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_CP046670	Alteromonas mediterranea strain AltCH17 chromosome, complete genome	6 crisprs	cas8f,cas5f,cas7f,cas6f,DinG,DEDDh,WYL,cas3,Cas9_archaeal,RT,csa3	0	11	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP046670_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_1

529404-529490

Orphan

Consensus_repeat	Method
GCCCTGAGCGAGTATACAGCCATGAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP046670_1

>merge|NZ_CP046670|1|529404-529490|CRISPRCasFinder
GCCCTGAGCGCGCAAAATGCCCTGAGCGAGTATACAGCCATGAGTGAGTCGCGAGCAAAAAGCCCTGAGCGAGTATTCAGCCCTGAG

>NZ_CP046670|1|1|529404-529490|CRISPRCasFinder
GCCCTGAGCGCGCAAAATGCCCTGAG	CGAGTATACAGCCATGAGTGAGTCGCGAGCAAAAA
GCCCTGAGCGAGTATTCAGCCCTGAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_012519942.1\|515513_515804_-\|cell-division-protein-FtsB	unknown	unknown	gnl\|CDD\|179156
NZ_CP046670.1\|WP_141151554.1\|526854_527937_+\|AraC-family-transcriptional-regulator	unknown	unknown	unknown
NZ_CP046670.1\|WP_157317097.1\|528821_529364_+\|RNA-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|234820
NZ_CP046670.1\|WP_071950723.1\|518032_519655_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|223910
NZ_CP046670.1\|WP_071968206.1\|525288_526794_+\|CYTH-domain-containing-protein	unknown	unknown	gnl\|CDD\|143624
NZ_CP046670.1\|WP_012517200.1\|539422_540139_-\|bifunctional-tRNA-pseudouridine(32)-synthase/23S-rRNA-pseudouridine(746)-synthase-RluA	unknown	unknown	gnl\|CDD\|236659
NZ_CP046670.1\|WP_012517189.1\|528030_528708_-\|DNA-mismatch-repair-endonuclease-MutH	unknown	unknown	gnl\|CDD\|179923
NZ_CP046670.1\|WP_157315560.1\|535457_536435_+\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635
NZ_CP046670.1\|WP_157315559.1\|524513_525290_-\|TIGR04211-family-SH3-domain-containing-protein	unknown	unknown	gnl\|CDD\|275056
NZ_CP046670.1\|WP_071950733.1\|537907_538231_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_071950730.1\|534390_535461_+\|response-regulator	unknown	unknown	gnl\|CDD\|381124
NZ_CP046670.1\|WP_071968212.1\|538374_539259_-\|DUF3530-family-protein	unknown	unknown	gnl\|CDD\|378799
NZ_CP046670.1\|WP_071950722.1\|515903_517619_-\|TIGR03545-family-protein	unknown	unknown	gnl\|CDD\|274640
NZ_CP046670.1\|WP_015066174.1\|533547_534381_+\|thymidylate-synthase	unknown	unknown	gnl\|CDD\|234984
NZ_CP046670.1\|WP_071968211.1\|536463_537810_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|341039
NZ_CP046670.1\|WP_071950721.1\|514791_515508_-\|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase	unknown	unknown	gnl\|CDD\|234670
NZ_CP046670.1\|WP_071968209.1\|531914_532721_+\|sulfite-exporter-TauE/SafE-family-protein	unknown	unknown	gnl\|CDD\|376667
NZ_CP046670.1\|WP_071970457.1\|529617_531909_+\|phosphoenolpyruvate--protein-phosphotransferase	unknown	unknown	gnl\|CDD\|182937
NZ_CP046670.1\|WP_012517193.1\|532725_533529_+\|prolipoprotein-diacylglyceryl-transferase	unknown	unknown	gnl\|CDD\|234599
NZ_CP046670.1\|WP_157315558.1\|520151_523949_+\|bifunctional-proline-dehydrogenase/L-glutamate-gamma-semialdehyde-dehydrogenase-PutA	unknown	unknown	gnl\|CDD\|237018

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157315560.1\|535457_536435_+\|diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	8.89058e-67
NZ_CP046670.1\|WP_012519942.1\|515513_515804_-\|cell-division-protein-FtsB	gnl\|CDD\|179156	PRK00888, ftsB, cell division protein FtsB; Reviewed.	4.30224e-38
NZ_CP046670.1\|WP_157317097.1\|528821_529364_+\|RNA-pyrophosphohydrolase	gnl\|CDD\|234820	PRK00714, PRK00714, RNA pyrophosphohydrolase; Reviewed.	1.92619e-101
NZ_CP046670.1\|WP_071950723.1\|518032_519655_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	5.02157e-67
NZ_CP046670.1\|WP_071968206.1\|525288_526794_+\|CYTH-domain-containing-protein	gnl\|CDD\|143624	cd07756, CYTH-like_Pase_CHAD, Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain. This subgroup belongs to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily. Members of this superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). A number of proteins in this subgroup also contain a C-terminal CHAD (Conserved Histidine Alpha-helical Domain) domain which may participate in metal chelation or act as a phosphor-acceptor. The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup have not been characterized.	7.06852e-70
NZ_CP046670.1\|WP_012517200.1\|539422_540139_-\|bifunctional-tRNA-pseudouridine(32)-synthase/23S-rRNA-pseudouridine(746)-synthase-RluA	gnl\|CDD\|236659	PRK10158, PRK10158, bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA.	1.13733e-97
NZ_CP046670.1\|WP_012517189.1\|528030_528708_-\|DNA-mismatch-repair-endonuclease-MutH	gnl\|CDD\|179923	PRK05070, PRK05070, DNA mismatch repair protein; Provisional.	3.40258e-143
NZ_CP046670.1\|WP_157315559.1\|524513_525290_-\|TIGR04211-family-SH3-domain-containing-protein	gnl\|CDD\|275056	TIGR04211, hypothetical_protein, SH3 domain protein. Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.	5.49919e-53
NZ_CP046670.1\|WP_071950730.1\|534390_535461_+\|response-regulator	gnl\|CDD\|381124	cd17593, REC_CheC-like, phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain. This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.75816e-62
NZ_CP046670.1\|WP_071968212.1\|538374_539259_-\|DUF3530-family-protein	gnl\|CDD\|378799	pfam12048, DUF3530, Protein of unknown function (DUF3530). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 272 to 336 amino acids in length. These proteins are distantly related to alpa/beta hydrolases so they may act as enzymes.	2.98121e-08
NZ_CP046670.1\|WP_071950722.1\|515903_517619_-\|TIGR03545-family-protein	gnl\|CDD\|274640	TIGR03545, TIGR03545, TIGR03545 family protein. This model represents a relatively rare but broadly distributed uncharacterized protein family, distributed in 1-2 percent of bacterial genomes, all of which have outer membranes. In many of these genomes, it is part of a two-gene pair.	3.71916e-90
NZ_CP046670.1\|WP_015066174.1\|533547_534381_+\|thymidylate-synthase	gnl\|CDD\|234984	PRK01827, thyA, thymidylate synthase; Reviewed.	0
NZ_CP046670.1\|WP_071968211.1\|536463_537810_-\|MFS-transporter	gnl\|CDD\|341039	cd17486, MFS_AmpG_like, AmpG and similar transporters of the Major Facilitator Superfamily. AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	5.76404e-90
NZ_CP046670.1\|WP_071950721.1\|514791_515508_-\|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase	gnl\|CDD\|234670	PRK00155, ispD, D-ribitol-5-phosphate cytidylyltransferase.	1.47398e-115
NZ_CP046670.1\|WP_071968209.1\|531914_532721_+\|sulfite-exporter-TauE/SafE-family-protein	gnl\|CDD\|376667	pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.	2.47319e-26
NZ_CP046670.1\|WP_071970457.1\|529617_531909_+\|phosphoenolpyruvate--protein-phosphotransferase	gnl\|CDD\|182937	PRK11061, PRK11061, phosphoenolpyruvate--protein phosphotransferase.	0
NZ_CP046670.1\|WP_012517193.1\|532725_533529_+\|prolipoprotein-diacylglyceryl-transferase	gnl\|CDD\|234599	PRK00052, PRK00052, prolipoprotein diacylglyceryl transferase; Reviewed.	3.63688e-115
NZ_CP046670.1\|WP_157315558.1\|520151_523949_+\|bifunctional-proline-dehydrogenase/L-glutamate-gamma-semialdehyde-dehydrogenase-PutA	gnl\|CDD\|237018	PRK11905, PRK11905, bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed.	0

>NZ_CP046670.1|WP_157317097.1|528821_529364_+|RNA-pyrophosphohydrolase
MIDADGFRANVGIVICNKMGQVFWARRYGQHSWQFPQGGIDEGESAEQAMYRELHEEVGLTPKDVTILSVTRNWLRYKLPKRLIRQGSNPVCIGQKQKWFLLQLDCNERDVNVLKTGHPEFDDWRWVSYWYPIRNVVSFKRDVYRRVMKEFSPIVMSAQQRPLQRQSAAPHKRGKKRRRG
>NZ_CP046670.1|WP_012517189.1|528030_528708_-|DNA-mismatch-repair-endonuclease-MutH
MQPPASPPSSPDSLLKRCHAIAGLTLGELAEMAHVAIPANLQRHKGWPGMLIEKWLGASAGSKPQQDFPELGIELKTIPIDANFSPLETTYVCFAPLLMSPGITWETSNVRNKLQQVLWLPIEGDRAIPLAERRVATGFYWRPNEHEDALLRHDWEELVEYIATGQVESITSRQGEALHIRPKAANGKVLTDALGPEGQRIKTRPRGFYLRKTFTQQILMNAFGG
>NZ_CP046670.1|WP_141151554.1|526854_527937_+|AraC-family-transcriptional-regulator
MTSAIFSYCLYALLGVYAVGFVRLFVQKVNLSSTRWLIGAFVCWPLFMLDEWLRLAHATDLAVIYGLSDVFAVLAITCCYRAIKPMLLAYPTARKRLWWPVVVTALFQCTVLLIPVEDKQQWLLSSPHGEPLVLWPAYIASLLTGFSVLLIGILITEHIQMYHRHLPEQAVDIKNLKMPKLAGVMGSLVGVAFMSILLVTAATFGFFPVPFWESFHHLMLGTAILIVLFSLTFIRRTSPSPLDYERLDEGKATPYEISSIISKAERYTLESKAYKTRFLTLSAFCKGADIDPTSLALALQLSERKNFRRFIFHYRLEYAKNVLLRSDAKLEAVAKRIGVNSEKFLSEYLVKHLHTPSQKK
>NZ_CP046670.1|WP_071968206.1|525288_526794_+|CYTH-domain-containing-protein
MSEIELKFVTGDDAHQAFTQRVLPLFEKHRIQVNSHREMRLENDYYDTEKLDFQNQKMGFRVRGNNGEYEQTLKTNGVVSGGLHKRMEYNVSLEKSQPDLALFDESVWPQGWDVSAKNTSLSKQFSTHFTRNAYVVALDDSEVEIVLDCGKASTEKASSPINEIELELMSGDINTLFTLAVLINDNMPVRLSDVSKAAQGYQLLHGFNAKIRHLPDFLALEDTTTTEEAFSRAVQTALAHWQHHEHVFCESGSIKMLAEVAKSVRLLLQSVSLYLPVLQCPELLALHKKLVAHAQKWGWQDDLQSLRYLLSKKSMFSKTLSKHPAVVSYLQGRQTGLMQAHEPEKLFFDNDATDIKLHAISLIQNKPWQKEATGYDHPVLDHAKGWLSQGWQTVQQSMPLSKTMGPVNYSAVEIMLRQTLWSGFLLGDLFVEERGNFRAPWLDLLTGIDELNALLMLKQSIDDAEVDSHDEVRKWTAEKLSTLIRIMERTRTVAMQRDVYW
>NZ_CP046670.1|WP_157315559.1|524513_525290_-|TIGR04211-family-SH3-domain-containing-protein
MVALSTADDADTLPLSLSFRNATTPFLDAKFRQKWNKLAFIAVNQYHLHVLNSKIGLHMIRKWLAAALIACSFQAFSLQDIADLEASSSHYIRDDLFIFVHTGPGRNYRILGSIEAGTPITVLARDNDAEFTQITDPEGRKGWVESKFVSNTMSQAEQLPIISEKLAESQSSLQTLQSDNAKLRQQLNDARQQVSKLTTTNDEQASQIIRLTAKVESANKDELVMWFTRGGLVAGIGILLGVMLTYLPKRKRRSSEWM
>NZ_CP046670.1|WP_157315558.1|520151_523949_+|bifunctional-proline-dehydrogenase/L-glutamate-gamma-semialdehyde-dehydrogenase-PutA
MLINDTLHTTSPLRQRIRDYYRISESVAVDQILPIAEVNPRARSRAWERARKMVLQIRREQEGHGGVDALLNEYSLSTAEGVVLMCLAEALLRVPDRATQDELIRDKLSKGQWTPHLGNSDSLFVNASAWGLLFTGNMVNYADKRKKEQFGLLKQTIGRLGEPVIRRAMNIAMRVMGRQFVMGETIEDAVDRAKEKETKGYVYSYDMLGEGARTMRDADRYYDAYVKAIKVIGKAANGRGPKRSPGISVKLSAIHPRFEFSHRERAMVDIPPRLKALCMMAKEYDIGLTVDAEEADRLELSLDIIEAVFRDDDLNGWTGFGLAVQAYQKRAIHVIEHLRDLTLEVGRPLMVRLVKGAYWDTEIKLTQQAGLEEFPVFTRKSSTDVSYHACANRLLEYRDTIYPQFATHNAYTASVIVELAGDDKEGFEFQCLHGMGDTLYDQVVTEDKIQCRVYAPVGEHEDLLAYLVRRLLENGANSSFVNAIVDDEKPVESLLEDPVEKTQRLKVRYNKLIKTPRGLYAPERDNSRGLDLTDTNAVTALKHELERWQDYYKVTDEVPEGATPVLSPTDHTDIVGYHYYATPDDMRKALDDTDAGFEAWSKRDVSERAEILNRTADALERHMAELIAICMREAGKVAQDSIDEVREAVDFCRYYAVRAEELAEDQRLLPRGVVLCISPWNFPLAIFLGQVAAALVTGNTVVAKPAEQTSIVAQRAVDIMHSVGLPEDALKLIVSPGKEVGETLLPDERIKAVMFTGSTQTGTLISQVLAERGGEQVPLIAETGGQNCMIVDSTALPEQVVDDVIHSGFQSAGQRCSALRVLFVQDDIADELTEMLIGALKELTVGDPTQLATDVGPVIDEKALKSLTDHQDYMEGKGKLLYRSEMPKGFENGTFFAPTLYEIENIDVLEREVFGPVVHIVRFKAKELDNVLEQINGTGYGLTMGIHSRIEERANELAAKSRAGNVYINRNMIGAIVGVQPFGGRGLSGTGPKAGGPNYLPRLMMERATPKPSHIDDVDGTDAALIGDEKIAERAHVMMDKAKAVEIQWRHTPINDRISMVRQLLAKIAKVDIVDDLADDLNRTLATARQQLTSVERKLAKAQTLPGPTGESNKLYLEPRGILVCFADKEVTFEYWLLSIVTALSTGNPVVSVVSEIFYEEAVEIQNKFESTGAPKGLFQVARLAHLDTLLMDEDLSGVVVDSSTERTARITAMLSSREGAILPVITAEYNDNLIQRLMTEKTISIDTTASGGNTSLMTLVEDDE
>NZ_CP046670.1|WP_071950723.1|518032_519655_-|methyl-accepting-chemotaxis-protein
MWLRKFSLIQRLGIIAALITLLFVLLTALVLNRHYEALKQKSYDENQHLVEVVHTLLGSFAKREDVDEATAKQLALEAVKALRYDGNNYFWIQDETPAMVMHPMKPALDGKDLRTFKDGNGKAFFIEMAQKVKAKGEGFVDYVWPLPGEEAPTDKISYVKAFKPWGWTVGSGIYLTNLEEEYAHLRNVIVVFCVVSVVLVILLIYVIGGSIVKPVQEVSERMKDISQGEGDLTRSLPETGQDEVTRLARYFNEYTEKMRQSLLGIRENINSLTQQAELVETSSKDSNAQAQTQNENMLQVAAAMEEMTTQINEVSNNADSAEKGTSSARSNVQHGASVVDSTVQDIRSLTSDIESVSNVVTELAAQTDSIGAVLDVIRGIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRTLASRTGQSTDEIQAMIEKLQSNAKNAVDAVKVSQAASSKTVDNAIQANQNLQEADRLMTEIADKSSEIARATEQQAEAATEANMRINALSGAADSSLRTADELAAASQALRSSCLAIMEIANRFKL
>NZ_CP046670.1|WP_071950722.1|515903_517619_-|TIGR03545-family-protein
MSSGSKGKPILLWVVGFFVLLFLVYVLFANTIIKSILESKLGESYGAEVNIDDFDHSLYPTTVTLKGIALTNPTKPSHNQVFVGEANADVALKPLLDDQVIVNNLNLLEVQFDTERPSEGEVYRVPERSLSFNEIKAKAQEAVPTVDELLARNPLKTTAAIENAKSAYETYGKGLKEDYQSLPNKERIAYYKTQVAELKDTNYKDPQALVQAKSAFDKLKEEMQADRALITDFTAKASDAKEALSKSVEALKQAPQEDYALLKGVIAGDQAALSQVTYFVFGDKAAEYTEYLMSAMQIVMPLIQGEEKSEAPAEVPSILVKEANVSVLWQNESITSKWNNITNVHEVFGNPTTFTIEAAGDVLKSFTSSGEFWIDGDGVDASQVWELAGVNMSDVSFSGNDTLNAVLKSALMKTNGSMKVTDNLLTGTGEVDLQQLVMEATGTSDITSAIAQALQTLTSLNMTMLLDGTLSNPDFNIKSDLDNKLAKAALSQLTASQQDKLDELNAKLNSMISSEQSLLSGELADVNSMLSAAQGDSAALQELLQAQLNNVVEQQKNKLFDKLKGKLGQGE
>NZ_CP046670.1|WP_012519942.1|515513_515804_-|cell-division-protein-FtsB
MLQGKWLPIVLLVLLGLLQYRLWFGKNSIPDYFSRKQEVQTQALQNANLAQRNALLKADINDLKIGLEAIEERARNELGLIKKGETFYRILPADSK
>NZ_CP046670.1|WP_071950721.1|514791_515508_-|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase
MTSPRVVAVIPAAGVGSRMQADRPKQYLSLNGKTILEHTIDALLNHPHIDDVIVAISQGDEYFDQLGLRQKPIRVVEGGKERADSVLNGILSLDENDWALVHDAARPCVDDADISNLLSLIGSEDVTGGILATPVRDTMKRVKPSSNIISHTEDRDGLWHALTPQLFPAMLLKRALQEGLAQGVSITDEASAMEFAGHSVAMVSGSPANIKITHPADLPLAEFYLKQKFSAQGDSAKN
>NZ_CP046670.1|WP_071970457.1|529617_531909_+|phosphoenolpyruvate--protein-phosphotransferase
MLTTLKRIVQEMNQIPALDTALFRLASRVKHTLNVDSCSIYLADYEAQEFILKATDGLHPDAVEQVRIGFSEGLIGLVGQREEPLNIVNAHSHPRFKHYPEVKEEKYNAFLGTPIINQRRVLGVITLQQAEMRRFSEDEEAFLVTLAAQLALEITNADIRGALTLSNSPDNIAQQKHVHGIAGSPGLAIGKGVSPDKSINLKNWVVRRSKSPQDQIKLYRKGVEVTRGHVDTLSNRLDDAIPDDVKSIFQLYHHLLDANSLGREVEEKIRQGWDAASSLKMVVESYAARFRAMDDPYMQERAIDIVDLSDRILANILYEANGQKVTEKVITEASILVADEVSAPMLAEFPKDKLKGIISIRGSNNSHAAILARAMGVPAVMGCQNVTPALLEDKEILLDGYSGEVIVSPERNIKSEFIQLIEEESAIAEKIDAEADKPCESVDGCRMSLYINAGLSAEVELNAEQIGAGVGLYRTEIPFMLRERFPSEQEQVKLYRQVLEAAPELPITMRTLDVGGDKPLPYFPINEENPFLGWRGIRLTLDHPEIFLVQVRAMLRASVGLSNLQIMLPMISTVSEVQESKRLINQAFYEISDEIAESGQTLNKPKLGIMLEVPSVLYQLPQLAKHVDFFSVGSNDLTQYLLAVDRNNTRVADLYNSYHPAVLGALYDVVQKANQNQVPVTICGEIAGEPAGALLLMGMGYRRLSMNGFNLRKINWLIRKVTLDECKQLLSLALTSVSHEEVFVHLNQYLETKGLGGLIRAGA
>NZ_CP046670.1|WP_071968209.1|531914_532721_+|sulfite-exporter-TauE/SafE-family-protein
MDPFVVIIVSCLILGSVVGILAGMLGIGGGLIIVPALSYLLVHFMGMTTETVMPVAIATSLSTIIFTGTSSALAHYKLGNIQRYIVLYTGLGIALGAIAGAQVASHMSGELLKDVFAVLVILIALQMIFGKQKASDNEASKGTLAAVGGTAGILSALMGIGGGALLVPALVWFRVNVRAAIGCAAFCGLVIAVFGTTSFVIAGWNAIDVPEHSLGYVYLPATAGIVATSMFTANIGAKLGQRVNVRVLKAMLACLLVLVSIRMILGIE
>NZ_CP046670.1|WP_012517193.1|532725_533529_+|prolipoprotein-diacylglyceryl-transferase
MEQSSYLVFPSIDPVIFSMGPLSVRWYGLMYLVGFIAAYLLAQKRLSQTSWSREQLSDLLFWSFVGVILGGRIGYVFFYQFGMFLDDPLYLFKIWAGGMSFHGGLLGVLAALFWRAKCMNTTFLRLGDFVAPLVPIGLGAGRIGNFLNAELWGRSTDVPWAVIFPNAGNIPRHPSQLYEFALEGVLLFIILWLYSAKKRPVGAVSGLFLLGYGSFRFIVEYFREPDAHIGLYQMGLSQGQLLCLPMIALGIGLIVRAYTRGKDRVEQ
>NZ_CP046670.1|WP_015066174.1|533547_534381_+|thymidylate-synthase
MKEYLALMRHVRDTGVKKEDRTGTGTLSVFGYQMRFNLQEGFPLVTTKKCHLKSIIHELLWFLKGETNIAYLKEHGVKIWDEWATDEGELGPVYGHQWRSWDRGDGTSVDQIAEVVEQIKNNPDSRRLIVSGWNPAVLPDTNYSPKENAAMGKQALPPCHTLFQFYVLDGKLSCQLYQRSGDIFLGIPFNIASYALLTMMIAQVCDLEPGDFIHTLGDAHLYSNHLEQVELQLSREPFERPTMEINPEVKDIFGFTFDDFTLKNYQSHPHIKAPVAI
>NZ_CP046670.1|WP_071950730.1|534390_535461_+|response-regulator
MSTPILICDDSGFARRQMARSLPDSWDVDISFAENGEQALTLIREGKGDVVFLDLNMPVMDGYQTMEEIRKHDLPCLVIVVSGDVQAQAREKMLALGALDFIRKPIDNDKLSLILSSYGIYSGETHSSGAKLQKVEEASQTKATASQRVTSTEEKLDACREMVNIAMGRAGESLAELLGEFIDLPIPNVNLIESNELSMAVAEINRNESVSAVSKGFISEGVSGEALVIFNDTNSQNIVELLKYPPSASSDKLALEALMDVSNILIGACLNGLSEQLKVAFSHTHPVLLGQHQGLSALLSDNVQRWGKLMAIEIGYAIKARDISFDLLLLFPGDAMSQVYSRLLDDSYDTDDKEGL
>NZ_CP046670.1|WP_157315560.1|535457_536435_+|diguanylate-cyclase
MNASIDTLSRSAVSQVPLELLDSIEVGIAVLDRNFTVQVWNKFLENHSAKKVDFIIGHSLFDHFPEIEEKWLRTKVDPVFNLKSPVFIIWEQRPYLFKFTCNRPVTCAAEYMYQNVTMFPIVDKDGNVERFCMLVYDVTEQALGKIGMEHLNQELKTASRVDGLTGLFNRRYWQERFDEMYKLCVRRDKPSTAVMLDIDHFKRINDTYGHQAGDKVIKMLAALIKRCVRETDLAGRYGGEEFAIILNDSTVEDARIVAERIRQLAQRLVVEHEGESINFTVSLGLAQFCSAFKGPLAWLECADKALYDAKESGRNQYRIYDTSQR
>NZ_CP046670.1|WP_071968211.1|536463_537810_-|MFS-transporter
MAQYAFELLPKAEVLLTALKTFNDKRYLSIFLFGISSGFPWIMIGSVLSAWLKDEGLSRSAIGLFGIIFATYSFNFLWSPLVDKLKPPLLGQRKGWIFAMQGCIVLLCLGMSQLSATYDLYYVALIGLLIAVASATQDIAIDGFRIDCVEKKDKDGMSAASSVATAGWWTGYGGLGAIPFFLADLTTWSWPNIYLLLSVIMVLLMCATCIADEPQIDREALLKKITDANATSSPLAYWIRTTLITPFAEFFNRNGVKLAASFLLFIFLFKIGEAFLGRMSIVFYKEVGFSNSDIATYSKLLNWWVTIVFSLLGGLVNIRYGIYRGLMIAGVAMAASNLLFALIAQTGPSTSLLAITVIVDGFTGAWSTVAMVAFISLLCNRAFSATQYALMASLSVAGRTLVASSSGIVVDSLNGNWSLFFIITAVMVIPSLCFLYSIRHHIKRVETA
>NZ_CP046670.1|WP_071950733.1|537907_538231_-|hypothetical-protein
MNVQDFVDNKAKQLCFYLRAFWQGELPIEEIELFFWDSMEEWGQIEYTLTQPYTQKERVFWHVLHQVHYWNGEKLTKDQFLIDELKNCVNFLEGLGHCPLDCVGIRP
>NZ_CP046670.1|WP_071968212.1|538374_539259_-|DUF3530-family-protein
MKRQTILLLFAVIVSLLPMTAHSNFLKDVSNAYLPGEVKTIMVGEGEAPIIEIGAKTPLPLGTAIVLTEPFPSSLTLSQGNSLADLLAEKGWNVVISPFHLPVTPSEPINEDTMPGSSDEGDSAPSSQPNEIHPRSNQLTQYLSFEMTVTALTVQLSALNNYLQDRGGYRMVIAQGMLATTFLSATEQQPALDPDTFIAISPFWPEESTNNLVIETMAQANYPVLDVSLNSFNDWESNTTLKRKIRAKNALKLHYRQINIPNNSLTFSIKNIHKPPQIQMVANSAIGWTRHLGW
>NZ_CP046670.1|WP_012517200.1|539422_540139_-|bifunctional-tRNA-pseudouridine(32)-synthase/23S-rRNA-pseudouridine(746)-synthase-RluA
MANPSFVYNPPMTPYLDILYQDEDMVVAHKPSGLLSVPGKALEHRDSLISRVNTVYPTATVVHRLDMATSGILVLALNKDSHRHISKQFELRLTQKRYFARVHGHIEEDSGEVDLPLICDWPNRPKQMVDFERGKKAITRFEVIERATDDAARRYTLVALYPITGRSHQLRVHMLALGHPILGDRLYAHDEALSMAPRLQLHAESLSLTHPTLEKWLHFKTPIPFSHYRPGALSIDRD

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Crispr_ID: NZ_CP046670_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_2

837897-839184

TypeI-F

I-F

Consensus_repeat	Method
GTTCATGGCCGCACAGGCCACTTAGAAA	PILER-CR
GTTCATGGCCGCACAGGCCACTTAGAAA	CRISPRCasFinder
GTTCATGGCCGCACAGGCCACTTAGAAA	CRT

21 spacers

cas6f,cas7f,cas5f,cas8f,cas3f

The CRISPR arrays of NZ_CP046670_2

>merge|NZ_CP046670|2|837897-839184|PILER-CR,CRISPRCasFinder,CRT
GTTCATGGCCGCACAGGCCACTTAGAAAATTGCCAAGTTGAATATAAAGTCTGTCATTGGGTTCATGGCCGCACAGGCCACTTAGAAACCCAACCGCCAACGCTGGGCCCGACCAATCAGGTTCATGGCCGCACAGGCCACTTAGAAAAGCTTGTGTTCATCGGTATCGCCGGACCTTTTGTTCATGGCCGCACAGGCCACTTAGAAATTGTACACTCGCTGAGGCATCCATTGATCTTCGTTCATGGCCGCACAGGCCACTTAGAAACAGAATGGGATGAATCAAGGCGGTAAAACTCCGTTCATGGCCGCACAGGCCACTTAGAAATCGCACCTAGTTCGCTAAAAAAATAATTAGTGGTTCATGGCCGCACAGGCCACTTAGAAATCTCTTATTTCCCAACGGCCATCTTGTATACGGTTCATGGCCGCACAGGCCACTTAGAAATTACGAAAAGGAGTTGGCAGCCTGAGCGATTCGTTCATGGCCGCACAGGCCACTTAGAAATTACTTTGAATGAGTAGTTACCGTAAGCGTTGGTTCATGGCCGCACAGGCCACTTAGAAATCTTTGTCATAAATGTCATTAGATACTAGCACGTTCATGGCCGCACAGGCCACTTAGAAACACAAAGAACAGCAAGCGGGGTTGATGTGATGGTTCATGGCCGCACAGGCCACTTAGAAATACCCCTGAATAGTGACCGAGGAGCGTCAAAGGTTTATGGCCGCACAGGCCACTTAGAAATAATAGCCGCAGCGCCGAAAATGTATGCGAAGGTTCATGGCCGCACAGGCCACTTAGAAATGACGTTAATTTATGAATGAGCATAATTGATTGTTCATGGCCGCACGGGCCACTTAGAAAATGGGTTATTATCCTCATGCTGTTGGCTGCTAGTTCATGGCCGCACAGGCCACTTAGAAACTTAGTTGATGATTCAAGTATACTTACTTTTTGTTCATGGCCGCACAGGCCACTTAGAAAAACGCTGTGAAGCAGGGGAAAACATGACAATCGTTCATGGCCGCACGGGCCACTTAGAAATTACATGCGGGTGGGCGCGTGTACAACTCTGAGTTCATGGCCGCACAGGCCACTTAGAAAAGCCGGATGAGTAGCCAGTAATGGGGCGTGACGTTCATGGCCGCACAGGCCACTTAGAAAAATCACCCGCGCCCTTTCTCTTTGTTGGGTTTGTCCATGGCCGCACAGGCCACTTAGAAATTGACTGGTTAATTTGATTTTTGGCATTTTTAGTTCATGGCCGCACAGGCCACTTAAAAA

>NZ_CP046670|2|1|837897-839184|PILER-CR
GTTCATGGCCGCACAGGCCACTTAGAAA	ATTGCCAAGTTGAATATAAAGTCTGTCATTGG
GTTCATGGCCGCACAGGCCACTTAGAAA	CCCAACCGCCAACGCTGGGCCCGACCAATCAG
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCTTGTGTTCATCGGTATCGCCGGACCTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	TTGTACACTCGCTGAGGCATCCATTGATCTTC
GTTCATGGCCGCACAGGCCACTTAGAAA	CAGAATGGGATGAATCAAGGCGGTAAAACTCC
GTTCATGGCCGCACAGGCCACTTAGAAA	TCGCACCTAGTTCGCTAAAAAAATAATTAGTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTCTTATTTCCCAACGGCCATCTTGTATACG
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACGAAAAGGAGTTGGCAGCCTGAGCGATTC
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACTTTGAATGAGTAGTTACCGTAAGCGTTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTTTGTCATAAATGTCATTAGATACTAGCAC
GTTCATGGCCGCACAGGCCACTTAGAAA	CACAAAGAACAGCAAGCGGGGTTGATGTGATG
GTTCATGGCCGCACAGGCCACTTAGAAA	TACCCCTGAATAGTGACCGAGGAGCGTCAAAG
GTTTATGGCCGCACAGGCCACTTAGAAA	TAATAGCCGCAGCGCCGAAAATGTATGCGAAG
GTTCATGGCCGCACAGGCCACTTAGAAA	TGACGTTAATTTATGAATGAGCATAATTGATT
GTTCATGGCCGCACGGGCCACTTAGAAA	ATGGGTTATTATCCTCATGCTGTTGGCTGCTA
GTTCATGGCCGCACAGGCCACTTAGAAA	CTTAGTTGATGATTCAAGTATACTTACTTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	AACGCTGTGAAGCAGGGGAAAACATGACAATC
GTTCATGGCCGCACGGGCCACTTAGAAA	TTACATGCGGGTGGGCGCGTGTACAACTCTGA
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCCGGATGAGTAGCCAGTAATGGGGCGTGAC
GTTCATGGCCGCACAGGCCACTTAGAAA	AATCACCCGCGCCCTTTCTCTTTGTTGGGTTT
GTCCATGGCCGCACAGGCCACTTAGAAA	TTGACTGGTTAATTTGATTTTTGGCATTTTTA
GTTCATGGCCGCACAGGCCACTTAAAAA

>NZ_CP046670|2|2|837897-839184|CRISPRCasFinder
GTTCATGGCCGCACAGGCCACTTAGAAA	ATTGCCAAGTTGAATATAAAGTCTGTCATTGG
GTTCATGGCCGCACAGGCCACTTAGAAA	CCCAACCGCCAACGCTGGGCCCGACCAATCAG
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCTTGTGTTCATCGGTATCGCCGGACCTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	TTGTACACTCGCTGAGGCATCCATTGATCTTC
GTTCATGGCCGCACAGGCCACTTAGAAA	CAGAATGGGATGAATCAAGGCGGTAAAACTCC
GTTCATGGCCGCACAGGCCACTTAGAAA	TCGCACCTAGTTCGCTAAAAAAATAATTAGTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTCTTATTTCCCAACGGCCATCTTGTATACG
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACGAAAAGGAGTTGGCAGCCTGAGCGATTC
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACTTTGAATGAGTAGTTACCGTAAGCGTTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTTTGTCATAAATGTCATTAGATACTAGCAC
GTTCATGGCCGCACAGGCCACTTAGAAA	CACAAAGAACAGCAAGCGGGGTTGATGTGATG
GTTCATGGCCGCACAGGCCACTTAGAAA	TACCCCTGAATAGTGACCGAGGAGCGTCAAAG
GTTTATGGCCGCACAGGCCACTTAGAAA	TAATAGCCGCAGCGCCGAAAATGTATGCGAAG
GTTCATGGCCGCACAGGCCACTTAGAAA	TGACGTTAATTTATGAATGAGCATAATTGATT
GTTCATGGCCGCACGGGCCACTTAGAAA	ATGGGTTATTATCCTCATGCTGTTGGCTGCTA
GTTCATGGCCGCACAGGCCACTTAGAAA	CTTAGTTGATGATTCAAGTATACTTACTTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	AACGCTGTGAAGCAGGGGAAAACATGACAATC
GTTCATGGCCGCACGGGCCACTTAGAAA	TTACATGCGGGTGGGCGCGTGTACAACTCTGA
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCCGGATGAGTAGCCAGTAATGGGGCGTGAC
GTTCATGGCCGCACAGGCCACTTAGAAA	AATCACCCGCGCCCTTTCTCTTTGTTGGGTTT
GTCCATGGCCGCACAGGCCACTTAGAAA	TTGACTGGTTAATTTGATTTTTGGCATTTTTA
GTTCATGGCCGCACAGGCCACTTAAAAA

>NZ_CP046670|2|1|837897-839184|CRT
GTTCATGGCCGCACAGGCCACTTAGAAA	ATTGCCAAGTTGAATATAAAGTCTGTCATTGG
GTTCATGGCCGCACAGGCCACTTAGAAA	CCCAACCGCCAACGCTGGGCCCGACCAATCAG
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCTTGTGTTCATCGGTATCGCCGGACCTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	TTGTACACTCGCTGAGGCATCCATTGATCTTC
GTTCATGGCCGCACAGGCCACTTAGAAA	CAGAATGGGATGAATCAAGGCGGTAAAACTCC
GTTCATGGCCGCACAGGCCACTTAGAAA	TCGCACCTAGTTCGCTAAAAAAATAATTAGTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTCTTATTTCCCAACGGCCATCTTGTATACG
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACGAAAAGGAGTTGGCAGCCTGAGCGATTC
GTTCATGGCCGCACAGGCCACTTAGAAA	TTACTTTGAATGAGTAGTTACCGTAAGCGTTG
GTTCATGGCCGCACAGGCCACTTAGAAA	TCTTTGTCATAAATGTCATTAGATACTAGCAC
GTTCATGGCCGCACAGGCCACTTAGAAA	CACAAAGAACAGCAAGCGGGGTTGATGTGATG
GTTCATGGCCGCACAGGCCACTTAGAAA	TACCCCTGAATAGTGACCGAGGAGCGTCAAAG
GTTTATGGCCGCACAGGCCACTTAGAAA	TAATAGCCGCAGCGCCGAAAATGTATGCGAAG
GTTCATGGCCGCACAGGCCACTTAGAAA	TGACGTTAATTTATGAATGAGCATAATTGATT
GTTCATGGCCGCACGGGCCACTTAGAAA	ATGGGTTATTATCCTCATGCTGTTGGCTGCTA
GTTCATGGCCGCACAGGCCACTTAGAAA	CTTAGTTGATGATTCAAGTATACTTACTTTTT
GTTCATGGCCGCACAGGCCACTTAGAAA	AACGCTGTGAAGCAGGGGAAAACATGACAATC
GTTCATGGCCGCACGGGCCACTTAGAAA	TTACATGCGGGTGGGCGCGTGTACAACTCTGA
GTTCATGGCCGCACAGGCCACTTAGAAA	AGCCGGATGAGTAGCCAGTAATGGGGCGTGAC
GTTCATGGCCGCACAGGCCACTTAGAAA	AATCACCCGCGCCCTTTCTCTTTGTTGGGTTT
GTCCATGGCCGCACAGGCCACTTAGAAA	TTGACTGGTTAATTTGATTTTTGGCATTTTTA
GTTCATGGCCGCACAGGCCACTTAAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_157315648.1\|830640_833805_+\|type-I-F-CRISPR-associated-helicase-Cas3	cas3f	cd09673_cas3f_CAS-I-F	gnl\|CDD\|274201
NZ_CP046670.1\|WP_157315646.1\|828453_829035_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157315649.1\|833813_835151_+\|type-I-F-CRISPR-associated-protein-Csy1	cas8f	cd09735_cas8f_CAS-I-F	gnl\|CDD\|187866
NZ_CP046670.1\|WP_081365697.1\|847796_848360_+\|DUF1566-domain-containing-protein	unknown	unknown	gnl\|CDD\|377878
NZ_CP046670.1\|WP_071950878.1\|841635_841962_+\|DUF3718-domain-containing-protein	unknown	unknown	gnl\|CDD\|378871
NZ_CP046670.1\|WP_071950877.1\|839837_840647_+\|metallo-mystery-pair-system-four-Cys-motif-protein	unknown	unknown	gnl\|CDD\|188567
NZ_CP046670.1\|WP_157315645.1\|827244_828429_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271182
NZ_CP046670.1\|WP_157315644.1\|826249_827248_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225497
NZ_CP046670.1\|WP_071950879.1\|842108_842870_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|197918
NZ_CP046670.1\|WP_157315651.1\|836170_837154_+\|type-I-F-CRISPR-associated-protein-Csy3	cas7f	pfam09615_cas7f_CAS-I-F	gnl\|CDD\|378222
NZ_CP046670.1\|WP_157315653.1\|843044_843458_+\|CidA/LrgA-family-protein	unknown	unknown	gnl\|CDD\|377131
NZ_CP046670.1\|WP_157315654.1\|843450_844161_+\|LrgB-family-protein	unknown	unknown	gnl\|CDD\|377236
NZ_CP046670.1\|WP_012517421.1\|840946_841276_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_071958661.1\|844441_845437_+\|response-regulator	unknown	unknown	gnl\|CDD\|381124
NZ_CP046670.1\|WP_157315643.1\|825950_826172_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP046670.1\|WP_157315650.1\|835150_836122_+\|type-I-F-CRISPR-associated-protein-Csy2	cas5f	cd09736_cas5f_CAS-I-F	gnl\|CDD\|378221
NZ_CP046670.1\|WP_157315647.1\|829678_830506_+\|WYL-domain-containing-protein	unknown	unknown	gnl\|CDD\|225253
NZ_CP046670.1\|WP_157315652.1\|837158_837767_+\|type-I-F-CRISPR-associated-endoribonuclease-Cas6/Csy4	cas6f	pfam09618_cas6f_CAS-I-F	gnl\|CDD\|378224
NZ_CP046670.1\|WP_071958662.1\|845436_845928_+\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|312075
NZ_CP046670.1\|WP_157315655.1\|846018_847794_+\|DUF1566-domain-containing-protein	unknown	unknown	gnl\|CDD\|377878

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157315648.1\|830640_833805_+\|type-I-F-CRISPR-associated-helicase-Cas3	gnl\|CDD\|274201	TIGR02562, conserved_hypothetical_protein, CRISPR-associated helicase Cas3, subtype I-F/YPEST. The helicase in many CRISPR-associated (cas) gene clusters is designated Cas3, and most Cas3 proteins are described by model TIGR01587. Members of this family are considerably larger, show a number of motifs in common with TIGR01587 sequences, and replace Cas3 in some CRISPR/cas loci in a number of Proteobacteria, including Yersinia pestis, Chromobacterium violaceum, Erwinia carotovora subsp. atroseptica SCRI1043, Photorhabdus luminescens subsp. laumondii TTO1, Legionella pneumophila, etc.	0
NZ_CP046670.1\|WP_157315647.1\|829678_830506_+\|WYL-domain-containing-protein	gnl\|CDD\|225253	COG2378, COG2378, Predicted transcriptional regulator [Transcription].	1.61916e-05
NZ_CP046670.1\|WP_157315649.1\|833813_835151_+\|type-I-F-CRISPR-associated-protein-Csy1	gnl\|CDD\|187866	cd09735, Csy1_I-F, CRISPR/Cas system-associated protein Csy1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins; Predicted subunit of the Cascade complex; signature gene for I-F subtype; also known as Csy1 family.	3.08409e-134
NZ_CP046670.1\|WP_081365697.1\|847796_848360_+\|DUF1566-domain-containing-protein	gnl\|CDD\|377878	pfam07603, DUF1566, Protein of unknown function (DUF1566). These proteins of unknown function are found in Leptospira interrogans and in several gamma proteobacteria.	2.80415e-37
NZ_CP046670.1\|WP_071950878.1\|841635_841962_+\|DUF3718-domain-containing-protein	gnl\|CDD\|378871	pfam12514, DUF3718, Protein of unknown function (DUF3718). This domain family is found in bacteria and viruses, and is approximately 70 amino acids in length. There is a single completely conserved residue C that may be functionally important.	1.67391e-18
NZ_CP046670.1\|WP_071950877.1\|839837_840647_+\|metallo-mystery-pair-system-four-Cys-motif-protein	gnl\|CDD\|188567	TIGR04052, hypothetical_protein_MettrDRAFT_3899, AZL_007920/MXAN_0976 family protein. Members of this rare protein family regularly occur next to a member of the MXAN_0977 subfamily (TIGR04039) of the di-heme cytochrome c peroxidase/MauG family (pfam03150). MauG itself (TIGR03791) is a protein modification enzyme responsible for the tryptophan tryptophylquinone (TTQ) modification involved in methylamine dehydrogenase activation. All members of this family have a motif of four spaced invariant Cys residues, while additional homologs outside the scope of this family lack the four Cys residues.	1.53747e-37
NZ_CP046670.1\|WP_157315645.1\|827244_828429_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271182	cd00801, INT_P4_C, Bacteriophage P4 integrase, C-terminal catalytic domain. P4-like integrases are found in temperate bacteriophages, integrative plasmids, pathogenicity and symbiosis islands, and other mobile genetic elements. The P4 integrase mediates integrative and excisive site-specific recombination between two sites, called attachment sites, located on the phage genome and the bacterial chromosome. The phage attachment site is often found adjacent to the integrase gene, while the host attachment sites are typically situated near tRNA genes. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	6.14751e-36
NZ_CP046670.1\|WP_157315644.1\|826249_827248_+\|hypothetical-protein	gnl\|CDD\|225497	COG2946, COG2946, Putative phage replication protein RstA [DNA replication, recombination, and repair].	5.26905e-24
NZ_CP046670.1\|WP_071950879.1\|842108_842870_+\|response-regulator-transcription-factor	gnl\|CDD\|197918	smart00850, LytTR, LytTr DNA-binding domain. This domain is found in a variety of bacterial transcriptional regulators. The domain binds to a specific DNA sequence pattern.	2.39591e-16
NZ_CP046670.1\|WP_157315651.1\|836170_837154_+\|type-I-F-CRISPR-associated-protein-Csy3	gnl\|CDD\|378222	pfam09615, Cas_Csy3, CRISPR-associated protein (Cas_Csy3). CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This entry, typified by YPO2463 of Yersinia pestis, is a CRISPR-associated (Cas) entry strictly associated with the Ypest subtype of CRISPR/Cas locus. It is designated Csy3, for CRISPR/Cas Subtype Ypest protein 3.	0
NZ_CP046670.1\|WP_157315653.1\|843044_843458_+\|CidA/LrgA-family-protein	gnl\|CDD\|377131	pfam03788, LrgA, LrgA family. This family is uncharacterized. It contains the protein LrgA that has been hypothesized to export murein hydrolases.	9.01316e-21
NZ_CP046670.1\|WP_157315654.1\|843450_844161_+\|LrgB-family-protein	gnl\|CDD\|377236	pfam04172, LrgB, LrgB-like family. The two products of the lrgAB operon are potential membrane proteins, and LrgA and LrgB are both thought to control of murein hydrolase activity and penicillin tolerance.	1.03451e-66
NZ_CP046670.1\|WP_071958661.1\|844441_845437_+\|response-regulator	gnl\|CDD\|381124	cd17593, REC_CheC-like, phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain. This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	1.11948e-61
NZ_CP046670.1\|WP_157315643.1\|825950_826172_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	2.78138e-10
NZ_CP046670.1\|WP_157315650.1\|835150_836122_+\|type-I-F-CRISPR-associated-protein-Csy2	gnl\|CDD\|378221	pfam09614, Cas_Csy2, CRISPR-associated protein (Cas_Csy2). CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This entry, typified by YPO2464 of Yersinia pestis, is a CRISPR-associated (Cas) entry strictly associated with the Ypest subtype of CRISPR/Cas locus. It is designated Csy2, for CRISPR/Cas Subtype Ypest protein 2.	1.7238e-110
NZ_CP046670.1\|WP_071958662.1\|845436_845928_+\|PAS-domain-containing-protein	gnl\|CDD\|312075	pfam08448, PAS_4, PAS fold. The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.	5.54841e-06
NZ_CP046670.1\|WP_157315652.1\|837158_837767_+\|type-I-F-CRISPR-associated-endoribonuclease-Cas6/Csy4	gnl\|CDD\|378224	pfam09618, Cas_Csy4, CRISPR-associated protein (Cas_Csy4). CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family, typified by YPO2462 of Yersinia pestis, is a CRISPR-associated (Cas) family strictly associated with the Ypest subtype of CRISPR/Cas locus. It is designated Csy4, for CRISPR/Cas Subtype Ypest protein 4.	3.25675e-64
NZ_CP046670.1\|WP_157315655.1\|846018_847794_+\|DUF1566-domain-containing-protein	gnl\|CDD\|377878	pfam07603, DUF1566, Protein of unknown function (DUF1566). These proteins of unknown function are found in Leptospira interrogans and in several gamma proteobacteria.	1.10066e-31

>NZ_CP046670.1|WP_157315652.1|837158_837767_+|type-I-F-CRISPR-associated-endoribonuclease-Cas6/Csy4
MKHYIDITLLPSDDIGIHFLWSKVMMQVHLALVEIQDDTKQVPVATSFPEYREYMNKKPGFLGQKLRLMALDESDLIRLDINRGLHRLSDYVHVRGIALIPETDSYESFSRENTKGSLEKHIRRRMKRHDETYEQALSNYDGYEQDDVNSLVPFIRLKSLTSGNEFCLNIDRKRVADNTDELPNHQRFNTYGLNRRAILPKF
>NZ_CP046670.1|WP_157315651.1|836170_837154_+|type-I-F-CRISPR-associated-protein-Csy3
MAELKLKTPSVLAFEAKLIPSDALMFAGNWGEERWDPIQVGEKAVRGTISNRLKAAMANDPVKLDAEVSKANLQTVDIAALNHKTDTLKVVFTLRVLSGLSTPSTCNRPDYQTALAEKISSYQTTVGFMELAERYAFNIASGRFLWRNRVGAQQIKIVVTVEGKTTEFDTQDYSLHTFSTDEKITQLANHIAKGLTEDHCLLKVEAYAQLGEGQSVYPSQELVMGGAKGDKSKFLYQLDGQAAMHSQKIGNALRTIDTWHPAADEVGPIAVEPYGSVTNRGAAYRQPKEKTDFYNLLDGWMLKGKEPSVEQQHYIMAMLIRGGVFGE
>NZ_CP046670.1|WP_157315650.1|835150_836122_+|type-I-F-CRISPR-associated-protein-Csy2
MSQYLLIKKLYIQNANAIAGLTYGFPAMTNFLGFAHAISRKLPNELNVTLDGVMVISHKNTVHVRQPKGWGDYVFALSRNPLTQQGNTAPINEEGRLSMEISLLIEMKGYQAGDQVTGEQLTSAVTRLLPTLRLAGGQIVRFESVSITPLDNELNTLRQLMPGFALIDRSDYLAAHFKALKEKDSATTQFDAWCDFTTLKYEAKRIVDSSSASNESDTDKAQWHYVRKPYPGYLVPINTGYCAISKVYEQGEIANIRDPLMPALFAEAAYSVGEWKSLHGLPSINSAIWRYQHKYPWYLAKSEPFVEDIVEPDSFDESSEMTF
>NZ_CP046670.1|WP_157315649.1|833813_835151_+|type-I-F-CRISPR-associated-protein-Csy1
MDMTLAEAIANYIEQRKKTKLEPLQKKRQKVLDKGDEVAIAAANTEYRSAALPIEESFEPKTWLTNAAKRAKQISLATHAAKFTHSDAKATSRLVVEHTVFDDAYLVTSSLKDKAIDAVGNAAALDVAKLLNLKVENESLIEQIRQGSSPALSEFTSDAALLSSWLEGFKEALGDKQLTVNSLTKQLYFPVSNTAESEYHLICPLFSSALCHQLHEKVTSSRYGTSKEVRDARKAGNYHSLMDVNFPETAIQTFGGSKPQNISQLNSERYGQTFLLNTSPPTFQSQVKPPLSQKTIFSNQFTRKVFASLREFKTFLESLKPHENNFRTRYKRDHYFVIPIIEQLLHYASSIQKIESGWALLPECNLKAEHALWLDHNNEDLSFQTERGKLNWLPVVANDFATWLIKQLKNDEHYLLGDVEHAYFHKLCLHHLTRFERVTPTKGDF
>NZ_CP046670.1|WP_157315648.1|830640_833805_+|type-I-F-CRISPR-associated-helicase-Cas3
MEQHVEEGRKAKKITKSINGWERIELIELAAGIAGLFHDFGKANDLFQKKLSPNTDLKSEPFRHEWVSLRLFEAFVAGRLDQQWLTELHALENPNHAKEIENRTIANIVRDDQRLTNPFNSFSEDAPFSKLVAWLIVSHHRLPLPTTKASKVDLKGQRNWLNVQFSCHWNSKNAENISDIYNSIIDANWSFSHGTPITSTTWQVKAKELARRALSSNLLRNAQELLHQRFIAHISRLSLMLADHYYSSLAPDESREKWQDHSYKVHANTDRATGQFKQQLDEHNIGVAHNAFLFARNLPALKHTLPAIGQHRLLSKNAEDVKYQWQDKAYKATKALSKESEKLGFFGINMASTGCGKTIANARIMYALSDEREGCRFSVALGLRTLTMQTGDAYRALLKLGDDELAVLIGSNAVKLLHQLDKDEKKNTASDNGSESAKDDYEHLFVSYEGQIYDGRLKRWLSSSPKLEQLVSAPVLVSTIDHLMPATESQRGGKQIAPMLRLLTSDLVLDEPDDFGLEDLPALCRFVNWAGMLGSRVLLSSATLPPGLISALYDAYVAGRKHFNEVHFPHNNETGVVCAWYDEHNSEVALIRDEQTFTQACKRFTDKRLKTLVNNEDILRKGQIVPTEAPPADTEEGTLGKDKDNERDQFIFKSVANTISQEIDRLHNAHYVKNNKGQRVSVGVVRMANINPMIEVAKNLLSTSPPDDTQFHFCVYHSQFPLALRSYKESRLDSILTRYDDNVFWAQPEIAKALSGSSVTNHVFVVLGTSVVEVGRDHDYDWAIAEPSSLRSIIQLAGRVQRHRKQPPTKPNIAVLDQNIRALKGERVAYCKPGFETPELPLSSRKLTDLVSTEITNISAIPRMVEPTMTKCDFMKDPLSDNKSAANSVSSFVIQEHRAIRTALNVIGGDINHEQFYNSPKPASLWWDESTPIDWSAEFIKQTAFRESAPQEEFTLQLSDMGELNWGQIDRTSLPYTFIKQNNRFTTESFSLAKGTCWWFDKSAQEIFHYFAEKMDGDIERVSQKLGVIGLRESKSDKPIDWAWHEQLGIYQGD
>NZ_CP046670.1|WP_157315647.1|829678_830506_+|WYL-domain-containing-protein
MELAQRYWMLELLAFWEGQVNTKPLMHAFNISRQSASAIINKYLSSNEDTLAYDVNQKAYVVTSAFNPKFINRTVDEYFDWQQVGKIPSFQARNPSTNQVRIQPLLRYVDPNTMRPLLKAMKCKTAVDCEYLSVTNNEPIGRLFYPHSFVKAANRWHVRGFCALRNNYLDFVLSRFRSVEYDGSKAINTEKEDVKWNTILYLILAPDPRLSEIQKQALEKDFDMKNGRITVRARGALVKYTLDDLQIKTKMLEADPQAQQLVCVNYGDIKQWLYD
>NZ_CP046670.1|WP_157315646.1|828453_829035_-|hypothetical-protein
MRAGLISLFLLLCTGCAMPTLSEPPAMLFDVDSSSLKKSQSAKVNDIKVRVGSYFELTGKVDVHDYLGDKYAVTTLNNHWLTRATPKVLDSLNGAFAEIFNGNEGENYQLEMVITKLSSNSVLSSDIESEVTYIFTNELSGNQTQAKVKAFGACSMGEYLEGILRTECSRIRSLRNNISQLASQLSSRQTVLQ
>NZ_CP046670.1|WP_157315645.1|827244_828429_+|tyrosine-type-recombinase/integrase
MKYSKFTDGLLRQASKESFVFRDVTVPQLQFRPAKAHRKIGYFHCLYSEDGVSTSKALGEYPIVNLQEARKQARKWLVEQHAKRYKLSNVERFTNVGELLDWYQSNNAQQKLDSLRTIKNKSHRVESLLRPYLSEVSISDCSSQLLDKAWLRPLNNRFSPSTLRGAFQTLKAAFKQAHGLRYIDENPLSDLNFTMLLPVPIKPKKAALAGLPLGEVIKQFQQFNAPDRFLCLLCLGFLTRNTETVMARWRDFDTEKMSWSIPEEHTKTGSALTLPLSTYSLKWLADYKRQQRRYCRSRFLFLVKQGRSSWSSSYAAQRIMKASRGRFTLHDLRKYGSTYLRDSGVDYYLVERLLNHKKTHLDATYIHTTLRTPLMKVIEYWHHNINEVLKITPH
>NZ_CP046670.1|WP_157315644.1|826249_827248_+|hypothetical-protein
MNKGVEPETVAKNYGKTNPEQNPVFIDFLKLRVDDVEAPNPYFEMIALQLLKYNLLISHRQCNRSRSYDCAYKIVTTTQAQNVVGKIEYSERYNRVLLELSGLGCACIEKVEPDYIWLQALVAQPAVTIRRIDLALDDENGLYQIEKIDKDYSRGRFNAESGKRPKKENLGNKVEGRTRYIGGPTAYKRGRFYEKGKQLKLAHCRPWMRHEVRFVSNDRDRIPDETIRNRADYFYSAFPRVLRKLLGKHSVIPVTERFMREYVSDMSSRVASCKRQYGPLIGTLTEHHGAKATCEMLSRIGRSKVIELPPLVDEVSLADCTDIIALQSGEAI
>NZ_CP046670.1|WP_157315643.1|825950_826172_+|helix-turn-helix-domain-containing-protein
MKVTTQTKLLSPQEVAEQLGVTLNTLAVWRCHGSSSLSYVKIGRCVRYRAEDVEAFINAHRFYHADKPVNVYD
>NZ_CP046670.1|WP_071950877.1|839837_840647_+|metallo-mystery-pair-system-four-Cys-motif-protein
MKMPFRMGAMPSLLLTALLALAGCDVIDFKGREPGEIPFKLVGVDTGACPMIMSIGQDRWNIDYFGFYLSKPEVRIDGKWQRVKFKQTKWQTPNEALLKFHNKCINPDDANSKLVLDVSEELLKLATNLRFTMGLPFDVNHADALTQPSPLNDSSMFSNRRNGHQFLRLDVSKNAKETREWSYHLGSAGCGSESEAARPETSCAFTNRVEFILPMTQLDTDLDLEISVSNIVAQVDINDAESCVFASSEVSPCDKLIQNLVHRPWIKWQ
>NZ_CP046670.1|WP_012517421.1|840946_841276_+|hypothetical-protein
MTEKPFITSGRNTIIHKIRKLDLLVINGDDHPPIIVTYKGIKQYEGKVPENKRDAKMMDMELVDVTTSDVFGDEKTLVFIQTLNGKEYKIDYSKVGTSMFIKIHQDSIF
>NZ_CP046670.1|WP_071950878.1|841635_841962_+|DUF3718-domain-containing-protein
MFMSRRVTQFALIGISLSLTVSAASAASYPKALENELIAVCKAVKSDSRLQLHRAVKATGLSMRDLHDGLVCNGQDMLTFAVTHNASETAQHIARRINASPSVLTAKR
>NZ_CP046670.1|WP_071950879.1|842108_842870_+|response-regulator-transcription-factor
MIALVFLQSVAMQTSLCTMLEKIGLFRHVYGAHSVGHSLALAEKHPQSIGFYSVSKSSRNLASKHWLAVGDKDEEAMLAFNHNASGFITSPFDEQQVRCTVEHVKAKHYCHKRDVQFNLLVKGLCKQYGVSESALLATLRQQLYKNAQPNVVGIRAENGWCCLNPADIKWIEAAGDYMCVQTLSESYIVRTTLCHLLKRLGEHHFKRCNRSVAVNAKYVMHIEQKLNQQRVVMRGGEAFKITHKYYYQYWHTG
>NZ_CP046670.1|WP_157315653.1|843044_843458_+|CidA/LrgA-family-protein
MRNAINTVVGAVLVFTAYYVGLLIVNLTSLPVPGPLVGLLLLVGVLFAFPQTERQVARAVTFPLKHMSLLFVPAVLGVSIYWSDIKANALAIAIAIIITTSFCLGLTAWLTQALLNTKSTHKTQLNNINKNEGDTND
>NZ_CP046670.1|WP_157315654.1|843450_844161_+|LrgB-family-protein
MIEALNHAFSLRGLFWISVSIVSYIAALWVNRLCKGHPAAHPIVTTALLVSLGLYLTHTSVTAYQHAASLLYWLLGPITVALALPIYRQWQKLKHYGWRLLISIAFGGVLAPIGAWLTLFVLDAPRAMQFTMLAKSITTPLAMETSAQIGGIPALAAVFVIVTGVVGAIMATSMFSLFNIANRQAQGIALGTVAHAVGTAKAIQMGEDVAAMATLGLCVNGIFTAVALPIVFGFFI
>NZ_CP046670.1|WP_071958661.1|844441_845437_+|response-regulator
MFSVLVCDDSLVARKQVAKCLPQDWEVAVHFAKNGQEALTALAEGKGDLLLLDLNMPVLDGYGTLEAIQKQGLKTKVIVVSGDIQPEAHDRVTSLGALDFIRKPVDPKKLAEVLDKYNILHAEEDEVVEASPLDPDIRDCYQEITNIAMGQAGDHLARTMNVFVELPIPNVNLIEVSELHMMLSDIECHEQVTAVCQGFLGPGVSGEALCILSDSSFDDVAKILNVEGEVDDQLQLELLMDAASILIGTCLTGLANQMDINFSQGHPIVLGQHRAITEIIAMNQIKWKRTLAIELSYGLEGYNVQCDLILLFTEESMKMMNSKLAHLLEDF
>NZ_CP046670.1|WP_071958662.1|845436_845928_+|PAS-domain-containing-protein
MSQHLDEFQEFHWMMDMLQTVDVGIVVLDRDFTVKVWNGFMESHSGLLPSEVRDKTLFSLFPAIKQDWFMKKAKPVFDLKTRAFMTWEQRPYLFKFPNYRPITGSESFMYQNITLSPLTSTTGKVDFISMMIYDMTDVAVGKKQLEALQVTMSEAQEAKSSYS
>NZ_CP046670.1|WP_157315655.1|846018_847794_+|DUF1566-domain-containing-protein
MQFNVFSISSYFPRAIVRGLVLFATALLLAACGGGGGGGDGDSGGDGGSGSGDLVINAGPDATVTEGVTYTLSAQVSGGDGTYTYNWSASPSLSITHEDTSDSAASFVAPLVNNATEYTLTVSVNDQSGNTASDFTVITVAPVNIAPEASIDVPEWDGLPANTFPGGVEVIFDGTGSSDSDSASSDGDISDYVWTQTSGTNVITGVDTNLSTLTIVTPIANEEQQLTFQLEVTDSEGATDVETVTITVQSETDTLPVVSAGVSQGVFSGEVVILEGEASTSIPSALPLTYSWERSNNVSSTDSGVTIRSVDDSDALSTFAIAPAVTTSTVVAYTLTVTDANGNSVEDTINVQIRPMPTPLLNDTGFLQQATNNALTEAQQNDFPGQDGQRGADIIEQNGLIEKAGRGKAGFDFTRLNANGDEQDASADTWSCVRDNVTGLVWEVKTDDGAFQDKDYTYSWYSEEVNGGFEGDQTGLNASCLLTSCNTSAYVQAVNAQGLCGFYDWRLPTHDELFSLMHLGIADDVAIDEDYFPNTGAVTTEPLWYWTSVPSADGVNSDDAQNAWALDFDSGVDNFLNKSSAARVRLVRAGR
>NZ_CP046670.1|WP_081365697.1|847796_848360_+|DUF1566-domain-containing-protein
MNKVVNVKKRNSHVLSSVKTLFASALLACTSLSTFAQECLSDGLETTPNDNFEAVTTSSLLDTTTDLVWKRCAEGQTWDGSTCSGEAVKYTWQQALVLAHEASNDDLLGWRLPNVKELATLTERDCVRPAINSSLFPATPPDDFWTSTPSADDPDRAWVVAFFNASHSIKEKDRFIYVRLVRTYTNE

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Crispr_ID: NZ_CP046670_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_3

1342407-1342486

Orphan

Consensus_repeat	Method
AAGTCGATAAGTGTCTGTCCACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP046670_3

>merge|NZ_CP046670|3|1342407-1342486|CRISPRCasFinder
AAGTCGATAAGTGTCTGTCCACCGTTACGTTCACCGGTACGTTAACCTTGCTTGGCGAAGTCGATAAGTGTCTGTCCATC

>NZ_CP046670|3|3|1342407-1342486|CRISPRCasFinder
AAGTCGATAAGTGTCTGTCCACC	GTTACGTTCACCGGTACGTTAACCTTGCTTGGCG
AAGTCGATAAGTGTCTGTCCATC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_157315795.1\|1332240_1333230_+\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176233
NZ_CP046670.1\|WP_071958866.1\|1334591_1337633_-\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_CP046670.1\|WP_071968486.1\|1329339_1329783_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|270284
NZ_CP046670.1\|WP_041912852.1\|1337636_1338719_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP046670.1\|WP_071960377.1\|1329792_1331037_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157315799.1\|1343059_1346239_-\|acriflavin-resistance-protein	unknown	unknown	gnl\|CDD\|223911
NZ_CP046670.1\|WP_157315800.1\|1346248_1347397_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP046670.1\|WP_071958865.1\|1334051_1334471_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341361
NZ_CP046670.1\|WP_071951137.1\|1354245_1355196_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212492
NZ_CP046670.1\|WP_157315796.1\|1333423_1333921_+\|DUF45-domain-containing-protein	unknown	unknown	gnl\|CDD\|224368
NZ_CP046670.1\|WP_157315803.1\|1355413_1356313_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|377694
NZ_CP046670.1\|WP_157315802.1\|1348653_1349265_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377153
NZ_CP046670.1\|WP_141151795.1\|1351090_1352233_-\|paraquat-inducible-protein-A	unknown	unknown	gnl\|CDD\|225542
NZ_CP046670.1\|WP_071951129.1\|1338914_1339529_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP046670.1\|WP_157315801.1\|1347550_1348651_-\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635
NZ_CP046670.1\|WP_157315794.1\|1331210_1332125_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP046670.1\|WP_024016013.1\|1349441_1351094_-\|intermembrane-transport-protein-PqiB	unknown	unknown	gnl\|CDD\|182747
NZ_CP046670.1\|WP_071951135.1\|1352387_1353401_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157315797.1\|1340050_1342171_+\|TonB-dependent-siderophore-receptor	unknown	unknown	gnl\|CDD\|227115
NZ_CP046670.1\|WP_141151796.1\|1353511_1354186_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370579

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157315795.1\|1332240_1333230_+\|zinc-binding-dehydrogenase	gnl\|CDD\|176233	cd08272, MDR6, 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.	4.36868e-164
NZ_CP046670.1\|WP_071958866.1\|1334591_1337633_-\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_CP046670.1\|WP_071968486.1\|1329339_1329783_-\|hypothetical-protein	gnl\|CDD\|270284	cd13566, PBP2_phosphate, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	0.00123505
NZ_CP046670.1\|WP_041912852.1\|1337636_1338719_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	3.87809e-49
NZ_CP046670.1\|WP_157315799.1\|1343059_1346239_-\|acriflavin-resistance-protein	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_CP046670.1\|WP_157315800.1\|1346248_1347397_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	6.38597e-38
NZ_CP046670.1\|WP_071958865.1\|1334051_1334471_+\|CBS-domain-containing-protein	gnl\|CDD\|341361	cd04584, CBS_pair_AcuB_like, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain. The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	2.51193e-42
NZ_CP046670.1\|WP_071951137.1\|1354245_1355196_-\|SDR-family-oxidoreductase	gnl\|CDD\|212492	cd05327, retinol-DH_like_SDR_c_like, retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	9.7657e-95
NZ_CP046670.1\|WP_157315796.1\|1333423_1333921_+\|DUF45-domain-containing-protein	gnl\|CDD\|224368	COG1451, COG1451, Predicted metal-dependent hydrolase [General function prediction only].	4.56005e-16
NZ_CP046670.1\|WP_157315803.1\|1355413_1356313_+\|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.	3.36071e-39
NZ_CP046670.1\|WP_157315802.1\|1348653_1349265_-\|hypothetical-protein	gnl\|CDD\|377153	pfam03886, ABC_trans_aux, ABC-type transport auxiliary lipoprotein component. ABC_trans_aux is a family of bacterial proteins that act as auxiliarires to the ABC-transporter in the gamma-hexachlorocyclohexane uptake permease system in Sphingobium japonicum. Gamma-hexachlorocyclohexane, or Lindane, can be used as the sole source of carbon in S.japonicum in aerobic conditions. Lindane is an insecticide.	2.3104e-25
NZ_CP046670.1\|WP_141151795.1\|1351090_1352233_-\|paraquat-inducible-protein-A	gnl\|CDD\|225542	COG2995, PqiA, Uncharacterized paraquat-inducible protein A [Function unknown].	4.94277e-98
NZ_CP046670.1\|WP_071951129.1\|1338914_1339529_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.15899e-15
NZ_CP046670.1\|WP_157315801.1\|1347550_1348651_-\|diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	3.26806e-60
NZ_CP046670.1\|WP_157315794.1\|1331210_1332125_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. 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.	2.19834e-80
NZ_CP046670.1\|WP_024016013.1\|1349441_1351094_-\|intermembrane-transport-protein-PqiB	gnl\|CDD\|182747	PRK10807, PRK10807, intermembrane transport protein PqiB.	1.01639e-141
NZ_CP046670.1\|WP_157315797.1\|1340050_1342171_+\|TonB-dependent-siderophore-receptor	gnl\|CDD\|227115	COG4774, Fiu, Outer membrane receptor for monomeric catechols [Inorganic ion transport and metabolism].	4.57585e-73
NZ_CP046670.1\|WP_141151796.1\|1353511_1354186_-\|hypothetical-protein	gnl\|CDD\|370579	pfam09603, Fib_succ_major, Fibrobacter succinogenes major domain (Fib_succ_major). This domain of about 175 to 200 amino acids is found, in from one to five copies, in over 50 proteins in Fibrobacter succinogenes S85, an obligate anaerobe of the rumen. Many members of this family have an apparent lipoprotein signal sequence. Conserved cysteine residues, suggestive of disulfide bond formation, are also consistent with an extracytoplasmic location for this domain. This domain can also be found in small numbers of proteins in Chlorobium tepidum and Bacteroides thetaiotaomicron.	7.28819e-46

>NZ_CP046670.1|WP_157315797.1|1340050_1342171_+|TonB-dependent-siderophore-receptor
MKFRLTSIATAIILSPAAFAADMEDIERLTVEGKYLSVNQSNSIKSPTPIIDVPQSLSIMTAEEITARGITSVGQIIDYTPGVNTSQGEGHRDSVVFRGVRSTADFYLDGNRDDVQYYRALYNVEQVEILRGPNALLFGRGGTGGILNRVSKKAKTGEKFVNYNVSANTFGAYNLQLDTNVDTGDKSALRINAMYESLDNHRDFFYGDRYGFNPTARFEVSDDTTVDVSYEYIDHERFIDRGVPTANGEPVEAFEEIVFGDPDNNYQTLGADVFRANVQHTFSDNLKGNFNAFYGDYDKVYSNFYAAGYDADAEVVTLDGYVDTTQRENLILSSNLVGEFATGSIEHTVIFGGEVINTKSNQDRYNPEFDSRVGANDPEGTLRNDQEMFNVSRPLNFRGLSGVNSAGNAVTATFYNGVDNTLNDDTHVDLDVYSFYVQDEIALSENFDLVLGARFDSFDIEVFNVKAAETRSRKDEEVSPRAGLVYKPQENISIYASYSESFLPRSGEQYANINGDADALDPDTFTNQEIGIKWDFNDSMSFTAAIFENEQTSLDNDPNDPESFVEVDSDVSGFELQLQGYITDKWYVTANYSNLDGENASGVELRELPENTMSVWTTYEVSDVFGFGIGATYQDESKVSTSDTSPVLPSYTRVDASAYYTLSDKTRLQLNIENLTDTLYFPNAHSTHQVTVGAPINARLSLIGSF
>NZ_CP046670.1|WP_071951129.1|1338914_1339529_+|TetR/AcrR-family-transcriptional-regulator
MTGNTRTRSDAKREAIIQAATQAFQEYGVNGTSMDKLAELANVSKRTVYNHFATKEDLVMHLVTKQFEDAKLSVTVVYDPARELSEQLCELIFQDIEFTVTEEHLDIARVAIGHFFYEPEKLKDEVAQLKAQETALHRWLKAAKADNKIDFDDLSRVVDEIDSLVKGQCFWPQLFKIEDVLSNQDKHNVAKNTVALILGRYAVT
>NZ_CP046670.1|WP_041912852.1|1337636_1338719_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MMRFTHLLFLSILSVSALTACSSEEPVKEQSQASPRYVKLATVSNIPDYDEFTFPAVVSAVKTVDLSFEVSGRLIQTDLVTGSDISKGKLLATIDRKPFERRVDESKTRLEQAKRELDRIEKMFAQKLVAQSSLDSAKTSYELAVIDLKNAEQDLSYTQLYAPFDAKVSQRLVENNSFVAAGTPIARLQDVSKIYFNINVPERLLTANIGRGIKQASATLATNRSQWYPVNYVEHSTQPDPVSQTYEVVFAMEPREELPLTPGARAVVKVSLQGSLYPEGLVVPVRSLVGNADAGFSVWVYNEASNSVTKQTVEVKHIEDELAIIESNGQSNLTLGQKVVAAGATQMRANMKVLPYQGEK
>NZ_CP046670.1|WP_071958866.1|1334591_1337633_-|efflux-RND-transporter-permease-subunit
MDIARYSIDKPVNVWLMVVILLLGGVLAMSKIGRLEDPAFTIKQVKVYTNYPGASAEKVEREVTERLEIAIQQMPQLKEVTSVSSPGLSEITVEVKSTYDSNLLPQIWDELRKRLRDTASSLPAGAQDPIVFDDFGDVYGLYYALSAPDFDTRELREFARIIRRDLLTTEGVAKVNVTGVQKEQIVAYINPYQLAGLGISFPDLAALFEDNLRPFNGGRIKVDEKNVRLIVERAPDRLEEISNLSVVVPGTNRSLRVADIATLKLEPADIQPVHVRYNGEEALTLSVSALTDVNIVDVGARVNAKVEKLLQELPVGITLTPIYDQASVVDESVTGFINNLVMSVAVVTLTLCLFMGWRSGVVVGAVLLVTVLGTILIMWLMDIQLQRISLGAMVIAMGMLVDNAIVVAEGMMLRMATGSTAKASASFIVKRTQWPLLGATVIGIAAFSGIGLSNDATGEFLYSLFAVVLVSLMISWVLAVTLVPVLGSYFYRKGINQTNNNEPSAMQKWFKGTLLSALRLRWITIGALFVITIVAYGSFGMVKQGFFPPSNAPLFFVHYWGPQDRDIRATEEVAKEAEKRILEMENVTAVTTFIGQGADRFTLTYAPKSANENYAFFMVRANELENIPAIQSALADKLTHLDFDASFYMERMQFGPGSGAKLEARFSGPDADVLRQLAEEAKARLFEDGQVKDIRHNWREKGFAINTQYDNYNAGIAGVSHSDFSQTIQYASSGVQLGTVQDGDYAYSIVAKMGKAEDTELQSIRESQVWSTQQRQYVPFTQVSQGLELMTEEMRIHRRDRVRTITVEAEPGDDETAAKALARIRPVIEDIDLPQGYSLEWGGEFESSSDAQKALGAGLPAGFLVMFIISVLLFGHARQPLIIWLVVPMAIVGVVTGLLATDMPFGFMSLLGFLSLFGMLIKNAIVLIEEIDLQIEEGLAIRQAIVEATISRVRPVSLAAVTTILGMAPLLFDAFFADMAVTIMGGLAFATVLTLIAVPVLYSLLFKVSYRKS
>NZ_CP046670.1|WP_071958865.1|1334051_1334471_+|CBS-domain-containing-protein
MGIANIMSTRVVSVHMDDSLQSLRELFAATGFHHLVVVHDNKLQGIISDRDLMKSVSPFVDTLSERLLDRATLDKRAHQIMTREVITLNPSDSVFAAITLFNNHKISCIPIIDEDRHPVGMVSWRDVMKFMQSRVEAKR
>NZ_CP046670.1|WP_157315796.1|1333423_1333921_+|DUF45-domain-containing-protein
MNEYARYFNGYPSNIVEQALKLIENNQLKHYLLKKYPEAHAITTDKLLYQYATDVKKRYLKNASPFGRAAFKKQGDMVTNALGTHTYRMQGKTRKHDLAINSDLLCAPGPLLKALVVHELAHFKEKEHNKAFYKLCCYMEPHYHQLELDLRLFCVAVSLGENPYA
>NZ_CP046670.1|WP_157315795.1|1332240_1333230_+|zinc-binding-dehydrogenase
MKAMVINEFGGTEQFTQSDIAEPTVKAGHVIVRIAASSVNTIDMMIRQSGADLPFAPQLPGVLGMDFAGTIEAVGEGVTNYKVGDEVYGCAGGLGDLKGSLAEKMLADVRLIAHKPKALSMKEAAGIPLVGITAFEGLTRALTSEGQKVLIHGGAGGVGHIAVQLAKHMQATVFATGGSDEQKEIIESLGASYIDYRSESVEDYVSKYTDGNGFDVIFDTVGGNNLQNSFAAAKLNGQVSTTLSLLETDLSPVHFRGLSLNVVFMLLPMIHNVGREAHGEILKELASIVDAGALKPIIDAEEYTFEQIAAAHDRLASGKAVGKVVVTVE
>NZ_CP046670.1|WP_157315794.1|1331210_1332125_-|LysR-family-transcriptional-regulator
MNIEHLKLFVRIASTANISLAGRELNISPAVASAHIGKLEDTLGVRLIHRTTRKVSLTDEGKLFLPHAQEVLDSIETAQAAVGSGAQTPQGTLRVTAPASFGRMHLVPAINEFLKQYPKLNIDFRFSDSILDVVEGGFDVAIRDAELKDSNLHAKKLADDKRIIVASKSYIEKNGAPQTPADLKNHKIVNLTGLEVWDFKGSHGTISIKTPNHLRMDNGEAVRDACIQGCGLTLTATWCSYPYLEDGELVQVLHDYPLATDCALWAVYPTNRLLAPKVRAFIDYLAERFSGTPYWDEKLSGIVA
>NZ_CP046670.1|WP_071960377.1|1329792_1331037_-|hypothetical-protein
MINKPFTFIAAAVSILVAQCVSADQEKLKVSGFGTLASATADTRIYQFRNDRSQAEYAKKDGFAFKPLSLIGVQLDYSVSDDLDFVGQFVYREQDEQNIDSITQMAFLRYDITPSWQVRAGRLAADIFHFSDTRDVSIAYPWVKVPTEVYGIVPARSFDGADISYLRRYRDFNLSVKGFWGEGESDFSSNAFEPITFENLRSLGIELTAFDWSVALKHTRTEAENDNFDTAFVAENVAQLQPFWGGAVDFSNSLTLRNATIQYTSLYANRYLGDWEVSGELSHIDSESVALRPSFNGFLNVSYLSGAHTFYGLFSFAKTDTYFLSEEQPNFPIIPATAELAIFVEEVASTLAHNQQTISVGWRWDLRENLAFKTQVERTDIDARGTGLRARNGLVVDDEEGVAHTLFLALSFSF
>NZ_CP046670.1|WP_071968486.1|1329339_1329783_-|hypothetical-protein
MKIFSRSPLIVTVVLLFTSFSCAAQVPDTIVVVTNQKNDVQILDKKGLIDLFMGKYSAFPNGKQATPIDVELDAKLKAQFYQALVGLPLARVNAYWSRLKFSGRVKPPAVEQTLDDVRQRLEADESALAYVYESSVTDKMKVVYRFD
>NZ_CP046670.1|WP_157315799.1|1343059_1346239_-|acriflavin-resistance-protein
MNNQNNTQSGIIAWFARNSVAANLLMFFIIIMGIASYFTIQRQMFPNIEINYITIEATYPGASPQEIEESIFIKVEEAVKDITEIKRTVSRAFRGGGAVTLEIDTKAELTDVLDKVKLRVDSIATFPAGMEPVNVSQVEFQQQVIEMPLVGDLPLSELKVLAKEVEDELLQLGSISLVEANTPDDEIAVEVKPDTLRKYGLTIGDITQAINSYSANISAGQLRTNSGIVSVRVENQYYSGDEFKQIPIKIGAGGAKVTLGDVAYINDGFEEGERYFKYNGMNAIYIAVKATKTQNTIPVAETVKAYIDQKNETLPQGISLQVLVDMTYYLNARLDMMLSNLIQGSILVALMLTLFLRFRLAVWVMVGLPVCFLGAMMLMPVFGVSINILSLFAFIMVLGIVVDDAIVIGESAYTEIESKGGGVDNVVRGAKRVATPATFGVLTTIAVFAPFTLSSGPEGAFFYNIAVVVILCLVFSLIESKLILPAHLAHTKFSPVKQDSWRARFNKRFFAFVNGPYKRTVTKAIEWRWAVLMMFVAMFMLSLGLIGANYVRMVPNPKVPHDFPSVKIEMNENVSDMTTINALKIVEQTILDVEEQIIDEFGQGMIRDRLAFNEDRTEGRILTPLVNEEDRPIDTFELARRWREAIPEITGMKSFTVIDDVNGDGDDGEFGYLLFGPDIDTLNAAGLKFIEMLQQQEGLFDVSSTIDPPSKEVQMTLLPVAYDLGLTLSNIASQVGAGFYGGEAQRVIRNGEEVKVMVRYPELTRERFADLKYSLITTPSGQEVMLGDVVALEEKPGISYIRREGGYRSVYIWGNIDEEKVEPNEVVTEIQDKLLPQLKELFPSVMTELGGDIEEQQAQQNEQILFFLAAMIMVYILLAVPLKSYGQPLIIMSVIPFSFTGAVFGHFVLGLDLSMMSNFGLIAAAGVVINDSLVMTDFVNQRRAQGYSIKEAVTEAGTARFRAITLTSITTFVGVLPIMFETSLQAAFVVPMAAALGFAVLYATLVTLILVPCLYLILLDLRGPFSFIKNKIVRRKSVNRNVDNSATHDYSPASSGASD
>NZ_CP046670.1|WP_157315800.1|1346248_1347397_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MKWMKFALPIGVLIVGYIGMKGIEASASDSVITEEVDTRPTVTIEALAPEDVRVQLTSYGEITPLETTNLSAQVSGEVQQWNPKFVSGGLVRRGETLFEIEADTYEAALLMAEANLASAEAQLIQEQAQADVAAREAKTMPNARVTDLYLRKPQVMSAKAALKSAQAQLKIAKRDLENCKVKAPYDALVVSRGISTGDYVTQGTPVAVINNIEYAEVTFPVAGFDRVFLADNTIGSEIAIEVDDIQGATVKGTVHRDTGVIDNNTRMSYFVARIEDPYAINSSKPIIKFGSYSTIAFEGKTLSDVYRVPQELITNRLLWTLDGEDRLTSQKVTVVREENGDFLIQGDFNANKVVMSLPEYPQNGMPVKVIETTTDLVTASAN
>NZ_CP046670.1|WP_157315801.1|1347550_1348651_-|diguanylate-cyclase
MLGPIKQYVLSGVNRRYKDETNRRIMVVNLFAAVGMSITLLLGSRAFIDGEYFLSTILFSASVIFALSQRLQVRVATAKARTWSITLLIFCLMALTLLLVITGGKDNTGPLWIYLVPPVTMFFAGFIRGLLALVAYTIACTIVLFGFNEAGFVANYSYAFKTRLLYSFATVTFLSAFYEYSRQKSYDTALYLSKQFERQAKHDHLTQLLNRRGAQQCLEREYARMQRNKRHFSIAIADIDRFKSINDSLGHEQGDEVLRQISNVFKTRLRSQDVLARWGGEEFMFIFNDTDEAGAVKALEQIRETLNNAPLNVNDSEIYISSSFGVCEVTPNIDTSSAIRLADKALYHAKEQGRNLVCAASTLPCR
>NZ_CP046670.1|WP_157315802.1|1348653_1349265_-|hypothetical-protein
MMMQSKATSSFTKRKTIYISTLAFLICFLSACSSAPTGLTYYLLHATGDVSYIQEDAKQTIVLDKITLPEYLKHRGLVYQTSDTNLHISTSHLWAEPVDEGLTKSLTGALAVKRVSLVRPDHYASEESVHMTLHIDDFVSTYEGEVVFSGQFVITRASGENTPHSFVFTSPLANDGFSSSVKAMRDAIEKLAVDISKAAVSAG
>NZ_CP046670.1|WP_024016013.1|1349441_1351094_-|intermembrane-transport-protein-PqiB
MTANDPNVNEAKVKPTSSISRIWIIPILVIVIGGWMVYYQWKNQGPLITIELHSAAGIEINKTPIKVRDLDVGQVKKITLKPDLDGVLVTARIDASAAHLLNENAKFWVVAPRISFSEVSGLNTLLSGSYIAMSANDKGKEQLHFTALERPPVTPPGTPGLHVMLKSDDEFAYKPGDPIIYKGFKVGEFEDATFNIEERVVYYDAFIEAPYHKLITNTTRFWDVSGVKLLLESNGVSVETGSLETLLANGITFGIPEGVPKGEQVLDNAFFTIYGDSTSASDARYKVAAEYLLLIDESVRGLTVGAPVEYRGIEIGNVTAINSFPAVEGNILERDYPIPVLINIYPGKARQPDTDEGLSAIKQTIRNWLHRDLRASLRMGNILTGGLYVDLQHVPDADGSGKIEVINGYEVIPTVSNEFTQLTQKADAILDKINQLPLKEMVENVQLAVDDMRLAAESVETASDDFDVLIGDIDAKALNSNLNQVLVSLDGLLKNYSEGGFNQSEIKETVDALQETMRNMQPLLLKLNQSPNSLIFSQGSESEIQPKAKN
>NZ_CP046670.1|WP_141151795.1|1351090_1352233_-|paraquat-inducible-protein-A
MAESNTLSIVCEQCHTKVNIPALAHRQRAVCPVCNHTLISHRDGASEKLLALSFSALIFLLLSLPFNFLTFKASGQKHSIDLPTGITVLIEHDYLSLAIITSLATLLLPGMVLAGLVLLCLAHLQGRRPFYLPRLFTLVKALLPWSMAEIFLVGTLVSLIKITELADVSIGLSFYAFIGFSAFTALCISQFDPTRYAMWLSQGAPPQPKPLSEVQAKVSIQRTWALLITACILYIPANLLPIMYTEFFGRETPNTIIGGVISLWESGSYPVAIIILVASVIVPVAKIIILAWLNFSVQREKTTSKQLRIRYYRITEAIGRWSMIDVFVVAVLVSLIQMGNTMSIYPGQAALAFCAVVFVTMIAAMTFDSRLIWQQWKQLP
>NZ_CP046670.1|WP_071951135.1|1352387_1353401_+|hypothetical-protein
MQVTNEIRSVYEKIKKPARRLLQKRRIGFLRFWLSITFAQRCYFLATSMLVLQLFLTIESSLFEAIMFGFALAGIISEVWPKFMTLWNSLPGKAVILFIYAIIANFALASASGLVNSITGVSSGALPYSHNFALILMVPGWFFVTTLMALVSGMLIIFIYLFFLLLLKPFGVQRLWHKPGYRYVLSTAVARFVWTLGVALQLSVLAGQVGLLSEFSAESTSQLITIENETETSIEESEPPLTEEQAEVTSELEGDLTALLTDAKQKSIRYKRAQRQALASFIYEFEADSRSRCAHPEGTRVIELNDYEILQIVQTPEDEIGYTYTVEPCRSAAIGLN
>NZ_CP046670.1|WP_141151796.1|1353511_1354186_-|hypothetical-protein
MTSTTAEPASVNSTSRKFESSVSTFQDLEGNRYKTVKIGKLEWFAENLRATQFQDGSPVASGFIPKDDEKNLFKYGRLYHWQDVNDERKLCPSGWRIATDEDWQSMERAIGIAKSDLAKEGWRGNNDIAITLKAEQPNTLFKKFDQAKVNQYHFGATAAGVKIGNWYITQGMYTEFWTSTSATDKEAYARTLAYSWWNSHKGEIRRAKLNKDYMFSVRCVRDAK
>NZ_CP046670.1|WP_071951137.1|1354245_1355196_-|SDR-family-oxidoreductase
MAKSNQFGKGGWTPSRIENANGKTFLITGANTGAGYEATRILLSKGAKVVMLNRSPSKSHDAIATLKREFGDDANVSYIRLDLSSLNAVRQSAKEILAQVPVIDALICNAAIAQISTQQFTEDGFESQLGVNHYGHFLLCGLLFDRINESEGRIVVVASEGHKMGLRTMQFDDMNWDKNYNPNKVYSQSKLAQMMFAYELQDKVKAHNKQVKVFVCHPGASNTTLIRESASFLTRISWAFMVKIGLAQSAEKGAYPEVMCATEENLKQRAYYGPTGLMNFGGPVGECRLEDFAVDKKVLTKLWAVSEEATGFAWSF
>NZ_CP046670.1|WP_157315803.1|1355413_1356313_+|helix-turn-helix-domain-containing-protein
MSKALIKQLIEEKVESSGLYATGIDGVQLFKITQPIECAPVVYEPSLTAIICGGKEAILNGEKYTFNTSKYTCCTMSMPVEAGIPDASKDSPLLGVYISLNSRMMTDLAIEFESVGGNFSQSSASSAPSGIASAHWDADFTEALYRLLLLTDNAIDIAMLSSARLRELYYSVLKGEAGSAVRGSFGVGNAIGRAIEYLASHVVENVTIDDMASKVGMSKAVFHRKFKQATNMSPIQFVKSMRLNNAAKRIADGTNVSVAAMDVGYVSSSQFSRDFKRMYGLSPKQWEKENKAKAATMLQ

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Crispr_ID: NZ_CP046670_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_4

1713449-1713587

Orphan

Consensus_repeat	Method
TCGTTAGCGTGGGTGTCTTTGTAAG	CRISPRCasFinder

2 spacers

DEDDh

The CRISPR arrays of NZ_CP046670_4

>merge|NZ_CP046670|4|1713449-1713587|CRISPRCasFinder
TCAATAGTGTGGGTGTCATCGTTAGTTTGTGCATTTAACACGGGGGCCAATTTTTCATTATCGTTAGCGTGGGTGTCTTTGTAAGATTTGTTCGACGCCTTCGGAGTTTCTTGCTCGTTAGCATGGGTGTCTTTGTAAG

>NZ_CP046670|4|4|1713449-1713587|CRISPRCasFinder
TCAATAGTGTGGGTGTCATCGTTAG	TTTGTGCATTTAACACGGGGGCCAATTTTTCATTA
TCGTTAGCGTGGGTGTCTTTGTAAG	ATTTGTTCGACGCCTTCGGAGTTTCTTGC
TCGTTAGCATGGGTGTCTTTGTAAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_157315946.1\|1727277_1728471_-\|23S-rRNA-(cytosine(1962)-C(5))-methyltransferase-RlmI	unknown	unknown	gnl\|CDD\|185082
NZ_CP046670.1\|WP_157315943.1\|1720656_1722003_+\|Na+/H+-antiporter-NhaC-family-protein	unknown	unknown	gnl\|CDD\|224671
NZ_CP046670.1\|WP_012518176.1\|1718147_1719059_+\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|366403
NZ_CP046670.1\|WP_071951327.1\|1702600_1704256_-\|DUF342-domain-containing-protein	unknown	unknown	gnl\|CDD\|377177
NZ_CP046670.1\|WP_157315942.1\|1719107_1720382_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|197666
NZ_CP046670.1\|WP_157315947.1\|1728622_1729600_+\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176180
NZ_CP046670.1\|WP_157315940.1\|1711084_1711504_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341392
NZ_CP046670.1\|WP_157315939.1\|1704382_1705813_-\|exodeoxyribonuclease-I	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|236979
NZ_CP046670.1\|WP_157315945.1\|1726926_1727178_+\|DUF2061-domain-containing-protein	unknown	unknown	gnl\|CDD\|225746
NZ_CP046670.1\|WP_157315937.1\|1698515_1699640_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|224423
NZ_CP046670.1\|WP_141151937.1\|1709876_1710920_+\|isoaspartyl-peptidase/L-asparaginase	unknown	unknown	gnl\|CDD\|366471
NZ_CP046670.1\|WP_071953208.1\|1701000_1702404_+\|transporter-substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|270426
NZ_CP046670.1\|WP_141151939.1\|1715000_1717706_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|273804
NZ_CP046670.1\|WP_141151936.1\|1706031_1709757_+\|response-regulator	unknown	unknown	gnl\|CDD\|236848
NZ_CP046670.1\|WP_141153089.1\|1713812_1714859_-\|acid-phosphatase	unknown	unknown	gnl\|CDD\|277324
NZ_CP046670.1\|WP_157315944.1\|1722103_1726132_+\|ATP-dependent-RNA-helicase-HrpA	unknown	unknown	gnl\|CDD\|182986
NZ_CP046670.1\|WP_015066941.1\|1697246_1698422_+\|acetyl-CoA-C-acetyltransferase	unknown	unknown	gnl\|CDD\|180261
NZ_CP046670.1\|WP_157315938.1\|1699632_1700868_+\|kynureninase	unknown	unknown	gnl\|CDD\|226363
NZ_CP046670.1\|WP_015066940.1\|1696493_1696901_-\|MerR-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133403
NZ_CP046670.1\|WP_015067025.1\|1726353_1726656_+\|PilZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|377796

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157315946.1\|1727277_1728471_-\|23S-rRNA-(cytosine(1962)-C(5))-methyltransferase-RlmI	gnl\|CDD\|185082	PRK15128, PRK15128, 23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI.	0
NZ_CP046670.1\|WP_157315943.1\|1720656_1722003_+\|Na+/H+-antiporter-NhaC-family-protein	gnl\|CDD\|224671	COG1757, NhaC, Na+/H+ antiporter [Energy production and conversion].	4.05623e-70
NZ_CP046670.1\|WP_012518176.1\|1718147_1719059_+\|diguanylate-cyclase	gnl\|CDD\|366403	pfam00990, GGDEF, Diguanylate cyclase, GGDEF domain. This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation 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. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, Structure 3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclisation of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.	1.30206e-28
NZ_CP046670.1\|WP_071951327.1\|1702600_1704256_-\|DUF342-domain-containing-protein	gnl\|CDD\|377177	pfam03961, FapA, Flagellar Assembly Protein A. Members of this family include FapA (flagellar assembly protein A), found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction.	3.14749e-131
NZ_CP046670.1\|WP_157315942.1\|1719107_1720382_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	4.33824e-12
NZ_CP046670.1\|WP_157315947.1\|1728622_1729600_+\|zinc-binding-dehydrogenase	gnl\|CDD\|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	2.35652e-155
NZ_CP046670.1\|WP_157315940.1\|1711084_1711504_+\|CBS-domain-containing-protein	gnl\|CDD\|341392	cd04629, CBS_pair_bac, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	5.06566e-50
NZ_CP046670.1\|WP_157315939.1\|1704382_1705813_-\|exodeoxyribonuclease-I	gnl\|CDD\|236979	PRK11779, sbcB, exonuclease I; Provisional.	0
NZ_CP046670.1\|WP_157315945.1\|1726926_1727178_+\|DUF2061-domain-containing-protein	gnl\|CDD\|225746	COG3205, COG3205, Predicted membrane protein [Function unknown].	2.47813e-22
NZ_CP046670.1\|WP_157315937.1\|1698515_1699640_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	3.57159e-13
NZ_CP046670.1\|WP_141151937.1\|1709876_1710920_+\|isoaspartyl-peptidase/L-asparaginase	gnl\|CDD\|366471	pfam01112, Asparaginase_2, Asparaginase.	1.66391e-136
NZ_CP046670.1\|WP_071953208.1\|1701000_1702404_+\|transporter-substrate-binding-domain-containing-protein	gnl\|CDD\|270426	cd13708, PBP2_BvgS_like_1, Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS 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.	6.7043e-86
NZ_CP046670.1\|WP_141151939.1\|1715000_1717706_-\|TonB-dependent-receptor	gnl\|CDD\|273804	TIGR01782, TonB-dependent_receptor, TonB-dependent receptor. This model represents a family of TonB-dependent outer-membrane receptors which are found mainly in Xanthomonas and Caulobacter. These appear to represent the expansion of a paralogous family in that the 22 X. axonopodis (21 in X. campestris) and 18 C. crescentus sequences are more closely related to each other than any of the many TonB-dependent receptors found in other species. In fact, the Crescentus and Xanthomonas sequences are inseparable on a phylogenetic tree using a PAM-weighted neighbor-joining method, indicating that one of the two genuses may have acquired this set of receptors from the other. The mechanism by which this family is shared between Xanthomonas, a gamma proteobacterial plant pathogen and Caulobacter, an alpha proteobacterial aquatic organism is unclear. [Transport and binding proteins, Porins].	0
NZ_CP046670.1\|WP_141151936.1\|1706031_1709757_+\|response-regulator	gnl\|CDD\|236848	PRK11107, PRK11107, hybrid sensory histidine kinase BarA; Provisional.	7.47779e-60
NZ_CP046670.1\|WP_141153089.1\|1713812_1714859_-\|acid-phosphatase	gnl\|CDD\|277324	cd07378, MPP_ACP5, Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	1.97135e-67
NZ_CP046670.1\|WP_157315944.1\|1722103_1726132_+\|ATP-dependent-RNA-helicase-HrpA	gnl\|CDD\|182986	PRK11131, PRK11131, ATP-dependent RNA helicase HrpA; Provisional.	0
NZ_CP046670.1\|WP_015066941.1\|1697246_1698422_+\|acetyl-CoA-C-acetyltransferase	gnl\|CDD\|180261	PRK05790, PRK05790, putative acyltransferase; Provisional.	0
NZ_CP046670.1\|WP_157315938.1\|1699632_1700868_+\|kynureninase	gnl\|CDD\|226363	COG3844, COG3844, Kynureninase [Amino acid transport and metabolism].	8.65366e-150
NZ_CP046670.1\|WP_015066940.1\|1696493_1696901_-\|MerR-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|133403	cd04776, HTH_GnyR, Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR. Putative helix-turn-helix (HTH) regulatory protein, GnyR, and other related proteins. GnyR belongs to the gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation in Pseudomonas aeruginosa. These proteins share 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. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	1.89936e-57
NZ_CP046670.1\|WP_015067025.1\|1726353_1726656_+\|PilZ-domain-containing-protein	gnl\|CDD\|377796	pfam07238, PilZ, PilZ domain. PilZ is a c-di-GMP binding domain which is found C terminal to pfam07317. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This domain forms a beta barrel structure.	7.2413e-13

>NZ_CP046670.1|WP_157315940.1|1711084_1711504_+|CBS-domain-containing-protein
MESLQVSDYMNTHPVKLNIDMPVAQAVEVLLASGQSGGPVLDTKGRVVGFLSEQDCIAQMIASSYYREQICRVGEIMKTPVVSVKPYMSVIELAQLLLKEKPRVYPVVDDDGVLLGCINRMAVLRAIDVQLNDGYQRAG
>NZ_CP046670.1|WP_141151937.1|1709876_1710920_+|isoaspartyl-peptidase/L-asparaginase
MNLARFSVSSNGWYKTLWTFSAVTAALLATNALAQEPKVAIAIHGGAGTILKSSMTAEKEAAYKNVLSKAVKHGYSLLKEGEKGEVAVVETIKILETSPLFNAGIGAVYTFDGEHELDASIMHGGSKNAGAVAGVKTIRSPIEAALLVMNESPHVMLSGEGAEQYAKENGLEQVKNTVFDTEFRKQALDKVKARMEKASSGYGTQQGNERFGTVGAVVLDRGGNIVAGTSTGGMTAKRYGRIGDSPVIGAGTYADNESCAVSATGHGEFFIRYHVAADICARMKYQGLTLAKAADTVVNDVLVKAGGDGGVIAIDSVGNIAMPFNSAGMYRASIDTEGKVSIAIYKD
>NZ_CP046670.1|WP_141151936.1|1706031_1709757_+|response-regulator
MDIVCLSSFTPKSTLSEAKGTFGLTVVLAVVLVILVVGLFESNIKAAATAQTYSALEKSAANAEAAADMQVLQYTNALNFLHQTPPISGIVRATANGNVDPKDSTTLDQWKHRLETIFVAFIENNSEIDQLRVIQSNDEGSEVIRVEREGGAVIIASDIDLQTKASRNYFKESVKSNKGEFYISSINLNREYGKLEFPYKAVIRLSLPILSDANERYGFIIMNVNARFLLDQMKQALAQNQSLYVTDNEGYFTLHPDSDKSFSKDLNPSINWQSEFVQPLKAGRARLSPVEGENILYSVSRAFTIGGGQQVAPFYLHVSTPKSYVTALINDKRMSVYSVLVAVTIIFTVALLFFYRSNRKNIELAKVRGESVAIVAISKDAIFSVDAFGKVKSWNMAAESLFGIPSQVIINQHFSSFKPLSPLGLETVLTKGGKQETFTTPYIDGEKNEHKLLITASTIWGDNSQFSGVAVVIRDVTDEHKAKDAIERVNFKLEEKVVSRTKELTKATEEARKASSVKSSFISNISHEMRTPLNGVVGSLSLLKRQPLNDKAEQLVSMMEISCNNLSVLINDVLDLSKIEAGKLDINHQLFEPLTLIESLAKVFAVKAATKGLELIVDTTGLPRVEINSDRHRLNQVLSNLLNNAIKFTEKGHIQLNAALYENDAGLQQLHFSISDTGVGIAPESQPKLFTAFTQADASVATQYGGTGLGLSICKQLTQLLGGDITFKSVVDVGSTFSFYVTLTEKTPDTEASLERALEMESAMLSGISIGVSAGYSPLEENICSLAMHVGADAYVLDSNADRIEWSTFNAVIVDESSPLINDLDNIWHAQTTEQEACALPVVFILQKIAGAPYQFNHIQPIYLPKPLFRSSFALVQQGIDAALGGYSSSMSELQPSEGNGPSDAAFETVKQTSDPQLSIEDANLLIVDDNLINREVAKGVLESLPGKMFTCCDGEEVIAFLQKCEKKGRRIHSILMDCQMPNMDGYETTRAIREGKAGPLHANVPIIAMTANAMLGEKEKCLEAGMDDFTTKPVIADVLIPKVKQWLIHQTMALKSEDAKRNNEIKSDAPALVDSLLNAINKEASCSGVQEEVSMDDLMSSHSDTNETDTSTSANESNAVSDIPAPDNGEVRESWDKDDAIARIMGDKALFSRVCELYSQSAPDKLKQLKGAVEEQDFAQVQVLSLKLKGMSADIGAVQLKKDFELVWELSKGAQWEKVKALLPSIDDDLNTFIELLAVA
>NZ_CP046670.1|WP_157315939.1|1704382_1705813_-|exodeoxyribonuclease-I
MHTPTFLWHDFETFGTSPQKDLPCQFAAVRTDMDLNVVGKPINIMSAIANDYLPHPEACLVTGITPQQTIRDGSNEADFAAKIYHEMSTPNTCSVGFNSIRFDDEVSRYLFYRNFYDPYSREWRNGNSRWDIIDVARACYALRPDGINWPLREDGSPSFRLEALTAANNIGHDNAHDALSDVYATISLAKLIKEKQPRLFDYALSLRNKHTVMQQIDLSKPSVLLHISSKLPASQGCCTWVMPIAKHPTNSNAFIVIDLSHDIDSVLNDSADEIKQALYAPSDTYDDARERPGLKLIHVNRSPFITTAKAMTEDNAQRLGLDRERCLDNYKKLASTPDLVSKIVAVYEEERHSSELDIDHALYSGGFLSDEDRRWCENVINAKPEDLATLGDKTQHEGLKKLLFRYRARNYPNTLTADEMTKWQYHRQARLTDPDFHGSITLETYMMRLESLAHEHSDNPEKQAILRALYQYAENL
>NZ_CP046670.1|WP_071951327.1|1702600_1704256_-|DUF342-domain-containing-protein
MNGVTISFDKSRTYINVMLNPSEFTSEVDIREIKKQLESGETKRLYVSEKALKSACDTANHYFKTGDGTIVQERIGERKNAEVEFRVPDDGMHANLVLTTPYGGKLPGLSTIKSLAIKNRVIRGVSTKKIESMLSNARRAEPGTVLEETIAKGLPAKNGKNSKFIPLVPNALERVLKPQADDGERVDMRNLGEIICVKVNTPVLRRTAPTQGRSGFDVKGNKLPAVAGEWVDFKMGSGTVVSDGDANLLMSAISGMPKYRDQIMNIDDTFISNGVNVGTGHVNYEGAVLVNGDVTEKMQIKAAGDVTINGFVESAHIEAGGDIIITEGAMGKVNDSQGEFQCKLVASGSIHVQHGQGIDIQCGGNITVGRQLAYSRLRCGGAVIVGQIDKPMGNLFACDIISQDRVEAGTLGAVSGSTLKVDFSPGFNQLLERKDSLDELLRQIRENNLKHKEKIALIQGKKIPKELQHKAAEALELFNNESALLEWLENKANDVKSAKENYQSDIKLIANKRLYPGVSAKLNNRNWRSEREYDRAQIHYDAHQWHYEPLI
>NZ_CP046670.1|WP_071953208.1|1701000_1702404_+|transporter-substrate-binding-domain-containing-protein
MLFLGASVFSAILKAGPEQQAAFTPSEEITYCIDPNWAPYEAIRNGIHVGISAQYMRLIAEIAELEFTLVPTESWQQSLEYVQQGKCKVIPMLNTSDYRKQFLDFSIPYFEAPNVLVAKAGTPMLQGYSGVGNRTVGIVQGYRQVEYISRHYPGLRLKLMPSEEEGLKQLANDEFDVMVGSLMSVNMHINNLKLKDINIVGYAEPFDSLAFGVNKSFGHLVDKLNFAIERIPESRKVEIYKQWNNVQIRYSRNYTVMILSTIIMLIGLLWLISRNRHVGAYKRIINQKNEEISSLQATLLEKNRTLGFLSAHDTITGLYNRNHMIQRAEEEISRFQRFQTTASLIILELTHSHDEGLSLEASSLEEPLKVVATQCLNTVREVDVVSRFSGEQFIILCPQTEVGAAKILADRLLNCVTSHYLLSDNFKVAIGMSELKQTEEFSDWMERTMKALYQSKRHGFGNVSIAP
>NZ_CP046670.1|WP_157315938.1|1699632_1700868_+|kynureninase
MINKVFSAEQLDDKDPLAHKAGAFSLPDNTIYLDGNSLGPLPKSAEKRALEVVQEQWGQGLITSWNKHQWISLPQQVGDKIGELIGAQQGQVICCDSISINLFKVLSAALKMNSGRKVIATTRDNFPTDIYMVQGLLDLLGEEYSIRYVDEASISSQLTDDIAVLMLTQVNFRSGLKLDMKDITEQAHAKGILTLWDLAHSAGAFPVCLDDCNVDFAVGCSYKYLNGGPGAPAFIYVARRHQDSYQQPLSGWMGHSAPFSFSPDYAPDSSVKQNLCGTPGVIGMSILDAALDVFDDVSLKAIDEKSKKLQAFFIAEAKRAGVLEHFGVASPPINCRGSQLALAHDEAYAICQAWIAEGVIADFRAPNILRIGFAPLYLSFADVEKAVTRLAIIMNEKRYENATFQQRQSVT
>NZ_CP046670.1|WP_157315937.1|1698515_1699640_+|alpha/beta-fold-hydrolase
MKNTVHITTFTRALFIALISLQQLAIAQSATFKSGSEPKFNYKDTQDITAVNKDIHRINTASKDTHVKNDARPPQSAPEIKQPANSDVKNDTHAKTSEIYKDTHDKPDELSGSSKTLTQVPYAALGVLPTREHDELFSYGESPLQHVYVWHGRNTKHDKLAGKAVVFVHGGCWLNAYGYDHASGFYKALADLGMGVFVMEYRRVGDKDGGWPGSLNDVTEAMITSLERIRGNGRYSKVYIAGHSAGGHLAMLAAQQLPQFTQSVSVEKVIGLAAITDINAYAVGANSCQTATAKFMHSMPDENPEAYQAATPNAKLINTPIVLMQGDADSIVPKLHATMAGAKQKIITNGGHFDWLHPDSTSFDALLEVIGEHD
>NZ_CP046670.1|WP_015066941.1|1697246_1698422_+|acetyl-CoA-C-acetyltransferase
MSNESVVIVAAKRTPMGGFNGSLSSLAATKLGEIAIKAACDEVDVSVIDEVIMGCVLPAGLGQSPARQASIGAGLPLSAGVTTINKVCGSGLKAVMMAHDLIKAGSASAVVAGGMESMSNAPYMLPKARTGYRMGHGQVIDHMMLDGLENAYDGKAMGCFAQDTADEENIGRGEMDEFALSSLSKAHEAINSGTFNDEIAPVTVSSRKGDTVVDTDEGPGSARPEKIPTLRPAFKKDGTVTAANSSSISDGAAALVVMSESKAKALGLTPLAKVVAHATNSIEPENFTVAPVGAMEKVLDKAGWTKEDVDLFEINEAFAMVTMLAIKKLGLDESKVNVKGGACALGHPIGASGARILVTLLHALKQSNGRKGIASLCIGGGEGVALAVEML
>NZ_CP046670.1|WP_015066940.1|1696493_1696901_-|MerR-family-DNA-binding-transcriptional-regulator
MNKYDDETTYAIGELAREFDITPRSIRFYEEQGLMSPSRTGQNRVYLNKDRVRLKLILRGKRLGFSLAEVKTLFDMYDTNPNSAVQLEAMLDMTEQKRAVLKQQLEDIQMLMTELDDVEARCREELAELKRGKIA
>NZ_CP046670.1|WP_141153089.1|1713812_1714859_-|acid-phosphatase
MLCFAFFFNSAWAQAKQQGPSQIGPTDIAPINTGPTQTVPYSHAYYEKTTIADLSVPDEAVSFLTLGDWGRNGHFYQKHVAKWLDIASYQLDAEFIATTGDNFYDNGIASVDDPYWISSYEAVYHQPHLFINWHPVLGNHDYRGNWQAQIDYSVKSRRWEMPAQYYSKTLALDDGATALLMFIDTSPLNPDYAREAKYQEAYEQGASEQLSWINTMLAQDQYTWKVVIGHHPLYSSGKRYGKTNAIKDVLEPVFHKHNVNLYIAGHEHDLQHNQLAGDELVHVVSGGGSEVRPVGNYEFTQFAKSTGGFVSVSMTAKSIFLNYIDHQGKKVYAHTINKPNTASSSSTL
>NZ_CP046670.1|WP_141151939.1|1715000_1717706_-|TonB-dependent-receptor
MKIKTAYSSLALACVTALGLSIASPVLAADGVIIGSVKDAAKARSYNGAKIKLIELGLVTEAGRDGTFRFPSIPKGTYTLEISYLGEDTVTQTIKVEDNDIARASVEFGTGETIDEILVRGQRSGQASAINQQRVSDRISSIVSADAIGQFPDQNAAESLQRLPGLSIERDQGEGRFVGIRGIDPNLNNVTINGLNIPSPESGVRSVALDVIPSELIQTLEVSKSVTPDMDGDAIGGSVAVKSVSAFDKARDTASVTVQASQNDLRDETSPKVSGTFTKKLSSKWGVAGAVSYFDRDFGSDNVESNGDDELEQRHYTITRERLGSALNIDFRPDFNNQYFLRTLYSEFSDDEYRQGNIFTFDGEDSEIERESKDRFESQSIFTVALGGEHQLDTWEANWQLGYAKSDEDEPDALYYIFKTENDSIDADLNTMRPTVSQNADAMDLSTYEVDEISFEDNYTKDTETSIKFDAARPINVGGYIGELKFGSKYRSREKDRDSSITIFDGDFDDLDAAQFGAASPDYSLDNFGPGLNRGVMRSYFNDNRESLEVDSLNSDVESRGATYVNEEDIFAAYIMGSVDIEKLHLVAGVRYERTDFSTSGMRVELVENEQTDVEEVVNTPWEAERDYDHWLPSVNARYTFSDKLQLRAAYTQTISRPKFEDVAAFQIIESKTEEDDGVFVTEREAEVGNPELQPYEAQNVDLSLEYYPGDVGVISAGLFYKNIDNFVVYADVAGTAGWEGFEEVIQPINGDSADLTGLELSWVKAFNNGFIVSANATFTDSEATTFLDGEKFETQLPNQSDRIGNLTIGYEANDFSVRLATTYKSENFEEIDGDMLRFEDDHVQMDFMARYYINDTMQVYFNGINLGDEPFYNYFDTRSQNAQYEEYGRTFELGFTWQLN
>NZ_CP046670.1|WP_012518176.1|1718147_1719059_+|diguanylate-cyclase
MFSFTNTTQFRHHTWWLAFTVSIVAIAISLALFLGNPKQSADISGLDIVGEGSIVLLTLAWILAALASRPPGKVTSLLVFGLGFFLFSATLDFLDEFLRYPDDAHWISMIESYPAAVGMVVMTAALYQWHLEQRALNLQLRRREWDYRDHDKIDPITQLYRAEYWKEQIQKLQQFNKSAVLAIIDINNFSLFNQQYGYTEGDRYLHEIAQLLVMNLRQHDLACRYAGDRFAILLPDVSPTQADIIIDEIKASIQHLAFRHQLNTNAIYTSARSTHVTLLPNQTLSTVLNAMLTELERPQKSAA
>NZ_CP046670.1|WP_157315942.1|1719107_1720382_+|helix-turn-helix-domain-containing-protein
MEISLSNFTVAASSHADEGGDTFGEKTKPIAELNELGVHAKKHVGVGVSVREGVGADSVGVSVREGVDADSVGVFAGTDVVQSTHDKVIAGYWLVKAVLDVALNRGANKNKLFRGTGIFEDALEPDSLISIKQYHLLLTNVQSQTKGADVSFLLGSALAAQWLHSPMHVLQTCDTLEALLTHLVHQQTFRWCSIPLCQFQCFTTNHKVMLIPQSTVGGAKLAQFVSEVSFASIVALLKGIAKQRVSVSFNFTCARPKNIADFETHLGLKVAFNCPFNSMCIEKHALDESMSTPVIHSPNMVTDKELGRYRLFERYPLISLPDYVRCHVYQTISAHNMGSALPELAEKLAISPATLKRKLKEFNTSYRQLSEEVWRNYALVLLSVHKANNEQAARQMGINDLPNFRRTVKRLTGKTPSELRLSNA
>NZ_CP046670.1|WP_157315943.1|1720656_1722003_+|Na+/H+-antiporter-NhaC-family-protein
MRENNATAPNSVLPNPMGLTPILLFVVLVVVTGVTTNDITAMPILVAFFISAGYGLCLNPKGKKVSFSEKVQTFCQGGGDKNIILLVLIFLLAGAFYAVTIDIGARDATVNMALQFVPSALILPGLFLICCFISFSMGTSMGTITALSPIGAGLATNLGLPIEMALGIVVGGAMFGDNLSFVSDTTIAATRTQGVQLKDKFRANLMVAVPACIVTMALLLIVDVDTSGIVEGGNYDFWRIVPYLCIIAFALTGFNVISVLAVGIASACVVGLVQGSFTMLSMMQSIQKGMGWMQDLAMIAITIGGIVALMHANGGITWLIERLTRRVTSKKGAEFSIAGLVSFLDITTANNTIAIVTAGPIAKDLNEKYGVDPRRTASLLDIFSCSFQGLVPYGAQLLSAAAVVGISPLAITPYCWYPMLIFVFGVAAIWFGFPRFNTPQDDELTQSA
>NZ_CP046670.1|WP_157315944.1|1722103_1726132_+|ATP-dependent-RNA-helicase-HrpA
MSSPIAIKPLYNKLDDCLSADKFRLKRRITLLAQKAKGLGESKGAAPGDKSEASKRKEHEDSTSHSANKGSQKNAQKSAEESLSTQFEKLKADINGSIEKRNWRKANLPKVEYPPLPVSDKKEDIKDAIANNQVVIVAGETGSGKTTQLPKICLELGLGVNGMIAHTQPRRLAARSVATRIAEELNTPLGEKVGFKIRFSDQVSERSYVKLMTDGMLLAEMQQDRFLNQYDTIIIDEAHERSLNIDFLLGYLRQLLDKRPDLKLIITSATIDPERFSKHFNNAPIIEVSGRTYPVEVRYHAPEDFDEDRDQSDAIVHAVDELMREAPGDILVFLSGEREIRDTQDALSKQHYRNTEIVPLYARLSAAEQNRIFQSHSGRRIVLATNVAETSLTVPGIKYVIDPGFARISRYSARSKVQRLPIEPISQASANQRAGRCGRVSDGICIRLYSEDDYLGRPEFTDPEILRTNLASVILQMLALGLGDIAAFPFVQPPDNRNINDGFRLLEEIQAIGKGKGKQKGKMQLTPLGRQIARLPIDPRYARMVIEAERTNALSEVMVIAAGLSIQDPRERPQEKRQQADEKHSEYQNKDSDFISLYNVWVAFREQQNALSQNQLRKWCKQQFINYLRMREWQDIVSQLKKSIAELGFGISKQEADYQSIHQAIASGLLSHMGFKDKEREYMGSRNSRFLIFPGSGLSKSQPKWVMAAELVETSKLFARMVAKIDPAWVEPLAEHVVQRSYSEPHWSKKRGAVIAFEKVTLFGLPIVMKRAKVYSLIDPPICHELFIREALVEGNTKLNYSFLEENQALLEQADEFEQKTRRRDLIVDDEELVSFYAKRIPLEANNDAAFKKWFRQHGSNDSLTFKEEDVYRQQPGQSVANAFPDVWRQGNITLPLRYNFEPNAVDDGVTVVIPLPVLNQVDNIGFDWLVPGLRHDLIVGLIKALPKRLRRNFVPAPNFAEACLADISETDKNNRPVPLLEAVTDKLRKMTGVIIESDEWNLAQLDKHLKMHFAVVNDNGDDIAKGDDLHALKQQCAGQVKQTFEKAATPELERSNIEQWDFENLPETFVQKVGGFEVQAFPALVEKGDKVDIALIEEADKAQALHKQGVNVLIKNAMPSPLNYLQSKLPNKAKLGLYFNPFGQVKALIDDCIFAGIDAIVTDYCEANKTDIRNKADFEACLDIARANINDKVLEIAKQVEQGLTLAHQCQKQMKGNVPLTMINALGDCKAHLAQLVFPGFVSQIGEARLDDWNRYIKGLARRLEKLPIDPNKDRMHQVTVEKSTKEWEKTCSKYPKGKVPQALLDVRWMIEELRVSLFAQQLGTAYPISAKRITLHLAEY
>NZ_CP046670.1|WP_015067025.1|1726353_1726656_+|PilZ-domain-containing-protein
MLGYDDKRNFFRMMVNSPCQLQITDDESSRTMQAMCKDISATGMSLEVDEPSIEVGTQVSVAIESSSSQIPSLAALATVVRCEPESESSCIIGVEISQMK
>NZ_CP046670.1|WP_157315945.1|1726926_1727178_+|DUF2061-domain-containing-protein
MKKTITFAVMHFAVAFTVAYLLTGSVVVGGAVALVEPAINTVAFYFHEMVWKKIEARKEGATTEFASETSAPVRRNQDISFAS
>NZ_CP046670.1|WP_157315946.1|1727277_1728471_-|23S-rRNA-(cytosine(1962)-C(5))-methyltransferase-RlmI
MSAQVILQPSRDKSLRRKHPWVFESAVAELKGRARIGDTVDVFDDEGDWLGRGAYSPHSKIRVRMWTFKKDESIDNGFFLRRLETALALRKRLFDPNKTNAFRWIASESDGLPGVTIDLYDNVAVVQLLSAGGEKHRDKIVWAITKLMPDVHVYERSDVDVRKKEGLEPVTGVLHGQPPMQVTVKENGINIVVDIESGHKTGFYLDQRDSRAAAAHYAKDADVLNCFSYTGTFSCYALSGGAKSVTNVDVSQPALDLAKHHVAINGYDDKRAHYLNKDVFKALRKYHEQNKQFDMVILDPPKFVDNKASLNRAARGYKDINMYGIHAVKSGGLLLTFSCSGLMPADLFQKVVADAALDAGRTIKIIARLNQASDHPIIGSYPEGYYLKGLVCEVTDD
>NZ_CP046670.1|WP_157315947.1|1728622_1729600_+|zinc-binding-dehydrogenase
MHYVDFAKGCKPDELTVKEQAGYSLTAGKVKVEVKAFGVNRADTLQRQGNYPPPPGESEILGLEVAGIVSEVASDVSSFKEGDRVCGLVAGGGYATEALVNPAHLMRIPQGMPFFEAAGLTEVFLTAFQCLRTIAHIKPAQRALIHGGASGVGLAATQLCRYWGVHSAVTASSQEKLSLCEKNGAEQLINYKQQAFDEVLKKAWPEGVDMVLDMVGGDYLNRNLQVLKRDGSVVYLAMLAGRYADNLDMAMLLGKRASIIGTTLRNRSDEYKANLIGEFETACIPAFESKELTVNIDTHYSIKDIDKPHGRLENNDTQGKLVVSW

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Crispr_ID: NZ_CP046670_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_5

1984638-1984701

orTypeII

Consensus_repeat	Method
GACTAAATAAGACAGGCATGTTT	CRISPRCasFinder

1 spacers

Cas9_archaeal

The CRISPR arrays of NZ_CP046670_5

>merge|NZ_CP046670|5|1984638-1984701|CRISPRCasFinder
TACTAAACAAGACAGGCATATTTGTTTCACGGATGGAGAAGACTAAACAAGGCAGGCTCTTTTG

>NZ_CP046670|5|5|1984638-1984701|CRISPRCasFinder
TACTAAACAAGACAGGCATATTT	GTTTCACGGATGGAGAA
GACTAAACAAGGCAGGCTCTTTTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_157317150.1\|1988264_1988666_+\|acyltransferase	unknown	unknown	gnl\|CDD\|227389
NZ_CP046670.1\|WP_157316040.1\|1986079_1987057_-\|transposase	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316036.1\|1981541_1982123_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_015067152.1\|1972576_1973824_+\|glutamate-5-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|234685
NZ_CP046670.1\|WP_157316041.1\|1987374_1988094_+\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|350237
NZ_CP046670.1\|WP_076010900.1\|1978736_1979507_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376158
NZ_CP046670.1\|WP_071959179.1\|1975900_1978012_+\|polyribonucleotide-nucleotidyltransferase	unknown	unknown	gnl\|CDD\|236995
NZ_CP046670.1\|WP_157316042.1\|1988698_1989292_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|224584
NZ_CP046670.1\|WP_071959178.1\|1973954_1974905_+\|mechanosensitive-ion-channel-family-protein	unknown	unknown	gnl\|CDD\|223740
NZ_CP046670.1\|WP_012518312.1\|1978173_1978467_+\|DUF1244-domain-containing-protein	unknown	unknown	gnl\|CDD\|226023
NZ_CP046670.1\|WP_071951487.1\|1990136_1990328_+\|YHS-domain-containing-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316039.1\|1985692_1985938_-\|cytochrome-C-biogenesis-protein-CcdA	unknown	unknown	gnl\|CDD\|377822
NZ_CP046670.1\|WP_071951486.1\|1989693_1990071_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_141152037.1\|1989352_1989589_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316038.1\|1985375_1985693_-\|plasmid-maintenance-protein-CcdB	unknown	unknown	gnl\|CDD\|376629
NZ_CP046670.1\|WP_157316037.1\|1982883_1983834_-\|IS110-family-transposase	unknown	unknown	gnl\|CDD\|226077
NZ_CP046670.1\|WP_015067154.1\|1974951_1975506_-\|HNH-endonuclease	Cas9_archaeal	cas9_archaeal	gnl\|CDD\|372995
NZ_CP046670.1\|WP_012518321.1\|1982475_1982856_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|366361
NZ_CP046670.1\|WP_157316035.1\|1979604_1981203_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_071953221.1\|1990508_1991363_+\|DUF1444-family-protein	unknown	unknown	gnl\|CDD\|237463

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157317150.1\|1988264_1988666_+\|acyltransferase	gnl\|CDD\|227389	COG5056, ARE1, Acyl-CoA cholesterol acyltransferase [Lipid metabolism].	0.000553492
NZ_CP046670.1\|WP_071953221.1\|1990508_1991363_+\|DUF1444-family-protein	gnl\|CDD\|237463	PRK13668, PRK13668, hypothetical protein; Provisional.	2.21697e-07
NZ_CP046670.1\|WP_157316039.1\|1985692_1985938_-\|cytochrome-C-biogenesis-protein-CcdA	gnl\|CDD\|377822	pfam07362, CcdA, Post-segregation antitoxin CcdA. This family consists of several Enterobacterial post-segregation antitoxin CcdA proteins. The F plasmid-carried bacterial toxin, the CcdB protein, is known to act on DNA gyrase in two different ways. CcdB poisons the gyrase-DNA complex, blocking the passage of polymerases and leading to double-strand breakage of the DNA. Alternatively, in cells that overexpress CcdB, the A subunit of DNA gyrase (GyrA) has been found as an inactive complex with CcdB. Both poisoning and inactivation can be prevented and reversed in the presence of the F plasmid-encoded antidote, the CcdA protein.	3.09923e-29
NZ_CP046670.1\|WP_157316041.1\|1987374_1988094_+\|NYN-domain-containing-protein	gnl\|CDD\|350237	cd11297, PIN_LabA-like_N_1, uncharacterized subfamily of N-terminal LabA-like PIN domains. This N-terminal LabA-like PIN domain is found in a well conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. LabA from Synechococcus elongatus PCC 7942, (which does not contain this C-terminal domain), has been shown to play a role in cyanobacterial circadian timing. The LabA-like C-terminal domains characteristic of this subfamily may be related to the LOTUS domain family (which also co-occurs with LabA-like N-terminal domains). The function of the N-terminal domain is unknown. The LabA-like PIN domain family also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	3.16166e-62
NZ_CP046670.1\|WP_076010900.1\|1978736_1979507_+\|hypothetical-protein	gnl\|CDD\|376158	pfam18735, HEPN_RiboL-PSP, RiboL-PSP-HEPN. RiboL-PSP-HEPN. Fused to endoRNase L-PSP ; in operon with ParB.	1.62309e-05
NZ_CP046670.1\|WP_071959179.1\|1975900_1978012_+\|polyribonucleotide-nucleotidyltransferase	gnl\|CDD\|236995	PRK11824, PRK11824, polynucleotide phosphorylase/polyadenylase; Provisional.	0
NZ_CP046670.1\|WP_157316042.1\|1988698_1989292_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	1.47768e-29
NZ_CP046670.1\|WP_071959178.1\|1973954_1974905_+\|mechanosensitive-ion-channel-family-protein	gnl\|CDD\|223740	COG0668, MscS, Small-conductance mechanosensitive channel [Cell envelope biogenesis, outer membrane].	6.53517e-13
NZ_CP046670.1\|WP_012518312.1\|1978173_1978467_+\|DUF1244-domain-containing-protein	gnl\|CDD\|226023	COG3492, COG3492, Uncharacterized protein conserved in bacteria [Function unknown].	3.14416e-40
NZ_CP046670.1\|WP_015067152.1\|1972576_1973824_+\|glutamate-5-semialdehyde-dehydrogenase	gnl\|CDD\|234685	PRK00197, proA, gamma-glutamyl phosphate reductase; Provisional.	0
NZ_CP046670.1\|WP_157316038.1\|1985375_1985693_-\|plasmid-maintenance-protein-CcdB	gnl\|CDD\|376629	pfam01845, CcdB, CcdB protein.	9.83468e-38
NZ_CP046670.1\|WP_157316037.1\|1982883_1983834_-\|IS110-family-transposase	gnl\|CDD\|226077	COG3547, COG3547, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	2.96101e-24
NZ_CP046670.1\|WP_015067154.1\|1974951_1975506_-\|HNH-endonuclease	gnl\|CDD\|372995	pfam14279, HNH_5, HNH endonuclease. This domain is related to other HNH domain families such as pfam01844. Suggesting that these proteins have a nucleic acid cleaving function.	8.81504e-22
NZ_CP046670.1\|WP_012518321.1\|1982475_1982856_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	gnl\|CDD\|366361	pfam00903, Glyoxalase, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.	1.93523e-10

>NZ_CP046670.1|WP_157316037.1|1982883_1983834_-|IS110-family-transposase
MKKSVVQNINVGVDVGKDFLDIHIRPLGEYLKVSNDKKGIGEALKRLRKLTIVRIVIEATGRYEMAFVSACAKAELPFSVVNPIHVKRFAGAIGRKAKTDKLDAALIAHFSEVIQPALSTLKPENIQKMADTVARRNQLLEIQTREKNRLQIMPKTVQSSIKAILTVLKKQIQKMDGELADLIESCPEYQAKSELVQSMPGIGKVSAAALISYLPELGMMNSKQVAALVGVAPMNKESGRYKGKQVTQGGRHQVRTVLFMAMMSAMQCNAKFKATYERLVAAGKPKKVAIIACVRKMVVILNSMVRDGVMWEEKAA
>NZ_CP046670.1|WP_012518321.1|1982475_1982856_+|glyoxalase/bleomycin-resistance/dioxygenase-family-protein
MEMNQVTLPVKNMEEAVKFYLVLGFIQIVDTPHYARFSCPKGNSTFSLSLELEEFKNGAIIYFETEKLDMLAESLVAKGVIFEQLPTEQRYLWKEAVLKDPSGNKIKLFWAGENRLSPPWKVEKRG
>NZ_CP046670.1|WP_157316036.1|1981541_1982123_+|hypothetical-protein
MKLIKVALFTLFISQIAAAEINVSLANGTEKEELKREQIFRLIEQHDLKKWWFTDKIVIDESARSPFSHPVLTLKASMPNNDHAGLSQLLHEQIHWFEGSRKEEVDNTVAELRNIYSSVPVGFPDGARSEFSTYLHLAVCLMELDALTQILGKEKAEAVIATNGKYFYKWIYKTVLQDQAQIREILKNNRLYI
>NZ_CP046670.1|WP_157316035.1|1979604_1981203_+|hypothetical-protein
MNKIEDLYGNDLETKYFYIFPVERLDLKNEESLGNIRIFPKGWIDIDDMFSNTIIMLQEDKDKFDSNIEKFKSNPLVVINDQTYADYPGSISSDLQIMTTAISKASIIIDYIKFEFCSLVTPKTMPARLGQVTSGETLLLMYNGKRSPFTRIIDTTIYSNTLTAGVGLDINSEIFTNFKLLNADIGEVGNIAKQALRMFSNALEENDNTGKFIEIMRLFEFVADPNSFTKFQKVRTKIAAHIAENSSDIHRLQEEFKYYSSGDNEDGLRTEIIHNGKSIEVLIPELSKQTDLFNKLQLYITKCIRDLVCFYNKSWVELEVIRDTKLEEAKKNKVKNKTVNYSKTAVLIDVNFLAESIEKFSPIYKELHPEGDFSNLKLEELVYQALLNCRLLEEKKTYKVFAFSNTIDDIPLVKIPISSLDGAKLKGNNCLFELVAFAFEEKVKKIESIFEVTHDIFQDKSSFDSSALTFQNVVFIGDDPEYIDLLKNMNAKDNRNLVVVKCSHYSQMEHRIPFFDVGHLVGMSFGLSASQL
>NZ_CP046670.1|WP_076010900.1|1978736_1979507_+|hypothetical-protein
MYPNTEAFLRLREQTQAVLDFTVLISNSVPLLKMTMKNIDKGIEGAQLAKPDHFKGEQNPDQLKSYAAEYKKNLSKYVLLSNFSYFEVYVVDAVEEMLGFHGGAEKLIEDARNRCQKHVNPTDQTIVKNRSKLQDSFKNKNKEKYQKFTRLLQDKNFKFPSELLSAYGVQKLCENLKNLKSVGIPELLIDGLHFPMTEAEVIEFHKIRDIRNKIAHGKRKTFDMPSAMKHTKFLRELSVRIDRHIVNNYFVIERFS
>NZ_CP046670.1|WP_012518312.1|1978173_1978467_+|DUF1244-domain-containing-protein
MDKQTQTEVEAAVFRRLVEHLDANKDVQNIDLMILADFCRNCLAKWYSAAASEQGADIDYEAAREVVYKMPYSEWKEKHQLPATDEQLEKLAARQGK
>NZ_CP046670.1|WP_071959179.1|1975900_1978012_+|polyribonucleotide-nucleotidyltransferase
MTPITKSFQYGQHTVTLETGVIARQATAAVLASMDDTSVLVTVVGKKEAKPDQDFFPLTVNYQEKAYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPEGFKNEVQVVVTVMSANPDIPTDIISMIGTSAALAISGIPFNGPIGAARVGFSNGEYILNTRAEEQAESELDLVVAGTEGAVLMVESEADVLSEETMLGAVMFGHEQLQTVVSAVNEFAAEVGTEKWDWAPEAENTALKDKVKALAEAEMTAAYQISDKLERKDAVTAVTEKALEAILAEDEEQDKKEVLDLLHDLESDVVRSRILSGAPRIDGREPAMIRALDVATGILPRTHGSALFTRGETQAIVAATLGTERDAQMIDELQGKRDSRFMLHYNFPPYCVGETGMIGSPKRREIGHGRLAKRGIQAVMPSEEEFPYVVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKASVAGIAMGLVKSDDNFVVLSDILGDEDHLGDMDFKVAGTTDGITALQMDIKIEGITKEIMQIALKQAKEARLHILNVMDEAIGGHREELSEFAPRIYTMKIDQDKIRDVIGKGGAMIRQITEESDTNIEIEDDGTIKIFATERAKADIAISKIEQVTAEIEVGKTYNGKITRIVDFGAFVEVLPGKEGLVHISQIAHERVNKVTDYLKEGEMVDVKVMEIDRQNRVRLSIKELLEKPAPKSDDAE
>NZ_CP046670.1|WP_015067154.1|1974951_1975506_-|HNH-endonuclease
MLVLRLNKAGMPQEWIDVEQAAKLYSQDKVLFELGSDGITLKGGWNHQGLQSQLTLSSIIACDGKVTDLSGKVALTNRYLFRRDSYLCMYCGQTFTPKQLTRDHIIPRSRGGKDVWTNVATACQRCNHAKGAKTPEEANMPLLAVPFRPNVYERFYLMNRRILADQMAFLEGHFSHQRNWTCHE
>NZ_CP046670.1|WP_071959178.1|1973954_1974905_+|mechanosensitive-ion-channel-family-protein
MEIVIDPTQLWEQLIAFANEYKLLTSLVLLIVLHFTKKGVLLLIRRISSQRGEDRRNQINILEQLGNAFIIIVLMMVWSSEIQTLAISIAAFMVAIVLATREFIQCFMGFIYYLGARPFRVGDWIQMNNIIGEVVEMDWAKTALLEVDPETFNYTGKHVYVPNSQLVTQTVRNLNFMRRYRLHSFEIVNEPTVNAYSLLPAFHARAQAHCEYFRDVAERYKGLIERHLEQEFIRIDPEVEIKTNELAKVVVKVSLFCPTAEAHELEHKMCSDWLSLWFRAQKEEQAMLMQQQSEFNTNISPSATTTDQQTTSSTGL
>NZ_CP046670.1|WP_015067152.1|1972576_1973824_+|glutamate-5-semialdehyde-dehydrogenase
MSIITELAQQAKKAARTLAILSESQKNAVLTDMAAAIRENKSKIIEVNEKEVARAKDNNLDAAMIDRLILNEERIESMAEGIEVIVELDDPVGKERVIGTRPNGIEIKKMRIPLGVVCMIYEARPNVTADAGALCFKSGNAVILRGGKEALDTSLAIAELMQDVLEKHNLPKALVTVVPNPDRALMQELMEQRDYIDVIIPRGGEGLINYVTDNAKVPVIQHFKGVCHLYVDKDADLEKALAILLNGKTQRTGVCNALEGLVVHQAVAGDFLPKVADAFKEKGVKVHVNKKGSQYFDGADVIAEDAYGEEYLGLEIAIRVVDDFEGAVDHIAQFGSNHTEVIITEDAEKGKLFQRAVDASVVMVNASSRFSDGSQLGLGAEIGIATTKLHAYGPMGLESLTSEKYLVNGEGQIRD
>NZ_CP046670.1|WP_157316038.1|1985375_1985693_-|plasmid-maintenance-protein-CcdB
MAQFDVYRNPSSKTNKAYPFLVDVQNSVIDQLATRLVVPLTKNKTKNSLYMKNLTPEIEFEGETYLFLTQQLSSIPDDVLKDCIGSLGQSRELLIDAIDFAITGI
>NZ_CP046670.1|WP_157316039.1|1985692_1985938_-|cytochrome-C-biogenesis-protein-CcdA
MQDLYDIHAPKKATNLSLNSDLLQKARDLKVNLSATLEQALKDKLKSVEEERWKKENKAAIAAYNEFIAENGCIGDEYRNF
>NZ_CP046670.1|WP_157316040.1|1986079_1987057_-|transposase
MPKARKSQISLSDTPYYHCISRCVRRAFLCGVENGKSFEHRRQWVEDRIHILSEVFAIDVCAYAVMSNHTHLVLHVNKEKADALSTEDVIQRWHKLYKGTLISQRYLSPDLRKELHETQIKAVELTAEVWRKRLFDISWFMRALNEYIARAANKEDDCTGHFWEGRFKSQALLDESALAACMAYVDLNPVRAKMAKTPETSDHTSIKYRINAARVGKTPKRLMPFAGNPRLEMPHGLPFTLPDYLQLVDITSRYIFPNKRGKVEHSLPSILERLNIEHEHWLTLTTQFETCFKHAAGKAIHLEQYAQNQHQQRVQGRHSAMRLLG
>NZ_CP046670.1|WP_157316041.1|1987374_1988094_+|NYN-domain-containing-protein
MSENGNDKLAVLIDADNAQAAICSELLAEVSKFGVANVKRAYGDWTTVSLKGWKSYLHKHAIQPIQQFSYTQGKNSTDSSLIIDAMDLLHEGKLDGFCLISSDSDFTRLASRIRESGLLVYGFGEKKTPEAFVAACDKFVFTEVLRSSTKQSVKDESKNLDLKAIVVDAVNAVSRDNDWAPLSGVGGYIIKNTPSFDPRNYGYDKLGQLVKSLAYLEFEERSFSDGSSNVHIYVREKGT
>NZ_CP046670.1|WP_157317150.1|1988264_1988666_+|acyltransferase
MSLCWALKRRVGKTRQACLRTFQVFWRHWNPIWGYYLSRNIMRPLASFLPVSLAILVTFLVSGALHDIAVSIVKWKIILFFTPWFGLMGLIVIFSKWAGISYGQVSWPVRALTNASFIFVSLGITYFLETLYA
>NZ_CP046670.1|WP_157316042.1|1988698_1989292_+|GNAT-family-N-acetyltransferase
MWFKDVELESENITLTPLTMAHADALVNAVTDGELWKLWFTSVPKAETISEYIATALEQKSKGLSLPFVVIQKASGEVIGSTRFCNADHVNQRVEIGYTWYSKAYQKTSCNTECKLLLLTHAFETLNAIAVEFRTSWHNQASRAAIARLGAKQDGVLRNHQRLPNGGYRDTVVFSIINTEWLAVKENLTFKLAMKSL
>NZ_CP046670.1|WP_141152037.1|1989352_1989589_+|hypothetical-protein
MPIKKWIFQYSIAFPILSALFSSVQYIKGQTVSYSVTFGLTWAFISIAIFATRRAYNFKQNIDCQLCNDLNGKEAQRK
>NZ_CP046670.1|WP_071951486.1|1989693_1990071_+|hypothetical-protein
MNSRIALLAFNTLGGAILSLTAFIAGGGSTSSLNLFYWGILPGLPFIVLAVLGAFNKKLSQRSLLFMTLAALLVTSASYGQVFVFVGGGANIGAGLMILYSPIAYIAAISIGWAIGELFHFNHGK
>NZ_CP046670.1|WP_071951487.1|1990136_1990328_+|YHS-domain-containing-protein
MEPINKFCPRSGKPVKPDSLTDYRGYTVGFCNPGCSSDFAKNFQASPNDTQYFDVLIKEKFGK
>NZ_CP046670.1|WP_071953221.1|1990508_1991363_+|DUF1444-family-protein
MKIFILAFVSFFISSAFAESILNESAFTQRYANAVITNTEVVSADIKGRLEIEMTYSGGGTSTAYLDNAYMNYLSDPEELDVIIESYISALTKNISDVKANMEKAHIFPVIKDKGYINHITELMSKNKEGEFPFFYEKLNDVLYILYAIDTPSSIKFMPKDDIANLGVEQKDLRDLSLSNLMNTVESLQIKGDPSTISMVVADGTYEASFLIYDALWSKENFPVKGDIVVYVPSRDVVIVTGSEDVDSLETVRETVHNPDNHWPHPVSNIGFIRKEDKWVKFYE

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Crispr_ID: NZ_CP046670_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP046670_6

1984982-1985204

orTypeII

Consensus_repeat	Method
GACTAAATAAGACAGGCATGTTT	CRISPRCasFinder

4 spacers

Cas9_archaeal

The CRISPR arrays of NZ_CP046670_6

>merge|NZ_CP046670|6|1984982-1985204|CRISPRCasFinder
GACTAAATAAGACAGGCATGTTTACGTAAACTTCGAACCAGCCACAAATGGGACTAAATAAGACAGACATGTTTGTGTAGCCCCTTAGTGGGAAGTTATGCGATTAAATAAGACATGCATCCTAGGGGACAATTACTAAAAACTAAAATAATTAACAAAAATAATTAACAAGACAGGCATCTTAGTGTGGACTAAACAACGACTAAAAAAGACAGGCATGTTT

>NZ_CP046670|6|6|1984982-1985204|CRISPRCasFinder
GACTAAATAAGACAGGCATGTTT	ACGTAAACTTCGAACCAGCCACAAATGG
GACTAAATAAGACAGACATGTTT	GTGTAGCCCCTTAGTGGGAAGTTATGC
GATTAAATAAGACATGCATCCTA	GGGGACAATTACTAAAAACTAAAATAATTAACAAAAA
TAATTAACAAGACAGGCATCTTA	GTGTGGACTAAACAAC
GACTAAAAAAGACAGGCATGTTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046670.1\|WP_157317150.1\|1988264_1988666_+\|acyltransferase	unknown	unknown	gnl\|CDD\|227389
NZ_CP046670.1\|WP_157316040.1\|1986079_1987057_-\|transposase	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316036.1\|1981541_1982123_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_015067152.1\|1972576_1973824_+\|glutamate-5-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|234685
NZ_CP046670.1\|WP_157316041.1\|1987374_1988094_+\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|350237
NZ_CP046670.1\|WP_076010900.1\|1978736_1979507_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376158
NZ_CP046670.1\|WP_071959179.1\|1975900_1978012_+\|polyribonucleotide-nucleotidyltransferase	unknown	unknown	gnl\|CDD\|236995
NZ_CP046670.1\|WP_157316042.1\|1988698_1989292_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|224584
NZ_CP046670.1\|WP_071959178.1\|1973954_1974905_+\|mechanosensitive-ion-channel-family-protein	unknown	unknown	gnl\|CDD\|223740
NZ_CP046670.1\|WP_012518312.1\|1978173_1978467_+\|DUF1244-domain-containing-protein	unknown	unknown	gnl\|CDD\|226023
NZ_CP046670.1\|WP_071951487.1\|1990136_1990328_+\|YHS-domain-containing-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316039.1\|1985692_1985938_-\|cytochrome-C-biogenesis-protein-CcdA	unknown	unknown	gnl\|CDD\|377822
NZ_CP046670.1\|WP_071951486.1\|1989693_1990071_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_141152037.1\|1989352_1989589_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_157316038.1\|1985375_1985693_-\|plasmid-maintenance-protein-CcdB	unknown	unknown	gnl\|CDD\|376629
NZ_CP046670.1\|WP_157316037.1\|1982883_1983834_-\|IS110-family-transposase	unknown	unknown	gnl\|CDD\|226077
NZ_CP046670.1\|WP_015067154.1\|1974951_1975506_-\|HNH-endonuclease	Cas9_archaeal	cas9_archaeal	gnl\|CDD\|372995
NZ_CP046670.1\|WP_012518321.1\|1982475_1982856_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|366361
NZ_CP046670.1\|WP_157316035.1\|1979604_1981203_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP046670.1\|WP_071953221.1\|1990508_1991363_+\|DUF1444-family-protein	unknown	unknown	gnl\|CDD\|237463

Protein	Function_ID	Function_description	E-value
NZ_CP046670.1\|WP_157317150.1\|1988264_1988666_+\|acyltransferase	gnl\|CDD\|227389	COG5056, ARE1, Acyl-CoA cholesterol acyltransferase [Lipid metabolism].	0.000553492
NZ_CP046670.1\|WP_071953221.1\|1990508_1991363_+\|DUF1444-family-protein	gnl\|CDD\|237463	PRK13668, PRK13668, hypothetical protein; Provisional.	2.21697e-07
NZ_CP046670.1\|WP_157316039.1\|1985692_1985938_-\|cytochrome-C-biogenesis-protein-CcdA	gnl\|CDD\|377822	pfam07362, CcdA, Post-segregation antitoxin CcdA. This family consists of several Enterobacterial post-segregation antitoxin CcdA proteins. The F plasmid-carried bacterial toxin, the CcdB protein, is known to act on DNA gyrase in two different ways. CcdB poisons the gyrase-DNA complex, blocking the passage of polymerases and leading to double-strand breakage of the DNA. Alternatively, in cells that overexpress CcdB, the A subunit of DNA gyrase (GyrA) has been found as an inactive complex with CcdB. Both poisoning and inactivation can be prevented and reversed in the presence of the F plasmid-encoded antidote, the CcdA protein.	3.09923e-29
NZ_CP046670.1\|WP_157316041.1\|1987374_1988094_+\|NYN-domain-containing-protein	gnl\|CDD\|350237	cd11297, PIN_LabA-like_N_1, uncharacterized subfamily of N-terminal LabA-like PIN domains. This N-terminal LabA-like PIN domain is found in a well conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. LabA from Synechococcus elongatus PCC 7942, (which does not contain this C-terminal domain), has been shown to play a role in cyanobacterial circadian timing. The LabA-like C-terminal domains characteristic of this subfamily may be related to the LOTUS domain family (which also co-occurs with LabA-like N-terminal domains). The function of the N-terminal domain is unknown. The LabA-like PIN domain family also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	3.16166e-62
NZ_CP046670.1\|WP_076010900.1\|1978736_1979507_+\|hypothetical-protein	gnl\|CDD\|376158	pfam18735, HEPN_RiboL-PSP, RiboL-PSP-HEPN. RiboL-PSP-HEPN. Fused to endoRNase L-PSP ; in operon with ParB.	1.62309e-05
NZ_CP046670.1\|WP_071959179.1\|1975900_1978012_+\|polyribonucleotide-nucleotidyltransferase	gnl\|CDD\|236995	PRK11824, PRK11824, polynucleotide phosphorylase/polyadenylase; Provisional.	0
NZ_CP046670.1\|WP_157316042.1\|1988698_1989292_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	1.47768e-29
NZ_CP046670.1\|WP_071959178.1\|1973954_1974905_+\|mechanosensitive-ion-channel-family-protein	gnl\|CDD\|223740	COG0668, MscS, Small-conductance mechanosensitive channel [Cell envelope biogenesis, outer membrane].	6.53517e-13
NZ_CP046670.1\|WP_012518312.1\|1978173_1978467_+\|DUF1244-domain-containing-protein	gnl\|CDD\|226023	COG3492, COG3492, Uncharacterized protein conserved in bacteria [Function unknown].	3.14416e-40
NZ_CP046670.1\|WP_015067152.1\|1972576_1973824_+\|glutamate-5-semialdehyde-dehydrogenase	gnl\|CDD\|234685	PRK00197, proA, gamma-glutamyl phosphate reductase; Provisional.	0
NZ_CP046670.1\|WP_157316038.1\|1985375_1985693_-\|plasmid-maintenance-protein-CcdB	gnl\|CDD\|376629	pfam01845, CcdB, CcdB protein.	9.83468e-38
NZ_CP046670.1\|WP_157316037.1\|1982883_1983834_-\|IS110-family-transposase	gnl\|CDD\|226077	COG3547, COG3547, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	2.96101e-24
NZ_CP046670.1\|WP_015067154.1\|1974951_1975506_-\|HNH-endonuclease	gnl\|CDD\|372995	pfam14279, HNH_5, HNH endonuclease. This domain is related to other HNH domain families such as pfam01844. Suggesting that these proteins have a nucleic acid cleaving function.	8.81504e-22
NZ_CP046670.1\|WP_012518321.1\|1982475_1982856_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	gnl\|CDD\|366361	pfam00903, Glyoxalase, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.	1.93523e-10

>NZ_CP046670.1|WP_157316037.1|1982883_1983834_-|IS110-family-transposase
MKKSVVQNINVGVDVGKDFLDIHIRPLGEYLKVSNDKKGIGEALKRLRKLTIVRIVIEATGRYEMAFVSACAKAELPFSVVNPIHVKRFAGAIGRKAKTDKLDAALIAHFSEVIQPALSTLKPENIQKMADTVARRNQLLEIQTREKNRLQIMPKTVQSSIKAILTVLKKQIQKMDGELADLIESCPEYQAKSELVQSMPGIGKVSAAALISYLPELGMMNSKQVAALVGVAPMNKESGRYKGKQVTQGGRHQVRTVLFMAMMSAMQCNAKFKATYERLVAAGKPKKVAIIACVRKMVVILNSMVRDGVMWEEKAA
>NZ_CP046670.1|WP_012518321.1|1982475_1982856_+|glyoxalase/bleomycin-resistance/dioxygenase-family-protein
MEMNQVTLPVKNMEEAVKFYLVLGFIQIVDTPHYARFSCPKGNSTFSLSLELEEFKNGAIIYFETEKLDMLAESLVAKGVIFEQLPTEQRYLWKEAVLKDPSGNKIKLFWAGENRLSPPWKVEKRG
>NZ_CP046670.1|WP_157316036.1|1981541_1982123_+|hypothetical-protein
MKLIKVALFTLFISQIAAAEINVSLANGTEKEELKREQIFRLIEQHDLKKWWFTDKIVIDESARSPFSHPVLTLKASMPNNDHAGLSQLLHEQIHWFEGSRKEEVDNTVAELRNIYSSVPVGFPDGARSEFSTYLHLAVCLMELDALTQILGKEKAEAVIATNGKYFYKWIYKTVLQDQAQIREILKNNRLYI
>NZ_CP046670.1|WP_157316035.1|1979604_1981203_+|hypothetical-protein
MNKIEDLYGNDLETKYFYIFPVERLDLKNEESLGNIRIFPKGWIDIDDMFSNTIIMLQEDKDKFDSNIEKFKSNPLVVINDQTYADYPGSISSDLQIMTTAISKASIIIDYIKFEFCSLVTPKTMPARLGQVTSGETLLLMYNGKRSPFTRIIDTTIYSNTLTAGVGLDINSEIFTNFKLLNADIGEVGNIAKQALRMFSNALEENDNTGKFIEIMRLFEFVADPNSFTKFQKVRTKIAAHIAENSSDIHRLQEEFKYYSSGDNEDGLRTEIIHNGKSIEVLIPELSKQTDLFNKLQLYITKCIRDLVCFYNKSWVELEVIRDTKLEEAKKNKVKNKTVNYSKTAVLIDVNFLAESIEKFSPIYKELHPEGDFSNLKLEELVYQALLNCRLLEEKKTYKVFAFSNTIDDIPLVKIPISSLDGAKLKGNNCLFELVAFAFEEKVKKIESIFEVTHDIFQDKSSFDSSALTFQNVVFIGDDPEYIDLLKNMNAKDNRNLVVVKCSHYSQMEHRIPFFDVGHLVGMSFGLSASQL
>NZ_CP046670.1|WP_076010900.1|1978736_1979507_+|hypothetical-protein
MYPNTEAFLRLREQTQAVLDFTVLISNSVPLLKMTMKNIDKGIEGAQLAKPDHFKGEQNPDQLKSYAAEYKKNLSKYVLLSNFSYFEVYVVDAVEEMLGFHGGAEKLIEDARNRCQKHVNPTDQTIVKNRSKLQDSFKNKNKEKYQKFTRLLQDKNFKFPSELLSAYGVQKLCENLKNLKSVGIPELLIDGLHFPMTEAEVIEFHKIRDIRNKIAHGKRKTFDMPSAMKHTKFLRELSVRIDRHIVNNYFVIERFS
>NZ_CP046670.1|WP_012518312.1|1978173_1978467_+|DUF1244-domain-containing-protein
MDKQTQTEVEAAVFRRLVEHLDANKDVQNIDLMILADFCRNCLAKWYSAAASEQGADIDYEAAREVVYKMPYSEWKEKHQLPATDEQLEKLAARQGK
>NZ_CP046670.1|WP_071959179.1|1975900_1978012_+|polyribonucleotide-nucleotidyltransferase
MTPITKSFQYGQHTVTLETGVIARQATAAVLASMDDTSVLVTVVGKKEAKPDQDFFPLTVNYQEKAYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPEGFKNEVQVVVTVMSANPDIPTDIISMIGTSAALAISGIPFNGPIGAARVGFSNGEYILNTRAEEQAESELDLVVAGTEGAVLMVESEADVLSEETMLGAVMFGHEQLQTVVSAVNEFAAEVGTEKWDWAPEAENTALKDKVKALAEAEMTAAYQISDKLERKDAVTAVTEKALEAILAEDEEQDKKEVLDLLHDLESDVVRSRILSGAPRIDGREPAMIRALDVATGILPRTHGSALFTRGETQAIVAATLGTERDAQMIDELQGKRDSRFMLHYNFPPYCVGETGMIGSPKRREIGHGRLAKRGIQAVMPSEEEFPYVVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKASVAGIAMGLVKSDDNFVVLSDILGDEDHLGDMDFKVAGTTDGITALQMDIKIEGITKEIMQIALKQAKEARLHILNVMDEAIGGHREELSEFAPRIYTMKIDQDKIRDVIGKGGAMIRQITEESDTNIEIEDDGTIKIFATERAKADIAISKIEQVTAEIEVGKTYNGKITRIVDFGAFVEVLPGKEGLVHISQIAHERVNKVTDYLKEGEMVDVKVMEIDRQNRVRLSIKELLEKPAPKSDDAE
>NZ_CP046670.1|WP_015067154.1|1974951_1975506_-|HNH-endonuclease
MLVLRLNKAGMPQEWIDVEQAAKLYSQDKVLFELGSDGITLKGGWNHQGLQSQLTLSSIIACDGKVTDLSGKVALTNRYLFRRDSYLCMYCGQTFTPKQLTRDHIIPRSRGGKDVWTNVATACQRCNHAKGAKTPEEANMPLLAVPFRPNVYERFYLMNRRILADQMAFLEGHFSHQRNWTCHE
>NZ_CP046670.1|WP_071959178.1|1973954_1974905_+|mechanosensitive-ion-channel-family-protein
MEIVIDPTQLWEQLIAFANEYKLLTSLVLLIVLHFTKKGVLLLIRRISSQRGEDRRNQINILEQLGNAFIIIVLMMVWSSEIQTLAISIAAFMVAIVLATREFIQCFMGFIYYLGARPFRVGDWIQMNNIIGEVVEMDWAKTALLEVDPETFNYTGKHVYVPNSQLVTQTVRNLNFMRRYRLHSFEIVNEPTVNAYSLLPAFHARAQAHCEYFRDVAERYKGLIERHLEQEFIRIDPEVEIKTNELAKVVVKVSLFCPTAEAHELEHKMCSDWLSLWFRAQKEEQAMLMQQQSEFNTNISPSATTTDQQTTSSTGL
>NZ_CP046670.1|WP_015067152.1|1972576_1973824_+|glutamate-5-semialdehyde-dehydrogenase
MSIITELAQQAKKAARTLAILSESQKNAVLTDMAAAIRENKSKIIEVNEKEVARAKDNNLDAAMIDRLILNEERIESMAEGIEVIVELDDPVGKERVIGTRPNGIEIKKMRIPLGVVCMIYEARPNVTADAGALCFKSGNAVILRGGKEALDTSLAIAELMQDVLEKHNLPKALVTVVPNPDRALMQELMEQRDYIDVIIPRGGEGLINYVTDNAKVPVIQHFKGVCHLYVDKDADLEKALAILLNGKTQRTGVCNALEGLVVHQAVAGDFLPKVADAFKEKGVKVHVNKKGSQYFDGADVIAEDAYGEEYLGLEIAIRVVDDFEGAVDHIAQFGSNHTEVIITEDAEKGKLFQRAVDASVVMVNASSRFSDGSQLGLGAEIGIATTKLHAYGPMGLESLTSEKYLVNGEGQIRD
>NZ_CP046670.1|WP_157316038.1|1985375_1985693_-|plasmid-maintenance-protein-CcdB
MAQFDVYRNPSSKTNKAYPFLVDVQNSVIDQLATRLVVPLTKNKTKNSLYMKNLTPEIEFEGETYLFLTQQLSSIPDDVLKDCIGSLGQSRELLIDAIDFAITGI
>NZ_CP046670.1|WP_157316039.1|1985692_1985938_-|cytochrome-C-biogenesis-protein-CcdA
MQDLYDIHAPKKATNLSLNSDLLQKARDLKVNLSATLEQALKDKLKSVEEERWKKENKAAIAAYNEFIAENGCIGDEYRNF
>NZ_CP046670.1|WP_157316040.1|1986079_1987057_-|transposase
MPKARKSQISLSDTPYYHCISRCVRRAFLCGVENGKSFEHRRQWVEDRIHILSEVFAIDVCAYAVMSNHTHLVLHVNKEKADALSTEDVIQRWHKLYKGTLISQRYLSPDLRKELHETQIKAVELTAEVWRKRLFDISWFMRALNEYIARAANKEDDCTGHFWEGRFKSQALLDESALAACMAYVDLNPVRAKMAKTPETSDHTSIKYRINAARVGKTPKRLMPFAGNPRLEMPHGLPFTLPDYLQLVDITSRYIFPNKRGKVEHSLPSILERLNIEHEHWLTLTTQFETCFKHAAGKAIHLEQYAQNQHQQRVQGRHSAMRLLG
>NZ_CP046670.1|WP_157316041.1|1987374_1988094_+|NYN-domain-containing-protein
MSENGNDKLAVLIDADNAQAAICSELLAEVSKFGVANVKRAYGDWTTVSLKGWKSYLHKHAIQPIQQFSYTQGKNSTDSSLIIDAMDLLHEGKLDGFCLISSDSDFTRLASRIRESGLLVYGFGEKKTPEAFVAACDKFVFTEVLRSSTKQSVKDESKNLDLKAIVVDAVNAVSRDNDWAPLSGVGGYIIKNTPSFDPRNYGYDKLGQLVKSLAYLEFEERSFSDGSSNVHIYVREKGT
>NZ_CP046670.1|WP_157317150.1|1988264_1988666_+|acyltransferase
MSLCWALKRRVGKTRQACLRTFQVFWRHWNPIWGYYLSRNIMRPLASFLPVSLAILVTFLVSGALHDIAVSIVKWKIILFFTPWFGLMGLIVIFSKWAGISYGQVSWPVRALTNASFIFVSLGITYFLETLYA
>NZ_CP046670.1|WP_157316042.1|1988698_1989292_+|GNAT-family-N-acetyltransferase
MWFKDVELESENITLTPLTMAHADALVNAVTDGELWKLWFTSVPKAETISEYIATALEQKSKGLSLPFVVIQKASGEVIGSTRFCNADHVNQRVEIGYTWYSKAYQKTSCNTECKLLLLTHAFETLNAIAVEFRTSWHNQASRAAIARLGAKQDGVLRNHQRLPNGGYRDTVVFSIINTEWLAVKENLTFKLAMKSL
>NZ_CP046670.1|WP_141152037.1|1989352_1989589_+|hypothetical-protein
MPIKKWIFQYSIAFPILSALFSSVQYIKGQTVSYSVTFGLTWAFISIAIFATRRAYNFKQNIDCQLCNDLNGKEAQRK
>NZ_CP046670.1|WP_071951486.1|1989693_1990071_+|hypothetical-protein
MNSRIALLAFNTLGGAILSLTAFIAGGGSTSSLNLFYWGILPGLPFIVLAVLGAFNKKLSQRSLLFMTLAALLVTSASYGQVFVFVGGGANIGAGLMILYSPIAYIAAISIGWAIGELFHFNHGK
>NZ_CP046670.1|WP_071951487.1|1990136_1990328_+|YHS-domain-containing-protein
MEPINKFCPRSGKPVKPDSLTDYRGYTVGFCNPGCSSDFAKNFQASPNDTQYFDVLIKEKFGK
>NZ_CP046670.1|WP_071953221.1|1990508_1991363_+|DUF1444-family-protein
MKIFILAFVSFFISSAFAESILNESAFTQRYANAVITNTEVVSADIKGRLEIEMTYSGGGTSTAYLDNAYMNYLSDPEELDVIIESYISALTKNISDVKANMEKAHIFPVIKDKGYINHITELMSKNKEGEFPFFYEKLNDVLYILYAIDTPSSIKFMPKDDIANLGVEQKDLRDLSLSNLMNTVESLQIKGDPSTISMVVADGTYEASFLIYDALWSKENFPVKGDIVVYVPSRDVVIVTGSEDVDSLETVRETVHNPDNHWPHPVSNIGFIRKEDKWVKFYE

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	124830-124861	2	0.938
NZ_CP046670_2	2.15\|838765\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838765-838796	32	MK241539	Alteromonas phage P24, complete genome	4565-4596	2	0.938
NZ_CP046670_2	2.5\|838165\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838165-838196	32	MK241539	Alteromonas phage P24, complete genome	5957-5988	4	0.875
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	66416-66447	5	0.844
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	68327-68358	5	0.844
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	69059-69090	5	0.844
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	84336-84367	6	0.812
NZ_CP046670_2	2.2\|837985\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	837985-838016	32	MN693665	Marine virus AFVG_250M94, complete genome	28283-28314	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NC_018516	Bacillus thuringiensis HD-789 plasmid pBTHD789-1, complete sequence	288823-288854	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP053970	Bacillus thuringiensis strain FDAARGOS_796 plasmid unnamed2, complete sequence	141624-141655	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP053979	Bacillus thuringiensis strain FDAARGOS_795 plasmid unnamed3, complete sequence	49836-49867	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP013277	Bacillus thuringiensis serovar israelensis strain AM65-52 plasmid pAM65-52-2-350K, complete sequence	268158-268189	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP039723	Bacillus thuringiensis strain BT-59 plasmid p2, complete sequence	35559-35590	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP009348	Bacillus thuringiensis HD1002 plasmid 2, complete sequence	268159-268190	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP009334	Bacillus thuringiensis strain HD1011 plasmid 2, complete sequence	223019-223050	7	0.781
NZ_CP046670_2	2.9\|838405\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838405-838436	32	NZ_CP045024	Bacillus thuringiensis strain JW-1 plasmid p2, complete sequence	267771-267802	7	0.781
NZ_CP046670_2	2.11\|838525\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838525-838556	32	MF098555	Cyanophage BHS3, partial genome	9380-9411	7	0.781
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	71680-71711	7	0.781
NZ_CP046670_2	2.12\|838585\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838585-838616	32	NZ_CP018030	Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence	72451-72482	7	0.781
NZ_CP046670_2	2.13\|838645\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838645-838676	32	NZ_AP014579	Burkholderia sp. RPE67 plasmid p1, complete sequence	900742-900773	7	0.781
NZ_CP046670_2	2.13\|838645\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838645-838676	32	NC_016626	Burkholderia sp. YI23 plasmid byi_1p, complete sequence	760926-760957	7	0.781
NZ_CP046670_2	2.21\|839125\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	839125-839156	32	NZ_CP015630	Borrelia turicatae strain BTE5EL plasmid lp159	24002-24033	7	0.781
NZ_CP046670_2	2.3\|838045\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838045-838076	32	NZ_CP034431	Bradyrhizobium sp. LCT2 plasmid pLCT2, complete sequence	67562-67593	8	0.75
NZ_CP046670_2	2.17\|838885\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838885-838916	32	MN693644	Marine virus AFVG_250M1161, complete genome	19441-19472	8	0.75
NZ_CP046670_2	2.6\|838225\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838225-838256	32	MF417889	Uncultured Caudovirales phage clone 10S_14, partial genome	6189-6220	9	0.719
NZ_CP046670_2	2.21\|839125\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	839125-839156	32	NZ_LR134433	Legionella adelaidensis strain NCTC12735 genome assembly, plasmid: 24	140733-140764	9	0.719
NZ_CP046670_2	2.5\|838165\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838165-838196	32	NZ_CP009865	Klebsiella pneumoniae subsp. pneumoniae strain KPNIH29 plasmid pKPN-80a, complete sequence	136816-136847	10	0.688
NZ_CP046670_2	2.15\|838765\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838765-838796	32	MN856021	Bacteriophage sp. isolate 135, complete genome	1653-1684	10	0.688
NZ_CP046670_2	2.15\|838765\|32\|NZ_CP046670\|PILER-CR,CRISPRCasFinder,CRT	838765-838796	32	MN855744	Myoviridae sp. isolate 408, complete genome	5113-5144	10	0.688

1. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 2, identity: 0.938

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
tacccctgaatggtgaccgaggtgcgtcaaag	Protospacer
***********.********** *********

2. spacer 2.15|838765|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MK241539 (Alteromonas phage P24, complete genome) position: , mismatch: 2, identity: 0.938

atgggttattatcctcatgctgttggctgcta	CRISPR spacer
atgggttatcatcctcatgctgttggctgctc	Protospacer
*********.*********************

3. spacer 2.5|838165|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MK241539 (Alteromonas phage P24, complete genome) position: , mismatch: 4, identity: 0.875

cagaatgggatgaatcaaggcggtaaaactcc	CRISPR spacer
cagaatgggatgaatcaaggcggcaagccacc	Protospacer
***********************.**. * **

4. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 5, identity: 0.844

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
tacccctgaatggtgaccgaggtgcgtcgttg	Protospacer
***********.********** *****.  *

5. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 5, identity: 0.844

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
tacccctgaatggtgaccgaggtgcgtctttg	Protospacer
***********.********** *****   *

6. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 5, identity: 0.844

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
tacccctgaatggtgaccgaggtgcgtctttg	Protospacer
***********.********** *****   *

7. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 6, identity: 0.812

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
aacccctgaatagtgaccgaggtgcatcgttg	Protospacer
 ********************* **.**.  *

8. spacer 2.2|837985|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MN693665 (Marine virus AFVG_250M94, complete genome) position: , mismatch: 7, identity: 0.781

cccaaccgccaacgctgggcccgaccaatcag	CRISPR spacer
cccaaccgccaacgctggcgccgaccgcgtcg	Protospacer
******************  ******.  . *

9. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NC_018516 (Bacillus thuringiensis HD-789 plasmid pBTHD789-1, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

10. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP053970 (Bacillus thuringiensis strain FDAARGOS_796 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

11. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP053979 (Bacillus thuringiensis strain FDAARGOS_795 plasmid unnamed3, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

12. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP013277 (Bacillus thuringiensis serovar israelensis strain AM65-52 plasmid pAM65-52-2-350K, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

13. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP039723 (Bacillus thuringiensis strain BT-59 plasmid p2, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

14. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP009348 (Bacillus thuringiensis HD1002 plasmid 2, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

15. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP009334 (Bacillus thuringiensis strain HD1011 plasmid 2, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

16. spacer 2.9|838405|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP045024 (Bacillus thuringiensis strain JW-1 plasmid p2, complete sequence) position: , mismatch: 7, identity: 0.781

ttactttgaatgagtagttaccgtaagcgttg-	CRISPR spacer
tctctttgaatgtgtatttaccgtaag-gtaat	Protospacer
*. ********* *** ********** ** .

17. spacer 2.11|838525|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MF098555 (Cyanophage BHS3, partial genome) position: , mismatch: 7, identity: 0.781

cacaaagaacagcaagcggggttgatgtgatg	CRISPR spacer
ccacaagaacagcaagcgggggtgatgtgggt	Protospacer
*   ***************** *******.

18. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 7, identity: 0.781

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
aacccctgaatggtgaccgaggcgcgtcttga	Protospacer
 **********.********** *****  ..

19. spacer 2.12|838585|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP018030 (Alteromonas mediterranea strain RG65 plasmid MRG65-300, complete sequence) position: , mismatch: 7, identity: 0.781

tacccctgaatagtgaccgaggagcgtcaaag	CRISPR spacer
aacccctgaatggtgaccgaggtgcgtcttga	Protospacer
 **********.********** *****  ..

20. spacer 2.13|838645|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_AP014579 (Burkholderia sp. RPE67 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.781

taatagccgcagcgccgaaaatgtatgcgaag	CRISPR spacer
cgaaagccacagcgccgaaaacgtatgcgaga	Protospacer
..* ****.************.********..

21. spacer 2.13|838645|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NC_016626 (Burkholderia sp. YI23 plasmid byi_1p, complete sequence) position: , mismatch: 7, identity: 0.781

taatagccgcagcgccgaaaatgtatgcgaag	CRISPR spacer
cgaaagccacagcgccgaaaacgtatgcgaga	Protospacer
..* ****.************.********..

22. spacer 2.21|839125|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP015630 (Borrelia turicatae strain BTE5EL plasmid lp159) position: , mismatch: 7, identity: 0.781

--ttgactggttaatttgatttttggcattttta	CRISPR spacer
cattactt--ttaatttgatctttgtcattttta	Protospacer
  **. .*  **********.**** ********

23. spacer 2.3|838045|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP034431 (Bradyrhizobium sp. LCT2 plasmid pLCT2, complete sequence) position: , mismatch: 8, identity: 0.75

agcttgtgttcatcggtatcgccggacctttt	CRISPR spacer
acatcgccgtcatcggtatggccggacgtttt	Protospacer
*  *.*.  ********** ******* ****

24. spacer 2.17|838885|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MN693644 (Marine virus AFVG_250M1161, complete genome) position: , mismatch: 8, identity: 0.75

aacgctgtgaagcaggggaaaacatgacaatc	CRISPR spacer
atgtcactaaagcaggggtaaaaatgacaatc	Protospacer
*   *  *.********* *** *********

25. spacer 2.6|838225|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MF417889 (Uncultured Caudovirales phage clone 10S_14, partial genome) position: , mismatch: 9, identity: 0.719

tcgcacctagttcgctaaaaaaataattagtg	CRISPR spacer
tagtttttagtacgctaacaaaataattagat	Protospacer
* *. ..**** ****** ***********

26. spacer 2.21|839125|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_LR134433 (Legionella adelaidensis strain NCTC12735 genome assembly, plasmid: 24) position: , mismatch: 9, identity: 0.719

ttgactggttaatttgatttttggcattttta	CRISPR spacer
tagcagtattaatttgctttttgccatttttt	Protospacer
* *    .******** ****** *******

27. spacer 2.5|838165|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP009865 (Klebsiella pneumoniae subsp. pneumoniae strain KPNIH29 plasmid pKPN-80a, complete sequence) position: , mismatch: 10, identity: 0.688

cagaatgggatgaatcaaggcggtaaaactcc	CRISPR spacer
gataatgggattaatccaggcggtaattaatg	Protospacer
 * ******** **** *********    .

28. spacer 2.15|838765|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MN856021 (Bacteriophage sp. isolate 135, complete genome) position: , mismatch: 10, identity: 0.688

atgggttattatcctcatgctgttggctgcta	CRISPR spacer
attggttaatatcctcatgctgtatctgagtt	Protospacer
** ***** **************   . . *

29. spacer 2.15|838765|32|NZ_CP046670|PILER-CR,CRISPRCasFinder,CRT matches to MN855744 (Myoviridae sp. isolate 408, complete genome) position: , mismatch: 10, identity: 0.688

atgggttattatcctcatgctgttggctgcta	CRISPR spacer
attggttaatatcctcatgctgtatctgagtc	Protospacer
** ***** **************   . . *

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

867535 : 876200

Streptococcus_phage(16.67%)

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_071950893.1\|867535_868828_-	phosphopyruvate hydratase	A0A1X9I5Z8	Streptococcus_phage	8.5e-135	59.7
WP_012517444.1\|868887_870519_-	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	3.2e-147	50.2
WP_157317109.1\|870655_873247_-	DNA mismatch repair protein MutS	A0A1V0SC35	Catovirus	2.2e-33	21.8
WP_157315663.1\|873407_873947_+	nicotinamide-nucleotide amidohydrolase family protein	B5TK85	Pseudomonas_phage	1.8e-25	44.5
WP_012517447.1\|874067_875114_+	recombinase RecA	A0A2D1GPX2	Mycobacterium_phage	2.5e-116	62.8
WP_012517448.1\|875378_876200_+	ATP-binding cassette domain-containing protein	A0A2H4PQG7	Staphylococcus_phage	1.4e-26	33.2

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_CP046670

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

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection