CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_LS483439	Acholeplasma laidlawii strain NCTC10116 chromosome 1	3 crisprs	DEDDh,cas3,csa3	0	1	3	1

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LS483439_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483439_1

458678-458756

Unclear

Consensus_repeat	Method
ATATTGTGCCGATAACGGCATAAT	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_LS483439_1

>merge|NZ_LS483439|1|458678-458756|CRISPRCasFinder
ATATTGTGCCGATAACGGCATAATGTTGACTTAGCGAATAAACTATGATATACTGATATTGTGCCGATAACGGCATAAT

>NZ_LS483439|1|1|458678-458756|CRISPRCasFinder
ATATTGTGCCGATAACGGCATAAT	GTTGACTTAGCGAATAAACTATGATATACTG
ATATTGTGCCGATAACGGCATAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483439.1\|WP_012242397.1\|466154_466643_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_LS483439.1\|WP_012242384.1\|449533_451177_+\|DEAD/DEAH-box-helicase	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|223587
NZ_LS483439.1\|WP_041633789.1\|451387_452761_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242392.1\|461909_462650_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242382.1\|448403_448850_+\|PTS-transporter-subunit-EIIA	unknown	unknown	gnl\|CDD\|273298
NZ_LS483439.1\|WP_012242399.1\|467914_469402_-\|alpha-amylase	unknown	unknown	gnl\|CDD\|200477
NZ_LS483439.1\|WP_012242379.1\|445841_446144_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274701
NZ_LS483439.1\|WP_012242388.1\|456645_458358_+\|phosphoenolpyruvate--protein-phosphotransferase	unknown	unknown	gnl\|CDD\|224006
NZ_LS483439.1\|WP_041633786.1\|448924_449434_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_041633799.1\|460463_461717_+\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	unknown	unknown	gnl\|CDD\|225174
NZ_LS483439.1\|WP_012242396.1\|465202_466012_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_LS483439.1\|WP_012242393.1\|462829_463243_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242387.1\|453373_456640_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379260
NZ_LS483439.1\|WP_012242390.1\|459710_460133_+\|DUF5071-domain-containing-protein	unknown	unknown	gnl\|CDD\|213039
NZ_LS483439.1\|WP_064211867.1\|463457_465050_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238504
NZ_LS483439.1\|WP_012242389.1\|458770_459691_+\|Fic-family-protein	unknown	unknown	gnl\|CDD\|225718
NZ_LS483439.1\|WP_041633790.1\|452757_453396_+\|DUF4194-domain-containing-protein	unknown	unknown	gnl\|CDD\|372745
NZ_LS483439.1\|WP_012242398.1\|466774_467851_+\|GGDEF-domain-containing-protein	unknown	unknown	gnl\|CDD\|143635
NZ_LS483439.1\|WP_012242380.1\|446143_448000_+\|heavy-metal-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319774
NZ_LS483439.1\|WP_064211871.1\|448073_448307_+\|heavy-metal-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|225328

Protein	Function_ID	Function_description	E-value
NZ_LS483439.1\|WP_012242384.1\|449533_451177_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|223587	COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].	3.14396e-153
NZ_LS483439.1\|WP_012242397.1\|466154_466643_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.20759e-07
NZ_LS483439.1\|WP_012242382.1\|448403_448850_+\|PTS-transporter-subunit-EIIA	gnl\|CDD\|273298	TIGR00848, Includes:_Phosphotransferase_enzyme_IIA_component, PTS system, fructose subfamily, IIA component. 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS].	4.31109e-31
NZ_LS483439.1\|WP_012242399.1\|467914_469402_-\|alpha-amylase	gnl\|CDD\|200477	cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	5.12518e-139
NZ_LS483439.1\|WP_012242379.1\|445841_446144_+\|hypothetical-protein	gnl\|CDD\|274701	TIGR03652, FeS_repair_RIC, iron-sulfur cluster repair di-iron protein. Members of this protein family, designated variously as YftE, NorA, DrnN, and NipC, are di-iron proteins involved in the repair of iron-sulfur clusters. Previously assigned names reflect pleiotropic effects of damage from NO or other oxidative stress when this protein is mutated. The suggested name now is RIC, for Repair of Iron Centers. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0.000294783
NZ_LS483439.1\|WP_012242388.1\|456645_458358_+\|phosphoenolpyruvate--protein-phosphotransferase	gnl\|CDD\|224006	COG1080, PtsA, Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism].	0
NZ_LS483439.1\|WP_041633799.1\|460463_461717_+\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	gnl\|CDD\|225174	COG2265, TrmA, SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase [Translation, ribosomal structure and biogenesis].	1.52592e-78
NZ_LS483439.1\|WP_012242396.1\|465202_466012_+\|helix-turn-helix-transcriptional-regulator	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.	1.71227e-10
NZ_LS483439.1\|WP_012242387.1\|453373_456640_+\|AAA-family-ATPase	gnl\|CDD\|379260	pfam13558, SbcCD_C, Putative exonuclease SbcCD, C subunit. Possible exonuclease SbcCD, C subunit, on AAA proteins.	9.01347e-28
NZ_LS483439.1\|WP_012242390.1\|459710_460133_+\|DUF5071-domain-containing-protein	gnl\|CDD\|213039	cd11743, Cthe_2751_like, Uncharacterized protein domain similar to Clostridium thermocellum 2751. Cthe_2751 has been found to form homodimers. Based on structural similarity to other families, a role in processing nucleic acids was suggested, though interactions with DNA could not be demonstrated.	1.52408e-08
NZ_LS483439.1\|WP_064211867.1\|463457_465050_+\|hypothetical-protein	gnl\|CDD\|238504	cd01031, EriC, ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter.	4.03542e-70
NZ_LS483439.1\|WP_012242389.1\|458770_459691_+\|Fic-family-protein	gnl\|CDD\|225718	COG3177, COG3177, Fic family protein [Function unknown].	4.2419e-36
NZ_LS483439.1\|WP_041633790.1\|452757_453396_+\|DUF4194-domain-containing-protein	gnl\|CDD\|372745	pfam13835, DUF4194, Domain of unknown function (DUF4194).	2.80878e-29
NZ_LS483439.1\|WP_012242398.1\|466774_467851_+\|GGDEF-domain-containing-protein	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	3.18201e-41
NZ_LS483439.1\|WP_012242380.1\|446143_448000_+\|heavy-metal-translocating-P-type-ATPase	gnl\|CDD\|319774	cd02079, P-type_ATPase_HM, P-type heavy metal-transporting ATPase. Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
NZ_LS483439.1\|WP_064211871.1\|448073_448307_+\|heavy-metal-associated-domain-containing-protein	gnl\|CDD\|225328	COG2608, CopZ, Copper chaperone [Inorganic ion transport and metabolism].	2.17969e-12

>NZ_LS483439.1|WP_012242388.1|456645_458358_+|phosphoenolpyruvate--protein-phosphotransferase
MTKLKGNGVSSGIAIAKVHQFKLNNMFAMNKYATDKAFEIKRLGDALYKADKELENLTKQAEERIGVEHAQIFSAQQMMINDPEMIKNAHVKINDFNLDAAYAFKQTMSEMIDMFELSDNPYIKERISDLEDISNRVLHILSGKTHSLYVFNEDVILVATDLVPSETINLDTTFIKGIVIEKGSKTSHSAILARNLGIPAITGVDVSKIHHDTLAIIDGHTGDILLEPSEDTIKTYQTKQQEALKLQSTYETIKDLKTATIDNHEVHLAANIGVDLDIQEALDANASGIGLLRTENQYLESDDFPTEDELFIFYEKVATSFETNEVTIRTLDIGGDKNLSYLNMRKELNPFLGNRAIRYSLSYPSLFKTQLRAILRANTHQNIKVMFPMISTLKELMDAKKILDETYQALKIEGHEVNYPKIGMMVEVPSAALGIEKFLPHIDFISIGTNDLIQYMFAADRMNERVAYLYQPYNPILLSTIKSMIDKTNKHGIIVSVCGEMAGHKAQSLLLIGLGIKHLSMHANLILENKYLISKTTYKALEEIAEKALLLDHPYEVEALINTYIKGLKY
>NZ_LS483439.1|WP_012242387.1|453373_456640_+|AAA-family-ATPase
MKKLTKIKLINWHLFTDQTIKIDGNTLISGENGAGKSTLLDALQYLLVGGKSGAKFNIAATDDAKRTLEGYVRGRIGAENKEFIRSGDVITHVALEFYDEQSDEFGIIGAVLELPKMGNLKERFYLLENLNLHDGIFMDKNTPRDYRSMKAYLKTLSIDFIPFDSQRQYRDALAKYFGIDAKKYSKILPKALAFRPIDLQSFVFEFLLDDEPIDIQSLKNNVTQLKRVEGQIRLDKEKLEKLEKIITLGESLNQNLDQITTNELIDQMAFIEKRETFLNHSENLLDKVNAKYEVLKRQKDDLDRQITSNDETILELETSRQNDDITRTLSNLKEQLHAKGNQYNEQKVIVSDLKATLNRELDLYRDFVNLNPNTHISAFLKYYSGHEENSNILELSSYIEGAQSAASGYLNALSVEKSELEKERNNILNELRIAENRLNALKRNVKTYPRNVQSLMDAINTELSNYYKKDVRVRAFSDLIEVKDEAWRDALEGYLNTRRFDLIIDPLYFNDALEVYDRVKNELSIYGVGLVNTAKIGEYTTCLPNSLAAKVTTDHPYARNYVNMTMGYVVTVDNLSDLKNHQRSITKSAMTYANHTARQINPSQYQVPYIGNSSTQLQVEMDTKLVGELTSDLKRVSNLLEKNQMSLRLLQQSKLGHIVSSNQIRYFDNIKQTRKEYIELEQKVANLSSNPKIAELESQLDEERNKKRQLRLDFEKLADQMADLRSEKTRILEQIEESRDALSNYLKEQKEWNQKYPTLLPIAYNQFNALKVRYQSNYDLISRDLAQSTIQIKSQNARAEADVVNLMRAYIINYHFGAAPDLSELIEFEKEYVLIKDNNLMKYEQEAIDLRKASETGFREEFVGKLRASIESAQIQIAELNQALTGKHFGTDSYELVTKPSENPEFRTYYDIIMDSDAVAKHTLFTENLSKRKEIILMELFNKIASFDPENDKFALQFLDYRYYMSYDIEVTNENGNKSYFSKVSKEKSGGETQVPFYIVIAASFQQLLSKNKRIDAGCMVLFDEAFNNMDESRIDAMMKFYNSLSIQLFIAVPPQRVSNIVNYVTTSLAIVKDNDFAIVEAFKREVI
>NZ_LS483439.1|WP_041633790.1|452757_453396_+|DUF4194-domain-containing-protein
MMNKNQAIKKLSEEFVVLKEAEKTVFSRIVNKLLQVNFITRKKIADANDYRFVLAYKEIFEAYFCLSDFELIIERHEEVLYIKNISNFNHLRLRKAESILLLIIRMLYQSKMNVITLDENVEIYLSEVHDELTKVGYLDNKRMTKETLKPSLQLLKSYNIIDYMDSKLNDDARIKIYPTILYVIRTDSIKELLDHIDDYVKGGNVNEEVDED
>NZ_LS483439.1|WP_041633789.1|451387_452761_+|hypothetical-protein
MHLFDNIPDTLFNVLSSPNKHIYVDCLFIIYDATNSIENAFQGERGYVIDKLVDYFDELKEDFQMGDSEVTTSRQKSVSVINVLKQNGWLGEEELGDYKTSLNLFDYSIKIIDLLKRIQMGEENEYTGEIYTVYSLLSSFDILDGLTIVEQAYQKIEDVLRKLKTLKANIYRFYFDLVKKDRKDDLQKVLEKLLIDYKTNFFDSAYYHLKTTDSLPRYKRSILENISYIYQNEGFMETMAEQALTKRKALQYNDAYNYVEERIRYIKDSIDAIEYLIEGIDNKNELYINAAASKIMFLTNTSEDLEGLMNRLFKIILSDKKVDYSQIFNLFRARNLDENSLQTVRRPRVDAVAEEIDYNQDISDEVKERKMASLLKANLFSKKEINNYVTYLLGDAPRILASHIELESNDDFVKLILIFLFSKSTGMVYDVRLLNYDTRIGHIKFTDFEIFVKGKSL
>NZ_LS483439.1|WP_012242384.1|449533_451177_+|DEAD/DEAH-box-helicase
MAILFNDLPILDTTKVALEKLGFTEATPIQEQAIPKMILGLDLIGQAQTGTGKTFAFGIPMVEKTDTSLRQTQGLILTPTRELTNQVYKEIIKLVKFYPELRVTTIVGGESYEKQFKELDRKPHIIVATPGRIIDHIDRGTVDLSHITTLTLDEADEMLKMGFQDDIERILQTTPETRQTVLFSATMPAFIKKIAKNYQKNPELIKIEAKSLTVDRITQAYFLVKEKEKQSLLERLLDFENPSTAIIFVNTKAGADRITESLQKAGFTADALHGDLKQSQRTYVMNRFRSKQLSILVATDVAARGLDVDDVEIIVNYDLPQQDEIYVHRIGRTGRAGKKGKAFTFVTPLKRRMLDMLAHYTKADIKRLEVPTADDVYKEQLKTFKHKIKTELANEYPNHLEAIKELLVDEGSKDQLLNYLLDSMLPTKKTYETIEIIPEKASRRSQDERGNDKGRKDSRSSRDASPARGSGQYVDFTLNIGKADGLTPPTLFKFMEKEYGIFSKNIGDIRHHKNETVFGLRKDSVRRLNAKKEVNYKGRKVVIKTLN
>NZ_LS483439.1|WP_041633786.1|448924_449434_+|hypothetical-protein
MRVEIWFDFNQESLEVINNLNNAFERFKHSKDVDILFRSLPQKEEHFKYHEIFQYGRKKGLKHSYLCTVFDLFKSKTDLTTGLESRLSPYHVDIKDLQTNLKDHKSLRIVKNQLEHAALQKIDTAPTLTFTHGFRLVGVSSISDIEQTLIKMYEKDSGIKYCIEEDCER
>NZ_LS483439.1|WP_012242382.1|448403_448850_+|PTS-transporter-subunit-EIIA
MNLFEIDHIHLDLEVSSKDELFDFIANALKALGRITESADFKKALEKRESEISTGLGEGLGMPHTLDTSVMFPTMLYIRLKNEIDYQAIDGLPVKEIYAIAMPNSYQKEHLELISKIATIYIDETSKQEIRALDTKESIHSFISKNLK
>NZ_LS483439.1|WP_064211871.1|448073_448307_+|heavy-metal-associated-domain-containing-protein
MKKTTIQLETLTCPSCLQKINNAVKGLDGVNKDSVNVMFNSSKVKLEFDDSKLDIDKIEQAIKSQGYEVIKSNTKDI
>NZ_LS483439.1|WP_012242380.1|446143_448000_+|heavy-metal-translocating-P-type-ATPase
MVSFIHKQRMKIMILSFLLIVSGFIAHYVFDQKLIFDVTFIIASVIGVLPIAISAFQALKVKVISIDLLVTIAVVGAFIIKAYEESAIVTFLFLFGAYLEQRTLNKTRSAIKALTEMAPETALKKMDDGEFLEVGIDDVEVTDILLVKTGAKVPVDGIVLSGSAYINEASITGEAVSVKKVVDSKVFAGTILDNGTIEIIAQKVGEDTTFGKIIELVEEAQDSKSEAEKFIDRFATWYTPFVLVLALIVWVITQDVALAITILVLGCPGALVIGVPVSNVAGIGNGARHGVLLKGSEVIGNFSKVDTIVFDKTGTLTIGHPVLRYEAYYELDKKDIIPYIYSVEKQSDHPLAKAITNHLKDAKTLPIDHTDVIKGGGIVASIHERKVFIGNTVLMKDNGIEIKSDIMDEISRLEHEGHSIVLTAIDEKLVSLMGIRDEVRPNLKKDLKHIKKMGVKNLIVLSGDNQGSVDIVAKELGLTKAIGNMLPEDKANYIKELMNEGHIIAFVGDGVNDSPSIALAHIGIAMGGGTDVAIETSDVVLMNDNINKLPHALGLAKATKHNMIQNILIAIGVVVVLLVSLFWGEWVNMSIGMLVHEASILVVILNAMRLLRFKTKIN
>NZ_LS483439.1|WP_012242379.1|445841_446144_+|hypothetical-protein
MKENSFKLARNTYMDKLKMYVPIVDRVHGKLHPEFHDVRRVFDVLDDKLNQSNLDLKNEFEALKVITNHYKVPHDVCESYEAVYQMLEELNKAYDESAVV
>NZ_LS483439.1|WP_012242389.1|458770_459691_+|Fic-family-protein
MEYKNISYFATKWNIKERRIRVLCTEGRIHGVKKVGKTWLIPEDAQKPIDKRYRQVNDLFFDSIDFSIIDEKKDTIDSHRPFSQNMTRQLRDKLIIEWTYNSNAIEGNTLTLSETKVVLENGITIKGKPLKDHLEIINHKEAIEYIEDLVSKNVKLSEYDIKAVHYLILKEIDSTNAGKYRQENVFISGAKHVPSVYLNVPYEMQKMIEKYQSWKDLHPVVRACYLHGEFVKIHPFIDGNGRTARLLLNFELIQSGYPPVVIKTENRADYYDTLDKAHTTNNYTDFIKIIVDLVNESENLYLYLIG
>NZ_LS483439.1|WP_012242390.1|459710_460133_+|DUF5071-domain-containing-protein
MTGDILKLLSELNWNNKEKQTIAIKVLSSRKDYNFKMLIAPLQNEFYENQGIWWKDIALGCAIVLSNKSDSEIINLLPDLLVWLQDLNWPGAVEVFERLKKIPYLLIKKYLNDTIYKAQIENDDQWIEWLTLLNKSLLTL
>NZ_LS483439.1|WP_041633799.1|460463_461717_+|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD
MRLKVKTNDLDYQGQGVTRIDDKVTFIKGMFDDEVGIIEITKSKKNFQQAKLVELIQKNKQRVSENSFDYAPFFGLSLKAECLWQQKITKETIKKITNLDVEVEDTITDGKKLNYRNKITLHVKHIGGSLKIGTYEENSNYLEPIETHHLALPVINDKITVLNKWLKTFKLETNDIKNFTLRTNGKDVMLIIGIKLKFEGTESIIDELKKHFESIYLNIEKRSFENLSDESIHVYGLETLKMTFNHLSFEIGPESFFQVNKDVAILMYDEIKKLTQNHTVIDAYAGMASIGQYIDAKKVYAIESNLDSIIQAKKILKVNQVDHVELIHGQVEEKLEAYIKHADAIVFDPPRSGLTESIIELVKLNQIKTIVYVSCDLKSLARDINGLKDLYDIKKIIPVRMFPSTIHMETITLLSLK
>NZ_LS483439.1|WP_012242392.1|461909_462650_+|hypothetical-protein
MVWLSKRSKDNFYDTLKILKNEKTMHFVYAELRKYIENTFGITVFNITIDKFGFFDRPKKNSFFYQKKYLLAIHVSSYSEREMMQNKVSVELANFPTAYKMVNDKIKQDLIMDKLIELTKLKNFKTKINKTNTYVDYRFGFTTDYAEILLDKIEKGITKEILNEFKEKAHIWRIEKMFSTVTIFYFTELDKIENEKNGITHIIRDRYLSRIKEIDSINLFKEEYIVFDTKENVDKNYGGNLFYYFR
>NZ_LS483439.1|WP_012242393.1|462829_463243_+|hypothetical-protein
MKKKIIVNPAIYPVFIIAIVGTIILIQRLITTETYINTAQEVATYIYMLAMVFSVFYLGRYIIKPVPLSYDNNEIVIKMYFRNDVRLSYKEIVKAEYYNRYMRLIIHTKHKKYKFTFVIKTSELKEILKKKVKDSDF
>NZ_LS483439.1|WP_064211867.1|463457_465050_+|hypothetical-protein
MMKEKTSLNHMLVIVLLYSGITGIITGLFLYLFRYLSSLLLELTYSIYLSVQSNLWYLPFFVIGLVVLAYLVSLLIKWEPHAGGGAISRAAGFVRGILLFNWLKTLISTFISAQLVFFAGLPFGIEGPSVIMGTAISGGVDDLGKAHPAHRKYLLTAGASAGFSIATGSIFAGTIFTLEEMHKKFSFMLLSVAMSGAVFASVTMRILDYVFGNHTAFFSLTNEFKNIPFEFIWLAPLLGIGAGLLAAGFNFLIDFFGNMSAYKFKKVPLFVKLTINFLLVGFVGLFVIETIGNGHHSIIEPLFDRQFSFGMIVLLIVLKIITIVVSSSGTTGGLFIPVLVIGALYAGIFNEVSILIGLNSEYTAAIVLIGMSVFFSTSMQAPITTIAFIIEASLHPETIIFMMVAILAGILIAELLHMKPLNEIALKRFMKIQDQNRVWNLYNAKATIQENAFVIGKTVRDILWPANTLIKELIQENQQNATNIAVHGGDRVLTYRDQILFQIQSFDIERTLKELQDLIGIQEVEIELIR
>NZ_LS483439.1|WP_012242396.1|465202_466012_+|helix-turn-helix-transcriptional-regulator
MEQLKTIILERRKTLRLTQKELAQKLNVSDKVISKWETGSSLPDITLINPLAELLGITVSELLSAKELSKPVLNEEVNLKIITKFKVLYFIALGLFIVSLLIFPFGNYLVTKNEEAIGMILIVISIIFLISSIITYLVNNVWFRGLYTKYFYRKPYDLVFYKYNLVVIDIVSITLYALTLMVNHLAFLLIIAIIISTIIFLGKHKLAKSTMYIFKNRNQLLFIIALYLISLLIFIISYLYGKSWMTIFFTIPLYISITSYKFYRLDYSN
>NZ_LS483439.1|WP_012242397.1|466154_466643_+|GNAT-family-N-acetyltransferase
MDFNHITIEYISDINSEQLQNIERSDVSESFVDSLDSINAYTNYGLEHHLKGHTYLIKYQNVLAGVLLIGEGISWETDPLELKDVPFYRLMDFIIIQKYRNVGLGSFVIEKVISNMYEEFGVRPIVLGVHKDNIGAEKFYYKHGFVKTNYMDDDDYYFIRWT
>NZ_LS483439.1|WP_012242398.1|466774_467851_+|GGDEF-domain-containing-protein
MFIKSMIKGLFFNMNPLFERNKHDIIRYNKQLIPIAFIFSLVTILIPMFFSLFRPSMLETLPAYLVIFSVFILLLILFNFKPFHEKPLVFAYTFGIVFFIFVVYLSIDRFQSRPAGTALIFFVVAPIIFVDKPYKINIYLVLMFIIHTILSFQYKTFDIASVDLLNTFISLVAGMLFGRIFLVTRLKNFDIHRALLIERETDFLTGLPNRRSLFEYAQKDTFKAYNYMGLMMFDIDRFKKYNDNYGHLNGDQVLTEFARLLEVFSKTYPVKFYRYGGEEFIGITYNLDKLEIINLANHIKMDTFKLKVPFEQITTSIGVTVTDKTDNIDINDLIEQADKALYSGKNSGRNKVIFYEKK
>NZ_LS483439.1|WP_012242399.1|467914_469402_-|alpha-amylase
MNNNKFKLRENDWRNGALVYQVLVDRFNPSSHLESKKGLYLYPKTLNDWHSLPKPGTFLEEHRYWSHELDFWGGDLNSLNERLEYIKHLGVDVLYLNPIFESLSNHKYDATNFLEISKEYGTKEDLKKLIQNVHAHDMKIMLDGVFNHVGVGNPMFQKALKHEGFRHFFDFNDSYPRGVRLWADAPSLPELNLEHEDVKNYIFKQDDSVIRTYIKMGIDGWRLDVAFDIGFDILSELRDYARKDKLDVMIVGEIWNYPEKWLKSIDGVMNFTFREITLRLLSGELSPHKAIHMLKDTIDDAGIEPILKSWNLLDNHDVARLKHLLPKLELQRLAQVMQFTLPGSPNLYYGTELGMDGANDPMNRAPMNWDLFNDKNETLKWTQSLISLHKRERSLKIGDFIAINADDLLCYMRITDKVEDTCIIAINPSKEDVSETVLLKDSRLMNYSNFKTVLGKAKPVTLLAGLMNFTLEPYGFVVLKPETKPQKSYTPYKRV

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Crispr_ID: NZ_LS483439_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483439_2

1062493-1062570

Orphan

Consensus_repeat	Method
CAATAAAGACATTGTCTCCAATTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LS483439_2

>merge|NZ_LS483439|2|1062493-1062570|CRISPRCasFinder
CAATAAAGACATTGTCTCCAATTTTTATTGGTGCAATAAGGTTTGTATTGCATCCAATAAAGACATTGTCTCCTATTT

>NZ_LS483439|2|2|1062493-1062570|CRISPRCasFinder
CAATAAAGACATTGTCTCCAATTT	TTATTGGTGCAATAAGGTTTGTATTGCATC
CAATAAAGACATTGTCTCCTATTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483439.1\|WP_012242973.1\|1056217_1057894_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242976.1\|1060787_1062125_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|181958
NZ_LS483439.1\|WP_158298328.1\|1057897_1058047_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242984.1\|1070944_1072075_-\|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)	unknown	unknown	gnl\|CDD\|340819
NZ_LS483439.1\|WP_012242982.1\|1068725_1069892_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340840
NZ_LS483439.1\|WP_012242968.1\|1051246_1052056_+\|YwaF-family-protein	unknown	unknown	gnl\|CDD\|378199
NZ_LS483439.1\|WP_012242975.1\|1058875_1060576_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242983.1\|1069878_1070952_-\|sugar-transferase	unknown	unknown	gnl\|CDD\|340825
NZ_LS483439.1\|WP_069586341.1\|1065052_1066492_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240533
NZ_LS483439.1\|WP_012242981.1\|1067629_1068739_-\|EpsG-family-protein	unknown	unknown	gnl\|CDD\|379716
NZ_LS483439.1\|WP_041634170.1\|1074208_1075408_-\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340825
NZ_LS483439.1\|WP_012242974.1\|1058096_1058750_-\|esterase	unknown	unknown	gnl\|CDD\|238866
NZ_LS483439.1\|WP_012242986.1\|1073193_1074207_-\|polysaccharide-biosynthesis-protein	unknown	unknown	gnl\|CDD\|275003
NZ_LS483439.1\|WP_012242972.1\|1054710_1055682_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_012242985.1\|1072076_1073186_-\|capsular-polysaccharide-biosynthesis-protein-CapF	unknown	unknown	gnl\|CDD\|187571
NZ_LS483439.1\|WP_012242969.1\|1052160_1053105_+\|L-lactate-dehydrogenase	unknown	unknown	gnl\|CDD\|133427
NZ_LS483439.1\|WP_012242971.1\|1053806_1054727_-\|transcriptional-regulator	unknown	unknown	unknown
NZ_LS483439.1\|WP_099750384.1\|1066484_1067579_-\|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)	unknown	unknown	gnl\|CDD\|223458
NZ_LS483439.1\|WP_012242978.1\|1063752_1065063_-\|phosphoglucosamine-mutase	unknown	unknown	gnl\|CDD\|100095
NZ_LS483439.1\|WP_012242970.1\|1053128_1053590_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LS483439.1\|WP_012242976.1\|1060787_1062125_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|181958	PRK09564, PRK09564, coenzyme A disulfide reductase; Reviewed.	6.87401e-137
NZ_LS483439.1\|WP_012242982.1\|1068725_1069892_-\|glycosyltransferase	gnl\|CDD\|340840	cd03812, GT4_CapH-like, capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).	1.60884e-78
NZ_LS483439.1\|WP_012242984.1\|1070944_1072075_-\|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)	gnl\|CDD\|340819	cd03786, GTB_UDP-GlcNAc_2-Epimerase, UDP-N-acetylglucosamine 2-epimerase and similar proteins. Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	1.29876e-137
NZ_LS483439.1\|WP_012242968.1\|1051246_1052056_+\|YwaF-family-protein	gnl\|CDD\|378199	pfam09529, Intg_mem_TP0381, Integral membrane protein (intg_mem_TP0381). This entry represents a family of hydrophobic proteins with seven predicted transmembrane alpha helices. Members are found in Bacillus subtilis (ywaF), TP0381 from Treponema pallidum (TP0381), Streptococcus pyogenes, Rhodococcus erythropolis, etc.	1.96158e-16
NZ_LS483439.1\|WP_069586341.1\|1065052_1066492_-\|hypothetical-protein	gnl\|CDD\|240533	cd13128, MATE_Wzx_like, Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).	9.51657e-17
NZ_LS483439.1\|WP_012242981.1\|1067629_1068739_-\|EpsG-family-protein	gnl\|CDD\|379716	pfam14897, EpsG, EpsG family. This family of proteins are related to the EpsG protein from B. subtilis. These proteins are likely glycosyl transferases belonging to the membrane protein GT-C clan.	0.00179261
NZ_LS483439.1\|WP_041634170.1\|1074208_1075408_-\|glycosyltransferase-family-4-protein	gnl\|CDD\|340825	cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.	1.83297e-65
NZ_LS483439.1\|WP_012242974.1\|1058096_1058750_-\|esterase	gnl\|CDD\|238866	cd01828, sialate_O-acetylesterase_like2, sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, 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 found in other serine hydrolases.	3.16439e-30
NZ_LS483439.1\|WP_099750384.1\|1066484_1067579_-\|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)	gnl\|CDD\|223458	COG0381, WecB, UDP-N-acetylglucosamine 2-epimerase [Cell envelope biogenesis, outer membrane].	1.28543e-176
NZ_LS483439.1\|WP_012242985.1\|1072076_1073186_-\|capsular-polysaccharide-biosynthesis-protein-CapF	gnl\|CDD\|187571	cd05261, CAPF_like_SDR_e, capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs. This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	2.01782e-160
NZ_LS483439.1\|WP_012242969.1\|1052160_1053105_+\|L-lactate-dehydrogenase	gnl\|CDD\|133427	cd05291, HicDH_like, L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases. L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.	6.19784e-175
NZ_LS483439.1\|WP_012242983.1\|1069878_1070952_-\|sugar-transferase	gnl\|CDD\|340825	cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.	7.10404e-11
NZ_LS483439.1\|WP_012242978.1\|1063752_1065063_-\|phosphoglucosamine-mutase	gnl\|CDD\|100095	cd05802, GlmM, GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0
NZ_LS483439.1\|WP_012242986.1\|1073193_1074207_-\|polysaccharide-biosynthesis-protein	gnl\|CDD\|275003	TIGR04130, L-fucosamine_synthetase, UDP-N-acetylglucosamine 4,6-dehydratase/5-epimerase. The FnlA enzyme is the first step in the biosynthesis of UDP-FucNAc from UDP-GlcNAc in E. coli (along with FnlB and FnlC). The proteins identified by this model include FnlA homologs in the O-antigen clusters of O4, O25, O26, O29 (Shigella D11), O118, O145 and O172 serotype strains, all of which produce O-antigens containing FucNAc (or the further modified FucNAm). A homolog from Pseudomonas aerugiosa serotype O11, WbjB, also involved in the biosynthesis of UDP-FucNAc has been characterized and is now believed to carry out both the initial 4,6-dehydratase reaction and the subsequent epimerization of the resulting methyl group at C-5. A phylogenetic tree of related sequences shows a distinct clade of enzymes involved in the biosynthesis of UDP-QuiNAc (Qui=qinovosamine). This clade appears to be descendant from the common ancestor of the Pseudomonas and E. coli fucose-biosynthesis enzymes. It has been hypothesized that the first step in the biosynthesis of these two compounds may be the same, and thus that these enzymes all have the same function. At present, lacking sufficient confirmation of this, the current model trusted cutoff only covers the tree segment surrounding the E. coli genes. The clades containing the Pseudomonas and QuiNAc biosynthesis enzymes score above the noise cutoff. Immediately below the noise cutoff are enzymes involved in the biosynthesis of UDP-RhaNAc (Rha=rhamnose), which again may or may not produce the same product.	4.13775e-173

>NZ_LS483439.1|WP_012242976.1|1060787_1062125_-|FAD-dependent-oxidoreductase
MKVVVIGCTHAGTAAVKSMLNHNKDIEVNVYERNDNVSFLSCGIALYVGGIVKDVNGLFYSSPEELRQLGANVFMEYNVEAIDYDKKTVTVKNLTTNEISVDSFDKLVLSTGSWPIIPRIPGISSSNVLLSKNFNQANEIIEQAKHAQKIVVVGAGYIGVELAEAFELLGKEVVLIDGEERIMPKYLDEEFTYHAQKAFTDNGVKLALGEKVDSFITSNDLVTHIKTNKATYETDLVIMCIGFKPNDTLYKGILETTPNGALITNEYMQTSNPDVFACGDNANIIYNPTDEVRYIPLATNAVRMGTLVGLNIVDQHVPYVGTQGTSGIKIYDLNISSTGLTEGVAQQAGIEYETITIHDHNRPEFMPSYDDVLLKLVYEKHTKRLLGGQILSKYDLTAQMNILSLAIQNKMTIEQLAFADFFFQPHYSKPWNLLNTAALAALNKN
>NZ_LS483439.1|WP_012242975.1|1058875_1060576_+|hypothetical-protein
MKDYLLDETSFILQFNRIPCNSESDILSSRPFGLVLRRYLQHTKKLENPDFKWILKIRQSDLISIYKALLVWPYEEVVQRLDALSHRLNRYHFFLFTEEFYNYWRKFERYGFLSRTRFDDDKSMNKRLINTTESFSNLVLNLYRTVTEKILDRNYHLLRQLPAGTQANLSLVSNPWTYDAPYTKLTDNRFVTGIVITPPLMIYSKSNTRTGIFKEVFNNPLKDIELHKNDYVVVAIKVGPFLTYAYIHNKFMKYAVTLGSLFEMVSFQEYKDKKPDLIYVYGINESKYDGTYYHDKENDIYAGFVSIDDKNDYFGYVKKMLLTLHNVKMIHEKKLPIHGAMFRLQLKGGKTKHVVIIGDSGAGKSETIESLRVVGEGKVTSIEIIYDDMGTFDIKDGKIVSYGTEIGAFVRLDDLDQGYAYKQIDRAVFLNPNKTNARVVLPAADYEFVMKDHKVDLLLYANNYDETKSGLEIFDASDDAAKIFEDGKRMAKGTTSEVGMTSTYFANPFGPVQHEELTKSLITTYFNKLKDNNIPVGVIYTKLALDGYEQKGPQEAALKLLEYLVK
>NZ_LS483439.1|WP_012242974.1|1058096_1058750_-|esterase
MKLTHQELKGLQQMIEKTSSKVLNTYSKDNVVNLFNQDVIFIGDSMIEFFNLKRYLPTLNALNRGVAGATTKLILDNLDVILGKINPKSIFISIGSNDLVLLEASVAEAYENIIKVLDVLKSKFPSAKLYYLSTTPVVSTQHPLYKKIYIGGRTNGELKSINFKVMNYAKSNDMTYLHQFDDLLDSEGYLNTNYTYDGIHLNPKGYEVYARNILSNL
>NZ_LS483439.1|WP_158298328.1|1057897_1058047_-|hypothetical-protein
MSNTKELYATYMTFSKNIKRIKIKPNYDIKCKLIGVINVVDSCKKIIGG
>NZ_LS483439.1|WP_012242973.1|1056217_1057894_-|hypothetical-protein
MKKIMLLLVVALSATILTANNAHAYDGVNRDSNGNITEVDLNGDVFVDGDYSAATWEINLEDMATDPYYKNAAIALPLQFVPMLEIKNKIFHFYKSLFVKYDAKLTSELILLLLAYETAMDELMIEQQNNAQSYYEKAIGYSIELILTKKLDKLAPVVQIFLDENMVMASVEVTMDNVIDAIADSIYDTENIEDPYTKFIVELVKGIGVETVQDFSHKSLGELVSSTGKNLGNLIIDTLVSQILSLPETLITQHPLGKLAFAAIYWMMGQEAQYAAEQYALILDNITAFLTALLNPYNMGKNIRFDYLIEHNINTNTISWSENYVEQEGFIANKHRGMAITFADTDVIYRNISSSYGVTNFTRDPDKYVQVKGRINLLNESQMYSEINNLFDKQYRAHNSNPNKFIFSSGYTERYYENRYTGIRYYAGFNLVRTPFRIKNADLSNAPTQTLYPSNYSTGYKVDITDATNKQNYKSGILRVFNNSTLIYEYNLSGSVQQILVPDLIHGKIYRFEIYVEYEMNFFITNNYRVYQREFTYLKSSGGGGGGGPKPPIQELMY
>NZ_LS483439.1|WP_012242972.1|1054710_1055682_-|hypothetical-protein
MFESIDIMKTLDSIRANHKIKIQDLVQGIMSRKTYTRLLNDEASISFYDLNKLLEKLSIPFLEFSLYVVNSIEGQFPMESSFFLTILRENYQKAYDEFYPGVMGKELKTIFGAKSVPATIELMLYKLNKQSKEVSLRNLHQKFDLKSILESRIIDDGISGILYSFVYLVGDSERRQIGNFIYKVIFDPSFRHYYSYTEISKTIIHVTGILSFTLLDKLDDEELNRLEKIVVGALDYHTKFRGTVFDHKIFRILYQFQKEKNLENDFIIFSYISSYLSVFEKGAIPHKLDVTKEDMIIFKNYLKKGLYQQNTMYEGMLKHGKIW
>NZ_LS483439.1|WP_012242971.1|1053806_1054727_-|transcriptional-regulator
MEKYGSYYKLLDELRIAKGYTIADLCEGIISERTYLRQIKNGSKVNFTIFSRLLDRLDTGMGQFMTYMIHFDKSDTGVNRFAIRVHMYHFMDIGPIYELILKYKSDNKIETLMVEAFKLEFEYLINKITKDEFKIHYQVILESLKSLGTENLIVHLIKFIYHSYFKEDNIIDPKKFGQMLIDYNSNLSLFFYIMLMDKFLSFMTQQETIDFDIYEQILKKFEAYFIYINVKNYETSLETYHAFLYHVKHDYKMRDSYLYKALMNSLVIHSTYAHEAYKDLIRHGFNLDVDQFLIDYTLSIESSLLR
>NZ_LS483439.1|WP_012242970.1|1053128_1053590_-|hypothetical-protein
MKNELKNELLKYLDGIRVKAKDDKDNYPDYMIKDKVKMDKLLIELLKSSQDVFMSKKSLFEYLSKIDDYIREEIDLLNPPTPVYNDLIVSVFENLMIASVIDDYELSYSYLKNAKEYMHYIRKNFALYLDTSIFPLELFRDLKPILEVMKNKG
>NZ_LS483439.1|WP_012242969.1|1052160_1053105_+|L-lactate-dehydrogenase
MKNRVVIVGTGFVGMSYAYALLNQGTLEEIILVDIDSRKAEGEAMDLNHGLAFAPRKMLIRSGTYEDCKDAKLVVITAGVNQKDGETRIDLLNRNAKIMQSVVKEIMKHGFNGIFLVATNPVDILTYIVWKSSGLPSNRVIGSGTSLDTARLRYEISQYINIDVRNIHAYILGEHGDSEFVCWSNAFVGVKPLKDVIDSMPAQIKFSDLDKIYLDVKNSAYEIIQRKRATYYGIGMALVRITKAIFNNENRILPISVFNDDDYDIDNLYIGLPAVLNENGVDHVVKLNLNDEELKSLKKSSSILKHSIDSITLE
>NZ_LS483439.1|WP_012242968.1|1051246_1052056_+|YwaF-family-protein
MKYLLDLLNSDMIKPEAYQSLSKSWFHYLSLVITILVIIKLTKTFKTADDIKLKRMLLVFGIVMLILEIYKQIIFTYQVNAYQWYAFPFQFCSTPMYLFVIYGLNKNKKVDQYLLSFLATYSTFAGIAVMLYPADVFIETIGINIQTIVHHGLMAAVGFSLLLTKAKISFKYFLKGSAVFSVLMVIAMIMNWVFNMQGIDATFNMFFINERFGSHLPILMDIEPLVPHLAFLAIYLFGFSFVASIIFMIGYLFRTIIYKEKYKLIDLFQ
>NZ_LS483439.1|WP_012242978.1|1063752_1065063_-|phosphoglucosamine-mutase
MKNNYFGTDGIRGIAFEKLNSKLAFKLGQAIAKKFSPSEIIIGQDTRLSSNMLAYGVAYGAALAGVNVKIAGVVSTPMIAYYSKVKDIIGVMITASHNPYTDNGIKVIKSGYKMLDEEELNLETYIDDNEVLSSTKLGSIEITHDVEDIYINVYQDLNIPKTSMKITYDSANGANYLISKKVIESFASHTYQIGNRPDGLNINLNVGSTHLESIINAVKSNGSDIGLSFDGDGDRLLVVDKDGTTFDGDYIVYIIAKYLKSKGKLKKDTVVLTQMSNPGMLKAFKTLGIKVLQTPVGDKYVSEEIMNHDLSIGGENSGHIIINDLLPSGDGLFAGVYILKILEEHKTSLKDYTKEVEMYPQKMVNIKNVDKEVLKHPEIIKLVEEVRRNLSEDSLLLVRPSGTEPLVRVTISCQDILELDKYMGLLVTKIQNLGRL
>NZ_LS483439.1|WP_069586341.1|1065052_1066492_-|hypothetical-protein
MNDLSKDTTITAVLRIASSNIIKLTSSILIAFLLPKLLGVEDFGYYKIFLLYATYMGIFHFGFADGIYLEYGGLNYSELDLNRFRIYTRFFIKIQTMLSLIGVTIVLLLVKNEYLILLIMLFIYIPIINLINYFQLISQAVSRFKEYSNRILLLSLLNIVIIAIMILMNISNYKVYILFLIIINFIILIGYFYTYRNIIVKPDHPILIKKREYFNLFKIGIPLLLANLTSTLVLTVDRQIVEIFFDLVDFSVYSFAYSMLAIITTLVSAVSIVIYPILKNVDKSNIQTTYSKLIQLIVIFVMFSLTAYFPLKWIIPKFLPEYSESLTIFMIALPGLMISSSITAIKHNFFKVLNKNNHYFYIAILSIIISIILNLIFYYVFLTKEAIAVSSVISLFVWYIITELYMIKFYKVKWKKNILLIIFSGGLFYGLSNLQNYIIFGFIYFTVVSLIIVFNYRSKIKRGYRSLLKKRNWCDKYEK
>NZ_LS483439.1|WP_099750384.1|1066484_1067579_-|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)
MVVFGTRPEAIKMCPLVNELKSRNNFITKVCVTGQHKQMLDQVLESFRIEPDYNLHIMKENQTLFDVTINILDKIKEVLDYEKPDLVLVHGDTSTTFVTALAAYYNQIAIGHVEAGLRTNNIYSPFPEEFNRQAVSIIARYNFAPTINALQNLMRENIDRSTIYVTGNTAIDALRTTIKQDYKHPIIDWAKGSKLILITAHRRENLGEPMRHMFNAINRIVSEFEDIKVVYPIHLNPIVRNLANEIFSNNARIRLIEPLDVVDFHNLMNASHLILTDSGGIQEEAPSLGKPVLVMRETTERPEGVEAGTLKLVGTEEKNIYDSFKLLLTDVNEYQKMAQSNNPYGDGFSSKRIVDIIEKNFWSE
>NZ_LS483439.1|WP_012242981.1|1067629_1068739_-|EpsG-family-protein
MNPNNILINRNDLKNLLLVILILILGVGVTNNFDYEAYSMSYSNLIETNFEKGYRFIENFFYSKGVHFNLFKAIIIGTSIFIILKLSNRYLPKKSKYIYYIIFMIYPLSFFAYSLRTTIATAFLYIGIILLIEKVRFSNLLFILLIYLASLFHISIVFFGIYLIIPILTKFINNRKDILTFNLVFTVIISLMIILSLNEVLLQYFIDLIWGLLSGIFNISSAKEDYITISGNYGYLLFVISNVLFFITFIIIKNYILKYKYTELDKLESNKKKYIFIEYAYLISLILFFLAPLLKVNTEFSRIYKIIFPIFISASILGVSIMKRCKERTIVKILIVITTVYCFIIYVLPYFHDILLPMITDNWIFTKLK
>NZ_LS483439.1|WP_012242982.1|1068725_1069892_-|glycosyltransferase
MKLNNDQFITKIAVFPGVFLNGGVEYVVEEIFNSMRDKNIVYDIYVSRNYEGPKDKQLIAKGVRIFYIPEMKNLNPLKYIRLIRKMLKSNGKYDYIHVHSIHSGVLNSIAGYFAGIKNRIYHVHNTSDPLLKGLRFPKLYRFVSTRMIRMFNNKYIACGKDAGIYIYGNKLVMKKVLILKNAINLEIFKPIHTTKYRKIALDRNDNTVFIGNAARFTEVKNQRFLIELIYEANLNGDYRLLLAGDGELKDIYEKLVSELNIKDKVYFLGNITDMNLFYNSLDVFILPSLHEGLPLSLVESQSCGIPSIASENITEEVDMGLNLMTRISLTEKKNKWINQIDRVISIDKPKLEDIAKGIRDKKYDLDSFKDQVLTIYKLKVEGAKHESK
>NZ_LS483439.1|WP_012242983.1|1069878_1070952_-|sugar-transferase
MSKIVIITVNNLYLTPYINNYTKHIATDFDIIYWNRDEITESSSAKNVFGFIGYINPKQSKLKKIVMYLKFRKYVKKILKSNKYEKIIFLNTMSAVLIGKNVGAKYIVDIRDYTFEHNIFFYNIEKKVIKGSELSVISSEGYRKFLPKHEYILVHNSQQLEDLPKKTNDKGKLTEIRPIIISFVGLIRFFEISKKIIIELKNDPRFKLNFIGKGSEMLRQFCISENVTNVQLISKFESNETMRYFEECDIVYNLYGNDNPSVIYALSNKLYYAAFLNKPILVNPNTFMYDISFKYHMGISVNLDSRTIADDIYEQFINLDFSTLKKGCDDFMNHVKIDNTNFDLKVSRFIGDENEIE
>NZ_LS483439.1|WP_012242984.1|1070944_1072075_-|UDP-N-acetylglucosamine-2-epimerase-(non-hydrolyzing)
MKKLKVMTVVGTRPEIIRLSAVIKKLNESEAVEHVLVHTGQNYDYELNEVFFKDFNLKKPDFFLNAATGTAIETIGNILIKMDPILEEVKPDAFLVLGDTNSCLTAIAAKRRKIPIFHMEAGNRCFDQRVPEETNRKIVDHIADINLPYSSIAREYLLREGIPADRIIKTGSPMFEVLMSKIDEINSSDVLSRLNLEKGKYFLVSAHREENINSSNFEKLVDTLNTIAETYKLPVIISTHPRTRKMIESKGVTFHPLVQALKPLGFIDYNKLQIDSKAVLSDSGTISEESSILKFRALNIREAHERPEAMEEAAVMMVGLNKDRIMQGLVVLENQFEDTIRYVSDYSMPNVSEKVLRIILGYTDYINQNVWRYKNE
>NZ_LS483439.1|WP_012242985.1|1072076_1073186_-|capsular-polysaccharide-biosynthesis-protein-CapF
MNILVTGAKGFIGKNLIAELKNQKFENIYLYDIDSTESELDLYCQSADFIFHLAGVNRPKDEKEFELGNFGFTSTLLDKLKRYNNKAPIMISSSIQADLDNPYGKSKKAGEELLFQYGKETGASVFVYRFPNVFGKWCRPNYNSAVATFSHNIANNLPITVNNPEHLMNLIYIDDVVKELISCLNGKPKMEGKYCKVLPVYEVKLGKIAELLYEFKESRTNKSIPNMMDGFTKKLYSNYLSYLPKDQFSYELKMNKDHRGSFTEFIKTIDRGQVSINISKPGITKGNHWHHTKNEKFLVVSGQGVIRFRDINSTEVIEYFVSGEKLEVVDIPPGYTHNIENLGTSDMVTVMWANEQFDPNNPDTIFVEV
>NZ_LS483439.1|WP_012242986.1|1073193_1074207_-|polysaccharide-biosynthesis-protein
MSDFNKDLKGKILLVTGGTGSFGNAVVSRFLSSDIKEIRILSRDEKKQEDMRKFYNNDKLKFYIGDVRDYNSIEGAFIGVDYVFHAAALKQVPSCEFYPMEAVKTNVVGSDNVITAAVKNGVKKAIFLSTDKAAYPINAMGMSKAMMEKNVVARSRQLRENDTVLCLTRYGNVMASRGSVIPLFLDQIEHNRSITITNPEMTRFMMTLEDAVDLVLYAFEHGEQGDLFVQKAPAATIDVLAKAVLELKQSKMEPVYIGTRHGEKLYEVLVTQEEMQKAIDLEGFYKIPADNRNLNYDKFIEKGSKALELSDSYHSHNTARLDVEGMKKLLLKLDLFK
>NZ_LS483439.1|WP_041634170.1|1074208_1075408_-|glycosyltransferase-family-4-protein
MFDKTILVLTILKIDFNLNKSLYSDLYFELSKNANVIVLSLTDNDNQVTKYSESLEVHNIKVSSSFQKSKIKKAINLLRLNTKLLRYVKSNLKDTTIDLVLYSTPPITLNKSIKYIKNHYHAKTYLLLKDIFPQNAVDLGMFSKKGLIHKYFRIKEKNVYNLSDNIGCMSQANLKYILNNNNIDKHKIEINPNSIEINQIIEISSHQKQEVLDTYGIAKDKFKMIYGGNLGEPQGIEFILKVILENENHNNIITIVGSGTQSNRIKKFIVDNNLVNTVFIDKLAKDKFDLLLSACDIGLIFLDARFTIPNFPSRLLSYLEYSKPVIAATDLNTDVGETIKNGGFGYWCESKNTDDFFKLVEKMKIENINNQFGKTGRIFLEKYYNVDNSAELILEKIEV

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Crispr_ID: NZ_LS483439_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483439_3

1174458-1174565

Orphan

Consensus_repeat	Method
ACCTGATATACCACCAATATAGTTAGTACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LS483439_3

>merge|NZ_LS483439|3|1174458-1174565|CRISPRCasFinder
ACCTGATATACCACCAATATAGTTAGTACCTGTAATATGAGCTAGGTTATAACTATTTTCAATGATTCCATAGTTTCTACCTGATATACCACCAATAAAGTTAGTACC

>NZ_LS483439|3|3|1174458-1174565|CRISPRCasFinder
ACCTGATATACCACCAATATAGTTAGTACC	TGTAATATGAGCTAGGTTATAACTATTTTCAATGATTCCATAGTTTCT
ACCTGATATACCACCAATAAAGTTAGTACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483439.1\|WP_012243063.1\|1186122_1187079_-\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_LS483439.1\|WP_012243051.1\|1145654_1146350_+\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_LS483439.1\|WP_012243071.1\|1194475_1194685_-\|heavy-metal-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|238219
NZ_LS483439.1\|WP_012243070.1\|1193723_1194383_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|132880
NZ_LS483439.1\|WP_012243068.1\|1192822_1193197_-\|SHOCT-domain-containing-protein	unknown	unknown	gnl\|CDD\|378276
NZ_LS483439.1\|WP_012243057.1\|1151884_1153378_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224319
NZ_LS483439.1\|WP_012243065.1\|1189414_1190305_-\|Ppx/GppA-phosphatase	unknown	unknown	gnl\|CDD\|274735
NZ_LS483439.1\|WP_012243059.1\|1154650_1164913_-\|cadherin-like-beta-sandwich-domain-containing-protein	unknown	unknown	gnl\|CDD\|378939
NZ_LS483439.1\|WP_012243066.1\|1190429_1191113_+\|SHOCT-domain-containing-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_041634953.1\|1184119_1184959_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_LS483439.1\|WP_012243069.1\|1193211_1193646_-\|SHOCT-domain-containing-protein	unknown	unknown	gnl\|CDD\|378276
NZ_LS483439.1\|WP_012243053.1\|1146985_1147573_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370431
NZ_LS483439.1\|WP_041634951.1\|1147657_1148656_-\|putative-sulfate-exporter-family-transporter	unknown	unknown	gnl\|CDD\|225411
NZ_LS483439.1\|WP_012243052.1\|1146394_1146826_-\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|223894
NZ_LS483439.1\|WP_012243055.1\|1148796_1149936_-\|C39-family-peptidase	unknown	unknown	gnl\|CDD\|379241
NZ_LS483439.1\|WP_012243056.1\|1150045_1151875_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|373999
NZ_LS483439.1\|WP_012243058.1\|1153377_1154637_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483439.1\|WP_041634249.1\|1191163_1192762_-\|bifunctional-diguanylate-cyclase/phosphodiesterase	unknown	unknown	gnl\|CDD\|238923
NZ_LS483439.1\|WP_012243050.1\|1144400_1145528_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173847
NZ_LS483439.1\|WP_012243064.1\|1187247_1189374_+\|AAA-domain-containing-protein	unknown	unknown	gnl\|CDD\|274529

Protein	Function_ID	Function_description	E-value
NZ_LS483439.1\|WP_012243068.1\|1192822_1193197_-\|SHOCT-domain-containing-protein	gnl\|CDD\|378276	pfam09851, SHOCT, Short C-terminal domain.	5.95252e-07
NZ_LS483439.1\|WP_012243051.1\|1145654_1146350_+\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	7.6999e-45
NZ_LS483439.1\|WP_012243071.1\|1194475_1194685_-\|heavy-metal-associated-domain-containing-protein	gnl\|CDD\|238219	cd00371, HMA, Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.	5.20475e-16
NZ_LS483439.1\|WP_012243070.1\|1193723_1194383_-\|hypothetical-protein	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	1.05459e-07
NZ_LS483439.1\|WP_012243057.1\|1151884_1153378_-\|hypothetical-protein	gnl\|CDD\|224319	COG1401, McrB, GTPase subunit of restriction endonuclease [Defense mechanisms].	1.58754e-10
NZ_LS483439.1\|WP_012243065.1\|1189414_1190305_-\|Ppx/GppA-phosphatase	gnl\|CDD\|274735	TIGR03706, exo_poly_only, exopolyphosphatase. It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds].	1.93855e-65
NZ_LS483439.1\|WP_012243059.1\|1154650_1164913_-\|cadherin-like-beta-sandwich-domain-containing-protein	gnl\|CDD\|378939	pfam12733, Cadherin-like, Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.	7.73194e-08
NZ_LS483439.1\|WP_041634953.1\|1184119_1184959_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	1.97405e-21
NZ_LS483439.1\|WP_012243069.1\|1193211_1193646_-\|SHOCT-domain-containing-protein	gnl\|CDD\|378276	pfam09851, SHOCT, Short C-terminal domain.	0.000409798
NZ_LS483439.1\|WP_012243053.1\|1146985_1147573_-\|hypothetical-protein	gnl\|CDD\|370431	pfam09323, DUF1980, Domain of unknown function (DUF1980). Members of this family are found in a set of prokaryotic hypothetical proteins. Their exact function, has not, as yet, been defined.	0.00115616
NZ_LS483439.1\|WP_041634951.1\|1147657_1148656_-\|putative-sulfate-exporter-family-transporter	gnl\|CDD\|225411	COG2855, COG2855, Predicted membrane protein [Function unknown].	2.01541e-69
NZ_LS483439.1\|WP_012243052.1\|1146394_1146826_-\|acyl-CoA-thioesterase	gnl\|CDD\|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	1.32223e-31
NZ_LS483439.1\|WP_012243055.1\|1148796_1149936_-\|C39-family-peptidase	gnl\|CDD\|379241	pfam13529, Peptidase_C39_2, Peptidase_C39 like family.	2.73217e-21
NZ_LS483439.1\|WP_012243056.1\|1150045_1151875_-\|hypothetical-protein	gnl\|CDD\|373999	pfam15665, FAM184, Family with sequence similarity 184, A and B. The function of FAM184 is not known.	0.00101008
NZ_LS483439.1\|WP_012243063.1\|1186122_1187079_-\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	1.80729e-173
NZ_LS483439.1\|WP_041634249.1\|1191163_1192762_-\|bifunctional-diguanylate-cyclase/phosphodiesterase	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	3.02257e-89
NZ_LS483439.1\|WP_012243050.1\|1144400_1145528_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	3.46286e-98
NZ_LS483439.1\|WP_012243064.1\|1187247_1189374_+\|AAA-domain-containing-protein	gnl\|CDD\|274529	TIGR03346, chaperone_ClpB, ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization].	0

>NZ_LS483439.1|WP_012243059.1|1154650_1164913_-|cadherin-like-beta-sandwich-domain-containing-protein
MKYKRIIALMFIFLATIIMNIQSTSAVSAKMEIYFEIGGQKNFTKAYLDQQYFEDPYDGDVVRADIYAVSLTGSTERLTNIQFDFSSNSKLQGISYVETLGTYVPFAGGRPENWFDSGTLNNSVILATSGGADASITTTPVKLATVLIKYNKNDPAENLEIEMIMEAASWDSGTIEYTGTDISLASIIIGDPNSTPDATLSALNITGTTTSKVYPFNVSATEVEGKITQNITIDYQDSIGGLTINPVFTKTSLGSSNYVKTESKASTNYQTGDTITITTTDGDATKIYEIKLTVSSESTNTGIELKLAQGDLGTITFNSVDNRYEIVTPFTENDIKILATTAYPFATLDKNEIRVTNIEQDVFTHIGDFNVTAENGSTTTNYPVYVKREKGSSDANIKIITNEYPQGLAPVGNVFTINYPHTKTSLSFQIAKNQTGQTIKYKEVGTTTYKDYTTGIISKSSLETGETYSYEVVVTPESQFPDEVVTYIVNFVIEPSNDTSIKTGDIKVQESGLTAINLNITNLVYTVSNNSSEFVTLTIDPGSKREAKIGEGTYQSAQLIHQISVASLNYGTNNFILTIKAQDGTEKEYTIKIEKKSDQAELESIIFRTDDGTVIANLDDFTFISSENKYTYSFDYGLFPSNLKLETKTSTKSIIKGTTTNQLITPLDFSGMYEVIKTTSLEVTSENGAVVKNYTIQITRTAADSNNDISAINIGGLPFSQFQIGDSNVTYNKVIVEPVGGINTLNFEVLLPTTSKATIKVGSTTFTKNETGRYSTNIPFVRGIEQNVTIIVTAQNGEKNTIIIPFVVATNDTTLKSLNIEGTDFVFDPAKLNNTININYSFNSNVTITASPQNVDSKVYIDGQVRINDTYVKAIGNGTTTFKVWVESEAGTKGSEYVINIVRAQAKTDNSLESFVLKTNNGEIIDLSFLSSKTNYTVTIDDRDELWPLIYSAEVNEQNYAYIGTKGTTSLIDQQFNVLSGATSNLTIQVYSEGGVLKTYTISIKRANDVKTFESVTVSGTGFVTQTFTAQEFISGVLDIGNIAYNVDRLNITFNMVDGSKSMITSNFIGDNQTGIWLFSKTGVIEGQFRVKSQAGNFGEYLKIRVNRQVAQSHKNLDDLEVMVNGNNILLDFDPTTNTYTLRVDRQVNTVTFVATVLSSDRSSVQTPFSLTDTSGLNHRYTYTYNLNDPAAQPSNVIDIIVKAEDGTSNTYKVTIWRKNVEIGIDNIVIKNGSTVIYTGDILSVPNLGEFDFQTNQLTFIVTPKDRFARISFNGGTTLFADEDGLITYTHTLVVGTNQIITLRIQSDLLSTEYAAEAKSQNYNFTYTRKAASTLAELDSLEIIVGGINLLDGVFDSSIIRYEGEYLRVDRTHMSVQISAVGKEFSTVTGLGIKEIKPGITNSYTITVTSQSGTHSKEYTVYIVSKNDDHEINNIKGNSNDIGFIDSEFEYTLDNVLYTVSSLPIHVVLNDTFANYYVNGVKNATSIPLQYGNNIIEIYGESEYGTKSGNTYRLNVYRNEPYKDTDISSLSITNISNSQNITYKADGTNYLVELPDTSSISNVKVDIELKNTDKQVLESTFNLSNIVLTYNGEGGLDQTITFKVSAEDNSTKTYQIRFVKNIVLSSDNSLSNVSIKNQDNQVVTFPFDELLANNSVVLNLPYSQKSLNIEITPTHNKAQVTPNKLNNISLVVGENTFEFSITAEDGTVSDPYTITIHRQAASKEINLNNLTVTDPLNSGLYLLGLDTLSPKGITFNPTTKTYNIKLDETYINEEIIINIVKGHIAQTITGPINAPLTLNHGTNRFEIFIKAEDETVTQGKYTIIIEVLYKSNSLQSLTVDGKALTVQDVNYFDTEKESVTITPVLTHQAHGSFVIKDSLGNVVTNTPNLNFDENVFTIEIKNEYGEIVKTHTLEITRLKSSEKTLSNVSLIGSNGTNYITFDPLTLTYTVEVPQNVEHVTLGAIIPAKATATGLGKYIINLDETITITFKVTAEDGSESEIYTIGVTRRALSTNNHLEEISIIDTLDPTNYLIGISGKNPDIVFDKTTNNYVINLGLEYLDIKYRNLIIRYVKSDTYQTVDKTNPSTLTLNKGANVFVVTVLAEDSINTQPFIYTITINVLNKENDLKHLTINGDVQDTSSNEIHYTTEEEQANILSESLFNDGSIILKDKVGKVITSPLNLEMGENKVSVEVLNAYNEVVQVYEVIITRLASSDNEFTATLTGTSGAQLLNFDKDIETYNINVDYLTTEVTLAIVKNAKATSFGEGVYTLVSGETKEITFYVEAENGDVSPLYTVYVTRLFNTEDKLANLGIKTNLEDLLTTANFDPENNLYQFSLNEYHTNVTFSYIANYGQTLSGTPFNVAQPLTHGLNVFEIEVQPEDLAIEAFIIRVEITIINSEINLQNLFIDGVDRLLPGESIIRLEDVSSDKKTLDIEAVLTDLYGTVKINGNLSEHFILDILPGENTIKIDVTSEDGSTTKTYTVLVKQLLDDLDTLDNILVKTQDNLYLLGDASVNPQIVFDALTNTYKFVVNETVEHIMIDVTNASTKQTVTGDLRIPLNIKHGINRFEISVQPEDLNKPARTYLIEVEKVNDEILIDQLLVGQTDIYEEGVLDYVMDSVTNDQKTIKVIPMISNFGTYVIYDTEGNLVQDHDVNLSFGQNTIRIVFTSESGKTTKTITLTIEQTYSSDNQIIDVRFFDASTNINRLNFDPEITTYDLEFPASTTIARLRVETHNKALVFINGVQEINTRKDFNLTSGNTITVKFYVIAENGDKGIEYTINVYKRKATDPVLSDNTNLLDVTIEIPINKLIFDFDPTIYEYNIQLPFGHDEMYIKGHTESKAATVFGEGAYALIPGLTKVIRLRVTAEDGTVAEKEYKFNITRALPNTDTTLKTLVIEDVNGNILAFDQSIFNPENRTYNITLNDDMKLNTVHVLAEKNHETQILYNTGIIQLHGEVEGYYNTIITVTVVAEDGSIGEYIIYVLHDLDFASLAEVKDISILGDDGISYFGLEFKNNIYVYEDILVPFNVDTTRLIVQTIGNVIYLDASNTEIEDNRLQSFGVGSQIVYRFRIESTNGSNTSEVYTIYVNRQLPDTNSLLETLEINGEMVRGFNPDIFEYTIVHPLQFEKYLDIYGVAQSDNSTVKGNDVYTLIEGQTRTITIEVKAQSGDVSSYKLHISYVNSNALLGELTVYEMIGEHDIQNTIPLLDDTLEYTIIIGKHTRYVNIKGFAKDQGGASIRGFGIREIGSEDTVVHITVTSGDGLEELTYVLTLRRDTSLSNLKEITLLQINNEEVITSDENDPFVYKYSLSNGTQSVKLNAVANNSSKVSINGSDFSTNNMGEIILTDIQESQVIKISVQAEDGSIQHYMVIIERVQQPSLLLTILLIISIILWVIAAMTYILKRIRKNNKKDKNQLIF
>NZ_LS483439.1|WP_012243058.1|1153377_1154637_-|hypothetical-protein
MNELQKSLISLGAIIIVLVLVYLSIHYYLKSLKKMKKHKMLTLNLVIKYKLFLEYLAYQEKKNHTFYLYLVKINNLSLVEHTYSDHTVRNYLTHIAKELSVYLPFGGKLAQTNQRDTFIVYYPSMDEDKELLGKQFKLLAQKTYHENGIHITKTASVATIDSFDLKALSSTLISSIKHLGAVTSHDDMVKEDYETYADLINKLKQVELELKTYQVETLKIKKTNEVFNELLINGSKLDVFLNKLPVSDMSWVNMMLVEMILNKLYHENIYANINIPVLLSTLEQETFIEYLQTIVKANQFLLENVILSIRLSNVTYEDELIKNILTLSNLGVKMSMHVDEIHQGLYLALQRYHIKRLEIDDKVMEHDMIAELLYFAKVNHIEVLYKTEKSIQDGSLLNVSHITKERLQFKADKQKRGRR
>NZ_LS483439.1|WP_012243057.1|1151884_1153378_-|hypothetical-protein
MDHFSNWVVEFFKTFFLDLWYLISGFFTGIYNLFIGYPIEYYHYLMDKSINFNLIDWILSIGFIIIFILLYVMTWLIIVQLVKRYFRFAKIEFDKMTLLNQMNMLERKVRDATVIHVEGPKLNLNDSKGKPKLATGSRFTKLNLIDDKYKYTVLPTLMTNKDKLSLSEIVTHFINYASSHHNIYYSEKIASTFIAGLATSKILILEGISGTGKTSLPYVFGKFIKNDASIISVQPSWRDRFEMMGYYNEFTKKFNETEFLTSLYDASYRTDINLIVLDEMNLARVEYYFADFLSLLELPNSDEWLIEVVPEQLIGDPMHLKEGQLQIPKNVWFIGTANNDDSTFGITDKVYDRASSIVMNEKAKPFKGQMLDRINISYDYLDELFKTAYKEHEISNKNLVALEKLDEFISETFQITFGNRIMNQLYKFIPIYVACGRSEIEGIDYIIARKIIRKFETLNLPFLKNELETLLQLFDQLFGKNQLKESKDMILKFIKQI
>NZ_LS483439.1|WP_012243056.1|1150045_1151875_-|hypothetical-protein
MNNKERIKFFQEELSKSIDIVYDTGYYPQILKPLSIQDKDLIKHLDKLEYKKFDEDWIVKIESFFPSLNQIISNIRNTLKYEEEILPVERTRRTSNESVRHILRNTKYIKDINEDDEVYPSKVLNTVSELDYGIYENRLIMTLIDRLYHYLLKRIEAIHTHIHGYKQTNFNLENEFKLGNSVYTLNFELNAKETFDSGEVDLHNKRILERTEAAFKVVSRMFHSDFMRIMSRYKKVVPPILKTQMIQKNADFRNAYTLWLYLDRLNVLDFTLQLQEASKALSDTSIDDIDKGLMALFTSVFVHSDMGISLLDSKDVSFQSLTPIKGDAETYVERVNVTIPEMVLEANLATEYHLEKAKQLMSRKELANLVIDNNPENTNYLKQVLLDQYSIADQIFNAYLKLNQDDDVFSQLLTYKHPVKKYEEALNRYLMTKAARQVKEKLFTDAVLLEDKWINLLTELQEDAIESIIKSGEKHDETLIQNMQKEVNKTLKALEKAETSKSKKALQDQRIKNNKAIKDIQDKYQAEIKTYREIQNKRMKAEKEKIALKLTQEKLRIKEREALKRKQEREKLVKEKQLKLKKLKEAHQKLKQSIKSNVTKTLTDYKNKK
>NZ_LS483439.1|WP_012243055.1|1148796_1149936_-|C39-family-peptidase
MKRYVITILTILLSSLLTACSLGDSNTDEEITDEPVIEEPIEVKVDGTKTIYADELWYVKEEAAIINLSLDSNKSIVLEDAAQQATYESEPIEVNHFNELVLSWNVKNLEDARITFFIALGDGTDFGSYQIMGLFKDENHMSFNSLDDPYGRVSIDTLINKDPSKNNYIKLKFTVIAGSADQLEIKNISVTTKSVDSALTYDASKLTNKVIDVAPMQQLSIPNIGNVICSPTSVAMVLNHYGYTFTQQEMAKKVYDNSKGIYGNWTFNASYAGSLDGIAARVEYIEDFSVVIDYILNDIPVVFSISTTSADQLNGAIMAFPAGHLVVLKGFEEINGVWHGVFNDPAEYEDSKVERKYPMEQVLKVWRQYTYIIVKSETI
>NZ_LS483439.1|WP_041634951.1|1147657_1148656_-|putative-sulfate-exporter-family-transporter
MKKYAPGVLVSLMIAGVSLAINNVLPVDLIGMALIALLLGMLLNPLLHKYDVLDSGIDWSAKYILRTGIILAGISLSFSQVFEAGKYALILLGFTFLTAFGVGYICRKLFKIDWKLTSMLSISTAICGGTAVATLGPVIEADNKDIAYALSATFIFDLLTVIVFPWIGVFLGMTDTTFGLWVGTAVNDTSSVVAAGYAFSELAGALATIVKLTRTLFIVPIVIIFSYIYARKNQNQGVSKINQKVNILAIFPWFILGFIAFIGVRSLNILSDDWVLSISSISKFFMATALGAIGLKTSFKEVTSVGVKPMMVAVIIDVSVVIVSFVVLSIMF
>NZ_LS483439.1|WP_012243053.1|1146985_1147573_-|hypothetical-protein
MHKLKELAKEDLKDITKTEKIKYAAPIDHQSFKMVAYIFMGLMIVNLFIFFLPFVDFEGGMSSSDTGYLVITWFNTSFEEGPIIALCITAIFIITIITLSLLIYTFISQGEITKAIAYKYMKKFNYVYIALVLILLIIVFNLIEAMRFRLSGEIYELPYPGIGLHMLLWVNMIVPILLGFIFKVISAKNQDNFIP
>NZ_LS483439.1|WP_012243052.1|1146394_1146826_-|acyl-CoA-thioesterase
MRSIPKLNLNEFPYITHDKLRYGDTDKQGHVNNAVFTTFYETGRVEIVYEPKHHILNENCSFVIAHIEMNFIAEIHWPGKLEIGTGITKIGNSSVTFLQSLYQDGKLVSTSESVLVQVNNDTKKSEALSEDSKNRLEKYMMNR
>NZ_LS483439.1|WP_012243051.1|1145654_1146350_+|Crp/Fnr-family-transcriptional-regulator
MEEKKLHPHNCIDRLELFNTLTSEQRQLVFKLIEHRHYSAGQMIYSPGESAGSIHIISRGKVRIYRLSESGREQLIRLLLPGEFTGELALFKEGIYEAYAESLEDTKICMIHHDDFKNLLKSYPAISVKMLSVLAKRLSISEQQSTWMSTETSKERLINFLIRSATLNKQGEMVVYLPMPKKDLASYLGTTPETLSRQFTILKKDGVITQSSKNYVKIHGLSHNDITCEIC
>NZ_LS483439.1|WP_012243050.1|1144400_1145528_-|acyl-CoA-dehydrogenase
MSVVLKEHQQMLHQMVVDFSRKEIKPLDMVIDKQKGYPKTLWDKIVETGFLGLIVPKEFGGADFDPVAEAQTIFDVASNSASVAFTLEGHYKTVDQLKKYGKASLKEKYLPEANKRIFGFGSTEPQGGSNVMGHTASAVKEGDYWILNGNKTMITNGGLAEVYLVLLKTAENELTCFLVDKDMPGFKYGKQEDFFGMRGTPVGEIFLENVKVTDEYMLGKIGEGVMIGDSAHYDARINMGAIAAGICQHALDIVLDYATERKAIDKPIIDLFSIQNKITEIAIAKENTQLLYEEAAKLKSQGKPYDKVSTMAKSYGSRAAFTSCDHALQVLGGYGYSNEYPVEHLLRDARALQIAEGSLEKMVIEIAKSVQMERV
>NZ_LS483439.1|WP_041634953.1|1184119_1184959_-|AraC-family-transcriptional-regulator
MDWIKQLNASIEYIEKNLDGSISSQQLSEIMMCSFENFQKVFSYISGKTLGVYIRERRLSKAGIELLESNEKIIDFAIKYGYSSQDAFTRAFKTFHGCLPSEVRKNIVQLNLTPKLSFQIKIIGEEQMNYRIEELSGFKVYGKEFDILTENAFEEVPKMWKTVKKDGTMETLMGMITNLKPCGILGIAANGQWGKSREMKYIVGVTKEDDPQVDNFKAIDFPKSTWVVFNVEKKVHVKKTYQDFYSIWLPNSEYKLADLPVIEAYGADNTQEIWFAIHK
>NZ_LS483439.1|WP_012243063.1|1186122_1187079_-|rhodanese-related-sulfurtransferase
MQKNYRVLLYYKYTAIENPEKFKDEHLAYCKSQDLLGRILVSSEGINGTLSGTFEQTENYMDYLKSLQGFEDIFFKIDEVDAHAFSKMHVRVKKELVNLSLEDDVNPLEITGKYLEPIEFYQKLQDPNTVVIDARNDYEFDLGHFRGAIKPEIKNFRDLPDWIRENKDQFKDKEILTYCTGGVRCEKFSGWLIKEGFNVAGQLHGGIHNYGTSKDTEGKLWDGKMYVFDERIAVDINKHEHVVVGRDYFTNEPCERYINCGNPECNKQILASEASEEKYLGSCSHACRIHPNNRYVKKHNLTTDFVLQHIASNLETQI
>NZ_LS483439.1|WP_012243064.1|1187247_1189374_+|AAA-domain-containing-protein
MQFNPMDDYSKDPDILKKFGRNIVELVKEGKVDPVIGREEEIRRIIKILSRKTKNNPVLIGEPGVGKTAIVEGLARRIVDKDVPLSLQNKIVYELDLAQLVAGAKFRGEFEERLKDVLNKIKESDGQIILFIDELHNIVGAGRADGAMDASNILKPMLARGELHCIGATTLNEYRLYIEKDSALERRFQKITVTEPTMEDTISILRGLKDRFEAHHGVHISDGAIIAATNLSARYITDRFLPDKAIDLIDEACASIRMEIDSMPVELDDVQRKILQLEIEKSALSKETDTLSKERLSKIKSEIDDLKLEEASLKSRWEKEKSQLNLSKRKKETLEQLKNELNTAYNEGNYSKAAELQYSKIPNLEKEISELSDTSTDDKLLTETVTPESIAEIVSKWTHIPVTKLVSGDREKLRNLRLSLGKRVLGQDHALELISNAILRHRAGIKDPNRPIGSFLFLGPTGVGKTEAAKALAENLFDSENHIVRIDMSEYMESHSVSRLIGAPPGYVGYDQGGQLTEKIRRMPYAIVLFDEIEKAHPEVFNILLQVLDDGHLTDGQGRTIDFKNTVIIMTSNIGSQYLLENASDAQEKIDKLLKQSFKPEFLNRIDEIITFNSLGFKVQVDITRKLLNELSEKLKEENIYITLGEDVQKYVIKNGFNEQFGARPLKRYIQRDIETFIAKAIISEDVLPNHHYEVIVDNDTLNIKLVS
>NZ_LS483439.1|WP_012243065.1|1189414_1190305_-|Ppx/GppA-phosphatase
MNYGIIDLGSNSLRLEIFTYENHKLTNIFSKREVVGLASYLLPEGYLSDLGIDSVIRVVKDFMEVSQSYKLEKLFMIATATIREARNQNEILTRIKTASGMKVELLDEEKEGYYGYKGVSLNHKIDRGLIVDIGGGSTELSLVTDGKLKDSVSLNLGSLNTYITYVKEIFPTTHEVERISSAVVAALKLHKVDKVDVKVAYGIGGTVQASLVLLQNFYQKKFDKLTRQNIQDLISKIDPTKKKTYLSIIRMIPERIHTIMPGLIILETLMNFFNIEEIIVSKSGIREGYLLEQIQK
>NZ_LS483439.1|WP_012243066.1|1190429_1191113_+|SHOCT-domain-containing-protein
MKKTYNLGLLTGGISLMLALIASFVLQDYFSESFLTLSFTFDTFILIAVAFMLILQFKSFDKIAAIVLVIYGAFNILYGIVGSQTLSDVINSTELEVIFILGLLLGHVLFEIAVLFVLLHLTQQRFEYKFTKKFVIVALSVSLLLLIAISPLVTFMTFQSIIRMVFSIISIIALYFCIQQMVTDTPIVVEAPAKAVPNKRLELSKLYERGIITQEEYQTRLDLIDKE
>NZ_LS483439.1|WP_041634249.1|1191163_1192762_-|bifunctional-diguanylate-cyclase/phosphodiesterase
MQNNVHQDEKKVKSAFRESTEITLAYFICAYAYIWFSDWLILEYVTDPNTAQVIQTLKGFISLGLIGLVYYIIVYRRVKKYLSNNEQLKKVLFELEYQNKQLTTLEEKHFNLAYFDALTGLINRNRLEIKVNRLIQNRTPFALLYLDIDDFGAINELKGHKWGDEALLLIAKELTKVGKEHIVARMSEDSFVLVFYQFEHLDEIKTLADLSINKVKNLMSKQSEAYFYSASAGVAIYPDHGLVYGDILRYANLALSAAKKNGKDQVVIYNTFMHESKEREYEITNAIKPSLQNNEFYVVYQPILDFKSGEIRKLEALLRWNHPSMGYIPPNNFIYLSEISGSILELTHFLYDKVFGQIKTWNEMGKHFTVDINISPKVLMHPTFIEDIGSYIKKHEIDHKQVIIEITESMALENIDQTIIVLKQLKEKGFLVALDDFGSGYSSLTYFKHLPVDIIKMDKDFIAKIDKSPTERHFLKFVLDLSHAMSKKIVLEGVETIEQIDILKLHDVDYVQGFYYYKPLEVSQLNEIILSK
>NZ_LS483439.1|WP_012243068.1|1192822_1193197_-|SHOCT-domain-containing-protein
MNKTFLTVAQVFAIISGVLFIFPGGLLIFPLVLAYFNFKAASVFDKAKKGEATKEQVTNYSIYLIFTSTIGGIFGLLAGTGVSSTDTEPVTVEQKLKQLDGLFDRGVISREEYEARRKAILENI
>NZ_LS483439.1|WP_012243069.1|1193211_1193646_-|SHOCT-domain-containing-protein
MNKTLLTISQVFVAIAAAVIGIYALIFMFVLGQIESDVTFNIVGLVMFIIVGFNIFVFIRIGQAKDNPYMKTEIIIYSIILLLTSNILGGVFALLGVLLEDNGQTQSESSSLEKRLKDLDNLFDKGLITLDEYHERRKKIIESV
>NZ_LS483439.1|WP_012243070.1|1193723_1194383_-|hypothetical-protein
MTLEQVMNDLKLNSNASRKKSLLKAGASENTYGVLLGYLRAYAKKIGTHHDLAFKLMHTLNTDAMLLAVMLFDVSKLSAKEAYDVLGIITFDQVLDDFMFRVVTLIEEVDVLYDMLKDSDSDMLKRALWAINVERVRLKIIDDNEVLYLLDNIQRNLVDETPKAQWMMNRCFAQIGITYEAYRTKVLNLSEELGVYKDMKVAPGCTSAYVPNWIHAVIK
>NZ_LS483439.1|WP_012243071.1|1194475_1194685_-|heavy-metal-associated-domain-containing-protein
MKTTVYIDGMHCKNCMAKVEKSLSTVEGVQSAKVNLDKGFAVLKTKDPVNHDVILDTIHTLGYEVKEIK

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_LS483439_1	1.1\|458702\|31\|NZ_LS483439\|CRISPRCasFinder	458702-458732	31	NZ_CP050081	Rhizobium leguminosarum bv. trifolii strain 31B plasmid pRL31b5, complete sequence	709334-709364	6	0.806
NZ_LS483439_1	1.1\|458702\|31\|NZ_LS483439\|CRISPRCasFinder	458702-458732	31	NZ_CP049731	Rhizobium leguminosarum strain A1 plasmid pRL12, complete sequence	744608-744638	6	0.806

1. spacer 1.1|458702|31|NZ_LS483439|CRISPRCasFinder matches to NZ_CP050081 (Rhizobium leguminosarum bv. trifolii strain 31B plasmid pRL31b5, complete sequence) position: , mismatch: 6, identity: 0.806

gttga-cttagcgaataaactatgatatactg	CRISPR spacer
-tcgattttagcgaatgaactatgctatacta	Protospacer
 *.** .*********.******* ******.

2. spacer 1.1|458702|31|NZ_LS483439|CRISPRCasFinder matches to NZ_CP049731 (Rhizobium leguminosarum strain A1 plasmid pRL12, complete sequence) position: , mismatch: 6, identity: 0.806

gttga-cttagcgaataaactatgatatactg	CRISPR spacer
-tcgattttagcgaatgaactatgctatacta	Protospacer
 *.** .*********.******* ******.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

593806 : 647484

Caldibacillus_phage(13.04%)

protease,integrase,transposase,portal,capsid,tRNA,terminase,head

attL 613160:613176|attR 627072:627088

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_012242508.1\|593806_594934_+\|tRNA	tRNA 2-thiouridine(34) synthase MnmA	NA	NA	NA	NA
WP_012242509.1\|594933_597183_+	ATP-dependent RecD-like DNA helicase	A0A0K2FLP8	Brevibacillus_phage	3.7e-61	28.1
WP_012242510.1\|597238_597982_-	esterase	NA	NA	NA	NA
WP_049751943.1\|597982_598789_-	hypothetical protein	NA	NA	NA	NA
WP_049751944.1\|598928_600122_+	DUF896 domain-containing protein	NA	NA	NA	NA
WP_064211832.1\|600118_601105_+	glyoxalase	NA	NA	NA	NA
WP_012242514.1\|601114_601561_+	MarR family transcriptional regulator	NA	NA	NA	NA
WP_012242515.1\|601557_602151_+	alpha/beta hydrolase	NA	NA	NA	NA
WP_012242516.1\|602219_602669_+	hypothetical protein	NA	NA	NA	NA
WP_012242517.1\|602661_603078_+	NUDIX domain-containing protein	NA	NA	NA	NA
WP_012242518.1\|603074_604217_+	23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD	F5CA72	Streptococcus_phi-m46.1-like_phage	1.1e-53	33.7
WP_012242519.1\|604423_604741_+\|transposase	transposase	NA	NA	NA	NA
WP_081423640.1\|604833_605166_+\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	1.2e-08	35.2
WP_081423642.1\|605448_605637_+\|transposase	IS3 family transposase	A0A2I6AZV9	Macacine_betaherpesvirus	1.4e-06	47.3
WP_012242520.1\|605788_605956_+	hypothetical protein	NA	NA	NA	NA
WP_041633885.1\|605986_607327_+	hypothetical protein	NA	NA	NA	NA
WP_041633889.1\|607386_609591_+	AAA family ATPase	NA	NA	NA	NA
WP_012242523.1\|609742_610417_+	adenylate/guanylate cyclase domain-containing protein	NA	NA	NA	NA
WP_012242524.1\|610401_610929_+	hypothetical protein	NA	NA	NA	NA
WP_012242525.1\|611013_611490_+	hypothetical protein	NA	NA	NA	NA
WP_012242526.1\|611764_612187_+	hypothetical protein	NA	NA	NA	NA
WP_012242527.1\|612231_612609_+	hypothetical protein	NA	NA	NA	NA
613160:613176	attL	NA	NA	NA	NA
WP_012242528.1\|613212_614931_-	recombinase family protein	A0A2K5B2B4	Erysipelothrix_phage	9.1e-92	40.7
WP_012242530.1\|615320_615920_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_041633899.1\|616174_616468_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_145961054.1\|616516_617470_+\|integrase	tyrosine-type recombinase/integrase	A7XX23	Thermus_virus	1.7e-07	23.6
WP_012242533.1\|617492_618239_+	phage antirepressor KilAC domain-containing protein	NA	NA	NA	NA
WP_012242534.1\|618222_618435_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_012242535.1\|618576_619500_+	DUF4373 domain-containing protein	D2IYU0	Enterococcus_phage	1.1e-14	38.5
WP_012242536.1\|619459_619906_+	hypothetical protein	NA	NA	NA	NA
WP_012242537.1\|620001_621489_+	SAM-dependent DNA methyltransferase	A0A2H4PQP4	Staphylococcus_phage	1.4e-43	29.2
WP_012242538.1\|621478_622738_+	restriction endonuclease subunit S	NA	NA	NA	NA
WP_012242539.1\|622742_625886_+	type I restriction endonuclease subunit R	A0A220A398	Liberibacter_phage	1.4e-66	27.9
WP_012242540.1\|625955_626942_+	hypothetical protein	NA	NA	NA	NA
WP_012242541.1\|627270_627795_+	hypothetical protein	A0A2K9V3J2	Faecalibacterium_phage	4.7e-07	31.1
627072:627088	attR	NA	NA	NA	NA
WP_064212048.1\|627730_628942_+	ParB N-terminal domain-containing protein	Q708N6	Streptococcus_phage	9.8e-101	48.9
WP_012242544.1\|629033_629360_+	hypothetical protein	NA	NA	NA	NA
WP_012242545.1\|629337_629772_+	hypothetical protein	NA	NA	NA	NA
WP_012242546.1\|629764_630151_+	hypothetical protein	U5JA61	Bacillus_phage	2.1e-12	35.3
WP_012242547.1\|630147_630453_+	hypothetical protein	NA	NA	NA	NA
WP_012242548.1\|630500_631649_+	methionine adenosyltransferase	A0A2H4PQS6	Staphylococcus_phage	6.9e-88	46.5
WP_012242549.1\|631614_631899_+	HNH endonuclease	A0A126HA81	Lactococcus_phage	2.6e-12	46.7
WP_041633907.1\|631964_632996_+	DUF4297 domain-containing protein	NA	NA	NA	NA
WP_012242551.1\|633005_634691_+	hypothetical protein	NA	NA	NA	NA
WP_064212045.1\|634807_636373_+	hypothetical protein	A0A1S5SA14	Streptococcus_phage	8.7e-41	31.1
WP_064212044.1\|636398_637226_+	DUF2971 domain-containing protein	NA	NA	NA	NA
WP_012242555.1\|637253_637586_+	hypothetical protein	A0A290GJQ7	Caldibacillus_phage	3.8e-07	32.4
WP_012242556.1\|637582_639220_+\|terminase	terminase large subunit	A0A290GJW3	Caldibacillus_phage	2.4e-110	40.6
WP_012242557.1\|639237_639762_+	hypothetical protein	NA	NA	NA	NA
WP_012242558.1\|639777_640992_+\|portal	phage portal protein	A0A290G4I4	Caldibacillus_phage	4.6e-42	31.8
WP_041633917.1\|640975_641170_+	hypothetical protein	NA	NA	NA	NA
WP_012242559.1\|641166_641763_+\|head,protease	HK97 family phage prohead protease	V5USG3	Enterococcus_phage	1.6e-24	39.6
WP_012242560.1\|641767_642895_+\|capsid	phage major capsid protein	H7BUQ0	unidentified_phage	1.9e-61	46.7
WP_012242561.1\|642920_643211_+	hypothetical protein	NA	NA	NA	NA
WP_012242562.1\|643197_643536_+	hypothetical protein	NA	NA	NA	NA
WP_012242563.1\|643519_643897_+	hypothetical protein	NA	NA	NA	NA
WP_012242564.1\|643886_644240_+	hypothetical protein	NA	NA	NA	NA
WP_012242565.1\|644229_644799_+	hypothetical protein	A6M958	Geobacillus_virus	2.9e-26	38.7
WP_012242566.1\|644800_645136_+	hypothetical protein	E3W8G2	Leuconostoc_phage	8.1e-05	36.4
WP_143215669.1\|645342_647484_+	hypothetical protein	G8CLB5	Synechococcus_phage	1.9e-14	29.3

DBSCAN-SWA_2

959183 : 969272

Bacillus_phage(33.33%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012242877.1\|959183_959411_-	helix-turn-helix transcriptional regulator	A0A2K5B261	Erysipelothrix_phage	2.8e-09	44.6
WP_049751954.1\|959677_960202_-	DUF1643 domain-containing protein	A0A2D2W2H2	Stenotrophomonas_phage	6.5e-09	25.8
WP_012242879.1\|960314_960728_-	hypothetical protein	NA	NA	NA	NA
WP_012242880.1\|960755_961040_-	HNH endonuclease	A0A0A8WJ48	Clostridium_phage	9.9e-12	49.3
WP_081423662.1\|961005_961311_-	methionine adenosyltransferase domain-containing protein	A0A2H4PQS6	Staphylococcus_phage	3.1e-11	43.9
WP_049751955.1\|962151_962334_-\|transposase	IS3 family transposase	A0A2I6AZV9	Macacine_betaherpesvirus	1.4e-06	45.5
WP_111724347.1\|962334_962937_-\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	1.5e-33	40.3
WP_041634117.1\|963041_963359_-\|transposase	transposase	NA	NA	NA	NA
WP_012242883.1\|963759_965571_-	ABC transporter ATP-binding protein	W8CYL7	Bacillus_phage	2.8e-51	27.7
WP_049751957.1\|965567_966734_-	ABC transporter ATP-binding protein	W8CYL7	Bacillus_phage	1.8e-35	29.8
WP_081423651.1\|966764_967319_-	ABC transporter ATP-binding protein	NA	NA	NA	NA
WP_012242884.1\|967395_968016_-	SAM-dependent methyltransferase	NA	NA	NA	NA
WP_111724348.1\|968012_969272_-	RNA polymerase sigma factor RpoD	F4YCU2	Synechococcus_phage	1.5e-40	37.6

DBSCAN-SWA_3

1114967 : 1124626

Enterococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012243023.1\|1114967_1115819_-	type II site-specific deoxyribonuclease	A0A2H4JAL2	uncultured_Caudovirales_phage	1.0e-27	33.2
WP_012243024.1\|1115815_1116586_-	site-specific DNA-methyltransferase	A0A249XUJ2	Enterococcus_phage	5.2e-31	36.1
WP_012243025.1\|1116578_1117406_-	DNA adenine methylase	A0A1S5PRR3	Streptococcus_phage	5.4e-58	43.6
WP_012243026.1\|1117655_1118234_+	recombinase family protein	M9Q1K0	Clostridium_phage	1.5e-11	28.5
WP_012243027.1\|1118228_1118609_-	(deoxy)nucleoside triphosphate pyrophosphohydrolase	NA	NA	NA	NA
WP_012243028.1\|1118592_1121553_-	DEAD/DEAH box helicase	A0A097BY72	Enterococcus_phage	3.8e-29	29.0
WP_143224621.1\|1121588_1122731_-	nucleotidyltransferase family protein	NA	NA	NA	NA
WP_049751963.1\|1122745_1124626_-	polysaccharide biosynthesis protein	A0A1V0SAI8	Catovirus	5.7e-23	27.1

Anti-CRISPR protein detection

Acr_ID: NZ_LS483439.1|WP_012242545.1|629337_629772_+|hypothetical-protein

Click the colored protein region to show detailed information

Acr ID

Acr position

Acr size

Homology with known anti

Neighbor HTH/AcRanker

Neighbor Aca

In prophage

Protospacer in prophage

NZ_LS483439.1|WP_012242545.1|629337_629772_+|hypothetical-protein

629337_629772_+

144 aa aa

hit_Aca_id	identity	query_coverage	hit_coverage
gnl\|BL_ORD_ID\|45	0.9791666666666666	1	0.993103448275862

593806-647484

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_LS483439

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

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

Click the colored protein region to show detailed information