETEYLEAEPGLPLGVSTGMERPDHTHPLPAGSILLFFTDGLVEHHARSIDEGLTALADLAATHAERPLNEFVQVLADHHPSDGQDDMALLALRIPASTRCPPPAAPDDEER
>NZ_CP043959.1|WP_150154491.1|2766536_2767070_+|2'-5'-RNA-ligase-family-protein
MRTVELLLDEAADAAVREAWRRLADAGLPSQARHRSPTNSPHLTLASCPELTAPIRWELAEVAAALPLPVRFDGLIRFERPTSVLAWSLELDSALADLHRRVWEAVVSDSPPETLSPFHEPGRWSPHITLGRTRRTGAFAGRRVPELLPPFPLSVHLTTLRSFDTETGTLEFLTART
>NZ_CP043959.1|WP_150154492.1|2767351_2767762_+|NAD(+)--rifampin-ADP-ribosyltransferase
MDEVWDEGPFYHGTKAELQIGDLLTAGFRSNYRPEIVMNHIYFTALRDGAGLAAEIAAGDGTPHVYVVEPTGEFENDPNVTDKKFPGNPTRSYRSREPLRIIGEVTDWTRLTPEALQMWRDRLAAIRSDDRAEIIN
>NZ_CP043959.1|WP_150157314.1|2767912_2768395_+|hypothetical-protein
MFALSGCSLVWNCEDTTAERGEAGVNVEVEDTSGRPMGVTAEVVDWRLGPHPQVPDEGDHVHFRLRFDGAETTSRIAVDLCAVDKERVAVGCRTVHWEEAFGPNGDRTADIWLAVDHPEQVADVLVIPNDQSYVGRTCEEDLKDGGGQHPPAPAVAGDQL
>NZ_CP043959.1|WP_150154493.1|2768435_2769590_-|transcription-termination-factor-Rho
MTTALDRPAPQTSARQQSQTVTVTGVLDVDATGKGHLRGPGLTAGSSDPVVSAALVRRHGLRKGDLVEGVLGDRRSLSEVARVDGRTPRSLAARPHFRDLTPLHPHRRLRLEHRASGLAGRVIDLLAPVGKGQRGLLVAPPKTGKTVLIQQLAAAVAGNHPECRLMVVLLDERPEEVTDMRRSVRGEVYASTFDRPAKQHIALAELVVERAKRLAEAGEDVVVLLDSLTRLCRAYNNAAGPGGRTLSGGVDAGALIGPKRFFGAARQTEEGGSLTILASALVETGSRADDFYFEELKGTGNMELRLSRESASRRLFPAVDITMSGTRREELLLTPQELSATQGLRRALQSRDGSADLETLLGRMRETPDNAAFLRQVRPTLPAG
>NZ_CP043959.1|WP_150154494.1|2769951_2770866_-|homocysteine-S-methyltransferase
MSTTASLASALADGTVVLDGGMSNQLAAAGHDLSDELWSARLLAEDPEAVTAAHLGYFEAGADVAITASYQATFEGFARRGIGRECASELLALSVECARTAASRARGPRRPLWVAASVGPYGAMLADGSEYRGRYGLTVAELERFHRPRAEVLASAAPDVLALETIPDTDEAEALLRAVRGLGVPVWLSYSAAGGRTRAGQPLEDAFALAARADEVIAVGVNCCTPEDADHAVAVASRVSGKPVVVYPNSGEQWDARARAWTGESTFAPSRVTGWRESGARLIGGCCRVGPETITSIADALRVS
>NZ_CP043959.1|WP_150154495.1|2770962_2773677_+|helix-turn-helix-transcriptional-regulator
MTTAHQGDGPPAVEGIGGSHEPHDMHDPHDVHDPHGDPFLRTRFAVPARPVTFLRRARLAGHLDQALRTPLTMVNGSAGAGKTLLVADWAAELDELPVAWLTTDADGQDPGMFWAYLLQALRTSGVPLPEDVGFPADAHRVGAALPARLAAALSGRDRPVVVVLDEFDRVTAPEVAEQLDFLLRHSGPGLRLVLVTRTEPLLPLHRHRTAGELTEIRDAELAFTPEEAALLLEAHGLDLPPAAVRGVVRRTRGWAAGLRLCALAAGEAPDPEIYLKEFEADRSAIADFLLAEVLKRQDDGTQELLLRVSVLDRFGPGLANAVTGRADAEAVLARLHRCNAFVQHLGHGVYRLHPLFGEILRAHLRMRRPGLEPELHRRAAVSLRRAGALPAALGHGAAADDWEFTAGALVDDLALGQFFTGPRSDTLAGLFARMGRQGTGPAPELVRAAGRLSRGELGGGLTHLRRARRHLRDHDGSTDPVDPAAARLSCAFLEALAARLAGAPDAAEDAVRAAEALRDVVPVELLDRHPELFALLLDHVGSTRLWAGDFTGARSALARAADLAPGAATALPREDALGRLGLIDCLNGWLRRAERTAHEALAETERFGLARPGGSGVERLVLAAVAVEREELGQAQALLDTAAESHPALRDPVLEAGRALTAARLHLARGEPGSAWKAVRTGVRADTESPWVRGETAVVAAAARLAEGRAQAAAALLSEVPRDQVACVVGAAWVQLAAGRPAAALGLLDQAAPEGRAGPAVTVRAALVRARAADAAGDGAAARRHVERAVAEARPERLRRPFTEAGPWLRPYLTAGRPAPRAGRSRGTGPHRNPAPPPPLVGELSGRERDVLRRLALAMSTEEIAADLYVSVNTVKTHLKSAYRKLSVGRRNEAVRRARELDLL
>NZ_CP043959.1|WP_150157315.1|2773822_2774299_+|hypothetical-protein
MRRTHADYTGGVYGSMLAASVIVGAGTLGDFPRIELMLLLLLTGGVFWIAHVHAHLFGARLAQRPPDRAVVLRVCREEWTIVKAALPPATAVGVSPVLGLGVQGGQWFALAVAVAGQVGWSVAAARQAGATRRLLVLSALVNLVLGLVILLSKLWLKH

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Crispr_ID: NZ_CP043959_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_9

3346768-3346923

Orphan

Consensus_repeat	Method
CCCCGGCCCACACCCGCGTCGGCGGGCCGTTGCGTAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_9

>merge|NZ_CP043959|9|3346768-3346923|CRISPRCasFinder
CCCCGGCCCACACCCGCGCCGGCGTCGCGGTGCGGAGCCCCGGCCCACACCCGCGTCGGCGGGCCGTTGCGTACGGGTGGGCGCGGCGGCACCCCGTAGCGCCGGGTTGCGCAGACTCCCCCCGGCCCACACCCGCGTCGGCGGGCCGTTGCGTAC

>NZ_CP043959|9|9|3346768-3346923|CRISPRCasFinder
CCCCGGCCCACACCCGCGCCGGCGTCGCGGTGCGGAG	CCCCGGCCCACACCCGCGTCGGCGGGCCGTTGCGTACGGGTGGGCGCGGCGGCACCCCGTAGCGCCGGGTTGCGCAGACTCC
CCCCGGCCCACACCCGCGTCGGCGGGCCGTTGCGTAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150154879.1\|3354347_3354806_+\|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase	unknown	unknown	gnl\|CDD\|274679
NZ_CP043959.1\|WP_150154880.1\|3354937_3355369_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|293786
NZ_CP043959.1\|WP_150154867.1\|3339035_3339938_+\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|275172
NZ_CP043959.1\|WP_150154878.1\|3352834_3353998_-\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP043959.1\|WP_150154870.1\|3341879_3343073_+\|HupE/UreJ-family-protein	unknown	unknown	gnl\|CDD\|379373
NZ_CP043959.1\|WP_150154869.1\|3341015_3341690_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380619
NZ_CP043959.1\|WP_150154868.1\|3339969_3340989_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP043959.1\|WP_150154866.1\|3338122_3339034_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224053
NZ_CP043959.1\|WP_150154875.1\|3349014_3349791_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|180462
NZ_CP043959.1\|WP_145824905.1\|3336024_3337044_+\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|380535
NZ_CP043959.1\|WP_150154881.1\|3355365_3355785_-\|VOC-family-protein	unknown	unknown	gnl\|CDD\|380093
NZ_CP043959.1\|WP_150154876.1\|3349822_3350998_-\|phytanoyl-CoA-dioxygenase	unknown	unknown	gnl\|CDD\|227609
NZ_CP043959.1\|WP_150154877.1\|3351107_3352142_+\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|380530
NZ_CP043959.1\|WP_150154873.1\|3346934_3347945_-\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP043959.1\|WP_150154872.1\|3345224_3346298_+\|DUF916-domain-containing-protein	unknown	unknown	gnl\|CDD\|368712
NZ_CP043959.1\|WP_150154871.1\|3343195_3345151_+\|metallophosphoesterase-family-protein	unknown	unknown	gnl\|CDD\|379868
NZ_CP043959.1\|WP_150157350.1\|3352235_3352811_+\|DUF1211-domain-containing-protein	unknown	unknown	gnl\|CDD\|377696
NZ_CP043959.1\|WP_150154864.1\|3334715_3335705_-\|5-dehydro-2-deoxygluconokinase	unknown	unknown	gnl\|CDD\|275175
NZ_CP043959.1\|WP_150154865.1\|3337043_3338117_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224093
NZ_CP043959.1\|WP_150154874.1\|3347941_3348946_-\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|275173

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150154879.1\|3354347_3354806_+\|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase	gnl\|CDD\|274679	TIGR03618, Rv1155_F420, PPOX class probable F420-dependent enzyme. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes. [Unknown function, Enzymes of unknown specificity].	1.25542e-23
NZ_CP043959.1\|WP_150154880.1\|3354937_3355369_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	3.52004e-19
NZ_CP043959.1\|WP_150154867.1\|3339035_3339938_+\|TIM-barrel-protein	gnl\|CDD\|275172	TIGR04379, myo-inositol_catabolism_protein, myo-inosose-2 dehydratase. Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars].	4.24917e-46
NZ_CP043959.1\|WP_150154878.1\|3352834_3353998_-\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	5.27861e-60
NZ_CP043959.1\|WP_150154870.1\|3341879_3343073_+\|HupE/UreJ-family-protein	gnl\|CDD\|379373	pfam13795, HupE_UreJ_2, HupE / UreJ protein. These proteins contain many conserved histidines that may be involved in nickel binding.	1.60777e-41
NZ_CP043959.1\|WP_150154869.1\|3341015_3341690_-\|hypothetical-protein	gnl\|CDD\|380619	cd19964, PBP1_BMP-like, periplasmic binding component of a basic membrane lipoprotein (BMP) from Aeropyrum pernix K1 and its close homologs in other bacteria. Periplasmic binding component of a family of basic membrane lipoproteins from Aeropyrum pernix K1 and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold.	5.59686e-10
NZ_CP043959.1\|WP_150154868.1\|3339969_3340989_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	7.74061e-51
NZ_CP043959.1\|WP_150154866.1\|3338122_3339034_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224053	COG1129, MglA, ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism].	8.07046e-99
NZ_CP043959.1\|WP_150154875.1\|3349014_3349791_-\|SDR-family-oxidoreductase	gnl\|CDD\|180462	PRK06198, PRK06198, short chain dehydrogenase; Provisional.	4.746e-145
NZ_CP043959.1\|WP_145824905.1\|3336024_3337044_+\|substrate-binding-domain-containing-protein	gnl\|CDD\|380535	cd06312, PBP1_ABC_sugar_binding-like, periplasmic sugar-binding domain of uncharacterized ABC-type transport systems. Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.	2.7291e-96
NZ_CP043959.1\|WP_150154881.1\|3355365_3355785_-\|VOC-family-protein	gnl\|CDD\|380093	pfam18029, Glyoxalase_6, Glyoxalase-like domain. This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.	1.31452e-20
NZ_CP043959.1\|WP_150154876.1\|3349822_3350998_-\|phytanoyl-CoA-dioxygenase	gnl\|CDD\|227609	COG5285, COG5285, Protein involved in biosynthesis of mitomycin antibiotics/polyketide fumonisin [Secondary metabolites biosynthesis, transport, and catabolism].	3.22916e-45
NZ_CP043959.1\|WP_150154877.1\|3351107_3352142_+\|substrate-binding-domain-containing-protein	gnl\|CDD\|380530	cd06307, PBP1_sugar_binding, periplasmic sugar-binding domain of uncharacterized transport systems. Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.	5.52181e-93
NZ_CP043959.1\|WP_150154873.1\|3346934_3347945_-\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	5.3167e-64
NZ_CP043959.1\|WP_150154872.1\|3345224_3346298_+\|DUF916-domain-containing-protein	gnl\|CDD\|368712	pfam06030, DUF916, Bacterial protein of unknown function (DUF916). This family consists of several hypothetical bacterial proteins of unknown function.	5.67534e-11
NZ_CP043959.1\|WP_150154871.1\|3343195_3345151_+\|metallophosphoesterase-family-protein	gnl\|CDD\|379868	pfam16656, Pur_ac_phosph_N, Purple acid Phosphatase, N-terminal domain. This domain is found at the N-terminus of Purple acid phosphatase proteins.	4.49067e-14
NZ_CP043959.1\|WP_150157350.1\|3352235_3352811_+\|DUF1211-domain-containing-protein	gnl\|CDD\|377696	pfam06736, DUF1211, Protein of unknown function (DUF1211). This family represents a conserved region within a number of hypothetical proteins of unknown function found in eukaryotes, bacteria and archaea. These may possibly be integral membrane proteins.	1.00174e-21
NZ_CP043959.1\|WP_150154864.1\|3334715_3335705_-\|5-dehydro-2-deoxygluconokinase	gnl\|CDD\|275175	TIGR04382, myo-inositol_catabolism_protein, 5-dehydro-2-deoxygluconokinase. All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars].	1.60591e-149
NZ_CP043959.1\|WP_150154865.1\|3337043_3338117_+\|ABC-transporter-permease	gnl\|CDD\|224093	COG1172, AraH, Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease components [Carbohydrate transport and metabolism].	3.74034e-64
NZ_CP043959.1\|WP_150154874.1\|3347941_3348946_-\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|275173	TIGR04380, hypothetical_protein_HOLDEFILI_04020, inositol 2-dehydrogenase. All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars].	6.8029e-115

>NZ_CP043959.1|WP_150154872.1|3345224_3346298_+|DUF916-domain-containing-protein
MHVLAVSRRTPRLPVRLTVLLRAAVLGLLTALALVCAHPTPAAAADGDVSWRVRTGANAYGDDRSSFSYAVNPGGTVEDTMVVTNRGRTPLRLAVYASDGYTTDAGQLDLLTRDKKSTGVGVWTRPEVTAVTVAPGKSADVPFTVTVPENATPGDHVGGLLTSLKQADTAAGINVDRRLGLRVAVRVGGELKPRLAVEDAHLDYHGSAGPFSKGSATVTYTVHNTGNALLSGRQEVAVEGPFGWLRTAAGDLPDTPALLPGERWKVTVPVADVAPGVRLTATAKVLPLLTDASGSTTPLKPVEGTAGAWAVPWTLTLLVLLLIAVVTAIVLLARRNRARRKAREAALVRDAVKAALG
>NZ_CP043959.1|WP_150154871.1|3343195_3345151_+|metallophosphoesterase-family-protein
MRPSSKTQTDGSVRRRVAGGAATAVLGLTMALGGGGAAPAVAADSAELSGVVLGVGADETQRTVTWYSTADTAQQLQVAPTATVTDGGFPADAATFAATGGANIASSGGFNRHATVTGLKENVEYSYRVGSEGNWSKTYTFRTRDFEGDYDFLFLGDPQIGSSGDAQKDGAGWADTLKVATEANPDAELLVSGGDHVESANDEKQWTSFLGPDQLRQVPLAATIGNHDVGGKAYEQHHFTPNTDRSDAYYDKDAATRSGGDYWFIHKDVLFIDINSNAQSDTKDAQHVDYITDVIKKHGSEAKWKVLVYHHSIYSPASHSYDQGNKDRRKDFTTAFSDLGIDMVLQGHDHSYSRSYAIKNGQKADPTEQPGQAEVYPGPGGVIYVTANSASGSKYYDIKKPDNSGTGVQGNGPDPLNPDNFWFNSVENQEHVRSYVRVKVRSDKLVLENVRSGTCATPNPAVDNGNVPCSNPDRPVGSVVDKVTVHPYNGDGQSLQVNVPDAAPGEFGWTIDGYNGLVDLGTATERDGDHFEAAGKINPLRVTDSRRSLAPWSVSANVSDFQDAGKKFSGSYLGWKPYVLNGGAGAKAASAVASGYDDKGAGLSVSRGLASAEQGHPRGEARLGADLDLKIPDSVAKGSYRATLTITALSS
>NZ_CP043959.1|WP_150154870.1|3341879_3343073_+|HupE/UreJ-family-protein
MSQRIRRTLLTLCLTVAALAGFGGPAQAHGFTSTVYADVVETDGRPRTTLELEYDLLVVSAADAEDDDALFREGTAAFENGDDRSRARVLDDHAKAAVGYVTRRFSLTSGGRPCTAHRAGDVTMTRREGVPYAVLVLDWTCADGDGPTLRSTLFPDREQYVKDTKTIVTYAVDGLSGSAALDAAHPSFSLDQAWYERFAEFFRLGAEHLLTGVDHILFLLALIVGSRTPREVVLAATSFTLAHSVTFLLAALGLVDVPADVVEPVIAASIAVVAGWHLWRLARRDDRRPTFGRGHFRLDRAGWTRLAVVFCFGLVHGLGFAGALGIDAAWSWTLLWSLAVFNLGIEAVQLALIGLSFPALAMLRHRAPRAGRLVTGLAAAGVAVMGLIWCVQRITET
>NZ_CP043959.1|WP_150154869.1|3341015_3341690_-|hypothetical-protein
MRSPLRAAAVLAAVAALATGCASADDWSRPHAAPTSVGALGPGFVDPTATPTPEATVTPRPGSWDDVHPPKGYRVVLLTAGDDRPTRSLVSAVQEWAEEEDVDLRTVTADDPTGYVAAVQEAMDMGPDLVVSAGNDLVDPLAAVTPSHLGQRFLVVGAELAEPTENVTAADWSGASFRGEGLGMSSTYDPASFTEARCAAAVRAGVAAVLNGLTGIVLWLDDVA
>NZ_CP043959.1|WP_150154868.1|3339969_3340989_+|Gfo/Idh/MocA-family-oxidoreductase
MNRREPLGIAVIGTGRMGADHVRRIDRVISGARVAAVVDIDGERAKAVAAGVDGCTAHTDAAEAMASDAVDAVLIASSGPAHEEALLAAFARDLPVLCEKPLTPDAASALRVVEAEQALGHRRVQVGFMRRYDTEYVRLKALLGSGQLGRPLMLHNRHRNVASPPFFTSSMLISDSVAHEVDATRWLLGHEITAVTVLRPAPSAGAPDGLRDPQFVVLETDGGALSDVEIFVNCGFGYQVQAEAVCERGTARIGDGHQLVTNMAGRWGGTIAQDWTERFAQAYDDEVRAWVDATRRGEVTGPSTWDGYAAAAVCEAGVRAMEEGGRVRVDLAQRPPLYA
>NZ_CP043959.1|WP_150154867.1|3339035_3339938_+|TIM-barrel-protein
MAVALDRIRVGSAPDSWGVWFPDDPQQVPWQRFLDEVAEAGYSWIELGPYGYLPTDPARLTDEVRSRNLSVSAGTIFCGLHRGPSEWDATWEQVSRVAALTQAMGAEHLVVIPSFWRDDKTAEILEPPELTTEQWGHLTRGMERLGREVKETYGLDIVVHPHADTHIDTEQHVERFLDSTDSRLVNLCLDTGHYAYCGGDSVKLIETYGERIGYLHLKQVDPEILADVVKNEIPFGPAVQRGVMCEPPAGVPELGPVLTAAQKLGVDLFAIVEQDMYPCEPDKPLPIAVRTRKFLRSCGA
>NZ_CP043959.1|WP_150154866.1|3338122_3339034_+|ATP-binding-cassette-domain-containing-protein
MTDKTTGTDGAVLTDTPAEGDRPLVELRAAGKSYGNIRALHGVDLTVHPGRVTCVLGDNGAGKSTLIKIISGLHRHTEGEFLVDGEPVHFSTPREALDKGIATVYQDLAVVPLMPVWRNFFLGSEMTKGPWPLRRLDIDRMKRTADEELRNMGIVLDDLEQPIGTLSGGQRQCVAIARAVYFGARVLILDEPTAALGVKQSGVVLKYIAMARDRGLGVIFITHNPHHAYMVGDQFNVLRLGTLELSADRSQVSLEELTNHMAGGAELAALKHELAQVRGVDTEGLPEAGVLRAPTAAAPEGKS
>NZ_CP043959.1|WP_150154865.1|3337043_3338117_+|ABC-transporter-permease
MSMAQQAEPAATTPPAPGPEQQKDGRTTRRPLALRLLARPEVGVFLGAVAVLVFFLFAAPPVRDGSSMANILYQSSTIGIMALPVLMIGGEFDLSAGVAVVTSALTASMLSYQLTLNVWVGVIVALLVSLAVGFFNGWLLVKTGLPSFLVTLGTFLILQGVNLAVTKLVTGNVATDNISDMDGFDQAKALFASSFEVGGVQVKITVIWWLVFAALATWVLLRTKYGNWIFAVGGNKESARAVGVPVTFTKISLFMLVGFGAWFVGMHNLFSFNTVQSGEGVGQELIYIAAAVIGGCLLTGGYGSAIGPVFGAFMFGMVQQGIVYAGWNPDWFKAFLGVMLLGAVLINLWVQRTATRR
>NZ_CP043959.1|WP_145824905.1|3336024_3337044_+|substrate-binding-domain-containing-protein
MDRSSHPRSRRVVPFVAVAAAAALTLAGCSSGSGGKKSEEGGADASAGKASTPQMTVALVTHQAPGDTFWDIVRKGAQTAADKDNVKLIYSADPNAGNQANLVQNAIDQKVDGIAVTLAKPDALKGVIAKAEAAGIPVVGINSGLSDWKDLGLLEFFGQDETVAGEAFGKKLNEVGAKNAVCVVQEQGNIGLTQRCAGLEKTFEGKTQVLNVNGTDMPSVKSTISAKLKQDSSIDYVVTLGAPFAPTAVQSVQEAGSKAKVATFDLNKELTGAIKDGDIQFAVDQQPYLQGYLAVDGLWLYKNNGNYSGGGEQPVLTGPAFVDKSNVDAVSQYAAKGTR
>NZ_CP043959.1|WP_150154864.1|3334715_3335705_-|5-dehydro-2-deoxygluconokinase
MATPQYFDLVTMGRIGVDLYPLQTGVPLSQVETFGKFLGGSAANVAVAAARLGRSTAVITRTGDDPFGTYLHEALKDFGVDDRWVTPVAALSTPVTFCEIFPPDDFPLYFYRRPKAPDLEIHPHELDLPAVRSAGIFWITGTGLSEEPSRTATLTALEARDKAGTTVFDLDWRPMFWRDPDQARPYYREALRHATVAVGNLDECEIATGVREPEACAEALLAAGVELAVVKQGPRGVLAVHRDGTRAEVEPVPVEVVNGLGAGDAFGGSLCHGLLAGWDLERTMRHANAAGALVASRLACSSAMPTESEVADLLARAVPPDAAGRPSQS
>NZ_CP043959.1|WP_150154873.1|3346934_3347945_-|Gfo/Idh/MocA-family-oxidoreductase
MSECAPLRIGILGAARITERALVAPARAGGHRLVAVAARDRSRAEVFAAAHGVERTLGSYAELLADPEVEVVYNPLANGLHGPWNLAALAAGKHVLTEKPSASNAAEAEEVREAARASGTVFMEAFHYLFHPVTRRLHELLASGELGELRHAEALVAIPAPEADDPRWSLPLAGGALMDLGCYGLHALRVLAPYAGGAPRPVAARAGERTGAPGVDEWLDADLLFPGGATGTARCHMAYDRLEMSLRIVGSRGEATAPNFVLPQLDDRVVIRTAEGERTEHLGTRSSYAYQLEAFAARVRREASLPLDADDAVATMRLIDACYTAAGLSPRPRTAP
>NZ_CP043959.1|WP_150154874.1|3347941_3348946_-|Gfo/Idh/MocA-family-oxidoreductase
MRIGILGLGRIGAFHAETLSGLDAVESLVVSDPFADAAKAAAERFGAQVADSPEALLAAGVDGVVVAAATDAHPHLITACVEAGVPVFCEKPVARTMTEGVEVLKAVAGRDVPVQIGYNRRFDAGFVAAHAAVRAGELGTLHTVRSTTLDPAPPPAAYIAASGGIFRDCSVHDFDIIRWVTGREVTEVYAVGGNRGADFIKEAGDADTTGAVLTLDDGTIAVVSNSRHNGRGYDVRMEIHGFADSIAVGLEDKLPLRSVEPGVTFPAGVPHDFFMDRFTDAYRAELTAFTEVVAGSRTSPCTIADALEAGWIAEACTLSLHEHRPVTLEEVRQA
>NZ_CP043959.1|WP_150154875.1|3349014_3349791_-|SDR-family-oxidoreductase
MGLLDDKVVLVNGGSQGVGAAVARAAVREGAVVAVSGRRPEPGEALVAELAGQGGKAMFVRADLADAEQARESVAQVVQAYGRIDCLVNSAGLTSRGTLLDTTPELFDQHIAINLKAPFFAMQAAVADMVRRAEPGTIVNVITSSAHGGQPFLAPYVAAKAGLMGLTRNAAHAHRWDRIRINGLNIGWTATEGEDATQRTFHGAGDDWRERAAARLPMGKLGRPDEIADFVVLLLSERSGVVTGSVIDWDQNVLGGLD
>NZ_CP043959.1|WP_150154876.1|3349822_3350998_-|phytanoyl-CoA-dioxygenase
MSASSSVQNPAPAAWLSRRDCDLDAFRALVEQATDAAGYGLASAVDRNVLLYDAERLALADRRSAQAELVRALTDGPGIVVIRGAFSDTSVVDRTTAVFDALIAQQRASGATAGDHFAKPGANDRVWNALEKAALHDPEAFADYYANDMIALVSTAWLGPGYQVTSQVNVVNPGGAAQTVHRDYHLGFLSDETAAAYPAHVHRLSPVLTLQGAVAHCDMPVESGPTLYLPHSQKYEPGYLAWRRPEFRAYFEEHHVQLPLAKGDAVFFNPALFHAAGANHSADIRRAANLLQVSSAFGRAMETVDREAVVGAVYPVLLARKAEGASEQWLENVIAASAEGYPFPTNLDNDPPVDGLAPPSQADVVRRALREGRTPRALRDELRAAAARRAS
>NZ_CP043959.1|WP_150154877.1|3351107_3352142_+|substrate-binding-domain-containing-protein
MGHPFPIREIARQAGLSEATVDRVLNGRGGVRESTAREVHRAVADLDRQRTQVRLVGRTFMVDIVMQSPERFSTAVRAALEAELPSLHPAVVRSRFHFRETGPAEELVAVLDRIARRGSQGVLLKAPDVPEVTAAVGRLAAAGVPVVTLVTDLPVSARVGHVGSDNRAAGATAAYLMGQWLGDRPGNVLTSLSSGFFRNEEEREMGFRSTMRARHPERTLVEIAEGQGLDATQYDLVRAALERDPEIRAVYSIGGGNIATLRAFQDAGRECAVFIAHDLDHDNTRLLREHRLSAVLHHDLRHDLREACHLVMRAHGALPPAGPILPSAIQVVTPYNMPAPAVGG
>NZ_CP043959.1|WP_150157350.1|3352235_3352811_+|DUF1211-domain-containing-protein
MALSDGVFAIAITLLVLDISVPQDLDPAQFHQALADTLPNLGAYAVSLAVLGGFWRDHRAIFRPVRQVDPDVIGLTVLGLGLAALLPFPTALVSEYGHERVSVVVYSAAVASLGAVHLALAAVIARRPWLRGGAEPVRDQFLYAIDLGATVVVFVVTIPLTLLVGPAAMWWWLVLLPVKVWLGRRENAAAG
>NZ_CP043959.1|WP_150154878.1|3352834_3353998_-|Gfo/Idh/MocA-family-oxidoreductase
MVDALGVAVVGFGWMGRVHTQAYARVAHHFPGLPLRPELITVAEEVPGRAEEAAAQFGFASTTRDWRDVAADPRVRAVSITAPNFLHREIGVALAEAGKHIWIEKPVGLTADDARAVADAAAKAGVQGAVGFNYRNAPAVEAARELIASGAIGTVTHARVRLFSDYAAHPDSALTWRYERERGGSGVLGDLASHGADLARFLLGDITSLTADTAIFCPERARPAGATAGHSRAAGGELGPVENEDYVSCLLRFASGARGVLEACRVSVGEQNNYGFEVHGTEGAVFWDFRRMNELGVSRGTGYQDQPVSTVYVGPRDGEFGAFQPGAANAMGYDDLKVIEAYRFLRSVAEGVPYGATLADAVRGAVVLDAMVRSAESGSWVTVDAPA
>NZ_CP043959.1|WP_150154879.1|3354347_3354806_+|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase
MTTRPGPRSLTDDALSDLLGAQRFGTLATVRRSGHPHLSTMVYDWDPDTRTVRFSTTADRVKVAHLRRDPHAALHVQGDDVWSFAVAEGEAELSDVTTVPGDAAGRELLDIVSRFARPDDEDAVLQQLVDERRLVIRLKVNRLYGTALDVEG
>NZ_CP043959.1|WP_150154880.1|3354937_3355369_-|ankyrin-repeat-domain-containing-protein
MNRRRQKKLTRRLVGAAPFGDSREIDALLRAGADPEARDPEGTTPLYAAAVHGAADNVRSLLKSGALPDTESGHGSEGTPLCGAACWGHTETVRVLLAHGADPCLREDHGTGRTPLRWAEEGPYPETVAVLIAAGAQGVGPRG
>NZ_CP043959.1|WP_150154881.1|3355365_3355785_-|VOC-family-protein
MRGRASHEPGTPRASRRDWWGVVLEAPDPSALARFYSELLGWEIGKEEPDGAVVAPPEGVGYVAFQLSDPYVPPVWPAREGAQRITMHLDFEVVDLPASVAHALQLGAREAGDQPQDNVRVMLDPAGHPFCLYLDEEQS

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Crispr_ID: NZ_CP043959_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_10

3762675-3762784

Orphan

Consensus_repeat	Method
AGGGGCGCGGGGAACCGCGCGCCCAGCCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_10

>merge|NZ_CP043959|10|3762675-3762784|CRISPRCasFinder
AGGGGCGCGGGGAACCGCGCGCCCAGCCCCACACCCCGCAGCCACCGCCGGCGCAGTCGAGCGGACCGCCACTCGCCCCCAGGGGCGCGGGGAACCGCACGCCCAGCCCC

>NZ_CP043959|10|10|3762675-3762784|CRISPRCasFinder
AGGGGCGCGGGGAACCGCGCGCCCAGCCCC	ACACCCCGCAGCCACCGCCGGCGCAGTCGAGCGGACCGCCACTCGCCCCC
AGGGGCGCGGGGAACCGCACGCCCAGCCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150155128.1\|3752017_3752839_-\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|252734
NZ_CP043959.1\|WP_145824569.1\|3763123_3763906_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213191
NZ_CP043959.1\|WP_150155140.1\|3772168_3773347_-\|S1-family-peptidase	unknown	unknown	gnl\|CDD\|365866
NZ_CP043959.1\|WP_150155129.1\|3754270_3755932_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP043959.1\|WP_150155133.1\|3763902_3764706_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213186
NZ_CP043959.1\|WP_145824579.1\|3750533_3750767_+\|DUF397-domain-containing-protein	unknown	unknown	gnl\|CDD\|377231
NZ_CP043959.1\|WP_150155132.1\|3761393_3762656_+\|PucR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|379258
NZ_CP043959.1\|WP_150155135.1\|3766730_3768014_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380566
NZ_CP043959.1\|WP_145824572.1\|3757284_3758190_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223489
NZ_CP043959.1\|WP_167534698.1\|3753620_3754112_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150157377.1\|3756334_3756529_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155137.1\|3768646_3769690_-\|L-glyceraldehyde-3-phosphate-reductase	unknown	unknown	gnl\|CDD\|381376
NZ_CP043959.1\|WP_150155134.1\|3765591_3766734_+\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119323
NZ_CP043959.1\|WP_145824567.1\|3764702_3765599_+\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119324
NZ_CP043959.1\|WP_145824578.1\|3750976_3751897_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379262
NZ_CP043959.1\|WP_150155136.1\|3768069_3768552_-\|cytoplasmic-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155139.1\|3770656_3771979_-\|triacylglycerol-lipase	unknown	unknown	gnl\|CDD\|367570
NZ_CP043959.1\|WP_150155130.1\|3755995_3756202_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155138.1\|3769912_3770452_+\|snapalysin-family-zinc-dependent-metalloprotease	unknown	unknown	gnl\|CDD\|280248
NZ_CP043959.1\|WP_150155131.1\|3758421_3761250_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197715

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150155128.1\|3752017_3752839_-\|SAM-dependent-methyltransferase	gnl\|CDD\|252734	pfam04672, Methyltransf_19, S-adenosyl methyltransferase. This family contains a SAM (S-adenosyl methyltransferase) domain, with a central beta sheet with 3 alpha-helices on both sides. Crystal packing analysis of the structure Structure 3giw suggests that a monomer is the solution state oligomeric form. An unidentified ligand (UNL, cyan) was found at the putative active site surrounded by the residues His57, His170, Phe171, Tyr216 and Met22. The UNL is likely to be a phenylalanine or phenylalanine-like molecule. (details derived from TOPSAN).	2.1307e-121
NZ_CP043959.1\|WP_145824569.1\|3763123_3763906_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213191	cd03224, ABC_TM1139_LivF_branched, ATP-binding cassette domain of branched-chain amino acid transporter. LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.	4.64023e-98
NZ_CP043959.1\|WP_150155140.1\|3772168_3773347_-\|S1-family-peptidase	gnl\|CDD\|365866	pfam00089, Trypsin, Trypsin.	4.79516e-14
NZ_CP043959.1\|WP_150155133.1\|3763902_3764706_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213186	cd03219, ABC_Mj1267_LivG_branched, ATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).	5.32538e-111
NZ_CP043959.1\|WP_150155129.1\|3754270_3755932_+\|hypothetical-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	0.00327546
NZ_CP043959.1\|WP_150155132.1\|3761393_3762656_+\|PucR-family-transcriptional-regulator	gnl\|CDD\|379258	pfam13556, HTH_30, PucR C-terminal helix-turn-helix domain. This helix-turn-helix domain is often found at the C-terminus of PucR-like transcriptional regulators such as Bacillus subtilis pucR and is likely to be DNA-binding.	1.36034e-16
NZ_CP043959.1\|WP_150155135.1\|3766730_3768014_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|380566	cd06343, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.	2.18057e-75
NZ_CP043959.1\|WP_145824572.1\|3757284_3758190_+\|alpha/beta-hydrolase	gnl\|CDD\|223489	COG0412, COG0412, Dienelactone hydrolase and related enzymes [Secondary metabolites biosynthesis, transport, and catabolism].	2.22809e-08
NZ_CP043959.1\|WP_145824579.1\|3750533_3750767_+\|DUF397-domain-containing-protein	gnl\|CDD\|377231	pfam04149, DUF397, Domain of unknown function (DUF397). The function of this family is unknown.	2.13159e-20
NZ_CP043959.1\|WP_145824567.1\|3764702_3765599_+\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119324	cd06582, TM_PBP1_LivH_like, Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	3.64478e-56
NZ_CP043959.1\|WP_150155137.1\|3768646_3769690_-\|L-glyceraldehyde-3-phosphate-reductase	gnl\|CDD\|381376	cd19150, AKR_AKR14A1, Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins. Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.	0
NZ_CP043959.1\|WP_150155134.1\|3765591_3766734_+\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	7.74295e-64
NZ_CP043959.1\|WP_145824578.1\|3750976_3751897_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379262	pfam13560, HTH_31, Helix-turn-helix domain. This domain is a helix-turn-helix domain that probably binds to DNA.	3.34402e-10
NZ_CP043959.1\|WP_150155139.1\|3770656_3771979_-\|triacylglycerol-lipase	gnl\|CDD\|367570	pfam03583, LIP, Secretory lipase. These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.	5.18343e-77
NZ_CP043959.1\|WP_150155138.1\|3769912_3770452_+\|snapalysin-family-zinc-dependent-metalloprotease	gnl\|CDD\|280248	pfam02031, Peptidase_M7, Streptomyces extracellular neutral proteinase (M7) family.	5.07607e-23
NZ_CP043959.1\|WP_150155131.1\|3758421_3761250_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197715	smart00421, HTH_LUXR, helix_turn_helix, Lux Regulon. lux regulon (activates the bioluminescence operon.	9.91713e-16

>NZ_CP043959.1|WP_150155132.1|3761393_3762656_+|PucR-family-transcriptional-regulator
MPHAVRPRTLLRPGPVPAPRSRTPRVRSLIDADALRVLHRAARVLLDDLPQLTDRLVAVLQEQEPAYRTAVEGDAVATWQEVHRSLRHSISSLLDPRGAREGARRCSWKIGATRAEQGLPLDAVLHAFRLGGSLVWQGLVDETSRAAPEDVRLLVHVASDVWDFVDEHSTIVADAYRQTERQLAWRRENRVRLLAAALLDGTSRIADLPEAAQALDLPEQGRYVVVAVEGARSAGCTAAQAALAPGVRVHWHTGMDTDHGIVLVVEGDAAAIVPDEQPPGVRVGVSSVVEGLAAVGEARQLADTALRLCPGQGGTVRLTEHLPAALVASSPDLAAALADRLLGPLAGLEPADAEVLLDTLATWLACDGSAQRASRRLYCHRNTVLNRLRRYEQLTGRSLSRPTDLIEAGLALTAHRLLNP
>NZ_CP043959.1|WP_150155131.1|3758421_3761250_+|helix-turn-helix-transcriptional-regulator
MTGHTTARQQQVAELLDALHTDGGVRVVTGEPGCGRTTFLKTAARLFRDGPVRHLGADRVRELDDALRTAATDGPLLVCVDDAHLWDAPSRAALGHAAARVRESGLPAVLLLTVAGHRPVDREFTGLPVLRLGPLTPGDAALLVEEATDGAVDPAVREELVTAAEGNPALLRASVQRLSPAQLAGARSLPRPLVDAEVLAGVAGGRLPGPPGECGDLLLTTAAAVRATGEEDADAGLVQRACGAVAEGPLPEVLARTEGRLRFRSALVGRAVYACALPEHRRAAHRALAGAAAEADGVLALLHRSWAVTGPASGLADALAAAAADPACPATPALRHHALVRAADLARDDADRARRNLAAAEHALLAGRASDARRLLDLARGPAEPASVRGGAELLRGAVLLADGPVDDARESFLLAAELLAPTAPHAAARATLGAADAAWSAGDPAACLSALAPTYAPPVTPLATACVRVPRTDTPEPSVVPAGSLAGGVGGSAAKTPRRCGQPSRRAARVGATAPRAAGIPSTAPVPDGGPPSGPPQGADVTRDHRDGMRAVLLGRFDLAAHPLRRVLERGLHGTDPATLLRSAAAALMLGEVTAARRAGARALAAARTSGSAALEPRALEYLAYAELRAGRHQLARTHAEEGLRTAERAGQRNTAAHHHAVLALAASIEGEVDLVCEHAEAALHTARRHGLAQAATLAHWAAARADLGAGRPREAAARLGPLVRPGARRGHFAVWMLAVPCFVEAAASAGRPQYAAAVVEDFALWAACGADPQAAAQLLRCRALLAAPDAADELYLRALGRHDDAGDFERARTELLYGKWLRRRRRLREARTRLEEARIGFERCGAGLWAQQAAAELRAGGAAPAAATEAGELARLTPQQLRIARCVAEGATNREVAFRLSVSTRTVDYHLRNVFATLGLRSRVELVRLVEQEEKTGARL
>NZ_CP043959.1|WP_145824572.1|3757284_3758190_+|alpha/beta-hydrolase
MQQHPHTSRRRTGRLAGLTAALAAVVGLSTLTGPGAHAAADNPYERGPAPTESSIEALRGPYAVSQTSVSRLAVTGFGGGTIYYPTTTADGTFGAIAISPGFTALESSISWLGPRLASQGFVVFTIDTNTTVDQPDSRGDQLLAALDYLTQRSSVRNRVDSGRLGVMGHSMGGGGSLEAAKDRPSLQAAIPLTPWNLDKTWPELRTPTLIFGADGDSIAPVASHAEPFYSNLPSSLDRAYLELNNATHFTPNSSNTTIAKYSISWLKRFIDNDTRYEQFLCPLPRPSLTIEESRGNCPHTS
>NZ_CP043959.1|WP_150157377.1|3756334_3756529_+|hypothetical-protein
MVHPPLGSGGRRVTVRGEIVGLAYADRDVVEFLRRVGLPEGERLLDDPAWVKWVGGRAHVYDAA
>NZ_CP043959.1|WP_150155130.1|3755995_3756202_-|hypothetical-protein
MPTRRELGMHEMWCGADTSGEPVWHVLTPDKTSTLCGVEKEEESPRRDTTDRHCFSCMRSFQAVVASR
>NZ_CP043959.1|WP_150155129.1|3754270_3755932_+|hypothetical-protein
MDGYYDLGAYGRPVTTTSPAAQLWFDRGLMWTYGFNHEEAVACFRRAADADPDCAMAHWGVAYALGPNYNKPWEAFDGEELTTTVEQTHAAVERAHRAAARATPVERALVEALRARYPQAHAAEDCSVWNEPYADRMLAVYESAPGDPDVAALCADALMNLTPWQLWDLRTGLPADGARTEEAKAVLDGALATEAGAHHPGVVHLYIHLMEMSPTPEAALTVADRLRGLAPDAGHLLHMPSHLEVLCGDYRRVVSDNTAAVAADEKYLRRAGAMNFYTLYRGHNHHFRLYGAMFAGQSAVALDAAARLEAAVPEKLLRVESPPMADWLEGFLAMRFHVLIRFGRWDDILSLPFPEDPRLYCVTTAMLRYARGIALAVTGDTGRADAEREEFRAAVDRVPETRMLFNNTCHDLLAIASAMLDGELAYRKGDHDTAFAALERAVELDDSLPYDEPWGWMQPTRHAYGALLLEQGRVAEAEAVYRADLGLDDTLPRPLQHPNNVWALHGFHECLLRGGKTGEAAIVARQLRQAAALADVPVEASCFCRLETHGACH
>NZ_CP043959.1|WP_167534698.1|3753620_3754112_+|hypothetical-protein
MNGIGITLRALHDGERDLETHLLTVAERHRTEHEVHHVATDVARWSREHAARLAALGPDHGVDLPGPRDHTAPGALTALREKTAQALGRRPGTGLLLLEDLRDLHLAAVRNSLNWEMLAQAAQATRDRELLELVSDCHPQTLRQMRWTNTMIKVLSPQLLVSV
>NZ_CP043959.1|WP_150155128.1|3752017_3752839_-|SAM-dependent-methyltransferase
MHTGKQLSTEIDATVPTAARMYDYYLGGKDNYAADRSAVEELDKVVPSTRRLALNNRRFLQRVVRTLTQEYGIRQYLDHGSGLPTQDNVHQVAQRIDPTTHVVYVDNDPMVLVHGRALLEQDKRTVVIQADMRETDGIFGHAETQRLINFDEPVCVLFNSVFHCIPDSDTDGPMAVANRVRERLAPGSFMVMCQLVSEDEKVRDFVTGFMDQVTQGHWGRVRQQKDVEALFDGLEILEPGLVEVSTWRPDTEVAPRQLTQEWIEFGGVGRIPG
>NZ_CP043959.1|WP_145824578.1|3750976_3751897_+|helix-turn-helix-domain-containing-protein
MSAASHRISRLEPYLDRPEPAPTLLKMLVGVQLAGFREDAGLSQDQAARSVGFSGAKLSRIESGKGRRPPTETDVRALLDLYGTDGYEASVLLKLLQRAGEPGWWQRYDKRLMPEWFDRLVGLQEAAATIRTFEIQYVPGLLQTAAYTRAVVERGLPHAPASEVQRRVELRMRRAELLMRQDAPQLWAVIDESVLLRVLGDRAVMREQLEHLAVMADRSNVTVQIVPLNVTNASAPAIPVTYLRFGGLDLPDVVYLEHIRSANFLEDRDETEEYRIVLDRLADEALKPRESVELLRRTIRERYSAQ
>NZ_CP043959.1|WP_145824579.1|3750533_3750767_+|DUF397-domain-containing-protein
MPGVRNGVRASQLDARWIKSRHSNAEGNCVEVAPLSGGDVAMRNSRDPDGPALVYTAAEVAAFLAGAKDGEFDHLVR
>NZ_CP043959.1|WP_145824569.1|3763123_3763906_+|ATP-binding-cassette-domain-containing-protein
MPEAPPDGLPALHVENVDVTYGRALSALRSVSLTVPPGAVVALLGANGAGKTTLLRAVSGTLRLHRGAVTAGHIRYGDTVLDGKDPVAAVRAGVVQVPEGRRVFAGLSVDENLRSGGLGLGRRGRAQVQEARDRVFTLFPRLAERTHQAAGLLSGGEQQMLAIGRALMAAPRLLLLDEPSLGLAPQMVYRIAEVIREINAQGTAVLLVEQNAGMALSLASHAHVLEVGETRLSGPADELARTDAVRRLYLGESAQDQGAA
>NZ_CP043959.1|WP_150155133.1|3763902_3764706_+|ATP-binding-cassette-domain-containing-protein
MNDRTTTAPPVLAVRDVTVRFAGLTALDGVSFTVAPGSVHALIGPNGAGKSTCFNVLSGLCRPAAGSVTLGDTELTRLAPHRIAALGVARTFQNIVTTQGTVADNLMLGRHALTRAGFTASALRLPSARREQRDHLARAREIAELTGLGAHFDTPVGLLPYGDRKRVELARALCLEPRVLLLDEPVAGMNAAERARTAEVVGELRAELGLSVVLVEHDMGLVMRLADDVTVLDFGRPIAHGTPDEVRQDPEVLRAYLGTDATGEDAA
>NZ_CP043959.1|WP_145824567.1|3764702_3765599_+|branched-chain-amino-acid-ABC-transporter-permease
MTDLLDSLLGGLALGAVYALVALGFVVIFKASGVLNFAHGSLLLFGGYLVAVLHDDLGFAGALALAVLVTAALAGALDRFLLQRGGTDAHSAHVQTIVTIGIDIVLLTELARRIGGDLLTLGDPWGDAVTELGPLTVADSRLAAIVVSAVVIGGVFALFRFTDWGLSLRAAAEDMEAAALMGVRLGRVRAGAWCLAGALAALAAVFLAAFPAPGLERTTGQIALNAFPAAILGGLASPTGALAGSLIIGLTESLVIGYQSELHVLGEGFGDVAPYAVMLLVLLVRPNGLFGAKGAARV
>NZ_CP043959.1|WP_150155134.1|3765591_3766734_+|branched-chain-amino-acid-ABC-transporter-permease
MSDRLTSLLTRRRATLLTVAVLLCLPPFYLDAFWLRIGLFSMAAAIGAVGLALLSGTAGQLSLGHAFFLAVGAYGYAWLAGDPGPGLPSALAAPLAVLMAGVAGGLFSPVAGRVKGIYLGIATLALVFLGHHVLLTADSVTGGFNGRSVQPLALGGLTFDGSDELTVLGVPFGAEERLWFLGLALFAVTWFTARGLLRSRPGRALAALRDSETAAAVMGVDVARHRSAAFVVSSMYAGLAGVLLALVFRRVVPDYFSLVLSVDYLAMIVIGGLGSVAGATAGAVFVTALPLLMTRYADQLPLVAAPGTADGAVGPTEAARYLYGAAIVLVLLYAPDGLHGLARRARDRLRRRRTPTSSPDPALPTPPPPAAAARPKEHTP
>NZ_CP043959.1|WP_150155135.1|3766730_3768014_+|ABC-transporter-substrate-binding-protein
MNTTYTRRPRRRAAGAVLAGTLAVLLAATGCSSKADDGDKGGDAADGVRTGPGVDADTIRLGALTDLTGPYATLGKSIVQAQQMWADETNAKGGICDRKVEIVVKDHGYDVQKAVTAYADIAPDVVALPQVIGSPVVAALLDDIERDKMLTFPQAWAASLLGKDAVQVLGTTYDVDMIAAVEFLTRTKGLKKGDTIGHVYFEGDYGANALEGSTWAAERAGMKVAGQKIQATDTDLSAQVSALRKQGVKAVLISAGPAQTASLVGVAASRGLKVPVVSSAPGFAPQLMETPAAPALAAMLSVVSAAPAVSSDLPGVERMVASYKKKYPDSPVDSGVLSGYNAAQLIGSDLAKACEAGGLSREDVVKAHRSQTNADTGLGTPQNFSDVNRPASVETYVLKPDAKAVGGVVNAEDAHTAPGVEEYLSAR
>NZ_CP043959.1|WP_150155136.1|3768069_3768552_-|cytoplasmic-protein
MQTFLPYPDFCGSALVLDRKRLGKQRVEALQVLRGLIVPGYGWRRHPAVRMWTGYEEALVRYGLDVCRVWRDRGHQDSCAATLVADLATVRPGAPVREQRELAQAGELPPWLGDDAVHRSHRSALVRKDPDVYRELFPDEPDDLPYVWPSSDRDPEAAAG
>NZ_CP043959.1|WP_150155137.1|3768646_3769690_-|L-glyceraldehyde-3-phosphate-reductase
MNHLASPDRYDGTMRYRRTGRSGLDLPLLSLGYWHNFGDDRSFESQRAIALRAFDLGITHHDLANNYGPPYGSAEINFGRLMKRDLAPYRDEMVISTKAGWDMWPGPYGQGGGSRKYLLASLDQSLERMGLEYVDIFYSHRLDATTPLEETMGALDTAVRQGKALYVGISSYDAERSRQAAEILHDLGTPLLIHQPSYNMLNRWIETDGLLDVAQEEGFGVIGFTALAQGLLTGRYLDGVPQDSRAAAATSFDAGWLTDDMLRRLRAVNDIAARRGQTLAQMALAWALRDPRVTSLVIGASRTEQLEQNVAALENLDFTAEELAEIDTYATEGGVDLWRDARQGALG
>NZ_CP043959.1|WP_150155138.1|3769912_3770452_+|snapalysin-family-zinc-dependent-metalloprotease
MRIRTLTGAVAAVFLLYGPVVGGQAVAVRTADPAAPEGETRVLTYDTSGAGEFASAVDRGATIWNDSVDGVELRPVTSGERADIRIVVDDGWPRTMPSSMGGGTVHLGRQAVDAGHSTVRIAAHELGHVLGLPDRKPGPCSSLMSGASAGPSCTVARPNAAEQAQVEKNFDGALAGLVM
>NZ_CP043959.1|WP_150155139.1|3770656_3771979_-|triacylglycerol-lipase
MSRINSVLTTVVATTACVCASASPAAATDPVVSRGVTIPAFYSPPAELPSGNGKLIRHEPLRLGLSLPGLDGRRLPGTATRLMYTSTDANGQPVAVTGAYIEPSADWKGTGPRPLVVVGSGTMGQGDQCAPSLALENPLTLTGETLSFGYENLAVYRLLATGAAVVVTDYVGLGATDRLHTYVDRVDEGHAMLDAARVARSVPGASVTAASRVGMYGYSQGGGASASAAELQSGYAPDVPLAGTYSGAPPANLTDVTKGIDGSALAGALGWSINGFAQTSPALRAVVEANMNDAGRKALEDISTTCVGDAILGYGFTRSTKWTKNGRSVGDIIAGEPAAQAVLDDQRIGRLRPTGPVRVVTGVQDDIVPHGQARQMAVDWCKKGGDVTYKAVRLPNLGDKLLTNHLAPLLTDQGDAIEWLTDRLKGKATSSNCWTMPLQP
>NZ_CP043959.1|WP_150155140.1|3772168_3773347_-|S1-family-peptidase
MRRRTGLTHAVVAAALLIGSFTAAGTLPASAHDAPATATAGGTEAAPASPGLLRAMQRDLGLTRAEAEERLAAEREATALAPKARKAAGSAYGGSWFDAGNGKLTVAVTPDADATTVRTLRDSGAAVRTVAHTERQLDAAKSRLDQLDAPAGVASWSVDPAANSVVVNVVDGRRADNDVRAFVGKAREAGPVTVRTVRTSPSTFAAGTVGGDPYYTGNVRCSIGFSVHGGFVTAGHCGGAGQQVRGWDGSYIGNFQGSSFPGDDYAWVNVGSGWWTVPVVLGWGTVPDQLVRGSAEAPVGASICRSGSTTHWHCGRVLAKNETVNYSQGAVHQMTKTSVCAEGGDSGGSFLSGDQAQGVTSGGWGNCSSGGETWFQPVNEILNRYGLTLHTA

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Crispr_ID: NZ_CP043959_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_11

4350482-4350594

Orphan

Consensus_repeat	Method
TGAGCGGCCCGGCGGACGGCGGGGGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_11

>merge|NZ_CP043959|11|4350482-4350594|CRISPRCasFinder
TGAGCGGCCCGGCGGACGGCGGGGGCGTCGCCGGTCTCCCGCCTGAACGGCCGGACGGACGGCGGAGGCGTTGCTGATCACCAGCCTGAGCGGCCCGGCGGACGGCGGGGGCG

>NZ_CP043959|11|11|4350482-4350594|CRISPRCasFinder
TGAGCGGCCCGGCGGACGGCGGGGGCG	TCGCCGGTCTCCCGCCTGAACGGCCGGACGGACGGCGGAGGCGTTGCTGATCACCAGCC
TGAGCGGCCCGGCGGACGGCGGGGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150155535.1\|4358371_4359514_+\|polyprenyl-synthetase-family-protein	unknown	unknown	gnl\|CDD\|173833
NZ_CP043959.1\|WP_150155521.1\|4340859_4341555_+\|hemerythrin-domain-containing-protein	unknown	unknown	gnl\|CDD\|376622
NZ_CP043959.1\|WP_150155523.1\|4343496_4343964_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155525.1\|4344620_4345553_-\|Rieske-2Fe-2S-domain-containing-protein	unknown	unknown	gnl\|CDD\|239550
NZ_CP043959.1\|WP_150157428.1\|4341618_4342308_-\|phosphodiesterase	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155531.1\|4351736_4352321_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP043959.1\|WP_150155532.1\|4352330_4352810_-\|universal-stress-protein	unknown	unknown	gnl\|CDD\|366180
NZ_CP043959.1\|WP_167534707.1\|4345645_4346710_-\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239028
NZ_CP043959.1\|WP_150155536.1\|4360313_4360697_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150155524.1\|4344096_4344624_-\|DUF1360-domain-containing-protein	unknown	unknown	gnl\|CDD\|369207
NZ_CP043959.1\|WP_150155530.1\|4350600_4351662_-\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176235
NZ_CP043959.1\|WP_150155527.1\|4346754_4347606_-\|phytanoyl-CoA-dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|368580
NZ_CP043959.1\|WP_150155533.1\|4353008_4354163_-\|DUF3103-family-protein	unknown	unknown	gnl\|CDD\|371456
NZ_CP043959.1\|WP_150155522.1\|4342324_4343500_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176243
NZ_CP043959.1\|WP_150155529.1\|4348923_4350441_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|129794
NZ_CP043959.1\|WP_150155538.1\|4361318_4362221_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|377694
NZ_CP043959.1\|WP_145828249.1\|4359602_4360181_-\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_CP043959.1\|WP_150155528.1\|4347748_4348768_+\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224525
NZ_CP043959.1\|WP_150155534.1\|4356649_4358230_+\|DUF2867-domain-containing-protein	unknown	unknown	gnl\|CDD\|187556
NZ_CP043959.1\|WP_150155537.1\|4360813_4361314_+\|N-acetyltransferase	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150155535.1\|4358371_4359514_+\|polyprenyl-synthetase-family-protein	gnl\|CDD\|173833	cd00685, Trans_IPPS_HT, Trans-Isoprenyl Diphosphate Synthases, head-to-tail. These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DDXX(XX)D) located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.	1.39876e-63
NZ_CP043959.1\|WP_150155521.1\|4340859_4341555_+\|hemerythrin-domain-containing-protein	gnl\|CDD\|376622	pfam01814, Hemerythrin, Hemerythrin HHE cation binding domain. Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor hemerythrin binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial NorA is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus the iron-sulfur cluster repair protein ScdA has been noted to be important when the organism switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger.	5.96275e-10
NZ_CP043959.1\|WP_150155525.1\|4344620_4345553_-\|Rieske-2Fe-2S-domain-containing-protein	gnl\|CDD\|239550	cd03467, Rieske, Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.	4.57846e-26
NZ_CP043959.1\|WP_150155524.1\|4344096_4344624_-\|DUF1360-domain-containing-protein	gnl\|CDD\|369207	pfam07098, DUF1360, Protein of unknown function (DUF1360). This family consists of several bacterial proteins of around 115 residues in length. Members of this family are found in Bacillus species and Streptomyces coelicolor, the function of the family is unknown.	5.91702e-39
NZ_CP043959.1\|WP_150155531.1\|4351736_4352321_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	8.64319e-13
NZ_CP043959.1\|WP_150155532.1\|4352330_4352810_-\|universal-stress-protein	gnl\|CDD\|366180	pfam00582, Usp, Universal stress protein family. The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.	2.22809e-31
NZ_CP043959.1\|WP_167534707.1\|4345645_4346710_-\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|239028	cd02110, SO_family_Moco_dimer, Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). .	1.21653e-112
NZ_CP043959.1\|WP_150155530.1\|4350600_4351662_-\|zinc-binding-dehydrogenase	gnl\|CDD\|176235	cd08274, MDR9, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	1.71537e-128
NZ_CP043959.1\|WP_150155527.1\|4346754_4347606_-\|phytanoyl-CoA-dioxygenase-family-protein	gnl\|CDD\|368580	pfam05721, PhyH, Phytanoyl-CoA dioxygenase (PhyH). This family is made up of several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins, ectoine hydroxylases and a number of bacterial deoxygenases. PhyH is a peroxisomal enzyme catalyzing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD) which is an inherited neurological syndrome biochemically characterized by the accumulation of phytanic acid in plasma and tissues.	8.07803e-08
NZ_CP043959.1\|WP_150155533.1\|4353008_4354163_-\|DUF3103-family-protein	gnl\|CDD\|371456	pfam11301, DUF3103, Protein of unknown function (DUF3103). This family of proteins with unknown function appear to be restricted to Proteobacteria.	4.83447e-69
NZ_CP043959.1\|WP_150155522.1\|4342324_4343500_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176243	cd08283, FDH_like_1, Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. 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.	0
NZ_CP043959.1\|WP_150155529.1\|4348923_4350441_+\|MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.55093e-63
NZ_CP043959.1\|WP_145828249.1\|4359602_4360181_-\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	1.48909e-45
NZ_CP043959.1\|WP_150155528.1\|4347748_4348768_+\|substrate-binding-domain-containing-protein	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	3.21334e-97
NZ_CP043959.1\|WP_150155534.1\|4356649_4358230_+\|DUF2867-domain-containing-protein	gnl\|CDD\|187556	cd05245, SDR_a2, atypical (a) SDRs, subgroup 2. This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. 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.	3.92169e-150
NZ_CP043959.1\|WP_150155538.1\|4361318_4362221_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|377694	pfam06719, AraC_N, AraC-type transcriptional regulator N-terminus. This family represents the N-terminus of bacterial ARAC-type transcriptional regulators. In E. coli, these regulate the L-arabinose operon through sensing the presence of arabinose, and when the sugar is present, transmitting this information from the arabinose-binding domains to the protein's DNA-binding domains. This family might represent the N-terminal arm of the protein, which binds to the C-terminal DNA binding domains to hold them in a state where the protein prefers to loop and remain non-activating. All family members contain the pfam00165 domain.	1.16013e-55

>NZ_CP043959.1|WP_150155529.1|4348923_4350441_+|MFS-transporter
MTASASGAGDRRPGARDDDYQPDPHRWRALWVTLVAGFMSLLDVTIVAVALPTIQTDLGASPAQVQWVVSGYALTFALALVTAGRLGDALDRRKIFLIALCGFVLFSAACGAAPGITLLVVARLAQGLAAGFMAPQNSALIQQMFRGAERGRAFGYFGATVGISSASGPIVGGAILALADGMQGWRWIFYVNVPIGVLAVLLGRRLLPRTRKSGRGHVDVPGVLLLGLGVLSFMFPLVQAESGGLSRMWWLFLVGAAILAVFVRRQRRLLARGATPLLDPRLFTTVRGYAIGAGVGTLYFIGFSGVWLVFALFYQHGLHYSPLESGLAVTPFAIGSAGAAVISGRLVDRFGRLLTVWGLAGVIVGLGGTALLLRFAPLDIAPWLAAPALFVGGIGGGFVVSPNITMTLRDVPVRMAGAAGGALQTGQRLGAAVGTAALPGLFYLMLARNDDFRSSLFIALGAALTAMLTSLALAAYDWLRDRRMRQAHGECPEEVANSPVHARQT
>NZ_CP043959.1|WP_150155528.1|4347748_4348768_+|substrate-binding-domain-containing-protein
MSSSLKDVAARAGVSARTVSNVVNGSARVAPETRRRVQEAIDELGYRPNLAARSLRAGRTGIIGLAIPELHSPYFAELAGLLVDEARRRSWTVVIDQTHGDAEAERRLLTGDGGRVMDGLIISPWALPAEDITAAARPLPVVLLGERDPQGLADRVAVDNVAAADEATTHLLSLGRRRVAAIGLQPHLGNGTAELRAEGYRTALRRAGITPCPAWERPVTALHRGDGARAMAHLLDSGDAPDAVFAFSDELALGALHTAYARGLRVPEDLAVVGFDDIEDGRFGRPTLTTVSPDKRQIAARALQCLADRIYSPLNDVPAADLTVPHRLAVRGSTVASAA
>NZ_CP043959.1|WP_150155527.1|4346754_4347606_-|phytanoyl-CoA-dioxygenase-family-protein
MSPYTHPGIAPAELDADVTADVQALYEDGITARKGAFTPEWADRLREDIETAFEEARSRPGGAVGRGPHRYYVEIHPERLRGFVDLVDHPWVRSVCTAVLGPDYRIVEVGFDVPLEGAVDQPWHRDFPMPEETRAERRLTSLAFNVTAVDTEEDMGPFEIAPGTQWDDSPEFGHGMFPPRTHYPRYEERAVRKYPRRGDISARSALTIHRGTRNHSAKARPVLVLGVDGPDATNGERHDTAVTRAYWEALPERVRRHLDCPVVDVLVPVTQKHTIEGLVMGDA
>NZ_CP043959.1|WP_167534707.1|4345645_4346710_-|molybdopterin-dependent-oxidoreductase
MWGKRDDMVVHQQEPFNAEPPGGALAGARITDVDTFYSRSHGPVPRLDPTDWRLTVDGLVAHPLRLSLAELRDRFEEAGATVTLQCAGNRRAGLMTVRDIPGETPWGPGAASTARFHGVRLADVLAHAGVAPEAAHIAFHAPDVSPSADPPQPYDVSVPRERATEPDVLLAWAMNGAPLPDVHGAPLRVVVPGWIGARSVKWLTRVTARTTPSDGYFQTTAYRLPGGEAGAEGVALGPFPLNCAVLTPQDGALVAPGPVEVTGYALAGQGRTVARVEVSTDGGRAWFRAALDEPAGPGVWQQWHITLDLPSGDADVLARAWDTTGAGMPASPASLWNPKGYVNTSWPRVRLRVR
>NZ_CP043959.1|WP_150155525.1|4344620_4345553_-|Rieske-2Fe-2S-domain-containing-protein
MGQNRMLWLLDALERDPGRDKLIDALGAGVRALPLGRVRDVLHGKWLGHPLHPMSIHLPIGSWMSAAVLDLTPGRSRQADLLVAVGLAGAAPAAVTGLTDWAELHREQQRVGLVHAVANTTAVGLYGASLVLRLTGRGTAGRALGFLGLTAVGVGGLLGGHMAYRQAAGVNHAEEVPHVVSDGWHRVGGVDEFPVGEPVRRVVDDVPVLVVREAGGEVHALAERCSHLAGPLSEGTVADGCVRCPWHGSVFRLSDGWNVEGPATAPQPAFDTRVTDGHVEIRLPGDGVPDTVDGPATAGATPGTDGGRTS
>NZ_CP043959.1|WP_150155524.1|4344096_4344624_-|DUF1360-domain-containing-protein
MTRTSEGGAVSRVKGVLRRVEHTYAEDGGRPIRGYLVAMSAFAAYTTGWALVVRRRGRPAPWDVALTAVATFRLSRLLSKGSVTSPLRAPFTTFVGPQGPAELHEEARSDDHRATVGELVTCPFCVSVWVASSLTAGQLLWPRATRTAMGAVTALAGADALQLTYGALVDRTTGD
>NZ_CP043959.1|WP_150155523.1|4343496_4343964_-|hypothetical-protein
MKRALWMVPVAAVGVAAARKAGAAARGGDDRAGDRWLTVTVNRPTEDVRQDGKLPDALERLSDRIDVRLRPAPGDRGTELAARLKEPTPPAPVSLPARLAGQDPRQEVRLALREAKAVLETGEVMLPDTPPTIRPTPGGRLVGLFGRRSGGEGVL
>NZ_CP043959.1|WP_150155522.1|4342324_4343500_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MKALCWEGVNKLSVEQVPDPELRNDQDIVVRLIAGTTCGSDLHLIGGYIPAMRAGDVIGHEFVGEVVETGSAVRKHKVGDRVVVCSFIGCGRCWYCANDLWSLCDNSNTNPGIGQALFGYETAGIFGYSHAMGGLRGSHAEYVRVPFADYGAFTVPEGIDDTSVLFLSDSVPTGWMGADLAGVKPGDVVAVWGCGAVGQMAARAAILLGAERVISIDRIPERLEMTERYVGAETIDYTTTDVAAELRERTGGRGPDVCIEAVGMEAHSDGPMHLYDQAKQQLRLQTDRPTAVRQAIHACRKAGTVFILGVFAGVVDKFPLGAVINKGLTVRGAQMHGQRYIPMLLDRLAAGEISTAHLATHSLSLDDAPTAYDMFKHKTDGCVRAVIRPGT
>NZ_CP043959.1|WP_150157428.1|4341618_4342308_-|phosphodiesterase
MHDTAHRAAERVARWRGAPAVHSTGVLCSGTLHVSGRGDAVWGVPWLDRHASYPATVRWSRALGTPRRLPDALGLAVRVEDAGGPGRPLDLLFTSSGAGRLGRHLPLLRPDALTGAYSTLLAYRTGGCERVLAAFPVHGPPHTPQPTLWRELARRPVRFRLCAAAPGEPWRPFASLILDAVYAAPGETTLSYDPNAHSLPGLHPAGRLNRLRDAAYAGSREGRGAEPPG
>NZ_CP043959.1|WP_150155521.1|4340859_4341555_+|hemerythrin-domain-containing-protein
MTVGAASFSLQDADSLGGDESILMRQRRDHARLDAMISRCQSEDLPADELDALWLDIVQLVFSHAFAEETVLWPLLRRVAPDGEALTRQVEEEHQEINELIARIERSPDDPRRAEWLQQAFALVRQDIRDEEDELLPHLRVAFDDRKLRRIGAAWEAVRATAPTRPHPGVPRRPPGNALRGVPLSVFDRLRDLAPGSGPAARRASLVAAGAVAAAGGAVVLAVRFARRTRS
>NZ_CP043959.1|WP_150155530.1|4350600_4351662_-|zinc-binding-dehydrogenase
MSEYMRAVRITRHGGPEVLEAAQVPVPVPRAGEALVRVTSVALNNTDLWTREGAYGRPGDPEARSGWRGPVDFPRVQGADVAGRVAAVGSGGDEGLVGRRVVVDPAVYDGDGPDAHPVGLMGSERDGGYAEYVTAPLDQLHDVTGSPLTDDQLASLPTAYGTALGMIERGRMREGETVLVSGASGGVGLALVQIARARGAQVVAVSSGTKIDAVREAGAHAVVDRAGDVIGQIRAAAPQGIDVGLDVVAGDLVSEGVPLLREGGRWVIAGALGGYGVHLDVRRLYLHNAQVIGSAMHTRAHFGLLMEMARQAAVEPVVAAAYPLDQAARAQEELARRNHVGKIVLHPGAACGR
>NZ_CP043959.1|WP_150155531.1|4351736_4352321_+|TetR-family-transcriptional-regulator
MDHGTDTPPLTPAGRRIVAAAEELFYERGITAVGVDLIAEHSGVTKRTLYNRFGSKENLVAAYLTERDRRWRSAVRAAVEVSGSEEEAVTAPFETLRAWSATDTRGCAFINALAELPDPEHPAHRVATDQKRWLLRLFEELADAAGCPDPATLAARLLVLHEGALATRPLGLGTLTTATDLARDLVRAAVRARD
>NZ_CP043959.1|WP_150155532.1|4352330_4352810_-|universal-stress-protein
MDDQHGAADRVVVGVDGSPSSRQALRWAVRQATLTGGTVRALTAWDYPQYHGALGWLPPSSGDEDALEARAREDLTRCVEETLGARPPAEVRTEVQYGTPASVLLRAARDASLLVVGSRGLGGFAGLLLGSVAQHCAQHAACPVVVVREDTATGIGDAD
>NZ_CP043959.1|WP_150155533.1|4353008_4354163_-|DUF3103-family-protein
MRPRHLRRRGALAVAATTLAVLCAGQSLGAPQAAAAPATAVPAPASPASEVHAAEDLAARAIAGALSDPVWNTRVRRAALASDEVAVTALADGTLRSTLAAADRRIAAAKGLDAGVGPLLRLRLGDPSMRGALTAGTPPWVAAATSDDGPVTAYDSEGRIHTLDAREAPAHPVYVVDLDGSRALAAGLDVLNEELARRGVRSTAPTARRTPLRDASATAAAAGFWTTRVAAVSLSDDQEPWIKGDAEIYTLVTGFGHDGKVRVDPVDMPYLDSDGVVYRPQQILVNWSSYKYDLADAVMMEDDGGTNYRDLAKAIAAVLLTVTDQGAYIPLVNAVLDAVPDDWWTDDPDYVDSWYTLARTDNGTRHGARGNGWMTLEPYFVQEL
>NZ_CP043959.1|WP_150155534.1|4356649_4358230_+|DUF2867-domain-containing-protein
MTVDRHGQGGSSAGAHCLVTGASGYIGGRLVPDLLETGHRVRCLARSPDKLRDHPWAPDVETVRGDVTDAASVAAAMDGVDVAYYLVHALGTGGDFEETDRRAARTFAEQAHAAGVRRIVYLGGLTPQGVPEHTLSPHLRSRAEVGRIFLDSPVPATVLRAAVVIGSGSASFEMLRYLTERLPVMVTPSWVHTRTQPVAVRDVLRYLVASATMPADVDRAFDIGGPDVLTYRDMMRRYAAVAGLRRRVIVPVPVLTPRLSSHWVGLVTPVPAGIARPLTESLRHEVVCREHDIAAYVPDAPGRPLPFDEALELALRRVREAQVATRWSSAAVPGAPSDPLPTDPDWAGGSLYRDERHRAVSASPEALWKVIEGIGGENGWYSFPLAWAVRGWLDRIVGGVGLRRGRRDPQRLRAGDSLDFWRVEEIEPGRLLRLRAEMRLPGLAWLEMRVETDGAGRTAYRQRALFHPRGLLGHAYWWSVSPFHAVVFGGMARNITRAAAGGNAPGGATGAGRVRRTRRRRAGVPN
>NZ_CP043959.1|WP_150155535.1|4358371_4359514_+|polyprenyl-synthetase-family-protein
MRELRSATEEPAERAGGPLTADAATRAVVRILGEVLDARMSEAYDVDAVFAREVAGRVSAFARRGGKRLRTAFAWCGWRAGGGSGDPVPLLRTGAALELVQTCALVHDDVMDGSHLRRGAPAVHVDLARLHRAEDMAGSAETFGHSAAVLAGDLALAWADDLMTDIVLDSPHGPRVYREWRAMRGEMVAGQYRDLQAQAAGASGVDEALTIATLKSALYTVERPLALGASLAGADEPVMTALRAAGRCTGLAFQLRDDLLGAFGDPALTGKPVGDDLRARKLTYLLAVALELGRANGDEEAVALLSPGSATLPDRAVEGVRAALERTGARDEVESKIAELADSALRHFDETGAPPAVRREFAALVARASGITTGCVREAV
>NZ_CP043959.1|WP_145828249.1|4359602_4360181_-|DNA-starvation/stationary-phase-protection-protein
MPSQPSDPSYTVPGLRTQDSGRIIELLQMRLHSLNDLHLTLKHIHWNVVGPHFIAVHEMIDPQVDKVRDMTDDLAERISTLGGEPNGTPGALVHARTWNDYSIGRAEAMEHLGALDLVYTSVIEDHREAMRETEEADPVTQDMLIEQLRGLELFQWFVRAHLESGGGRLSTRGATTETGAAGQAAEQARHQP
>NZ_CP043959.1|WP_150155536.1|4360313_4360697_-|hypothetical-protein
MGLMLFPGDSDLTSPDVARSYGGFTMFRRWSARAEGCELDEMDGFGGERPWGDVPTTLEPLLDHPDDAGPDFPPSRCAAMLPRLQEIAAQEHDGSGGPDVARHLDDVRRLVVVLRLCVERDVECVFG
>NZ_CP043959.1|WP_150155537.1|4360813_4361314_+|N-acetyltransferase
MSWLPRDFVHPLHVGIPDGGGHRLRPISGADAPLDYPTVMGSRERLFSIFGPAWGWPSATMSYEANLADLERHAAEIEAHESFNYTVENAERTALKGCVYIDPPEKEGADAEISWWVVDEEVGGALERALDAFVPRWIAEDWPFRRPRFIGRDLTWDEWMKLPDIG
>NZ_CP043959.1|WP_150155538.1|4361318_4362221_-|helix-turn-helix-domain-containing-protein
MGLDELRTLLERHARPDATTAIDGVLASRIDRQDPPGPSMSGTVLAVIAQGAKRLALGERVYEYGPGQYLVASVDLPVTGQFLQVDAEHPALGFGLVLEPSAIAELLLQAGPGDLPRAGGVPSAIAVSDAPAALLDAIVRLLRLLDEPRDRAVLAPLLKREILWRLMTGEQGATVRHLGLTDSGLSHVSRAVRWIREHYAQAFRVEDVARMTGMSVSAFHRNFQAVTAMSPIQFQKQIRLQEARLLLATRPGDVTAVGRRVGYDNPSQFSREYRRQFGAPPSRDAARLRDTGGVPAAVAP

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Crispr_ID: NZ_CP043959_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_12

5022105-5022229

Orphan

Consensus_repeat	Method
CTGGAGCTGACCGGCAAGGAGCTGCGTTCGTGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_12

>merge|NZ_CP043959|12|5022105-5022229|CRISPRCasFinder
CTGGAGCTGACCGGCAAGGAGCTGCGTTCGTGATCACGCATCACACCGGGACCGGCCGGGGGTCCGGGGGTTGTCCCCCGGGAAGGCACAGCCTGGAGCTGACCGGCAAGGAGCTGCGCTCGTGA

>NZ_CP043959|12|12|5022105-5022229|CRISPRCasFinder
CTGGAGCTGACCGGCAAGGAGCTGCGTTCGTGA	TCACGCATCACACCGGGACCGGCCGGGGGTCCGGGGGTTGTCCCCCGGGAAGGCACAGC
CTGGAGCTGACCGGCAAGGAGCTGCGCTCGTGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_145825158.1\|5023002_5024079_+\|heme-A-synthase	unknown	unknown	gnl\|CDD\|224528
NZ_CP043959.1\|WP_150156000.1\|5027778_5029866_+\|transketolase	unknown	unknown	gnl\|CDD\|223100
NZ_CP043959.1\|WP_150156002.1\|5032542_5033595_+\|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA	unknown	unknown	gnl\|CDD\|213538
NZ_CP043959.1\|WP_150155994.1\|5020209_5020923_-\|ArsR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225222
NZ_CP043959.1\|WP_024887259.1\|5017213_5017531_-\|non-heme-iron-oxygenase-ferredoxin-subunit	unknown	unknown	gnl\|CDD\|239604
NZ_CP043959.1\|WP_150155997.1\|5024036_5024774_-\|nucleotidyltransferase	unknown	unknown	gnl\|CDD\|379178
NZ_CP043959.1\|WP_004989638.1\|5014362_5014695_-\|metal-sulfur-cluster-assembly-factor	unknown	unknown	gnl\|CDD\|225062
NZ_CP043959.1\|WP_150155990.1\|5013391_5013934_-\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225767
NZ_CP043959.1\|WP_150155991.1\|5013933_5014254_-\|multidrug-efflux-SMR-transporter	unknown	unknown	gnl\|CDD\|224987
NZ_CP043959.1\|WP_150155993.1\|5017527_5018712_-\|Fe-S-cluster-assembly-protein-SufD	unknown	unknown	gnl\|CDD\|223791
NZ_CP043959.1\|WP_145825150.1\|5015167_5016424_-\|SufS-family-cysteine-desulfurase	unknown	unknown	gnl\|CDD\|131034
NZ_CP043959.1\|WP_150155998.1\|5024855_5025962_-\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|368185
NZ_CP043959.1\|WP_145825154.1\|5018791_5020213_-\|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl\|CDD\|131035
NZ_CP043959.1\|WP_150156001.1\|5029900_5031019_+\|transaldolase	unknown	unknown	gnl\|CDD\|235117
NZ_CP043959.1\|WP_145825168.1\|5034489_5035329_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223472
NZ_CP043959.1\|WP_150155992.1\|5016420_5017206_-\|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl\|CDD\|223473
NZ_CP043959.1\|WP_167534588.1\|5026472_5027426_-\|protoheme-IX-farnesyltransferase	unknown	unknown	gnl\|CDD\|235293
NZ_CP043959.1\|WP_093546387.1\|5014691_5015156_-\|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	unknown	unknown	gnl\|CDD\|273918
NZ_CP043959.1\|WP_167534587.1\|5026046_5026379_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156003.1\|5033591_5034377_+\|6-phosphogluconolactonase	unknown	unknown	gnl\|CDD\|273494

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_145825158.1\|5023002_5024079_+\|heme-A-synthase	gnl\|CDD\|224528	COG1612, CtaA, Uncharacterized protein required for cytochrome oxidase assembly [Posttranslational modification, protein turnover, chaperones].	4.55563e-31
NZ_CP043959.1\|WP_150156000.1\|5027778_5029866_+\|transketolase	gnl\|CDD\|223100	COG0021, TktA, Transketolase [Carbohydrate transport and metabolism].	0
NZ_CP043959.1\|WP_150156002.1\|5032542_5033595_+\|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA	gnl\|CDD\|213538	TIGR00534, Putative_OxPP_cycle_protein_OpcA, glucose-6-phosphate dehydrogenase assembly protein OpcA. The opcA gene is found immediately downstream of zwf, the glucose-6-phosphate dehydrogenase (G6PDH) gene, in a number of species, including Mycobacterium tuberculosis, Streptomyces coelicolor, Nostoc punctiforme, and Synechococcus sp. PCC 7942. In the latter, disruption of opcA was shown to block assembly of G6PDH into active oligomeric forms. [Protein fate, Protein folding and stabilization].	6.21585e-95
NZ_CP043959.1\|WP_150155994.1\|5020209_5020923_-\|ArsR-family-transcriptional-regulator	gnl\|CDD\|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	4.01794e-52
NZ_CP043959.1\|WP_024887259.1\|5017213_5017531_-\|non-heme-iron-oxygenase-ferredoxin-subunit	gnl\|CDD\|239604	cd03528, Rieske_RO_ferredoxin, Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.	1.40775e-49
NZ_CP043959.1\|WP_150155997.1\|5024036_5024774_-\|nucleotidyltransferase	gnl\|CDD\|379178	pfam13427, DUF4111, Domain of unknown function (DUF4111). Although the exact function of this domain is not known it frequently appears downstream of the family Nucleotidyltransferase, pfam01909. It is also found in species associated with methicillin-resistant bacteria.	0.00219045
NZ_CP043959.1\|WP_004989638.1\|5014362_5014695_-\|metal-sulfur-cluster-assembly-factor	gnl\|CDD\|225062	COG2151, PaaD, Predicted metal-sulfur cluster biosynthetic enzyme [General function prediction only].	1.08025e-31
NZ_CP043959.1\|WP_150155990.1\|5013391_5013934_-\|TetR-family-transcriptional-regulator	gnl\|CDD\|225767	COG3226, COG3226, Uncharacterized protein conserved in bacteria [Function unknown].	5.44033e-30
NZ_CP043959.1\|WP_150155991.1\|5013933_5014254_-\|multidrug-efflux-SMR-transporter	gnl\|CDD\|224987	COG2076, EmrE, Membrane transporters of cations and cationic drugs [Inorganic ion transport and metabolism].	3.5521e-29
NZ_CP043959.1\|WP_150155993.1\|5017527_5018712_-\|Fe-S-cluster-assembly-protein-SufD	gnl\|CDD\|223791	COG0719, SufB, Cysteine desulfurase activator SufB [Posttranslational modification, protein turnover, chaperones].	4.8784e-90
NZ_CP043959.1\|WP_145825150.1\|5015167_5016424_-\|SufS-family-cysteine-desulfurase	gnl\|CDD\|131034	TIGR01979, Probable_cysteine_desulfurase, cysteine desulfurases, SufSfamily. This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP043959.1\|WP_150155998.1\|5024855_5025962_-\|amidohydrolase-family-protein	gnl\|CDD\|368185	pfam04909, Amidohydro_2, Amidohydrolase. These proteins are amidohydrolases that are related to pfam01979.	3.41963e-08
NZ_CP043959.1\|WP_145825154.1\|5018791_5020213_-\|Fe-S-cluster-assembly-protein-SufB	gnl\|CDD\|131035	TIGR01980, UPF0051_protein_slr0074, FeS assembly protein SufB. This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP043959.1\|WP_150156001.1\|5029900_5031019_+\|transaldolase	gnl\|CDD\|235117	PRK03343, PRK03343, transaldolase; Validated.	0
NZ_CP043959.1\|WP_145825168.1\|5034489_5035329_-\|ABC-transporter-permease-subunit	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	2.08789e-76
NZ_CP043959.1\|WP_150155992.1\|5016420_5017206_-\|Fe-S-cluster-assembly-ATPase-SufC	gnl\|CDD\|223473	COG0396, sufC, Cysteine desulfurase activator ATPase [Posttranslational modification, protein turnover, chaperones].	7.40177e-145
NZ_CP043959.1\|WP_167534588.1\|5026472_5027426_-\|protoheme-IX-farnesyltransferase	gnl\|CDD\|235293	PRK04375, PRK04375, protoheme IX farnesyltransferase; Provisional.	7.89712e-147
NZ_CP043959.1\|WP_093546387.1\|5014691_5015156_-\|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	gnl\|CDD\|273918	TIGR01994, Iron-sulfur_cluster_assembly_scaffold_protein_IscU, SUF system FeS assembly protein, NifU family. Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	8.58371e-61
NZ_CP043959.1\|WP_150156003.1\|5033591_5034377_+\|6-phosphogluconolactonase	gnl\|CDD\|273494	TIGR01198, 6-phosphogluconolactonase_6PGL., 6-phosphogluconolactonase. This enzyme of the pentose phosphate pathway is often found as a part of a multifunctional protein with [Energy metabolism, Pentose phosphate pathway].	9.24827e-84

>NZ_CP043959.1|WP_150155994.1|5020209_5020923_-|ArsR-family-transcriptional-regulator
MKNVGEASHEELATGERSTRNRVARSILDHGPSTVAELAERLKLTQAAVRRHLDALAADNVVEARDRRVYGARSRGRPAKAFALTDCGRDAFDQSYDKLAVDALRWIAEREGGGEAIAAFARARIAGQAGAYRKAVEGVPPEKRTEALAKALSADGYAATARSAPVGEQLCQHHCPVAHVAEQFPQLCEAETEFFAELLGTHVQRLATIAHGDGVCTTFIPKISHNASASTSGRNPA
>NZ_CP043959.1|WP_145825154.1|5018791_5020213_-|Fe-S-cluster-assembly-protein-SufB
MTLPTETAHPELEGLGNYEYGWADRDEAGASARRGLNEEVVRDISGKKNEPEWMTKLRLKGLRLFEKKPMPNWGSDLSGIDFDNIKYFVRSTEKQAESWEDLPEDIKNTYDKLGIPEAEKKRLVAGVAAQYESEVVYHQIREDLEEQGVIFLDTDTALKEHPELFKEYFGTVIPVGDNKFASLNSAVWSGGSFIYVPPGVHVEIPLQAYFRINTENMGQFERTLIIVDEGAYVHYVEGCTAPIYKSDSLHSAVVEIIVKKNARCRYTTIQNWSNNVYNLVTKRAVAYEGATMEWVDGNIGSKVTMKYPAVYLMGEHAKGETLSIAFAGEGQHQDAGAKMVHMAPNTSSNIVSKSVARGGGRTSYRGLIEIGEGAPGAKSNVLCDALLVDTISRSDTYPYVDVREDDVSMGHEATVSKVSEDQLFYLMSRGLSEFEAMAMIVRGFVEPIAKELPMEYALELNRLIELQMEGAVG
>NZ_CP043959.1|WP_150155993.1|5017527_5018712_-|Fe-S-cluster-assembly-protein-SufD
MAEAQNIPVGSTTAGSIAVAAESTVATRMSAPPSFDVADFPVPHGREEEWRFTPLERLRGLHDGTATATDEGVKIAVEAPEGVTVETVGRDDARLGRTGAPADRVAAQAYSAFTRASVVTVPKETVLTEPIRIAVHGDGGTAYGHQVIELGAFAEALVVIDHTGDAVLAANVEYVLGDGAKLTVVSVQDWDDKAVHVAQHNALVGRDASFKSVVVTFGGDVVRLHPRVIYAGPGGEAELFGLYFTDAGQHQEHRLLVDHNVPHCKSNVVYKGALQGEEAHAVWIGDVLIEAKAEGTDTYEMNRNLVLTDGARVDSVPNLEIETGEIVGAGHASATGRFDDEQLFYLMARGIPEKDARRLVVRGFFAELVQQIGVPDIEERLIAKIEEELEAAVA
>NZ_CP043959.1|WP_024887259.1|5017213_5017531_-|non-heme-iron-oxygenase-ferredoxin-subunit
MTFVRVCGLGELEEDTPKRVELDGTPVSVVRTEGEVFAINDICSHANVSLSEGEVDDCHIECWLHGSRFDLRSGKPDALPATRPVPVYPVKIEGDDVLVSLTQES
>NZ_CP043959.1|WP_150155992.1|5016420_5017206_-|Fe-S-cluster-assembly-ATPase-SufC
MATLEIRDLHVTVEADNATKEILKGVDLTVKQGETHAIMGPNGSGKSTLAYSLAGHPKYTITGGTVTLDGEDVLEMSVDERARAGLFLAMQYPVEVPGVSVSNFLRTSATAIRGEAPKLRTWVKEVREAMERLNMDPAFAERNVNEGFSGGEKKRHEILQLELLKPKVAILDETDSGLDVDALRVVSEGVNRVRESGQVGTLLITHYTRILRYIKPDHVHVFAAGRIAESGGPELADKLEAEGYEAYAKHDGVDTKGGASE
>NZ_CP043959.1|WP_145825150.1|5015167_5016424_-|SufS-family-cysteine-desulfurase
MTQLPGLLDTEAIRKDFPILDRQVHDGRKLVYLDNAATSQKPRQVLDALGEYYERYNANVHRGVHVLAEEATALYEGARDKVAEFVNAPSRDEVIFTKNASESLNLVANMLGWADEPYRVDHETEIVITEMEHHSNIVPWQLLAQRTGAKLKWFGLTDDGRLDLSNIDEIITEKTKIVSFVLVSNILGTVNPVEAIVRRAQEVGALVCIDASQAAPHMPLDVQALQADFVAFTGHKMCGPTGIGVLWGRQELLEDLPPFLGGGEMIETVSMSSSTYAPAPHKFEAGTPPIAQAVGLGAAIDYLSAIGMDKILAHEHAITEYAVKRLLEVPDLRIIGPSTAEDRGAAISFTLGDIHPHDVGQVLDEQGIAVRVGHHCARPVCLRYGIPATTRASFYLYSTPADIDALVDGLEHVRNFFG
>NZ_CP043959.1|WP_093546387.1|5014691_5015156_-|SUF-system-NifU-family-Fe-S-cluster-assembly-protein
MKLDSMYQDVILDHYKNPHGRGLRDGDAEVHHVNPTCGDEITLRVKYDGTTISDVSYEGQGCSISQASASVLNDLLVGKDLAEAQKIQGTFLELMQSKGKIEPDDAMEEVLEDAVAFAGVSKYPARVKCALLSWMAWKDATAQALGADAERTTA
>NZ_CP043959.1|WP_004989638.1|5014362_5014695_-|metal-sulfur-cluster-assembly-factor
MSETVEMKPASEEELREALMDVVDPELGIDVVNLGLIYGIHVDDSNVATVDMTLTSAACPLTDVIEDQAKSATDGLVSELRINWVWMPPWGPDKITDDGREQLRALGFNV
>NZ_CP043959.1|WP_150155991.1|5013933_5014254_-|multidrug-efflux-SMR-transporter
MGYLLLAGAIAAEVCATTAMKYSDGFSRLWPSLLTVLGYVVSFALLAQTLRTVAVGTAYAIWAGVGTAAIATIGMVFLGEGMTVAKAAGIALIIIGVVVLNLGGAH
>NZ_CP043959.1|WP_150155990.1|5013391_5013934_-|TetR-family-transcriptional-regulator
MARRHDPERRQRIIDAAIRVVGRSGIAGLTHRTVAREADVPLGSTTYHFHTLDELMVAALRQANEGFAKVIASRGGLEDPRTDLADELAGLMGEWLGGERTGVELEYELYLAALRRPALRPVAAEWCEDVAALLSRRTDPVTARALVALMDGICLQVLLTGTPYDEAYAREVLGRLLPPS
>NZ_CP043959.1|WP_145825158.1|5023002_5024079_+|heme-A-synthase
MPGTDPRESVHKRRPTMGRVPNVTRADAQAALRNPLAFIAARWTPDPRTVRRAALTALVMSVVIVVTGGAVRLTGSGLGCPTWPKCTDDSLTTTSEMGLHGVIEFGNRLLTYVLCAAVGWAIIAARSQKPYRRSLTRLGWTQFWVVMGNAVLGGIVVLVGLNPYTVAAHFLLSSALIAVATVMWQRTREGDTEPRPLVGKAVQQLVWFLVGASVLLIAAGTVVTGAGPHAGDSSEVPRMPLDWETVSKLHAVLAWIVVTLTFALWFVLKAVDAPRGPLARTRELFLVLLAQGLIGYVQYFTDLPEVLVGLHMFGSCVMWIWVLRVLLSLRERPEETAPAATPVPAQEPATSPSIAGPR
>NZ_CP043959.1|WP_150155997.1|5024036_5024774_-|nucleotidyltransferase
MQQTDALLDRFLTGLAPLSPVAVWAHGSLAGGDYVEGRSDLDLIAVLPPPIGPRTVWRLAVLHARLRAEPLAAGLHCTYLTPDTTEGAERRHLTWAHERLFRRTVTPVTRTELHTFGRVLYGAPPVDVLPPVPDGELAAYVLRDQRDYWRPHVDRSDLWTRDIWVDLGMVTFARVTVTVREGRLISKREALEVLPALGAPEEVVADIRARRYGGTVATDEKWIQRRAELVRGYLGPAIDGLVAGS
>NZ_CP043959.1|WP_150155998.1|5024855_5025962_-|amidohydrolase-family-protein
MIDPPSLVDQYCHGVLRTELGLGTFEAQLARTEGPPAPGTTLFDTQTGFAVRRWCPPLLGLEPHCPPSRYLARRRELGSVEAGRRLLRGSGITAYLVDTGLSDDLTDPAELGRAGEAEAHEIVRLEQLAEQVADTSGTVESFLANLAESVHAAAAHAVAFTSVAGLRHGLALSPEPPQAGEVRGAAGRWLAARGAGGRLSDPVLLRHLLWIAVASGLPLQLHAGLGAPGARVDRTDPVLLTDFVRATAGLGTDLVLLHGYPYHRHAAHLAGVFPHVYADCGAALVRTGARAATVLAEVLELAPFGKILFSSGARGLPELHVVGAHLFREALGRILGTWVAEGAWSLDDARRVAAMIASGNASRVYGLD
>NZ_CP043959.1|WP_167534587.1|5026046_5026379_-|hypothetical-protein
MADTQQVDPKDGQKAARLAKRIGGFAKEHGGAEGQVAYLGQRGARIVLVGEDGAWGDVFAPSMEIARQAVEKAGITVHEEFDGEFAAKVRTGPYEWSRMAGIQVGGPSND
>NZ_CP043959.1|WP_167534588.1|5026472_5027426_-|protoheme-IX-farnesyltransferase
MCVTAVESRPAGVLGTSQSPAHRPFGARVMAFVALTKPRIIELLLITTVPVMFLAQQGVPDLTLVLLTCVGGYLSAGGANALNMYIDRDIDALMDRTSQRPLVTGMVSPREALVFGITLAVASTLMFGLTVNWLSAWLSLGALLFYVVVYTMILKRRTAQNIVWGGIAGCMPVLIGWSAVTNSMSWAPVVLFLVIFFWTPPHYWPLSMKVKEDYARVGVPMLPVVAGNKAVARQIVLYSWVMVGVSLLLTPMGYTGWFYTAVALAAGGWWLWEAHALLNRAKAEVTGAKLKEMRLFHWSITYVSLVFVAIAVDPFLR
>NZ_CP043959.1|WP_150156000.1|5027778_5029866_+|transketolase
MSTKPTTTDLEWTELDQRAVDTARVLAADAVQKVGNGHPGTAMSLAPAAYTLFQKVMRHDPADADWVGRDRFVLSAGHSSLTLYTQLYLAGFGLELDDLKSFRTWGSRTPGHPEYGHTTGVETTTGPLGQGVANAVGMAMAARYERGLFDPEAPAGESPFDHFVYCIAGDGCLQEGISAEASSLAGHQKLGNLVLLWDDNHISIEGDTETAVSEDTVKRYEAYGWHVQRVAPKPDGDLDPNAIYDAIQEAKKVTDRPSFIAMRSIIAWPAPNAQNTEAAHGSALGDDEVAATKRVLGFDPEKSFEVSDEVIGHTRKALERGQAARAVWEKSFQQWRDNNPERAAEYDRIAAGELPKGWQDALPVFEPGKGVATRAASGKVLQALGAVIPELWGGSADLAGSNNTTIDKTSSFLPAGNPLPEADPYGRTIHFGIREHAMAAEMNGIALHGNTRIYAGTFLVFSDYMRNAVRLSALMHLPVTYVWTHDSIGLGEDGPTHQPVEHLAALRAIPGLNVVRPADANETAIAWREILRRWTKEFGKGAPHGLALTRQGVPTYEPNEDAARGGYVLFEAEGGEPEVVLIATGSEVHVAVEARERLQADGVPTRVVSMPSVEWFEEQDQGYRDRVLPPSVKARVAVEAGIGLTWHRFVGDAGRIVSLEHFGASADGKVLFQEYGFTAENVAAVARESIAAARR
>NZ_CP043959.1|WP_150156001.1|5029900_5031019_+|transaldolase
MTDALKRLSDEGVAIWLDDLSRKRITSGNLAELIDQQHVVGVTTNPTIFQKAISEGDGYDTQLTDLAARKVTVEEAVRMITTADVRDAADILRPVFDATDGQDGRVSIEVDPRLAHDTRATVAEAKQLAWLVDRPNTLIKIPATEAGIPAIAEVIGLGISVNVTLIFSLERYRKVMDAFLTGLEKAKARGLDLSKIHSVASFFVSRVDTEIDKRIDALGTDEAKALRGKAAIANARLAYQAYEEVFSTDRWAALEREGANKQRPLWASTGVKDKAYKATMYVDELVAPNTVNTMPEATLFATEEKGEIRGNAVAGTYEQARADLDAVEALGIAYDEVVRLLEDEGVDKFEASWNDLLKSTEAELQRLAPSEG
>NZ_CP043959.1|WP_150156002.1|5032542_5033595_+|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA
MKTDLTDTTASKINKALVKARRAIGTPAVGMVLTLVIVTDEENAYDALKAAGDASREHPSRTLVVIKRVSRSPRDRTQSRLDAEVRVGADAGTGETVVLRLHGEVVDHAQSVVLPLLLPDAPVVVWWPVNAPLDPANDPLGALAQRRVTDTYACEQPVKELAARADAYTPGDTDLSWTRITPWRSMLAAALDQVACEVQGVEVEGEEFNPSCELLAMWLADRLDVPVRRTRSAGPGLTAVRMDTDCGPIVLDRADGSLATLAIQGQPRRAVALKRRDTAELIAEELRRLDPDDTYASALRYGVERLKQGNGGDAPAKGERQAVPAPVESVAKGPAAEATAEAPVKRAAVK
>NZ_CP043959.1|WP_150156003.1|5033591_5034377_+|6-phosphogluconolactonase
MSTAPQLVVHRDKELMAQAAAARLITRIVDAQASRGEASVVLTGGRNGNGLLAALAAAPARDAIDWPRLDLWWGDERFLPEGDPDRNVTQAREALLDAVPLDPKRVHAMPASDGPHGSDVEAAADAYARELAAAAGPEDHGAVPAFDVLMLGVGPDTHVASLFPELPAVRETERTVVGVHGAPKPPPTRVTLTLPAIRAAREVWLLAAGEDKAEAAAIALSGAGEIQAPAAGAHGRARTLWLLDAPAASQLPRTLYPPATA
>NZ_CP043959.1|WP_145825168.1|5034489_5035329_-|ABC-transporter-permease-subunit
MNAIRRGLSSAVVQAFLVVIGLVWITPLAGLFLSSLRSAEDTAKGGWWTVLTSPGQLSFDNYSALLENSGMTQAFWNTVLISVPTTVLVVVVAALAGYAFAWLEFPGRDAVFLGVVALLVVPVQIGLLPVAKLFGQLGLFGTIPGVVLFHVAYGLPFAVFLLRNYFAEMPKEMLEAARMDGGSEWRIFTRLVLPVGRPAIASLAIFQFLWVWNDMLVALLFADSSSQPLTVELQSQIRQFGSNVDVLAPGAFLSLVVPVVVFFAFQRHFVQGVMAGSVK

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Crispr_ID: NZ_CP043959_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_13

5094747-5094884

Orphan

Consensus_repeat	Method
TCGTGAGGGCTGGTCGCGCAGTTCCCCGCGCCCCTTCAGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_13

>merge|NZ_CP043959|13|5094747-5094884|CRISPRCasFinder
TCGTGAGGGCTGGTCGCGCAGTTCCCCGCGCCCCTTCAGGGGGGCTCCGGCCACGGCGAAGGGGCGGTCACCGTCGACGCGCGACCGGCCCGGAACTCGTGAGGGCTGGTCGCGCAGTTCCCCGCGCCCCTTCAGGGG

>NZ_CP043959|13|13|5094747-5094884|CRISPRCasFinder
TCGTGAGGGCTGGTCGCGCAGTTCCCCGCGCCCCTTCAGGGG	GGCTCCGGCCACGGCGAAGGGGCGGTCACCGTCGACGCGCGACCGGCCCGGAAC
TCGTGAGGGCTGGTCGCGCAGTTCCCCGCGCCCCTTCAGGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150156040.1\|5089914_5090592_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|340413
NZ_CP043959.1\|WP_150156049.1\|5102275_5102989_-\|uracil-DNA-glycosylase	unknown	unknown	gnl\|CDD\|381681
NZ_CP043959.1\|WP_150156039.1\|5088830_5089691_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|238045
NZ_CP043959.1\|WP_150156051.1\|5103813_5104512_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_CP043959.1\|WP_145825214.1\|5098181_5099699_+\|glycerol-kinase-GlpK	unknown	unknown	gnl\|CDD\|234594
NZ_CP043959.1\|WP_145825213.1\|5097240_5098143_+\|MIP-family-channel-protein	unknown	unknown	gnl\|CDD\|240230
NZ_CP043959.1\|WP_150156043.1\|5091411_5092101_-\|DUF899-family-protein	unknown	unknown	gnl\|CDD\|377584
NZ_CP043959.1\|WP_150156052.1\|5104965_5105346_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP043959.1\|WP_150156038.1\|5087617_5088421_-\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|252734
NZ_CP043959.1\|WP_150156047.1\|5100116_5101253_+\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176242
NZ_CP043959.1\|WP_150156046.1\|5099737_5099923_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150157475.1\|5092229_5093579_-\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238623
NZ_CP043959.1\|WP_150156053.1\|5105396_5106008_-\|dephospho-CoA-kinase	unknown	unknown	gnl\|CDD\|179560
NZ_CP043959.1\|WP_093766710.1\|5088545_5088830_-\|DUF397-domain-containing-protein	unknown	unknown	gnl\|CDD\|377231
NZ_CP043959.1\|WP_150156037.1\|5085772_5087263_+\|glutamate-synthase-small-subunit	unknown	unknown	gnl\|CDD\|237213
NZ_CP043959.1\|WP_150156042.1\|5091069_5091255_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156048.1\|5101268_5102234_-\|prolyl-aminopeptidase	unknown	unknown	gnl\|CDD\|130316
NZ_CP043959.1\|WP_150156050.1\|5103110_5103797_+\|RNA-binding-S4-domain-containing-protein	unknown	unknown	gnl\|CDD\|224109
NZ_CP043959.1\|WP_150156044.1\|5093729_5094680_+\|endonuclease	unknown	unknown	gnl\|CDD\|197338
NZ_CP043959.1\|WP_150156041.1\|5090588_5091041_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150156040.1\|5089914_5090592_+\|ATP-binding-protein	gnl\|CDD\|340413	cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.	1.24097e-18
NZ_CP043959.1\|WP_150156049.1\|5102275_5102989_-\|uracil-DNA-glycosylase	gnl\|CDD\|381681	cd10031, UDG-F5_TTUDGB_like, Uracil DNA glycosylase family 5, includes Thermotoga maritima TTUDGB and similar proteins. Uracil DNA glycosylase family 5 includes Thermus thermophilus HB8 TTUDGB (also called UDGb) which is not only a UDG acting on double-stranded uracil-containing DNA, but also a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA (except for the C/I base pair), as well as a xanthine DNA glycosylase acting on both, double-stranded and single-stranded xanthine-containing DNA. TTUDGB also excises thymine from G:T mismatched DNA, and removes analogs of uracil from DNA, including 5-hydroxymethyluracil (hmU) and 5-fluorouracil (fU). This subfamily also contains Bradyrhizobium diazoefficiens family 5 homolog Blr5068 (UdgB) which has been found to efficiently excise uracil from ssDNA and dsDNA. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Similar to family 4 UDGs, members of this family possess four conserved cysteine residues required to coordinate the [4Fe-4S] iron-sulfur cluster. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.	1.82451e-116
NZ_CP043959.1\|WP_150156039.1\|5088830_5089691_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	9.75593e-08
NZ_CP043959.1\|WP_150156051.1\|5103813_5104512_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.28278e-14
NZ_CP043959.1\|WP_145825214.1\|5098181_5099699_+\|glycerol-kinase-GlpK	gnl\|CDD\|234594	PRK00047, glpK, glycerol kinase GlpK.	0
NZ_CP043959.1\|WP_145825213.1\|5097240_5098143_+\|MIP-family-channel-protein	gnl\|CDD\|240230	PTZ00016, PTZ00016, aquaglyceroporin; Provisional.	2.51356e-71
NZ_CP043959.1\|WP_150156043.1\|5091411_5092101_-\|DUF899-family-protein	gnl\|CDD\|377584	pfam05988, DUF899, Bacterial protein of unknown function (DUF899). This family consists of several uncharacterized bacterial proteins of unknown function.	3.4879e-101
NZ_CP043959.1\|WP_150156052.1\|5104965_5105346_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	3.01171e-09
NZ_CP043959.1\|WP_150156038.1\|5087617_5088421_-\|SAM-dependent-methyltransferase	gnl\|CDD\|252734	pfam04672, Methyltransf_19, S-adenosyl methyltransferase. This family contains a SAM (S-adenosyl methyltransferase) domain, with a central beta sheet with 3 alpha-helices on both sides. Crystal packing analysis of the structure Structure 3giw suggests that a monomer is the solution state oligomeric form. An unidentified ligand (UNL, cyan) was found at the putative active site surrounded by the residues His57, His170, Phe171, Tyr216 and Met22. The UNL is likely to be a phenylalanine or phenylalanine-like molecule. (details derived from TOPSAN).	2.05249e-130
NZ_CP043959.1\|WP_150156047.1\|5100116_5101253_+\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176242	cd08282, PFDH_like, Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH). Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. 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.	0
NZ_CP043959.1\|WP_150157475.1\|5092229_5093579_-\|amidohydrolase-family-protein	gnl\|CDD\|238623	cd01298, ATZ_TRZ_like, TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.	6.01265e-156
NZ_CP043959.1\|WP_150156053.1\|5105396_5106008_-\|dephospho-CoA-kinase	gnl\|CDD\|179560	PRK03333, coaE, dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional.	1.27809e-91
NZ_CP043959.1\|WP_093766710.1\|5088545_5088830_-\|DUF397-domain-containing-protein	gnl\|CDD\|377231	pfam04149, DUF397, Domain of unknown function (DUF397). The function of this family is unknown.	4.8922e-18
NZ_CP043959.1\|WP_150156037.1\|5085772_5087263_+\|glutamate-synthase-small-subunit	gnl\|CDD\|237213	PRK12810, gltD, glutamate synthase subunit beta; Reviewed.	0
NZ_CP043959.1\|WP_150156048.1\|5101268_5102234_-\|prolyl-aminopeptidase	gnl\|CDD\|130316	TIGR01249, Putative_proline_iminopeptidase, proline iminopeptidase, Neisseria-type subfamily. This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.	5.79508e-96
NZ_CP043959.1\|WP_150156050.1\|5103110_5103797_+\|RNA-binding-S4-domain-containing-protein	gnl\|CDD\|224109	COG1188, COG1188, Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog) [Translation, ribosomal structure and biogenesis].	3.04215e-30
NZ_CP043959.1\|WP_150156044.1\|5093729_5094680_+\|endonuclease	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	1.9221e-19

>NZ_CP043959.1|WP_150156044.1|5093729_5094680_+|endonuclease
MLLGTWNLENLYRPGGPFGPGDEAAYASKLAALAAVITELDPGLLGVQEVGDPGALEDLAGLLDDGWHVALSEHADSRGIRVGFLSRTELTVVADTAVFPARILPVQADDTGLTAGRAGRGFLAVEVAGERGPLRVAVCHLKSKLLTYPDGRFQPRDEGERARYAAYALYRRAAEAAALRALADELLEGDGRERDVAVLGDLNDEVQAATTQMLLGPPGSEIGTPGYDRPDRGDAFRLWDVAPLIPAAERYSRVNSGRRELIDHVLLSHRLVRRVSVAGTGLPDDGPPRLPSVGTDPGERRGVAGSDHAPVWVRVG
>NZ_CP043959.1|WP_150157475.1|5092229_5093579_-|amidohydrolase-family-protein
MESPAGLIITGCTVLTHDDQERVGFRENAAVVVRDGAVAEVTDAGAVAGRAADEWIDARGQVALPGLINCHTHAPMVALRGLAEDLPTEEWFNDVVWPVESNLTGRDVTLGARLACAEMIRAGVTCFADHYFGMDAVAPVVAESGMRALLGEAYFSSQGPGGRERSLEFALGHQGSADGRITTALAPHAPYTVNDADLAATAELARAHGLPVHLHAAENRDQTEASLARHGVTPVEVLSRTGVLDTDVLIAHGTGIVESDLPLLQRAGGRTAVATAPRGYLKFAWPTTTPVRALRDIGVPVGLATDGAASNNSLDVWESMALTSLIQKSVEGDPRWLTSRQALHHATLQSARAVGLDGSVGRIAPGHRADIVLVDLTGPHTQPVHDLAATLVHSARAADVRTTVVDGRILMRDRRLLTVDVPETVRELGERLPALTERSHGRRIQRYDT
>NZ_CP043959.1|WP_150156043.1|5091411_5092101_-|DUF899-family-protein
MSLPEIVPRAEWRAAREELLDKEKAVTRALDALRAERRRLPRVPVDREYVFEGGDGRATLLDLFQGRRQLVVHHFEFAPEWETGCRCCSAFLDQIGHLAHLQARRTTFAAVSRAPFTRILPFKARMGWTVPWYSSYPGDFDADFEVFSEEGGTPVQRPGVSCFLREGDRVFHTYSAYGRGLEGLGSTTSLLDLTALGRQEPWEEPEGRAWAVGAPVAQAHLRYHDEYDL
>NZ_CP043959.1|WP_150156042.1|5091069_5091255_-|hypothetical-protein
MNGRTVLERFPAGGPRGSWPAEEFAHARRLEGLPAEVVMDLATDMFLVIVRGERAGGEVVA
>NZ_CP043959.1|WP_150156041.1|5090588_5091041_+|hypothetical-protein
MTGAGGTRVVSLDSLVRLQRGRTATDTPRRLPVPDGMTAPMGCDAVAVPARFGPLVLPRLPRVGCVYADEAHWWWLVPSDSDYALDWPAPAHYAAGAVLPDGPAATGDAGLPGLIHRPDGTLPYTPPIPLYLALCRLTGTTPAWSRPVTA
>NZ_CP043959.1|WP_150156040.1|5089914_5090592_+|ATP-binding-protein
MASVIPSAPLGTDAAAASVDLGAAPATAPSGDDAVRRFRFELAAHPGSPARARRLTRARLSGWSVCEDTCDTAALVVSELVTNAIVHTASSHVVCELHDGDDLVRIAVRDEGCAPDRPRANTRQQPEEEHGRGLLLVDALCHAWGAHEHGPGLLVWAELPRQADTPHEPAEPHNDLGWGARPKPGPAGGSEDGDSDGDESARSHPAEKRLDLPAGRHPGRDGGRA
>NZ_CP043959.1|WP_150156039.1|5088830_5089691_-|helix-turn-helix-domain-containing-protein
MSEPRSAPTVGQVVLGRRLLDLRERAGLKREEAARILRVAPATVRRMEMAEVALKIPYLQLLLKAYGVSDEEADAFVQLAEDANKPGWWQRFHDILPGWFSMYVSLEGAASLIRSYEPHFVPGLLQTEDYARGVLRSGAIGQTRPDDIERHVDLRMQRQELLTREDAPRLWVVMDETALRRRVGGPEVMRAQIDKLLEAAALPNVTLQVATFDSGPHPGTYGPFVLFRFAMPELPDMVYSEYLTGAVYLDARTEVATHLEVMDRMAAQAATAHRTKEILRDLRKEL
>NZ_CP043959.1|WP_093766710.1|5088545_5088830_-|DUF397-domain-containing-protein
MELIKPPKTQPRARAHAGRIYNGMPARELGSEGWHKPWSGGNGGNCLEAMKLDDGRIAVRQSTDPDGPALIYTSAEMTAFIEGAKAGEADFLLS
>NZ_CP043959.1|WP_150156038.1|5087617_5088421_-|SAM-dependent-methyltransferase
MTGQHPVEIDTTRPHPARMYDWYLGGKDNYPVDEAMGRQMLALDPRVPVMARVNRAFMQRATRWLAGQGVRQFLDVGTGIPTEPNLHQVAQRIAPDARVVYCDNDPIVLAHAAALLRGTDEGVTDYLQADVRDPDTILEGARKILDFDEPIGLSLIALLHFVPDEDGAHELVRRLLDAMPSGSHLVISHATADFTPEESEAAVAKLRAAGVTLALRSREEFTRFFDGLDLVEPGVEVPHLWHPELGDPVPGQEDGVIPGYGAVARKP
>NZ_CP043959.1|WP_150156037.1|5085772_5087263_+|glutamate-synthase-small-subunit
MADPKGFLTTPRQDWPRRPVEERVRDWDEVYVPGGLLPIISTQADRCMDCGVPFCHEACPLGNLIPEWNDLVSREDWRAAAERLHATNNFPEFTGRLCPAPCEAGCVLAINQPAVTIKNVECAIADRAWEEGFAAPAPPDRLSGRTVAVIGSGPTGLAAAQQLTRAGHTVAVYERDDRIGGLMRYGIPEFKMEKHHLERRVEQMRAEGTKFRTSTTVGRDVDAAELRSRYDALVIATGATAWRELPVPGRELAGIHQAMEYLPLANRVREGDLETSPLSAEGRHVVIVGGGDTGADCLGTAVRERAASVTQLDIYHRPGAERDEEAEPWPTYPKLYRLSAAHEEAGALGTAPAADADARLFAASTLRFEGDGEGRVSALRLVEVDAGRRPVPGTERVLPADMVLLALGFSGPDQRDGLTAQLGVKLEPRGTVARGADFATNVPGVFAAGDAARGQSLIVWAIAEGRAVAAAVDGYLTGGTSRLPAPIGPYDRPMTA
>NZ_CP043959.1|WP_145825213.1|5097240_5098143_+|MIP-family-channel-protein
MAERIAPARRRGYREGLGGEMLAEFLGTFVLILLGIGSVAVALVGLPGSGRQFVDFGPANWLIICWGWGFGVIFGVYVAGGISGAHLNPAVTLAFTVRRDFPLKKLPAYWLAQLLGAFVAAALVYACYHWAIDAADAKAGLARDQSLGTYSIFATFPAEYFGDSWWGPLLDQIVGTGILLLLICALIDLKNVAPLANLHPFLIGLVVVAIGMTFGTNAGYAINPARDFGPRLFTYFEGWGDIALPGTFGWFSSYWWIPIVGPLIGGVIGVLVYDLLIKPVINARARAMEAQEEGPATEDV
>NZ_CP043959.1|WP_145825214.1|5098181_5099699_+|glycerol-kinase-GlpK
MPEFVGAVDQGTTSTRFMIFDHAGNEVAKHQLEHQQILPRSGWVEHDPVEIWERTNTVIQNALRDGGLTASDLRAIGITNQRETTVVWDPRTGRPYYNAIVWQDTRTDSIAAALERDGHGDTIRHKAGLPPATYFSGGKIKWLLDNVDGLREAAEAGNALFGNTDAWVLWNLTGGPNGGIHATDVTNASRTMLMNLETLDWDDELLGIFGIPRSMLPAIHPSSDAEAYGQARTSRPLGAAVPITGVLGDQHAATVGQVCFSPGEAKNTYGTGNFLVLNTGTELVRSQNGLLTTVAYQFAGSPAVYALEGSIAVTGAAVQWLRDQLKIIGSAPDSEQLARSVEDNGGMYFVPAFSGLFAPYWRSDARGAIVGLSRFNTGAHIARATLEAICYQSRDVVEAMEQDSGVHLDVLKVDGGVTANDLCMQIQADVLGVPVSRPVVAETTALGAAYAAGLATGFWSDTDELRSHWQESKRWEPQWSEDRRQQGFQDWKRAVERTLDWVTVD
>NZ_CP043959.1|WP_150156046.1|5099737_5099923_-|hypothetical-protein
MAAQRLGTLLVAVPGLSGTPPGTTVTVRGRGASVDAFVNGDWLPLSWWEFSDGLREDIADR
>NZ_CP043959.1|WP_150156047.1|5100116_5101253_+|alcohol-dehydrogenase-catalytic-domain-containing-protein
MKAVVYKGPFEVAVEDVDNPTIQHPNDVIVRVTSTAICGSDLHMYEGRTAAEPGITFGHENMGTIAEVGPGVTSLKEGDRVVMPFNVACGFCRNCVEGFTGYCLTVNPGFPGGAYGYVAMGPWKGGQAEYLRVPYADFNCLKLPPGTEHEQDFVLLADIFPTGYHGCELAQVRPGESVTVYGAGPVGLMAAYSALLRGAKKVFVVDRVAERLQKAEEIGAVPINFAEGDPVEQIQDQTEGMGTDKGIDAVGYQASAGGGTDREEPATVLNSLVRTVRATGMLGIPGLYVPSDPGAPDEQSKQGMLLVAVGKLFEKGLKLGTGQCNVKRYNRQLRDMIIEGRAKPSFVVSHELPLDQAPSAYDKFDKRIEGYTKVVLHP
>NZ_CP043959.1|WP_150156048.1|5101268_5102234_-|prolyl-aminopeptidase
MARYPEIEPYDHGMLDVGDGNRLYWETSGNPRGKPAVVLHGGPGSGAGAGLRRYFDPAAYRIVLFHQRGAGRSEPSAADPATDMGVNTTPHLMADLERLRAHLGIERWLVWGVSFGSALGLRYAQTHPGVVSELVLTGVTTGSPAEVGLLTRGLGQIFPEAHARFLAELPEGRRAGNLAAAYNRLLESPDPEVRARAAQAWTDWETAIIPAPPGSVERFRDPAYRLSFARTVTHYWGNDHFFGDGGEEGVVLRDAHLLKGIPGTLVQGSLDFGNLLGIVWRLHHAWPDSELIVVDDAGHDAGATGDDALVAATDRYARRPA
>NZ_CP043959.1|WP_150156049.1|5102275_5102989_-|uracil-DNA-glycosylase
MDPRGLTRLDRRISGCRACPRLVDWREEVARTKRAAFADWTYWGRPVPGFGPSDARLLIIGLAPAAHGGNRTGRMFTGDRSGDVLYQALYDVGLASQPTSTHADDGLELYGVRVTAPVHCAPPANKPSPAERDTCRPWLVQELHLLRPTVRAAVVLGAFGWQAALPAFAEAGWTVPRPRPAFGHGTHVVLGAADGPSLGLFGCFHVSQRNTFTGKLTPAMLRDVLRTAAEAAGLSPT
>NZ_CP043959.1|WP_150156050.1|5103110_5103797_+|RNA-binding-S4-domain-containing-protein
MVAEGARDDKVAGAAGDAAADGPADGAGTTPEPADPKIAAAVAAAEAAGPQNGETVRIDSWIWAVRLVKTRSMGAAACKGGHVRVNGERVKPSHSVRVGDEVRVRVETRERVVFVKRLIRKRVGAPVAVQCYIDNSPPPPPREAVAPAGVRDRGAGRPTKRDRREMERLRALGGPGPFGGFAGPAAPGSPSAGTSAGTDGPGGPAGPGGRGKPGGRGTGGGSRRGRNR
>NZ_CP043959.1|WP_150156051.1|5103813_5104512_-|methyltransferase-domain-containing-protein
MKPTMREGHEGTGPGVITPDGCAVELYERLPVGEEPDVVAAAVPAGARILELGSGVGRMTHALVERGFEMTAVDESAEMLRRVRGARTICGPVERLDLGETFDVVLLASFLVHTGDTEVRRGMLRTCVRHLAEGGCVLIQREGEDYHTDVPRERTDPAGFTVRIVSVEPLGDGVDSVHAEYVFPDATWTQTFRARPLTREQFEAALAEEGLRVDRYLTEDRMWVRAVPVSRG
>NZ_CP043959.1|WP_150156052.1|5104965_5105346_-|tetratricopeptide-repeat-protein
MPETSGVPGRTPETHVIDFRAAEHLLASRDPRGAVKLLDGVIDVHPENTAARLLRARAFFAAAQLRPAELEFSLVLEREPDNAFAHFALARTYQRQGRPHPAKRHFRLAAALDPNPEYLKAARFDD
>NZ_CP043959.1|WP_150156053.1|5105396_5106008_-|dephospho-CoA-kinase
MLTVGLTGGIGAGKSEVSRLLVERGAVLIDSDRIAREVVEPGTPGLAAVVEAFGEEILAEDGSLDRPRLGALVFGDPEKLARLNAIVHPLVGARSRELEEAAPEGAVVVHDVPLLTENGLAPLYDLVIVVDASPETQLDRLVRLRGMSEEDARARMAAQAGREQRREIADIVVDNDVPLDALRRRVEEVWAELVRRAQASPSE

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Crispr_ID: NZ_CP043959_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_14

5613088-5613223

Orphan

Consensus_repeat	Method
GGGACCGGCAAGGGATTGGGGAGACGCCCCGCGGTCACACCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_14

>merge|NZ_CP043959|14|5613088-5613223|CRISPRCasFinder
GGGACCGGCAAGGGATTGGGGAGACGCCCCGCGGTCACACCCCGAGGCGCCCCGCCGACGCCCCCCACGGGCCCGCGGCCACGCGCGGAGGACGGGGACCGGCAAGGGATTGGGGAGACGCCCCCGCGGTCACACC

>NZ_CP043959|14|14|5613088-5613223|CRISPRCasFinder
GGGACCGGCAAGGGATTGGGGAGACGCCCCGCGGTCACACCC	CGAGGCGCCCCGCCGACGCCCCCCACGGGCCCGCGGCCACGCGCGGAGGACG
GGGACCGGCAAGGGATTGGGGAGACGCCCCCGCGGTCACACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150156381.1\|5608613_5610725_+\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239155
NZ_CP043959.1\|WP_150156387.1\|5617482_5620083_+\|nitrite-reductase-large-subunit	unknown	unknown	gnl\|CDD\|184951
NZ_CP043959.1\|WP_150156380.1\|5607776_5608454_+\|DUF218-domain-containing-protein	unknown	unknown	gnl\|CDD\|225500
NZ_CP043959.1\|WP_150156378.1\|5605415_5606723_-\|deoxyguanosinetriphosphate-triphosphohydrolase	unknown	unknown	gnl\|CDD\|235098
NZ_CP043959.1\|WP_150156391.1\|5623415_5623826_+\|excalibur-calcium-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|214891
NZ_CP043959.1\|WP_150156375.1\|5599881_5601204_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|235640
NZ_CP043959.1\|WP_150156384.1\|5614615_5615260_+\|class-F-sortase	unknown	unknown	gnl\|CDD\|320678
NZ_CP043959.1\|WP_150156389.1\|5620654_5621812_+\|DUF839-domain-containing-protein	unknown	unknown	gnl\|CDD\|253386
NZ_CP043959.1\|WP_150156386.1\|5616265_5617483_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224171
NZ_CP043959.1\|WP_167534609.1\|5603628_5603955_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156382.1\|5610753_5612400_-\|peptidase-M4-family-protein	unknown	unknown	gnl\|CDD\|341060
NZ_CP043959.1\|WP_150156392.1\|5623980_5626728_-\|pyruvate,-phosphate-dikinase	unknown	unknown	gnl\|CDD\|236446
NZ_CP043959.1\|WP_150156383.1\|5612599_5613013_+\|gamma-glutamylcyclotransferase	unknown	unknown	gnl\|CDD\|377602
NZ_CP043959.1\|WP_150156376.1\|5601491_5603399_-\|DNA-primase	unknown	unknown	gnl\|CDD\|235551
NZ_CP043959.1\|WP_150156377.1\|5604060_5605326_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223523
NZ_CP043959.1\|WP_150156390.1\|5621962_5622409_+\|excalibur-calcium-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|214891
NZ_CP043959.1\|WP_150156379.1\|5606772_5607573_-\|sirohydrochlorin-chelatase	unknown	unknown	gnl\|CDD\|225049
NZ_CP043959.1\|WP_150156385.1\|5615288_5616071_-\|TSUP-family-transporter	unknown	unknown	gnl\|CDD\|182593
NZ_CP043959.1\|WP_150157495.1\|5622447_5623035_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156388.1\|5620079_5620433_+\|nitrite-reductase-small-subunit-NirD	unknown	unknown	gnl\|CDD\|379380

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150156381.1\|5608613_5610725_+\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|239155	cd02754, MopB_Nitrate-R-NapA-like, Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.	0
NZ_CP043959.1\|WP_150156387.1\|5617482_5620083_+\|nitrite-reductase-large-subunit	gnl\|CDD\|184951	PRK14989, PRK14989, nitrite reductase subunit NirD; Provisional.	0
NZ_CP043959.1\|WP_150156380.1\|5607776_5608454_+\|DUF218-domain-containing-protein	gnl\|CDD\|225500	COG2949, SanA, Uncharacterized membrane protein [Function unknown].	8.08988e-55
NZ_CP043959.1\|WP_150156378.1\|5605415_5606723_-\|deoxyguanosinetriphosphate-triphosphohydrolase	gnl\|CDD\|235098	PRK03007, PRK03007, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional.	0
NZ_CP043959.1\|WP_150156391.1\|5623415_5623826_+\|excalibur-calcium-binding-domain-containing-protein	gnl\|CDD\|214891	smart00894, Excalibur, Excalibur calcium-binding domain. Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated.	2.08796e-08
NZ_CP043959.1\|WP_150156375.1\|5599881_5601204_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|235640	PRK05901, PRK05901, RNA polymerase sigma factor; Provisional.	5.91904e-162
NZ_CP043959.1\|WP_150156384.1\|5614615_5615260_+\|class-F-sortase	gnl\|CDD\|320678	cd05829, Sortase_F, Sortase domain found in the class F family of sortases. Class F sortases are mainly present in Actinobacteria, Chlorobacteria and Firmicutes. Their functions are largely unknown.	4.39191e-53
NZ_CP043959.1\|WP_150156389.1\|5620654_5621812_+\|DUF839-domain-containing-protein	gnl\|CDD\|253386	pfam05787, DUF839, Bacterial protein of unknown function (DUF839). This family consists of several bacterial proteins of unknown function that contain a predicted beta-propeller repeats.	6.56364e-26
NZ_CP043959.1\|WP_150156386.1\|5616265_5617483_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|224171	COG1251, NirB, NAD(P)H-nitrite reductase [Energy production and conversion].	5.6155e-104
NZ_CP043959.1\|WP_150156382.1\|5610753_5612400_-\|peptidase-M4-family-protein	gnl\|CDD\|341060	cd09597, M4_TLP, Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease. This peptidase M4 family includes several endopeptidases such as thermolysin (EC 3.4.24.27), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, protealysin, and bacillolysin (EC 3.4.24.28). Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence, and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The active site is found between two sub-domains; the N-terminal domain contains the HEXXH zinc-binding motif while the helical C-terminal domain, which is unique for the family, carries the third zinc ligand. These peptidases are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing. It has also been used in production of the artificial sweetener aspartame.	1.01005e-112
NZ_CP043959.1\|WP_150156383.1\|5612599_5613013_+\|gamma-glutamylcyclotransferase	gnl\|CDD\|377602	pfam06094, GGACT, Gamma-glutamyl cyclotransferase, AIG2-like. GGACT, gamma-glutamylamine cyclotransferase, is a ubiquitous enzyme found in bacteria, plants, and metazoans from Dictyostelium through to humans. It converts gamma-glutamylamines to free amines and 5-oxoproline.	1.26715e-21
NZ_CP043959.1\|WP_150156376.1\|5601491_5603399_-\|DNA-primase	gnl\|CDD\|235551	PRK05667, dnaG, DNA primase; Validated.	0
NZ_CP043959.1\|WP_150156377.1\|5604060_5605326_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|223523	COG0446, HcaD, Uncharacterized NAD(FAD)-dependent dehydrogenases [General function prediction only].	6.57216e-68
NZ_CP043959.1\|WP_150156390.1\|5621962_5622409_+\|excalibur-calcium-binding-domain-containing-protein	gnl\|CDD\|214891	smart00894, Excalibur, Excalibur calcium-binding domain. Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated.	8.71808e-08
NZ_CP043959.1\|WP_150156379.1\|5606772_5607573_-\|sirohydrochlorin-chelatase	gnl\|CDD\|225049	COG2138, COG2138, Sirohydrochlorin ferrochelatase [Inorganic ion transport and metabolism].	4.54258e-29
NZ_CP043959.1\|WP_150156385.1\|5615288_5616071_-\|TSUP-family-transporter	gnl\|CDD\|182593	PRK10621, PRK10621, hypothetical protein; Provisional.	1.09826e-35
NZ_CP043959.1\|WP_150156392.1\|5623980_5626728_-\|pyruvate,-phosphate-dikinase	gnl\|CDD\|236446	PRK09279, PRK09279, pyruvate phosphate dikinase; Provisional.	0
NZ_CP043959.1\|WP_150156388.1\|5620079_5620433_+\|nitrite-reductase-small-subunit-NirD	gnl\|CDD\|379380	pfam13806, Rieske_2, Rieske-like [2Fe-2S] domain.	2.24824e-44

>NZ_CP043959.1|WP_150156383.1|5612599_5613013_+|gamma-glutamylcyclotransferase
MNLPFFVYGTLRPGEVNHDRFLRGRTAHEEAGRLRGAVLYEGPGYPYAVETPDGEVRGELVTALPEAYAELLARLDRLEEYVPGDPRNLYDRVARPVVRETGGATVRAWVYVAAPAVAARLRARGTRVEGGDWRGMR
>NZ_CP043959.1|WP_150156382.1|5610753_5612400_-|peptidase-M4-family-protein
MSPIRHARRPRLAVAGAAVTGAALLAAALTPTTAGAADRPTRAAAVQAAASVLADRAGALGLTAAQDTKVRDVVVDADGSRHVRYDRTYRGLPVLGGDFVLHLAPDGSYRDVTRATRAAIDLPTVSPRLPAPRAAGLAANLLRAAHLGETLNRLTARPELVVDALHGAPRLAWRTDAVAQDSAGNPVARTVLTDAHTGTRIDTWDRLESVSGDGRSLYGGTVPLETTRTASGYELTDPTRGGTYTGDAGNRTDLCVLVVCVVRAPAPVVTDADNHWGTGSTADRATVAVDAQYGTDVTWDYYEDVHGRRGIAGDGKGSYNRVHYGNAYNNAFWDDRCFCMTYGDGDGTLMGPLVSLDVAGHEMTHGVTSKTAGLTYSGESGGLNEATSDIFGTLVEFHAANTQDPGDWLIGEEVVRDGFGKDALRFMDRPSKDGSSADCWDASVKDLDVHHSSGVANHFAYLLAEGSGAKTVGGTAHNSPTCDGSTVTGIGRAKLGTIWYRALTVHMTSSTDYAGARTATLKAAADLYGEGGAEHRAVAAAWSAVGVG
>NZ_CP043959.1|WP_150156381.1|5608613_5610725_+|molybdopterin-dependent-oxidoreductase
MRNTVTSTHCPYCALQCGMNLTPAADGRTVEVGERADFPVNRGALCGKGRTAPAVLSSAVRLTSPLVRSAAGTLEPASWEEALDRVAEGVGGARAAHGADAVGVFGGGGLTNEKAYSLGKFARVVLGTSQIDYNGRFCMSSAAAAGSRAFGLDRGLPFPLEDIPRTGCVILVGSNPAETMPPALRYFTELKENGGTLIVVDPRRTRTAEHADLHLAPRPGTDLALALGLLHLVVAEGRTDEEYIRERTAGWEEARAAAMAHWPEYVERITGVPVPQLRQAVRMFCEPEHAMVLTARGPEQQSKGTDTVSAWINLALATGRPGRPLSGYGCLTGQGNGQGGREHGQKADQLPGYRKLTDPAARAHVAQVWGVDPDSLPGPGRSAYELLDALGTDIRALLLMGSNPVVSAPRAAHVEERIRSLDFLAVCDVVLSETAELADVVLPVTQWAEETGTTTNLEGRVLLRRRAITPPAGVRSDLEVLHELAARLGGEGSPEKRFPADPEEVFEELRRASEGGPADYSGITYRRLAEENGVFWPCPSPGAAAEGGVHPGTPRLFLDRFATEDGRARFVPVSHRAAAEEPDEEYPVLLTTGRVVAQYQSGAQTRRVDELNTAAPGPFVELHPRLARRIGAAEGEPVAVVSRRGRAVAPARITTSIRPDTVFMPFHWAGEGRANTLTNPALDPTSRMPEFKACAVRLEAIRP
>NZ_CP043959.1|WP_150156380.1|5607776_5608454_+|DUF218-domain-containing-protein
MRRITVRRPRLPRTRAGQRRLVRAVVAVCVLALLPATWLRLSTGDRLRTTADVPRTEVAVVFGAGLWDGEPSPYLAHRLDAAAELYRAGRIRVVLVTGDNSREDYDEPDAMRAYLTRHGVPDARIVSDYAGFDTWDSCVRARKIFGVDRAVLISQGFHIRRAVALCEAAGVTSYGVGVDDRHDVTWYYGGAREVLAAGKAALDAAFRPDPHFLGPEEPGVRRALR
>NZ_CP043959.1|WP_150156379.1|5606772_5607573_-|sirohydrochlorin-chelatase
MTAYPMHPGARPRPAVPPPALVVVAHGSRDPRALATVRRLLARVRALRPGLPVHLGHIELNAPLLPGTLDELGASGTASAVLVPLLFGRGHHVTRDIPDAAAAAPLPTRVADPIGPHPLLVDALHARLTEAGWQAPRDAESRRASAVVLAAAGSRAPASRADTERIAALLAARLGVPVVPAYASAADPTVPDAVRALAARGRTRVAVASCFTAPGRFATECATAAPGTVSAPLGTHPAMARLLLHRYDQALRTAAPVTGAAALAPA
>NZ_CP043959.1|WP_150156378.1|5605415_5606723_-|deoxyguanosinetriphosphate-triphosphohydrolase
MEGITSDTSAPPANHVPPAGYDPSAVERWAAEPDKRPGRTAFQRDRARVLHSGALRRLAGKTQVVTPGEQSQVWDASPRTRLTHSLECAQVGRELGAALGCDADLVEAACLSHDLGHPPFGHNGEQALNEFAEDCGGFEGNAQSLRLLTRIEPKRFTPEGSVGLNLTRAALDAATKYPWPRGSHPTDPASVKFGVYDDDRPVFEWLRKDAPGTRTCFEAQVMDWADDVAYSVHDVEDGLHAGHIDPNCLHADPEREAVFAVAVGRYVPADTDTAELADALDRLLAQEWWPHGYDGTAVAQARLKDATSQLIGRFCLAAEGATRQAWGGGRLTRYGAELVVPRSTRMECAVLKAVADRYVMQRAEQERLRADQRIVVMELAEALTARAPDGLDPQFRSLFDRAPDDRARKRVVVDQIASLTDASARSLHARLTGRA
>NZ_CP043959.1|WP_150156377.1|5604060_5605326_-|FAD-dependent-oxidoreductase
MVDADQTFVIVGGGLAGARAAETLRAEGFTGRVILICDERDHPYERPPLSKGYLLGKAERDSVFVHEPAWYARHDIELHLGQTVDAVDRAAKTVRFGEDGTTVRYDKLLLATGAEPRRLDIPGTDLAGVHHLRRLAHSERLKGVLTSLGRDNGHLVIAGAGWIGLEVAAAARSYGAEVTVVHRGQTPLHSVLGPELGQLFAELHRDHGVRFHFGATLTEITGQDGMVLAARTDDGEEHPAHAVLAAIGAAPRTSLAEAAGLELADPASGGGVLVDERLRTSDPDVHAAGDVASFPHALFDTRMRVEHWANALNGGPAAARAMLGRDEIYDRVPYFFTDQYDLGMEYSGWAPPGSYDQVVIRGDAGKREFIAFWVREGRVLAGMNVNVWDVTDPIQRLIRSREAVDTEALADPHVPLESLAG
>NZ_CP043959.1|WP_167534609.1|5603628_5603955_+|hypothetical-protein
MSAGAQHVRDGRPLHRSGLTVTAGGAVRVALHGSGVAVTAGGAVRVGSGSPLPFQRLDDGGVAGRALQRRQPPHGGRGAGPRRTGGVGRARGSRRGPGGTGAVVLLVL
>NZ_CP043959.1|WP_150156376.1|5601491_5603399_-|DNA-primase
MAGRINDEDVKAVRDAVPIDAVVSEYLQLRNAGGGNLKGLCPFHDEKSPSFQVSPSKGLFHCFGCQEGGDTITFVMKIDHLSFSEAVERLAGQAGITLRYEEGGYNPTHQRGERIRLVEAHKLAAEWYAEQLATSPEADAGRVFLADRGFDQAAALHFGVGYSPQGWDHLTRFLRGKGFSDKELVLSGLAQEGRRGPIDRFRGRLMWPIRDIGGDVVGFGARKLYEADNGPKYLNTPDTAIYRKSQVLYGIDLAKKDIAKSSRAVVVEGYTDVMACHLAGVTTAIATCGTAFGGDHIKILRRLLMDNGSARVIFTFDGDAAGQKAALRAFEDDQKFAAETYIAIAPDGMDPCDLRLAKGDEAVADLVEPRTPLFEFALRQIVRRYDLDTPAGRAGALDEAAPIVARIKNSGAQHEVAVQLAGMLGILDTQFVVKRVAQLARWARDRGGKGPAPEQRRPGGAPQQYAAPSAPRGPALNLRNPVFATERELLKLALQRPELVSPAVDAYGVDEFTAPPYAAVRQAILDAGGAEYGVQDPQEYLIRVRDAAPDDTVRAMVTELAVEAIMRRAVDEVYAGEVLVRVRRRAVERRVREVNGKLARLSNHADQAELSAVQNELWVLQQYDQALREHGAAAL
>NZ_CP043959.1|WP_150156375.1|5599881_5601204_-|sigma-70-family-RNA-polymerase-sigma-factor
MPESSERGRPVGDGSHTPAGPLIAYGTDSGEAVDSAPEVPLPHPPAAIILEVAPVQTQTLTQTDTDVAGATPDADLLVAMPARSRVAQHPATGPEPPARALEPVEPAEPAEPAEPGEEPGDVAVEPVDLSRVRPETGGPSADLFRQYLREIGRIPLLTAAEEVDLARRVEAGLFAEEKLRLTPDLDSRLAHDLDRLVVMGRMAKRRLIEANLRLVVSVAKRYVGRGLTMLDLVQEGNLGLIRAVEKFDYARGFKFSTYATWWIRQAMSRALADQARTIRVPVHVVELINRVVRVQRRMLQERGYEPTPQEVAAHLDLPPERVGEVLRLAQEPVSLHAPVGEEDDVALGDLIEDGDAASPVESAAFLLLRQHLDAVLSTLGERERKVVQLRYGLVDGRPRTLEEIGRLFGVTRERIRQIESKTLNKLRDHAYADQLRGYLD
>NZ_CP043959.1|WP_150156384.1|5614615_5615260_+|class-F-sortase
MRRFRRTRSPGNTAIAAVTVCALCAGAVLLRDGRADSPPQPSAAQAHSETDAHGPARSSVPALPPSPPDRVRIPAIDVDAPLTGLGLTGTGSLDVPPNDRPDLAGWYEAGTTPGERGTAIIAGHVDNADGPAVFYSLGALDKGSTVEVARRDGTVAVFTVDAVEAYDARDFPDAKVYGATDRPELRVITCGAGYSPATGYRGNVVVYAHLTGTR
>NZ_CP043959.1|WP_150156385.1|5615288_5616071_-|TSUP-family-transporter
MPDITLTTVVLLCVAALAAGWIDAVVGGGGLLLLPALLLGLPAGTPAAHALGTNKAVAIVGTTGAAVTYARKAPVDVRTAVRIGLAALAGSSGGAFLAAGMSTEVLKPVIMVVLLAVAAFVILRPAFGTAPAPGPATRRQILAAIGLAGLGIGFYDGLIGPGTGTFLVLALTALLHLDLVTASATAKIVNCCTNAGALATFAWQGAVLWQLAVVMAVFNLAGGMLGARTALKRGSGFVRVVLLTVVFALVANMAYEQWLA
>NZ_CP043959.1|WP_150156386.1|5616265_5617483_+|FAD-dependent-oxidoreductase
MTSNERVVVIGSGLAGVRLARRLGELGTPVTLIGEEEHPPYNRVLLAEVLAGRYRPEVIALPAPAELVRARVTGIDRGRRTVACAEGSEIAYGRLVLATGSNPVLPPLRGLFTEDHALPRGVHAFRTLDDCLGLSAEVRPGIRAVVIGGGLLGVSAARALAVRGAQVVLAQQSERLMERQLDPAASALVRRHLTGLGVEVHTECRVRDVRCVGGAVRSVEMADGYALDADLVVLACGVHPRVSLAQAAGLDVAKGVVVDDELRTSDPYVHAVGDCAQHAGTVYGLATPALEQADALAALLAGDTTARYTGTRSLTRLTLTGPDSPFDLAAFGETEVLPGDDVVQLTDATRGTYRKVVVRDDRLVGGVLVGELGTVGALARAWEGAEPLPSDGGPLLHLLTNDGGS
>NZ_CP043959.1|WP_150156387.1|5617482_5620083_+|nitrite-reductase-large-subunit
MPTDTSTIVLVGHGMVGQRFLEALAERGLTATHRVVVLCEEPRPAYDRVQLTSYFSGRTPEDLSLTDARFIEDHGIELHVGDPAEHVDREARTVTARSGLVVGYDVLVLATGSYPFVPPVPNKDAEGCFVYRTIEDLLAIEEYARRKATVGAVVGGGLLGLEAAGALKDLGLTSHIVEFAPRLMPVQVDEGGGAALLRTIEDMGLSVHTGVGTQEIVVDEAGAVTGMRLSDGSELAADMVVFSAGVRPRDQLARDCGLTVGERGGITVDEQCRTVADPHVFAIGECALAADGRVYGLVAPGYEQAETAAATIAEDEAAFTGADLSTKLKLLGVDVASFGDAHGTAGDCLDVVYSDSRAGLYKKLVIGRDGTLLGGILVGDAEAYGTLRAFTGSVPPVAPESLVLPAGAGAPAVLGPSALPDEAVICSCHNVTKGAVRGAVTDHACTTVPEVKKCTKAGTGCGSCVRVLGQLVDAELEASGVEVDKGLCACFSQTREELYEIVLALRIASHRELLDRYGREGARGGDGCEVCKPTVGSVIASLAPAIGASTYVLDGEQAALQDTNDHFLANLQRNGSYSVVPRIPGGEVAPEKLIVIGEIARDFGLYTKITGGQRIDMFGARVEQLPLIWARLVDAGFESGHAYGKSLRTVKSCVGQTWCRYGVQDSVRMAIDLELRYRGLRSPHKLKSAVSGCQRECAEARSKDFGVIATAGGWNLYVGGNGGATPRHADLLAQDLSDAELIRLIDRFLMFYIRTADRLERTSVWLDRIPGGLDHVRDVVVHDSLGICDELESLMAAHVAHYRDEWAETINDPEKLARFVSFVNAPDTPDPVVAFVPERDQIKPDLPLLSIGLRPADDVLEGSTQR
>NZ_CP043959.1|WP_150156388.1|5620079_5620433_+|nitrite-reductase-small-subunit-NirD
MTLALETTTGLTIRLRLEDDWFEVCDLGAMIPGRGVAALLPDGRQAAVFTDRAGRLYALDNRDPFTGAAVLSRGLTGTHRGRPFVASPLLKQRFDLETGRCLDDDTVRVTTYEVEAA
>NZ_CP043959.1|WP_150156389.1|5620654_5621812_+|DUF839-domain-containing-protein
MERRTFLRATALGGSSAVLGGTLWRGAAYAAPAQPGTGPYGALGTADANGIALPAGFTSRVIARSGQRVGSTSYTWHNAPDGGACYADGSGWIYVSNSEINPSGGASAVKFSATGAITGAYRVLSGTRQNCAGGKTPWNTWLSCEEVDRGYVYETDPWGVKAAVRRDAMGRFKHEAAAADPVRRVIYLTEDVSDGCFYRFRPTTWGDLSSGTLEVLVGGSGTSGPVSWARVPDPSGATATRNQISGAKRFNGGEGCHYANDTCWFTTKGDNRVWQYDAAAQTVELAYDDSLVPSGTAPLTGVDNVTGSSSGDLFVAEDGGNMEICVITPDDVVAPFLRVSGQSGSEITGPAFSPDGSRLYFSSQRGTSGSSSGGITYEVKGPFRA
>NZ_CP043959.1|WP_150156390.1|5621962_5622409_+|excalibur-calcium-binding-domain-containing-protein
MIPFRTSAAALLTAVALAAVPATAVAHDGNHPFENCTDAYDNGYSDIPKSDTEHYGTHLDRDNDGVGCDQPPSDFVPRDESDDDGAGAGAGAEDSGAEKENGGGTDLAETGGSDTTPYLAAGGAAVVLLGLAAGAAVMIAARRRRDNR
>NZ_CP043959.1|WP_150157495.1|5622447_5623035_-|hypothetical-protein
MRRAAWVALCGWVAALVTACVSYLTLRWVAVPIVVGLVLCLTFGGLLIWLHRAGWIALLSLAPGLMVLVGAVQYAPELALEVRGVRESVVIVADSADGTGGSNHRLTLRTEDGRELAERMTYKGDRAPRPGQRLEVIRDPEGVVPMERADQVDAAGRLHGAFAGLVTWTLMAALAGWRGHVRRRQGKEGSLLLSL
>NZ_CP043959.1|WP_150156391.1|5623415_5623826_+|excalibur-calcium-binding-domain-containing-protein
MHLTRSTLTALAALTLAALPVTASAHDGDHPFKSCPQAYDNGYSRLSSGDDHYGPELDPDGDGIACDEPPSGFIPRDHTEVGGDTTPVADTTTAARSDDLADEDSALTTYVTTGVAAVVLAGGIVLIASRLRRNRT
>NZ_CP043959.1|WP_150156392.1|5623980_5626728_-|pyruvate,-phosphate-dikinase
MSENKDPHVAQSGTSVESVKFVYDFTEGNKDLKDLLGGKGANLAEMTNLGLPVPPGFTITTEACKVYLDSGEEPAALRDEVSAHLDALEQKMGKKLGQADDPLLVSVRSGAKFSMPGMMDTVLNIGLSDKSVQGLAKQAGDDRFAWDSYRRLIQMFGKTVLGVDGELFEDALEAAKAAKKVTVDTELEAADLKKLVTKFKKIVKTECGRDFPQDPREQMDLAIKAVFDSWNGERAKLYRRQERIPHDLGTAVNVCSMVFGNLGPDSGTGVAFTRDPASGYQGVYGDYLQNAQGEDVVAGIRNTVPLAELEQIDKKSYDQLMQIMETLENHYKDLCDIEFTIERGQLWMLQTRVGKRTAGAAFRIATQLVDQGLIDEAEALCRVNGAQLAQLMFPRFDDEAKVEQVGRGIAASPGAAVGKAVFDSYTAVKWSRSGEKVILIRRETNPDDLDGMIAAEGILTSRGGKTSHAAVVARGMGKTCVCGAEELEVDTKRRRMTVPGGRVVEEGDVISIDGSSGKVYLGEVPVVPSPVVEYFEGRMHPGADDADELVEAVHRMMAFADRKRRLRVRANADNAEDALRARRFGAQGIGLCRTEHMFLGDRRELVERLILADTQVEREESLKGLLPLQKQDFVELFEAMDGLPVTIRLLDPPLHEFLPDITELSVRVALAESRQEPHENELRLLQAVHRLHEQNPMLGLRGVRLGLVIPGLFTMQVRAIAEAAAERRNAKGDPRAEIMIPLVGTVQELEIVREEADKVIAEVEEATGTRLKLAIGTMIELPRAALTAGQIAEAAEFFSFGTNDLTQTVWGFSRDDVEASFFTAYLEKGIFGVSPFETIDQDGVGSLVQSAAKAGRETRPDLKLGVCGEHGGDPESVHFFHEVGLDYVSCSPFRIPVARLEAGRAAVTSEGSDHR

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Crispr_ID: NZ_CP043959_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_15

6286856-6286969

Unclear

Consensus_repeat	Method
GGGGGCTGATCGCGCAGTTCCCCGCGC	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_CP043959_15

>merge|NZ_CP043959|15|6286856-6286969|CRISPRCasFinder
GGGGGCTGATCGCGCAGTTCCCCGCGCCCCTTCAGGGCCCTGACGGGCCCTAGACCTCACGCCCTACGGGGCATGTGCGGGTCGGTGGGGGGCTGCTCGCGCAGTTCCCCGCGC

>NZ_CP043959|15|15|6286856-6286969|CRISPRCasFinder
GGGGGCTGATCGCGCAGTTCCCCGCGC	CCCTTCAGGGCCCTGACGGGCCCTAGACCTCACGCCCTACGGGGCATGTGCGGGTCGGTG
GGGGGCTGCTCGCGCAGTTCCCCGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_150156766.1\|6277775_6279164_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224172
NZ_CP043959.1\|WP_150156771.1\|6285514_6286801_-\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035
NZ_CP043959.1\|WP_150156778.1\|6295328_6296117_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150157534.1\|6296183_6296951_-\|DUF1524-domain-containing-protein	unknown	unknown	gnl\|CDD\|377857
NZ_CP043959.1\|WP_150156777.1\|6294726_6295242_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156776.1\|6292327_6294526_-\|N-6-DNA-methylase	unknown	unknown	gnl\|CDD\|280533
NZ_CP043959.1\|WP_150156770.1\|6284378_6285320_-\|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|369056
NZ_CP043959.1\|WP_150156767.1\|6279632_6280577_-\|Ppx/GppA-family-phosphatase	unknown	unknown	gnl\|CDD\|223326
NZ_CP043959.1\|WP_150156765.1\|6276269_6277583_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|225139
NZ_CP043959.1\|WP_150156764.1\|6273664_6276196_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|226957
NZ_CP043959.1\|WP_150156769.1\|6283288_6283993_-\|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|369056
NZ_CP043959.1\|WP_150156775.1\|6290401_6291043_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|130706
NZ_CP043959.1\|WP_150156768.1\|6280573_6281110_-\|DUF501-domain-containing-protein	unknown	unknown	gnl\|CDD\|224424
NZ_CP043959.1\|WP_150156773.1\|6288041_6288692_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372652
NZ_CP043959.1\|WP_150156774.1\|6288866_6290405_-\|protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP043959.1\|WP_145826947.1\|6281138_6281615_-\|septum-formation-initiator-family-protein	unknown	unknown	gnl\|CDD\|368217
NZ_CP043959.1\|WP_150156772.1\|6287029_6288022_-\|nucleoside-triphosphate-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|237065
NZ_CP043959.1\|WP_150156779.1\|6297220_6300754_-\|transcription-repair-coupling-factor	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|224118
NZ_CP043959.1\|WP_150157533.1\|6291267_6292233_-\|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl\|CDD\|224214
NZ_CP043959.1\|WP_145826946.1\|6281731_6283021_-\|phosphopyruvate-hydratase	unknown	unknown	gnl\|CDD\|234617

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_150156766.1\|6277775_6279164_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|224172	COG1252, Ndh, NADH dehydrogenase, FAD-containing subunit [Energy production and conversion].	6.76567e-104
NZ_CP043959.1\|WP_150156771.1\|6285514_6286801_-\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	6.34606e-99
NZ_CP043959.1\|WP_150156779.1\|6297220_6300754_-\|transcription-repair-coupling-factor	gnl\|CDD\|224118	COG1197, Mfd, Transcription-repair coupling factor (superfamily II helicase) [DNA replication, recombination, and repair / Transcription].	0
NZ_CP043959.1\|WP_150157534.1\|6296183_6296951_-\|DUF1524-domain-containing-protein	gnl\|CDD\|377857	pfam07510, DUF1524, Protein of unknown function (DUF1524). This family of uncharacterized proteins contain a conserved HXXP motif. A similar motif is seen in protein families in the His-Me finger endonuclease superfamily which suggests this family of proteins may also act as endonucleases.	3.02188e-21
NZ_CP043959.1\|WP_150156776.1\|6292327_6294526_-\|N-6-DNA-methylase	gnl\|CDD\|280533	pfam02384, N6_Mtase, N-6 DNA Methylase. Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.	5.89491e-35
NZ_CP043959.1\|WP_150156770.1\|6284378_6285320_-\|LysM-peptidoglycan-binding-domain-containing-protein	gnl\|CDD\|369056	pfam06737, Transglycosylas, Transglycosylase-like domain. This family of proteins are very likely to act as transglycosylase enzymes related to pfam00062 and pfam01464. These other families are weakly matched by this family, and include the known active site residues.	7.91128e-30
NZ_CP043959.1\|WP_150156767.1\|6279632_6280577_-\|Ppx/GppA-family-phosphatase	gnl\|CDD\|223326	COG0248, GppA, Exopolyphosphatase [Nucleotide transport and metabolism / Inorganic ion transport and metabolism].	1.3287e-85
NZ_CP043959.1\|WP_150156765.1\|6276269_6277583_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|225139	COG2230, Cfa, Cyclopropane fatty acid synthase and related methyltransferases [Cell envelope biogenesis, outer membrane].	1.22229e-115
NZ_CP043959.1\|WP_150156764.1\|6273664_6276196_+\|FtsX-like-permease-family-protein	gnl\|CDD\|226957	COG4591, LolE, ABC-type transport system, involved in lipoprotein release, permease component [Cell envelope biogenesis, outer membrane].	3.96756e-24
NZ_CP043959.1\|WP_150156769.1\|6283288_6283993_-\|LysM-peptidoglycan-binding-domain-containing-protein	gnl\|CDD\|369056	pfam06737, Transglycosylas, Transglycosylase-like domain. This family of proteins are very likely to act as transglycosylase enzymes related to pfam00062 and pfam01464. These other families are weakly matched by this family, and include the known active site residues.	3.02114e-38
NZ_CP043959.1\|WP_150156775.1\|6290401_6291043_-\|hypothetical-protein	gnl\|CDD\|130706	TIGR01645, Ro_ribonucleoprotein-binding_protein_1, poly-U binding splicing factor, half-pint family. The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP\|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.	4.40219e-06
NZ_CP043959.1\|WP_150156768.1\|6280573_6281110_-\|DUF501-domain-containing-protein	gnl\|CDD\|224424	COG1507, COG1507, Uncharacterized conserved protein [Function unknown].	3.38184e-63
NZ_CP043959.1\|WP_150156773.1\|6288041_6288692_-\|hypothetical-protein	gnl\|CDD\|372652	pfam13624, SurA_N_3, SurA N-terminal domain. This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.	3.14252e-13
NZ_CP043959.1\|WP_150156774.1\|6288866_6290405_-\|protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.27695e-100
NZ_CP043959.1\|WP_145826947.1\|6281138_6281615_-\|septum-formation-initiator-family-protein	gnl\|CDD\|368217	pfam04977, DivIC, Septum formation initiator. DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.	1.00267e-11
NZ_CP043959.1\|WP_150156772.1\|6287029_6288022_-\|nucleoside-triphosphate-pyrophosphohydrolase	gnl\|CDD\|237065	PRK12334, PRK12334, nucleoside triphosphate pyrophosphohydrolase; Reviewed.	2.04382e-108
NZ_CP043959.1\|WP_150157533.1\|6291267_6292233_-\|YihY/virulence-factor-BrkB-family-protein	gnl\|CDD\|224214	COG1295, Rbn, Ribonuclease BN family enzyme [Replication, recombination, and repair].	2.16904e-32
NZ_CP043959.1\|WP_145826946.1\|6281731_6283021_-\|phosphopyruvate-hydratase	gnl\|CDD\|234617	PRK00077, eno, enolase; Provisional.	0

>NZ_CP043959.1|WP_150156771.1|6285514_6286801_-|cytochrome-P450
MPDQSPPSPTSELFSWEFAANPYPAYAWLREHAPVHRTKLPSGVDAWLVTRYADARRTLADNRLSKNPAHHDEGAHAKGRTGIPGERQADLMTHLLNIDPPDHTRLRRLVSKAFTPRRVAEFAPRVQELTDDLIDRFTANGSGTADLIHDFAFPLPIYAICDLLGVPREDQDDFRDWAGMMIRHGGGPRGGVARSVKKMRGYLAELIHRKREALSAEPAPGEDLISGLIRASDHGEHLTENEAAAMAFILLFAGFETTVNLIGNGTYALLTHPGERERLQRALAAGDRGLLETGVEELLRYDGPVELATWRFATEPVVIGGQRVETGDPVLVVLAAADRDPERFDGPDTLDLARRDNQHLGYGHGIHYCLGAPLARLEGQTALATLLTRLPDLRLAADPDDLRWRGGLIMRGLRTLPVEFSPPPTGQG
>NZ_CP043959.1|WP_150156770.1|6284378_6285320_-|LysM-peptidoglycan-binding-domain-containing-protein
MLSGNGRHRRPRQAPALLVAAGVTGSAIAIPLLGAGAANAADGETWDRVAECESGGSWSQNTGNGYYGGLQLTQDDWENNGGLEYAPSADQASRGQQIAVAERILAGQGVGKWRACGLLTGLNQDTASPNVDTGVAGDAASGTPRDAGSSDASGSPETSDSSASPSPSATTGTSTGKRDGADGRTSPSASTTPRSDESDKSGQTSGSSAVTDAEDGGPGRHRGSTAEEGERTDGAPASTGRHAAPSVEVTPEAGDDRYTVENGDSLTSIADSLALTGGWTALYAENQQVIGEDPNLILPGQRLLVSDGADADR
>NZ_CP043959.1|WP_150156769.1|6283288_6283993_-|LysM-peptidoglycan-binding-domain-containing-protein
MLFSSKGKHRRPSKATRAIAIAGVTGAAVAAPLMAAGNASAATASEWDAVAQCESGGNWSINTGNGYYGGLQFSASTWAAYGGTQYAGSADQATKAQQIEIAEKVLAGQGKGAWPVCGTGLSSASYNGSSAESSSQDSGSTEARESEQKASRSAERPAAPKQTEQKAEKKTVTTPTGKKVEKGDGEYKVVKGDTLSSIAAEQDVKGGWAKLFKLNDDIVDDADLIYPGQQLHLK
>NZ_CP043959.1|WP_145826946.1|6281731_6283021_-|phosphopyruvate-hydratase
MPSIDVVVAREILDSRGNPTVEVEVGLDDGSTGRAAVPSGASTGAFEAVELRDGDAGRYLGKGVEKAVLAVIEQIGPELVGYDATEQRLIDQAMFDLDATDNKGSLGANAILGVSLAVAHAASEASDLPLFRYLGGPNAHLLPVPMMNILNGGSHADSNVDIQEFMIAPIGAESFSEALRWGAEVYHTLKKVLKGKGLATGLGDEGGFAPNLGSNREALDLILEAIKEAGYTPGEQIALALDVAASEFYKDGVYTFEGKERTAAEMTEYYAELVDAYPLVSIEDPLFEDDWEGWKTITDKLGDKVQLVGDDLFVTNPERLARGIDEGAANALLVKVNQIGSLTETLDAVELAQRNGFKCMMSHRSGETEDVTIADLAVATNCGQIKTGAPARSERVAKYNQLLRIEEILDDAAVYAGRSAFPRFRSANQ
>NZ_CP043959.1|WP_145826947.1|6281138_6281615_-|septum-formation-initiator-family-protein
MAVKDRDRFSTATRIRLIGEQTAARVYRSQTKRQARRSRLTGRAALLVLVICSLVVALAYPMRQYVSQRAEIADQQKEQDETRQRVERLRDLKARWQDDAYAEQEIRRRLHYVMPGETGYIVIDPGPAESSRSDLEAADRPWYANVWDGVDKADAADQ
>NZ_CP043959.1|WP_150156768.1|6280573_6281110_-|DUF501-domain-containing-protein
MDTPPPTTPRSEPTDADVEAFKQQLGRPPRGLRAIAHRCPCGQPDVVETAPRLPDGTPFPTLYYLTCPRANSAIGTLEANGVMKEMTERLGTDPELAAAYRAAHEDYIRRRDLIEELKNFPSAGGMPDRVKCLHVLVAHSLAAGPGVNPLGDEALAMLPEWWSKGPCVTPADEKEDGR
>NZ_CP043959.1|WP_150156767.1|6279632_6280577_-|Ppx/GppA-family-phosphatase
MTRVAAIDCGTNSIRLLVADADPATGELTDLERRMTIVRLGQGVDRTGRLAPEALERTFAACREYAEVVKKHGASEHLRFVATSASRDAENRDDFVRGVVDILGVEPEVITGDQEAEFSFTGATKELTGRDDLRRPFLVVDIGGGSTEFVVGDDHVRAARSVDVGCVRMTERHLVRDGAVTDPSTEEQIAAMRADVEAALDRAEEAVPLREARTLVGLAGSVTTVSAIAQDLPEYDPAAIHHSRVSRDRVREITEWLLRSTHAERAKVPSMHPGRVDVIGAGALVLLTIMERTGAREVVVSEHDILDGIAWSVA
>NZ_CP043959.1|WP_150156766.1|6277775_6279164_-|FAD-dependent-oxidoreductase
MSTTERPRILVVGGGYVGLYAARRIQKKMRYGEATVTVVDPRSYMTYQPFLPEAAAGSISPRHVVVPLRRVLPKAEVLTGRVTTIDQDRKVATIAPLVGEAYELPFDYLVIALGAVSRTFPIPGLAEQGIGMKGVEEAIGLRNHVLEQLDKADSTTDEEIRRKALTFVFVGGGFAGAETIGEVEDLARDAAKYYKTVSREDMRFILVDAADKILPEVGPKLGAYGKEHLESRGVEVYLSTSMDSCVDGHVVLKNGLEVDSNTIVWTAGVKPNPALSRFGLPLGPRGHVDTEPTLQVKGTDYIWAAGDNAQVPDLVGRKAGNENAWCPPNAQHALRQAKVLGDNVISGMRGFPQKEYSHANKGAVAGLGVHKGVAMIVMGKMKIKVKGRLAWYMHRGYHGMAMPTWNRKIRVFADWTLGMFLKREVVSLGAIESPREEFYEAAKPAPAPAAAQEPKKTEAKAS
>NZ_CP043959.1|WP_150156765.1|6276269_6277583_-|methyltransferase-domain-containing-protein
MTDAAPRLKGILEQLLGAPLPVRIRTWDGSQAGPPDSPVLVVRNRRALRHLLFKPGELGLARAWVAGDLTIEGDLYTALDSLAGLIWERGEDARTLAQSLRDPDFRSAVRRLFAMAGPPLPPAPPREEVRRPRRGLHTKRSDKRAISHHYDVGNDFYEIVLGPSMVYSCAYWPAPPPEGTLEQAQHDKLELVARKLDLRPGQRLLDVGCGWGSMALHAAREHGVSVVGITLSQEQAAYARKRIAEEGLTDRIEIRVQDYRDVADGPFDAISSIGMAEHVGSERYLEYATVLHRLLKPGGRLLNHQIARRPQRDESSYQVDEFIDAYVFPDGELAPLGTTVSLLERAGFEVRDVESIREHYALTLRRWVDNLQADWTRAVSLTGPGRARVWQLYMAASALAFERNRIGVNQVVAVRTPESGVSEMPLRARVWGAPGPA
>NZ_CP043959.1|WP_150156764.1|6273664_6276196_+|FtsX-like-permease-family-protein
MFRTALRNVFAHKARLLMTVLAVMLGVAFVSGTLVFADTLSNAFRNQSAKSYDDVAVAVTSYADPDNPEEAPGLSGKDLDRISAVDGVAGVYGRVEGFAGVADPDGKLIGVGWSNKGSNFAPGENGKDPAYTFTDGSGPVKDGQIALDEESAAKGEYEVGDRVRVATNGPVKEYTLSGVFTTEDGAVNAGGSLVLFDTAVAQEQYLRQGYFEDATIVAAPGADDAKILAAVEPLLPDTAKAQTGTALADEQADQIEQGMGNLKQVLLGFAGIALFVGVFLISNTFTMLVAQRTKEIALMRAVGASRRQITRSVLAEAAVVGLVASAVGFVLGVGLAVGLRSGMAAFDMKMPDGPLVLSATPVISAFAVGVLITVFAAWLPGRRAAKIPPVAAMNSVHAVATTKSLVLRNSIGGAVTALGAAAIVAGASTGGDDGRMYIGAGAFLALIGVIILIPLLSRPVIALVRPLLVGPFGVAGKLAGQNAVRNPRRTGATASALAIGLTLVTGLSVLGVTVGTAIDKMTTDNIKADYMVTMANGGDLDRSALTALEKAEGVSAVSPQQDAYLQAGDDYVSASAVTPGDIERVLNVDVVSGDAGMLAEGQIAVAETTAKSKGWKPGDRIPFTFADEKKTTLTVGAVYKDSEFLSPVLVDTAVVDGHEAKPYIRQIFVKVDGGQTAANEQALVDALGDNPAITVMDRQDIRDEFGGAINTLLNVMYGLLAMALIIAVLGVVNTLAMSVFERQQEIGMLRAIGLDRRRVKRMVRLEAVVISVFGAVVGIGLGTFLGWAIGETVAEEIPGYALVLPWGRIGIFVVLAGLVGVLAALWPARNAARLNMLNAIKAE
>NZ_CP043959.1|WP_150156772.1|6287029_6288022_-|nucleoside-triphosphate-pyrophosphohydrolase
MNATSPAPTPEAAVGRVVLLTTSHRVAPGLLSWPAWQVLRAADRVLCADGAHPQLPYLREAGIAVEEAAPTAEEVVDACAGGRTVVVVATGEGEPALTDGLARLAGGGRVRMPELELLPASYDLPGARLLDLVQVMDRIRAECPWSSRQTHEGLAKYGIEEAYELVEAIEQGDREELREELGDVLLQVVFHARIAEEHPDEPFSVDDVAGGIVAKLIHRHPHVFGEETALTPEDVKAHWMRTKAEEKRRESVTDGVPLGQPALALATKLAGRVRGADLSVPLPSGEGVGYELLALAARAEAEGVDAEAALRAAARVYRDAIRSAEKVTGA
>NZ_CP043959.1|WP_150156773.1|6288041_6288692_-|hypothetical-protein
MHRRRRTALLLTAAIAAAAPLLTACGNDAHPGAAAVVGGERITVSQLENRVDEVRAAQRAAVPDEAQYQQAIARTGGLTRDTLHSMVLDRVLERAARDAGVTVSDREVQQLRSGFEEQAGGAKALETAWLQQYGVPPQRLDENLRLQVTAQKLAQRLGTDTSRPEFWKALSDASEELDVDLNPRYGEWDAEKSSRVDAKTPWIKDVTATDGPPLAL
>NZ_CP043959.1|WP_150156774.1|6288866_6290405_-|protein-kinase
MSVTTGRVVAGRYELSTLIGQGGMGQVWTAYDKRLDRRVAVKLLRPDKVAGQEADELRRRFVRECRVTAQVDHPGLVTVHDAGSEGEELFLVMQYVDGADLGDHLAEHDPYPWQWAVAVAAQLCAVLSAVHAVPIVHRDLKPRNVMVKQDGTVTVLDLGVASVMDADTTRLTHTGTPIGSPAYMAPEQAMGGAVGPYTDLYALGVLMHELLSGDVPFAGSTALGVLHRHLYEPPVPVRRLRPEVPEALEALVLRLLAKDPQHRPDSAQEVYEHLALLLPARGTPTGAPLDPTRPFLRPHAPWPDRARTPAPQPAPAAPPAPVAEKADVAAAVDEVKRLLGEGRITQAVDILGSILPVAADQHGEHSPVVRTLRKQYAATLLDDGQYRRALPELRRLADERAAEAGQADPQSLRYRYEAAQCLEQLGEPAAALAEYRALLAYYENQYVAAGDPQLAHDVRRRIGHLLLALGDRAAAHDTLVRLLHDVERAQGPGHPLAVEIRRTLQWLGQVRG
>NZ_CP043959.1|WP_150156775.1|6290401_6291043_-|hypothetical-protein
MYGHGAAPPTPSTGSVITQRVLYTAAGVLCCGLLACVPLFRVAVLRGRVFDWIAAWASIPLSIACLAVVGSLPEEDWRTDAALAAVMILGACAGAYYLTVDTRLPRQRNLYAGAVPPSPHATTMHAPGVHSAYGFPQQATPYPPTPVPQPQPPHAPHPPHGPVPPVPAPVPPPQAQPPQRPAPARIDQVRAELDELSDYLRRQDGQRGPEGGR
>NZ_CP043959.1|WP_150157533.1|6291267_6292233_-|YihY/virulence-factor-BrkB-family-protein
MGTAVHVPQTRDMLGDELSGDEALSALRRYGGLRLLADSFTRFRYADGFTNARALAFQVVLGLVPFTVVLVGLATSVHTESVGRVIELTLGRIVPGASADVVEKAFEGTRRSADSDVWSTVALWLGLGFAVLNLASAMAQIERGANRIYGIERDRPFVRKYGRALALAFTAGLPMVLGFLVLVAGETVGDAVARTLGHGTGGSAWWAVLDVPAGLLLAWVASAVILRWSPRRGQPGYTWLAFGSAVHLVLWISATWLLALYVGRSGAFGAVYGPLTAFIALLLWANLTAVALFLGIAFAAQLEAARAGIRTPVEPDPGPGA
>NZ_CP043959.1|WP_150156776.1|6292327_6294526_-|N-6-DNA-methylase
MQDNATEVTAAGIARLAGVGRAAVSNWRRRHADFPRPVGGTETSPAFALTEVEAWLRRHRKLAEVPLKERVWQQLVGHPEGPVTALIHAGCALLLIHDRPPVWLDISSGTDERLAALLPEALDEVLTPRALGSPCPGQPDGSRVHTRDAVNTRPSTPAATPTPTAAAPAAPGASTPADAAAPAPAEPRAALELLTASRLLPSVPLLRGVAELAAGTGARHTFEFLLGRHLDANPRQYTLTPPDLAALMAALAGTPATVLDPACGTGALLRAVASRPDRVLYAQDGARDLAALTALRLALHTRAPVHAAAGDTLRADAHPGLRADAVLCHPPFNERNWGHDELAYDPRWEYGFPARTESELAWVQHALARLREGGTAVLLMPPAAASRRSGRRIRSDLLRRGALRAVVALPAGAAPPYSVPLHLWVLRRPDRAPAQPEVLLVDAGRFTDDGRGGPDWPGVGETVLDAWQAFDGAGRIDQRPGLARSVPVIELLDDDVDLAPARHLPPPADTGGAGRLAGVRERLDETLRLTSRLAPPPAEPVPPAASGRLPLTTVGELARAGALVMRTGGHGGPARVPVLTDHDVLAGTAPSGTLPESEEEPVLTEAGDVVLPVLGGGAVARVVDEATAGAVLGRNLVLLRPDPAALDAWFLAGFLRGTANHRRASSYASTATRLDVRRLQLPRLAPDEQRRYGARFRDLDAFERALREAGRLGEQLVRGMYDGLTDGTIAPD
>NZ_CP043959.1|WP_150156777.1|6294726_6295242_+|hypothetical-protein
MGMKTKIALGAVVGIVVIGAVSANAGDGDGGSTGKDTSASADRQAGGAKDAGAGTGADAKPDAKADTKADTGQETGKKASQAEQFKAFVKENGTAQEKEAVAHVTKVQGADDRNDIFDTADVYTDFTGGIMGEGTGPAKLIASAFADWKQSENGLVTVYDADGELLGNGQF
>NZ_CP043959.1|WP_150156778.1|6295328_6296117_+|hypothetical-protein
MRRTALATLCLVAVAGTALTGCQSGEDGKDKASGSPRQSEEARKTEANEPFAGLTGGEITERAVAATTGASSLRFKGEIPDEESGGTLRIDLALDKKGDCAGTLGMGDRGRTELIKAGDTLYLKYDEAFLRAQSEGEPQADVDAVVEMMAGKWTKMSATGADAEDIAAFCDLDEVLGEARDGSSDATRGKATTVDGTPALTLTEKDGKDRYTFYVATDGEPYLLKLVSTSATDPGSVTFTGFGKPVPARKPAGEIIDLDALG
>NZ_CP043959.1|WP_150157534.1|6296183_6296951_-|DUF1524-domain-containing-protein
MGWGSRVRRTGGAAAVAVVLLAGCESIPEVDVPAAGGSGGAAPDGHAVSPLDNPDGTRPGLAPLTDAKERAAAAAVIDKVATKGRGPKTGYDRDEYGYAWMDTADGVPLARNGCDTRNDILQRDGQKVTFRSGSDCVVVSLTLVDPYTGKSIEWRKQKAAEVQIDHVIPLSYSWQMGASRWAESKREQLANDPLNLLPVDGGANSAKRDSGPASWLPPAKGIRCAYAVRFAQVADKYELPVTTADKAAMREQCRA
>NZ_CP043959.1|WP_150156779.1|6297220_6300754_-|transcription-repair-coupling-factor
MSLHGLLDAVVKDTALAEAVTAATDGNRTHVDLVGPPAARPFAVAALARDTGRPVLAVTATGREAEDLAAALRSLLPPEGVVEYPSWETLPHERLSPRSDTVGRRLAVLRRLAHPRPDDPETGPVSVVVAPVRSVLQPQVKGLGDLEPVSLRSGQSADLNEVVEALAAAAYARVELVEKRGEFAVRGGILDVFPPTEEHPLRVEFWGDDVEEIRYFKVADQRSLEVAEHGLWAPPCRELLLTPQVRERAAALAEDHPELGELLGKIAEGIAVEGMESLAPVLVDDMELLLDVLPKGAMAVVCDPERVRTRASDLVATSQEFLQASWAATAGGGEAPIDVGAASLRALADVRDRARELDMMWWTVSPFAADEELDGDTLKLGMHAPETYRGDTARALADTKGWLADGWRAVYVTEGQGPASRTVEVLGGEGIAARLDGDLGELTPSVVHVSCGCIDHGFVDPVLKLAVLTETDLTGQKASGREGARMPARRRKTIDPLTLEAGDHIVHEQHGVGRYIEMVQRTVQGATREYLVVEYAPAKRGQPGDRLYIPTDQLEQITKYVGGEAPTLHRLGGADWTKTKARAKKAVKEIAADLIKLYSARMAAPGHAFGGDTPWQRELEDAFPYAETPDQLTTIAEVKEDMEKSVPMDRLICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLVQQHFGTFSERYAQFPVTVKALSRFQTDTEAKAVLEGLREGSVDVVIGTHRLFSSETKFKDLGLVVVDEEQRFGVEHKEQLKKLRANVDVLTMSATPIPRTLEMAVTGIREMSTITTPPEERHPVLTFVGPYEQKQIGAAIRRELLREGQVFYIHNRVESIDRAAARLREIVPEARIATAHGQMSEQALEQVVVDFWEKKFDVLVSTTIVESGIDISNANTLIVERGDNFGLSQLHQLRGRVGRGRERGYAYFLYPPEKPLTETAHERLATIAQHTEMGAGMYVAMKDLEIRGAGNLLGGEQSGHIAGVGFDLYVRMVGEAVADYRRQLETGEIEEEPPLEVKIELPVDAHVPHDYAPGERLRLQAYRAIASANSEEDIKAVREELVDRYGKLPEPVENLLLVAGLRMLARACAVGEIVLQGNNIRFAPVELRESQELRLKRLYPGTLVKANARQVLVPRPKTAKVGGKPLVGRDLLGWVGEFLTSVLGS

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Crispr_ID: NZ_CP043959_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043959_16

6414190-6414299

Orphan

Consensus_repeat	Method
CAGCAGTACGGCTCGGGAAACATCGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043959_16

>merge|NZ_CP043959|16|6414190-6414299|CRISPRCasFinder
CAGCAGTACGGCTCGGGAAACATCGGCACGGCTCAGCACAGCGGCAGCGGGGGCATCCAGGCATCATGAGCGGCGACCACATTCAGCAGTACGGATCGGGAAACATCGGC

>NZ_CP043959|16|16|6414190-6414299|CRISPRCasFinder
CAGCAGTACGGCTCGGGAAACATCGGC	ACGGCTCAGCACAGCGGCAGCGGGGGCATCCAGGCATCATGAGCGGCGACCACATT
CAGCAGTACGGATCGGGAAACATCGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043959.1\|WP_145826826.1\|6420044_6420236_-\|DUF397-domain-containing-protein	unknown	unknown	gnl\|CDD\|377231
NZ_CP043959.1\|WP_150156852.1\|6412462_6413188_+\|transporter-substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|270341
NZ_CP043959.1\|WP_150156855.1\|6414751_6415195_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156853.1\|6413237_6413432_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150157537.1\|6409843_6410311_-\|DUF4240-domain-containing-protein	unknown	unknown	gnl\|CDD\|379426
NZ_CP043959.1\|WP_150156847.1\|6405491_6406784_+\|M6-family-metalloprotease-domain-containing-protein	unknown	unknown	gnl\|CDD\|274507
NZ_CP043959.1\|WP_150156857.1\|6416707_6417343_-\|DUF4352-domain-containing-protein	unknown	unknown	gnl\|CDD\|378684
NZ_CP043959.1\|WP_024884288.1\|6415959_6416319_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156849.1\|6408767_6409523_+\|UTRA-domain-containing-protein	unknown	unknown	gnl\|CDD\|225099
NZ_CP043959.1\|WP_150156851.1\|6411705_6412062_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043959.1\|WP_150156846.1\|6404529_6405171_-\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP043959.1\|WP_145826827.1\|6418251_6418761_+\|glutathione-peroxidase	unknown	unknown	gnl\|CDD\|238207
NZ_CP043959.1\|WP_145826825.1\|6420462_6421320_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|238045
NZ_CP043959.1\|WP_150156858.1\|6417470_6418178_+\|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	unknown	unknown	gnl\|CDD\|378065
NZ_CP043959.1\|WP_150156850.1\|6410677_6411286_-\|superoxide-dismutase	unknown	unknown	gnl\|CDD\|223678
NZ_CP043959.1\|WP_150156856.1\|6415204_6415876_-\|enoyl-CoA-hydratase/isomerase-family-protein	unknown	unknown	gnl\|CDD\|215151
NZ_CP043959.1\|WP_150156860.1\|6421635_6422388_-\|GPP34-family-phosphoprotein	unknown	unknown	gnl\|CDD\|377552
NZ_CP043959.1\|WP_150156848.1\|6406896_6407706_+\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|252734
NZ_CP043959.1\|WP_150156845.1\|6402775_6404332_-\|DHA2-family-efflux-MFS-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|129794
NZ_CP043959.1\|WP_150156859.1\|6418823_6419675_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133382

Protein	Function_ID	Function_description	E-value
NZ_CP043959.1\|WP_145826826.1\|6420044_6420236_-\|DUF397-domain-containing-protein	gnl\|CDD\|377231	pfam04149, DUF397, Domain of unknown function (DUF397). The function of this family is unknown.	1.09887e-11
NZ_CP043959.1\|WP_150156852.1\|6412462_6413188_+\|transporter-substrate-binding-domain-containing-protein	gnl\|CDD\|270341	cd13623, PBP2_AA_hypothetical, Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic binding protein fold. This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	6.03419e-72
NZ_CP043959.1\|WP_150157537.1\|6409843_6410311_-\|DUF4240-domain-containing-protein	gnl\|CDD\|379426	pfam14024, DUF4240, Protein of unknown function (DUF4240). This presumed domain is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 169 and 263 amino acids in length. This domain is often associated with the WGR domain pfam05406.	3.54537e-15
NZ_CP043959.1\|WP_150156847.1\|6405491_6406784_+\|M6-family-metalloprotease-domain-containing-protein	gnl\|CDD\|274507	TIGR03296, hypothetical_protein, M6 family metalloprotease domain. This model describes a metalloproteinase domain, with a characteristic HExxH motif. Examples of this domain are found in proteins in the family of immune inhibitor A, which cleaves antibacterial peptides, and in other, only distantly related proteases. This model is built to be broader and more inclusive than pfam05547.	6.85638e-55
NZ_CP043959.1\|WP_150156857.1\|6416707_6417343_-\|DUF4352-domain-containing-protein	gnl\|CDD\|378684	pfam11611, DUF4352, Domain of unknown function (DUF4352). Members of these family are putative lipoproteins that fall into the Antigen MPT63/MPB63 (immunoprotective extracellular protein) superfamily.	5.56516e-05
NZ_CP043959.1\|WP_150156849.1\|6408767_6409523_+\|UTRA-domain-containing-protein	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	1.40357e-44
NZ_CP043959.1\|WP_150156846.1\|6404529_6405171_-\|TetR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	7.1784e-09
NZ_CP043959.1\|WP_145826827.1\|6418251_6418761_+\|glutathione-peroxidase	gnl\|CDD\|238207	cd00340, GSH_Peroxidase, Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.	6.85179e-85
NZ_CP043959.1\|WP_145826825.1\|6420462_6421320_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	3.03935e-12
NZ_CP043959.1\|WP_150156858.1\|6417470_6418178_+\|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	gnl\|CDD\|378065	pfam08843, AbiEii, Nucleotidyl transferase AbiEii toxin, Type IV TA system. This family was recently identified as belonging to the nucleotidyltransferase superfamily. AbiEii is the cognate toxin of the type IV toxin-antitoxin 'innate immunity' bacterial abortive infection (Abi) system that protects bacteria from the spread of a phage infection. The Abi system is activated upon infection with phage to abort the cell thus preventing the spread of phage through viral replication. There are some 20 or more Abis, and they are predominantly plasmid-encoded lactococcal systems. TA, toxin-antitoxin, systems on plasmids function by killing cells that lose the plasmid upon division. AbiE phage resistance systems function as novel Type IV TAs and are widespread in bacteria and archaea. The cognate antitoxin is pfam13338.	0.00804469
NZ_CP043959.1\|WP_150156850.1\|6410677_6411286_-\|superoxide-dismutase	gnl\|CDD\|223678	COG0605, SodA, Superoxide dismutase [Inorganic ion transport and metabolism].	6.24844e-81
NZ_CP043959.1\|WP_150156856.1\|6415204_6415876_-\|enoyl-CoA-hydratase/isomerase-family-protein	gnl\|CDD\|215151	PLN02267, PLN02267, enoyl-CoA hydratase/isomerase family protein.	4.78101e-44
NZ_CP043959.1\|WP_150156860.1\|6421635_6422388_-\|GPP34-family-phosphoprotein	gnl\|CDD\|377552	pfam05719, GPP34, Golgi phosphoprotein 3 (GPP34). This family consists of several eukaryotic GPP34 like proteins. GPP34 localizes to the Golgi complex and is conserved from yeast to humans. The cytosolic-ally exposed location of GPP34 predict a role for a novel coat protein in Golgi trafficking.	6.58111e-43
NZ_CP043959.1\|WP_150156848.1\|6406896_6407706_+\|SAM-dependent-methyltransferase	gnl\|CDD\|252734	pfam04672, Methyltransf_19, S-adenosyl methyltransferase. This family contains a SAM (S-adenosyl methyltransferase) domain, with a central beta sheet with 3 alpha-helices on both sides. Crystal packing analysis of the structure Structure 3giw suggests that a monomer is the solution state oligomeric form. An unidentified ligand (UNL, cyan) was found at the putative active site surrounded by the residues His57, His170, Phe171, Tyr216 and Met22. The UNL is likely to be a phenylalanine or phenylalanine-like molecule. (details derived from TOPSAN).	9.49028e-119
NZ_CP043959.1\|WP_150156845.1\|6402775_6404332_-\|DHA2-family-efflux-MFS-transporter-permease-subunit	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	9.79498e-65
NZ_CP043959.1\|WP_150156859.1\|6418823_6419675_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|133382	cd01107, HTH_BmrR, Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.	2.43516e-34

>NZ_CP043959.1|WP_150156853.1|6413237_6413432_-|hypothetical-protein
MADQGWHDDSEYHEAVRRAERATRFGWSAIAWTTGTLGCALVTVALLFVAAMVAAVYVMVASHY
>NZ_CP043959.1|WP_150156852.1|6412462_6413188_+|transporter-substrate-binding-domain-containing-protein
MTPIDAELAHDLAPTGVLRASINLGNPVLAQGTPDEPSGVTVELAREVAARLALPVQFICFDAARKSYAAMADGRADLCFLAVDPDREKEVAFTTPYVHIEGVYAAPVDSEFVSADDVDRDGVRIGVKKGSAYDLHLSRTLRHATVVRGDEGVDVFHAENLDVAAGIRQPVTAHVAGRGELRLLEPAFMTIRQAMGTPKERRPRTTQFLSELVAELVASRFVAEALRRSGQDPALAAPTPV
>NZ_CP043959.1|WP_150156851.1|6411705_6412062_-|hypothetical-protein
MSDQPSRLDLLRFARRVVVQQATAAVRQLDGWIADEERREAERRRGGEMRPSPPEWLLQYGLNRRNVDAVHVGDCWAAAKSGRCRPASREQVVEALRHGVVACVHCRPDTALGLLDNP
>NZ_CP043959.1|WP_150156850.1|6410677_6411286_-|superoxide-dismutase
MGTYALPDLPYDYSALAPAITPEILELHHSKHHAAYVKGANDTLEQIAEVRDTDQITPTGLVGLEKTYAFNLSGHVLHSIFWQNLSPDGGDRPDGALATAIDEHLGGFEAFKKQLTVATTSVQGSGWGVLAWEPLGKRLIVEQVYDHHGNVGQGSTPLLVFDAWEHAYYLQYKNVRPDYVTKLWDLVNWEDVAARYAAAAGA
>NZ_CP043959.1|WP_150157537.1|6409843_6410311_-|DUF4240-domain-containing-protein
MTWADFWALMATVNGEAAEESCQRLAEELSRRPVSDIVGFAERHAEALYHLDQEKFGTLPVVDLTARFGSPFPQSADVFLYARCAVVAAGQAVWESVFFDVDKFAPYTSSERDGEWLLYVPDKAYELATGKEWDRPTRYCFESYSNRDGWPELRD
>NZ_CP043959.1|WP_150156849.1|6408767_6409523_+|UTRA-domain-containing-protein
MAATDDRRPKYQRIADSLREAIRSGEYGPGDRLPGENDLMAAHSVARMTARQAIGVLRDEGIAEARKGAGVFVRAFRPLRRRGIQRLARDQWGNGRSIWSADIESRALEVDQVSVSEETAPAHISAVLNLTAEAVMCVRRRRFVVDNKPVLLATSYLPLSLVAGSAITQEDTGPGGTYARLAELGHEPVHFREEIRSRMPSPDELTQLSLAPGTPVILICRTAFTDEGHPVEVNEMTLDAASYVLEYDFDA
>NZ_CP043959.1|WP_150156848.1|6406896_6407706_+|SAM-dependent-methyltransferase
MSAASLEARKRIRTDQPHTARIWNYWLGGKDNYPVDQATGDQIRTLHPGIGDYALADRQFLGRAVRYLAGECGIRQFLDIGTGLPTADNTHEVAQRIAPDSTVVYVDNDPIVLAHAEALLTSTPEGSTSYLDEDLRNIDAILEQAAKTIDFSRPVALILLGVVIFVEKDEEAYGTVRRLMDALPPGSHLVLSHTITRPDMPDVDAAVAFWNENGTPKLTQRTPEAVTRFFDGLELLEPGVVSCNHWRPEDPSADLPAEVAMFGGVGRKG
>NZ_CP043959.1|WP_150156847.1|6405491_6406784_+|M6-family-metalloprotease-domain-containing-protein
MQPQPSRRRISPRRLAALASVGALTLAVCSSAGNGHLSPATTAPGAGPSALSQSSAHGPCMISSEREVQMSEGVPTSPGYTRSTGTVRALTLMIDFSDAPGEGDALDRYREFFPQTREWFATSSYGRLDYRPELPVPDWLRMPKSFREYGIERGAPFDPGYRELIRDLVSEADAEVDFQSYDLVNVLVTPNAGPAALDTVLSVTFAGNDEAPTADGTPVSNASFVYSRQDDGSGSYDRTGYRVLPHENGHVFGLPDLYTAEGGGAVGHWDIMSEDWGANNDFLAWHKWKLGWLDISQVSCVARHGSGEYVLTPLARAGGPKLVFIPLDAHSGYAVELRTRAGNDEAVCRPGILIYRVDADVDTGMGPITVHDATRDSGGCTRAPNVHAELSDATFTPGQNFVDREEGVRVAVLTGGAEEYRIRVTRTSAQ
>NZ_CP043959.1|WP_150156846.1|6404529_6405171_-|TetR-family-transcriptional-regulator
MQTATPLTRKAPRPRADALRNRERIVTAAREMFVEFGPEVPFDEIARRAGVGNATVYRNFPDRDALVREVVCSVMDRTVRAAEQALSETGDAFEALERFAHAAADERISALCPMISSTFDQSHPDLEDARRRVESLAVQLMDRARAAGQLRDDVEYGDLLVGVAQLSRPPAGTGCGSADRFVHRHLQLFLDGMRAPARSVLPGSAVTVEDLRR
>NZ_CP043959.1|WP_150156845.1|6402775_6404332_-|DHA2-family-efflux-MFS-transporter-permease-subunit
MSETVSPAGKAPSRPGAGGPDANRWKALAFIAIAQLMVVLDATIVNIALPSAQQDLGISDGNRQWVVTAYALAFGGLLLFGGRIADLWGRKRAFVVGLGGFALASALGGAATNEAMMFGARALQGAFGALLAPAALSLLAVMFTDGKERAKAFGIYGAIAGGGGAVGLILGGFLTEYLNWRWTFFVNIPFAVIAAAGAYFVIREPAGGRNRSPLDVPGVILSTLGLVALVYGFTRAESAGWSDTLTIAMFVASAVLLVSFVAVEARVKAPLLPLRVVTERNRGGVYLSLGLAIIAMFGLFLFLTYYLQVVKGYSPVRTGFAFLPMIAGMITGSTQIGARLMTRVAPRLLMGPGFLVAALGMLLLTQLEIGTSYAAVLLPGMLLLGLGMGTAFMPAMSLATTGVEPRDSGVASAMVNTSQQVGGAIGTALLNTIAASATTAYVADHIGGATSRSQQQLVQLQGQVQGYTSAIWFAVGILVAAAAIALTLINAGRPGGTAVAGSSDASVEDEVAVPVAMH
>NZ_CP043959.1|WP_150156855.1|6414751_6415195_+|hypothetical-protein
MGASEWDYYVPYQEDLDAALQELRREVFEAGDYYWVNGDKWLAKDSTGPLPRSLDELWDDELVQEAGTHSILDIVRVLGPDDTPDYRTVEPVTGAEARELLGTEVLTRAHVKDFDVFPRSRWVGRCAVLHDGDGKPQEIYFWGHSGD
>NZ_CP043959.1|WP_150156856.1|6415204_6415876_-|enoyl-CoA-hydratase/isomerase-family-protein
MPSLDRQENVFVLDLGDGENRFHPDWIAAVGAALDEVEKAEGPRALVTAATGKFWSNGLDLEWLFANADHYHDYVVSVHELFARLLALPVITVAALQGHTFAAGAMLSLAHDFRVMRADRGYWCLPEADIDIPFTPGMSSLIQSRLAPQTAHEAMITARRYGGGDAAAAAIVDRAVPEDEVRSTALELAQSLAPKAGTTLGTIKSRMYASTLTTLRDTTNPLG
>NZ_CP043959.1|WP_024884288.1|6415959_6416319_-|hypothetical-protein
MVKPDELIVDIAARVEAGQSSQMSLTVVTGGAVITGRLAPEAVWRKRVSEVLNASDRLGEFAAVFDAPVKNDGPPTHLHFHVARILQGTVGIPETGGMYRVAIEDVSAWTVGDFSYSDH
>NZ_CP043959.1|WP_150156857.1|6416707_6417343_-|DUF4352-domain-containing-protein
MTQPNDPNQQQPQPPYVNRQPYPQQPAYGVPGVQPPPRKKGRFVRFAGFGCVGVLGLVVVIAAVSASGDSDDGGDRAAAPSGSVSAPAGADGKASTKEGSARSGPVRITAERTEFSRTVLADGSGYTSVLITVVNNGDDEVSVNPLYFTITDTRGTKHTAELGVDEKQIDAVELAPGENISGTVTGKGGFTPKYVTYTDGLLGDPVRVDVS
>NZ_CP043959.1|WP_150156858.1|6417470_6418178_+|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein
MTSPPLGVDAVHERLAGDLLAAGAPYGLLLAGGEAVRAHRLVDARVSGGVDLATEHPAGMPEIAGAVRTGLEERGWPVEVAVVDPLAARLLVGDDPAGARWRVDIRKEVLWRPAVVTAAGPALSLEDLVGTRVRALADRGLPRDLVDVHAAADRWSPPELEELGRRHAPDTFDLAELQSRLTGTEWLDDREFRAHGLDSPAVGDLRRWAQAWADDIAERLVEGEDPEEQGEGPEG
>NZ_CP043959.1|WP_145826827.1|6418251_6418761_+|glutathione-peroxidase
MTTTENNSAAPLDIEIGALNGGSADLSQYAGRAVLVVNVASKCGLTPQYAGLERLHERYAEQGFTVLGVPCNQFLGQEPGSAEEIAEFCSATYGVTFPMTEKVEVNGGGRHALYERLVGFADAEGHSGDVRWNFEKFLIGRDGAVVARFSPQTEPESAEVVAAVEKALG
>NZ_CP043959.1|WP_150156859.1|6418823_6419675_+|MerR-family-transcriptional-regulator
MTENAGVDEELLPIGAFAARTRLSAKALRLYDRTGLLVPARVDADTGYRFYRAGQVERARLVALLARLVALLRQLDMPLARIAEIVDADGGTAGAERLAAYWADVEARHAARRTLADHLRGRLSGGAPRYGKFTVDLVDVPEQVIVTESRHVLADELPAWIGAALGRLEEGARAYVGVTGAPFVVYHAEVSVESDGPAEACVPVADAAAARAWAEEGGRARGTTVRVEPAMRLARTRITKAQVAHPQILAAFEAVEEWMRERGLTYAGPCREVYFADWDAAGP
>NZ_CP043959.1|WP_145826826.1|6420044_6420236_-|DUF397-domain-containing-protein
MAIRLGATETWTTSSYTNNNGACVMVRSTTEEALELGDTKIPEGPKLAFPVDAWSAFVASVRS
>NZ_CP043959.1|WP_145826825.1|6420462_6421320_-|helix-turn-helix-domain-containing-protein
MASNVNPTVRRRRLGQELRRLRELKGMTAEEVAERLLVSQSKISRLENGRRSISQRDVRDLCGVYEVEDQRIVDSLMQMAKDSRQQGWWHAFGDIPYSVYIGLETDAESLRVYEPQIITGLLQTRAYAEAIVQGGSPESSEQENDKRVEVRLRRQSRITAEQDPLRLWVVLDEASLHRVVGSRQVMREQLEHVMELSQLPHVTVQVLPFEVGAHAGINGQYSILEFADAADSSVVYIEGVTSDLYLEKPHDVQKYTVMYEHLRAQSLNVEQSRQLVERLAKDYAR
>NZ_CP043959.1|WP_150156860.1|6421635_6422388_-|GPP34-family-phosphoprotein
MGRSRRTIPEELLLLALDPTTGTTAQPQSLDLGLAGAQLVELALAGRIAPDGDRIAVVVPRPTGDPTLDCALELLRRRGAPVRAVHWIGGPRLGLRQTYLSHLERCGMVHAVAGQMCGVLPTTRYQATDTEISREIRARLDSAIRTGVPPDPRTAALAALAHAVGLGKHLYPGNEGRSSRSRLRDLIRHDPMGGLVAHAVMDVQNGVAAQPRRNSAPAGRQAPGGRGAPEPARGVPAQPRHGSMARAVAH

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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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

153794 : 191940

Mycobacterium_phage(33.33%)

integrase,plate,tail

attL 172638:172653|attR 180482:180497

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_150151023.1\|153794_154298_+\|tail	lamin tail domain-containing protein	NA	NA	NA	NA
WP_150151026.1\|154431_155265_-	GlcNAc-PI de-N-acetylase	NA	NA	NA	NA
WP_167534649.1\|156076_156505_+	SRPBCC family protein	NA	NA	NA	NA
WP_150151032.1\|156809_157025_+	type II toxin-antitoxin system VapB family antitoxin	NA	NA	NA	NA
WP_150151035.1\|157021_157432_+	PIN domain-containing protein	NA	NA	NA	NA
WP_150151038.1\|158090_158513_-	PIN domain-containing protein	NA	NA	NA	NA
WP_150151040.1\|158509_158725_-	type II toxin-antitoxin system VapB family antitoxin	NA	NA	NA	NA
WP_150151043.1\|159175_159985_-	UTRA domain-containing protein	NA	NA	NA	NA
WP_150151046.1\|160065_160350_+	hypothetical protein	NA	NA	NA	NA
WP_150151055.1\|160824_161121_+	hypothetical protein	NA	NA	NA	NA
WP_167534431.1\|161080_161821_+	UTRA domain-containing protein	NA	NA	NA	NA
WP_150151058.1\|161817_162123_+	hypothetical protein	NA	NA	NA	NA
WP_103542833.1\|162423_162729_-	hypothetical protein	NA	NA	NA	NA
WP_150151061.1\|164116_167572_+	N-6 DNA methylase	NA	NA	NA	NA
WP_167534432.1\|167969_168434_-	NUDIX domain-containing protein	NA	NA	NA	NA
WP_150151064.1\|168452_169232_+	UTRA domain-containing protein	NA	NA	NA	NA
WP_004929398.1\|169371_169728_+	hypothetical protein	NA	NA	NA	NA
WP_150151067.1\|169731_171087_+	plasmid transfer protein	NA	NA	NA	NA
WP_150151070.1\|171170_171848_+	DUF2637 domain-containing protein	NA	NA	NA	NA
WP_150151073.1\|171867_172062_+	hypothetical protein	NA	NA	NA	NA
WP_150151076.1\|172063_172255_+	Mobile element transfer	NA	NA	NA	NA
WP_078948898.1\|172266_172422_+	hypothetical protein	NA	NA	NA	NA
WP_150151079.1\|172434_172755_+	SpdD-like protein	NA	NA	NA	NA
172638:172653	attL	NA	NA	NA	NA
WP_150151082.1\|172844_174242_+	replication initiation protein	NA	NA	NA	NA
WP_150151085.1\|174244_174454_+	excisionase family DNA-binding protein	NA	NA	NA	NA
WP_150151088.1\|174453_175620_+\|integrase	tyrosine-type recombinase/integrase	A0A249XT84	Mycobacterium_phage	5.1e-46	33.0
WP_167534416.1\|176040_176199_+	hypothetical protein	NA	NA	NA	NA
WP_024886422.1\|176334_176910_+	dCTP deaminase	I4AZP2	Saccharomonospora_phage	2.7e-77	71.4
WP_150151092.1\|176906_177416_+	phosphoribosyltransferase	NA	NA	NA	NA
WP_150151095.1\|177427_178333_-	zinc-binding dehydrogenase	NA	NA	NA	NA
WP_145829171.1\|178458_178827_+	MerR family transcriptional regulator	NA	NA	NA	NA
WP_150151098.1\|178885_179887_-	YIP1 family protein	NA	NA	NA	NA
WP_150151101.1\|179959_181252_-	zinc ribbon domain-containing protein	NA	NA	NA	NA
180482:180497	attR	NA	NA	NA	NA
WP_150151104.1\|181248_181845_-\|tail	phage tail protein	NA	NA	NA	NA
WP_150151107.1\|181841_183800_-\|plate	putative baseplate assembly protein	NA	NA	NA	NA
WP_150151110.1\|183799_184258_-	GPW/gp25 family protein	E3SKD2	Synechococcus_phage	1.0e-10	30.5
WP_150151113.1\|184257_186165_-	VgrG-related protein	NA	NA	NA	NA
WP_150151116.1\|186164_186902_-	LysM peptidoglycan-binding domain-containing protein	NA	NA	NA	NA
WP_024886434.1\|186973_187399_-\|tail	phage tail protein	NA	NA	NA	NA
WP_167534433.1\|190808_190967_-	hypothetical protein	NA	NA	NA	NA
WP_150151119.1\|190963_191497_-	hypothetical protein	NA	NA	NA	NA
WP_024886438.1\|191496_191940_-\|tail	phage tail protein	NA	NA	NA	NA

DBSCAN-SWA_2

2696399 : 2703042

Bacillus_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_150154404.1\|2696399_2697119_+	response regulator	W8CYM9	Bacillus_phage	7.5e-40	38.3
WP_150154406.1\|2697121_2698234_+	HAMP domain-containing histidine kinase	W8CYF6	Bacillus_phage	1.3e-19	31.5
WP_150154408.1\|2698354_2699356_-	NAD-dependent epimerase/dehydratase family protein	Q58M85	Prochlorococcus_phage	1.5e-22	28.8
WP_150157312.1\|2699459_2700866_-	HAMP domain-containing protein	W8CYF6	Bacillus_phage	5.4e-18	28.0
WP_145828753.1\|2700904_2701594_-	response regulator	W8CYM9	Bacillus_phage	2.1e-31	35.6
WP_150154410.1\|2701884_2703042_+	ATP-binding cassette domain-containing protein	Q6GZ03	Mycoplasma_phage	5.6e-13	41.1

Anti-CRISPR protein detection

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

2. NZ_CP043960

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

250259 : 286025

Erysipelothrix_phage(33.33%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_167534762.1\|250259_251141_-\|transposase	IS5 family transposase	NA	NA	NA	NA
WP_150157727.1\|251897_252347_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_167534746.1\|252691_252856_+	hypothetical protein	NA	NA	NA	NA
WP_167534747.1\|254032_254233_-	peptidoglycan-binding protein	NA	NA	NA	NA
WP_167534748.1\|254922_255285_-	peptidoglycan-binding protein	NA	NA	NA	NA
WP_150157730.1\|255802_256771_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_150157731.1\|257580_257979_+	hypothetical protein	NA	NA	NA	NA
WP_150157732.1\|258056_258608_-	NUDIX domain-containing protein	NA	NA	NA	NA
WP_150157733.1\|258800_259571_-\|transposase	transposase	NA	NA	NA	NA
WP_150157734.1\|260877_262242_-	FAD-dependent oxidoreductase	NA	NA	NA	NA
WP_150157735.1\|264332_264530_+	hypothetical protein	NA	NA	NA	NA
WP_150157736.1\|266043_266502_-	acyl-CoA thioesterase	NA	NA	NA	NA
WP_150157737.1\|266617_267178_-	OsmC family protein	NA	NA	NA	NA
WP_150157839.1\|267357_267906_+	TetR family transcriptional regulator	NA	NA	NA	NA
WP_150157738.1\|267931_268117_+	hypothetical protein	NA	NA	NA	NA
WP_150157739.1\|268222_268519_-	hypothetical protein	NA	NA	NA	NA
WP_150157740.1\|268630_269578_+	hypothetical protein	NA	NA	NA	NA
WP_150157741.1\|269585_270335_-\|transposase	transposase	NA	NA	NA	NA
WP_150157742.1\|271038_272463_-	mycothione reductase	A0A2K5B2C5	Erysipelothrix_phage	1.1e-42	26.9
WP_150157743.1\|272823_273987_-	citrate synthase/methylcitrate synthase	NA	NA	NA	NA
WP_150157744.1\|274288_275026_-	hypothetical protein	NA	NA	NA	NA
WP_167534749.1\|277160_277898_+	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_150157746.1\|277965_278598_+	TetR family transcriptional regulator	NA	NA	NA	NA
WP_150157747.1\|278677_279469_+	glucose 1-dehydrogenase	A0A0M4JSW6	Mollivirus	1.0e-05	28.5
WP_150157748.1\|279663_280368_+	CatB-related O-acetyltransferase	M1HKK6	Paramecium_bursaria_Chlorella_virus	7.4e-24	34.9
WP_150157749.1\|280573_281404_+	hypothetical protein	NA	NA	NA	NA
WP_150157750.1\|281739_282510_+\|transposase	transposase	NA	NA	NA	NA
WP_150157751.1\|283258_284410_-\|transposase	IS630 family transposase	NA	NA	NA	NA
WP_150157752.1\|284463_284778_-	hypothetical protein	NA	NA	NA	NA
WP_150157753.1\|285254_286025_-\|transposase	transposase	NA	NA	NA	NA

DBSCAN-SWA_2

291457 : 371843

Bacillus_phage(25.0%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_150157756.1\|291457_292549_+\|transposase	IS630 family transposase	NA	NA	NA	NA
WP_150157757.1\|293751_294462_-	thioredoxin domain-containing protein	NA	NA	NA	NA
WP_167534763.1\|300045_300844_+\|transposase	IS5 family transposase	A0A0M5M147	Mycobacterium_phage	2.7e-22	32.3
WP_150157840.1\|302335_303262_-	ABC transporter permease	NA	NA	NA	NA
WP_150157759.1\|303330_304275_-	ATP-binding cassette domain-containing protein	A0A2H4PQG7	Staphylococcus_phage	1.7e-15	29.6
WP_150157841.1\|304302_304734_-	GntR family transcriptional regulator	NA	NA	NA	NA
WP_150157760.1\|306493_307147_-	disulfide bond formation protein DsbA	NA	NA	NA	NA
WP_150157762.1\|308950_310039_+	NADH:flavin oxidoreductase	NA	NA	NA	NA
WP_150157763.1\|310079_310880_+	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_150157764.1\|312483_313428_-	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_150157765.1\|317525_318293_+\|transposase	transposase	NA	NA	NA	NA
WP_150157766.1\|318412_318775_+	MerR family transcriptional regulator	NA	NA	NA	NA
WP_150157767.1\|319238_319988_+\|transposase	transposase	NA	NA	NA	NA
WP_150157768.1\|320544_321633_+	NADH:flavin oxidoreductase	NA	NA	NA	NA
WP_150157769.1\|322445_323195_-\|transposase	transposase	NA	NA	NA	NA
WP_150157770.1\|325431_326238_+\|transposase	IS5 family transposase	NA	NA	NA	NA
WP_150157842.1\|326259_326568_+	hypothetical protein	NA	NA	NA	NA
WP_150157771.1\|326632_327007_-	MerR family transcriptional regulator	NA	NA	NA	NA
WP_150157772.1\|328247_329109_+\|transposase	IS5 family transposase	A0A0N9SHJ4	Paenibacillus_phage	1.3e-22	45.4
WP_150157757.1\|332026_332737_+	thioredoxin domain-containing protein	NA	NA	NA	NA
WP_167534750.1\|333188_333533_-\|transposase	transposase	NA	NA	NA	NA
WP_167534751.1\|333600_334467_-\|transposase	IS630 family transposase	NA	NA	NA	NA
WP_150157775.1\|336332_338216_-	thioredoxin domain-containing protein	A0A2H4J5W3	uncultured_Caudovirales_phage	2.3e-40	32.4
WP_150157776.1\|340065_340914_-	N-acetyltransferase	NA	NA	NA	NA
WP_150157777.1\|340910_341813_-	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_150157843.1\|342710_343232_+	DUF4396 domain-containing protein	NA	NA	NA	NA
WP_150157778.1\|344725_345466_-	alpha/beta hydrolase	NA	NA	NA	NA
WP_150157779.1\|345947_346655_+	response regulator	W8CYM9	Bacillus_phage	2.0e-29	35.3
WP_150157844.1\|346665_348483_+	HAMP domain-containing protein	W8CYF6	Bacillus_phage	1.7e-27	27.4
WP_150157780.1\|348503_349559_-	alpha/beta hydrolase	NA	NA	NA	NA
WP_150157781.1\|350313_351747_+	glutamine synthetase	NA	NA	NA	NA
WP_150157782.1\|351778_352819_+	carbon-nitrogen hydrolase family protein	NA	NA	NA	NA
WP_150157783.1\|352815_353508_+	C26 family cysteine hydrolase domain-containing family	NA	NA	NA	NA
WP_150157784.1\|353623_354355_+	FCD domain-containing protein	NA	NA	NA	NA
WP_150157786.1\|355139_356345_-	FAD-dependent oxidoreductase	NA	NA	NA	NA
WP_150157787.1\|356341_356599_-	ferredoxin	NA	NA	NA	NA
WP_150157788.1\|356595_357510_-	pyridoxamine 5'-phosphate oxidase family protein	NA	NA	NA	NA
WP_150157789.1\|357714_358179_-	VOC family protein	NA	NA	NA	NA
WP_150157790.1\|358355_358940_+	CGNR zinc finger domain-containing protein	NA	NA	NA	NA
WP_167534752.1\|360587_361313_-	FCD domain-containing protein	NA	NA	NA	NA
WP_167534753.1\|361555_361948_+	ATP-binding protein	K4I2X3	Streptomyces_phage	1.7e-06	54.7
WP_150157793.1\|362776_362962_+	hypothetical protein	NA	NA	NA	NA
WP_150157794.1\|363013_363397_-	toxin Doc	NA	NA	NA	NA
WP_167534754.1\|363396_363636_-	hypothetical protein	A0A1B3AYL7	Gordonia_phage	8.9e-06	46.8
WP_167534755.1\|364338_364824_+	hypothetical protein	NA	NA	NA	NA
WP_150157846.1\|364816_366019_-\|transposase	IS110 family transposase	NA	NA	NA	NA
WP_150157796.1\|367026_367434_+	hypothetical protein	NA	NA	NA	NA
WP_150157798.1\|370131_370905_-	hypothetical protein	NA	NA	NA	NA
WP_150157799.1\|371072_371843_+\|transposase	transposase	NA	NA	NA	NA

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_CP043959

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP043960

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection