CRISPRimmunity

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_CP009239	Cellulophaga lytica strain HI1, complete genome	6 crisprs	DEDDh,cas3,WYL,PrimPol	0	3	0	0

1. NZ_CP009239

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP009239_1

• CRISPR_ID: NZ_CP009239_1
• CRISPR_location: 140058-140427
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 6 spacers

Consensus repeat of NZ_CP009239_1

Consensus_repeat	Method
AGTATCTGGTTCTGCAGATATTAA	CRISPRCasFinder
TCTGGNTCTGGAGANATN	CRT

spacers of NZ_CP009239_1

>1.1|140082|39|NZ_CP009239|CRISPRCasFinder
TGGGAAAACAACATTAGTAAGTAATACTTTTGAAACTAG
>1.2|140145|33|NZ_CP009239|CRISPRCasFinder
CCTAAAAGTTAAAACAAAAGAACTAAAAGCTAG
>1.3|140202|33|NZ_CP009239|CRISPRCasFinder
TCTTAGTGGCTCTGCTACCGACTTTACTGTTAG
>1.4|140259|36|NZ_CP009239|CRISPRCasFinder
TGCATATGATTTAGAAGCAGACTATGTAAAAGCATT
>1.5|140319|30|NZ_CP009239|CRISPRCasFinder
GGTAACTGCAAAAGAAACTATAGACGCTAG
>1.6|140080|45|NZ_CP009239|CRT
ATTGGGAAAACAACATTAGTAAGTAATACTTTTGAAACTAGTATA
>1.7|140143|39|NZ_CP009239|CRT
AACCTAAAAGTTAAAACAAAAGAACTAAAAGCTAGTATG
>1.8|140200|39|NZ_CP009239|CRT
AATCTTAGTGGCTCTGCTACCGACTTTACTGTTAGAGTT
>1.9|140257|42|NZ_CP009239|CRT
TCTGCATATGATTTAGAAGCAGACTATGTAAAAGCATTAGTA
>1.10|140317|36|NZ_CP009239|CRT
AAGGTAACTGCAAAAGAAACTATAGACGCTAGAGTA
>1.11|140371|39|NZ_CP009239|CRT
AAATACAGAGGAAATCCTAAAAAAATAGAAAGTAAAACC

CRISPR arrays and Neighbor proteins around NZ_CP009239_1

CRISPR arrays

The CRISPR arrays of NZ_CP009239_1

>merge|NZ_CP009239|1|140058-140427|CRISPRCasFinder,CRT
ATTATCTGGCTCTGGAGATATTATTGGGAAAACAACATTAGTAAGTAATACTTTTGAAACTAGTATATCTGGCTCAGGAGACATAAACCTAAAAGTTAAAACAAAAGAACTAAAAGCTAGTATGTCTGGATCTGGAGACATAAATCTTAGTGGCTCTGCTACCGACTTTACTGTTAGAGTTTCTGGTTCTGGAGACATCTCTGCATATGATTTAGAAGCAGACTATGTAAAAGCATTAGTATCTGGTTCTGCAGATATTAAGGTAACTGCAAAAGAAACTATAGACGCTAGAGTATCTGGTTCTGGAGATATTAAATACAGAGGAAATCCTAAAAAAATAGAAAGTAAAACCTCTGGTTCTGGTGGTGTT

>NZ_CP009239|1|1|140058-140372|CRISPRCasFinder
ATTATCTGGCTCTGGAGATATTAT	TGGGAAAACAACATTAGTAAGTAATACTTTTGAAACTAG
TATATCTGGCTCAGGAGACATAAA	CCTAAAAGTTAAAACAAAAGAACTAAAAGCTAG
TATGTCTGGATCTGGAGACATAAA	TCTTAGTGGCTCTGCTACCGACTTTACTGTTAG
AGTTTCTGGTTCTGGAGACATCTC	TGCATATGATTTAGAAGCAGACTATGTAAAAGCATT
AGTATCTGGTTCTGCAGATATTAA	GGTAACTGCAAAAGAAACTATAGACGCTAG
AGTATCTGGTTCTGGAGATATTAA

>NZ_CP009239|1|1|140062-140427|CRT
TCTGGCTCTGGAGATATT	ATTGGGAAAACAACATTAGTAAGTAATACTTTTGAAACTAGTATA
TCTGGCTCAGGAGACATA	AACCTAAAAGTTAAAACAAAAGAACTAAAAGCTAGTATG
TCTGGATCTGGAGACATA	AATCTTAGTGGCTCTGCTACCGACTTTACTGTTAGAGTT
TCTGGTTCTGGAGACATC	TCTGCATATGATTTAGAAGCAGACTATGTAAAAGCATTAGTA
TCTGGTTCTGCAGATATT	AAGGTAACTGCAAAAGAAACTATAGACGCTAGAGTA
TCTGGTTCTGGAGATATT	AAATACAGAGGAAATCCTAAAAAAATAGAAAGTAAAACC
TCTGGTTCTGGTGGTGTT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_013619769.1|140512_141832_-|MFS-transporter-permease	unknown	unknown	gnl|CDD|341035
NZ_CP009239.1|WP_038504435.1|138625_139702_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013619765.1|137542_138100_+|RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|224511
NZ_CP009239.1|WP_034644547.1|138096_138645_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013619762.1|133694_134075_+|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl|CDD|236880
NZ_CP009239.1|WP_038504432.1|134132_134825_-|(d)CMP-kinase	unknown	unknown	gnl|CDD|234579
NZ_CP009239.1|WP_013619777.1|147523_147814_+|DUF3817-domain-containing-protein	unknown	unknown	gnl|CDD|378962
NZ_CP009239.1|WP_034644550.1|142898_143432_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_038504446.1|147821_148550_-|diphthine--ammonia-ligase	unknown	unknown	gnl|CDD|238952
NZ_CP009239.1|WP_013619758.1|129563_129896_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_038504440.1|144988_145891_-|MBL-fold-metallo-hydrolase	unknown	unknown	gnl|CDD|293840
NZ_CP009239.1|WP_034644551.1|144457_144985_+|DUF1572-domain-containing-protein	unknown	unknown	gnl|CDD|311521
NZ_CP009239.1|WP_013619761.1|131589_133422_-|30S-ribosomal-protein-S1	unknown	unknown	gnl|CDD|235775
NZ_CP009239.1|WP_013619772.1|143556_144045_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl|CDD|376583
NZ_CP009239.1|WP_013619760.1|130839_131379_-|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR	unknown	unknown	gnl|CDD|235365
NZ_CP009239.1|WP_013619764.1|134879_137324_-|endopeptidase-La	unknown	unknown	gnl|CDD|223542
NZ_CP009239.1|WP_013619773.1|144044_144455_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl|CDD|376583
NZ_CP009239.1|WP_038504437.1|141916_142726_-|M48-family-metallopeptidase	unknown	unknown	gnl|CDD|320690
NZ_CP009239.1|WP_038504443.1|146047_147439_+|dihydrolipoyl-dehydrogenase	unknown	unknown	gnl|CDD|235798
NZ_CP009239.1|WP_013619759.1|129902_130829_-|aspartate-carbamoyltransferase-catalytic-subunit	unknown	unknown	gnl|CDD|234849

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_013619769.1|140512_141832_-|MFS-transporter-permease	gnl|CDD|341035	cd17482, MFS_YxiO_like, Bacillus subtilis YxiO, Listeria monocytogenes BtlA, and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis MFS-type transporter YxiO, and similar proteins including Listeria monocytogenes BtlA. The function of B. subtilis YxiO is still unknown, and L. monocytogenes BtlA is a putative secondary transporter involved in bile tolerance and general stress resistance. This 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.	2.23862e-93
NZ_CP009239.1|WP_013619765.1|137542_138100_+|RNA-polymerase-sigma-factor	gnl|CDD|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	7.21134e-38
NZ_CP009239.1|WP_013619762.1|133694_134075_+|LysM-peptidoglycan-binding-domain-containing-protein	gnl|CDD|236880	PRK11198, PRK11198, LysM domain/BON superfamily protein; Provisional.	4.99993e-24
NZ_CP009239.1|WP_038504432.1|134132_134825_-|(d)CMP-kinase	gnl|CDD|234579	PRK00023, cmk, (d)CMP kinase.	3.24224e-112
NZ_CP009239.1|WP_013619777.1|147523_147814_+|DUF3817-domain-containing-protein	gnl|CDD|378962	pfam12823, DUF3817, Domain of unknown function (DUF3817). This domain is of unknown function. It is sometimes found adjacent to pfam07690 and pfam03176 which are both transporter domains.	1.3469e-29
NZ_CP009239.1|WP_013619773.1|144044_144455_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl|CDD|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	1.14314e-73
NZ_CP009239.1|WP_038504446.1|147821_148550_-|diphthine--ammonia-ligase	gnl|CDD|238952	cd01994, Alpha_ANH_like_IV, This is a subfamily of Adenine nucleotide alpha hydrolases superfamily.Adeninosine nucleotide alpha hydrolases superfamily includes N type ATP PPases and ATP sulphurylases. It forms a apha/beta/apha fold which binds to Adenosine group. This subfamily of proteins is predicted to bind ATP. This domainhas a strongly conserved motif SGGKD at the N terminus.	6.13284e-59
NZ_CP009239.1|WP_038504440.1|144988_145891_-|MBL-fold-metallo-hydrolase	gnl|CDD|293840	cd16282, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	1.65785e-65
NZ_CP009239.1|WP_034644551.1|144457_144985_+|DUF1572-domain-containing-protein	gnl|CDD|311521	pfam07609, DUF1572, Protein of unknown function (DUF1572). These proteins, from several diverse bacteria, share a short conserved sequence towards their N termini.	1.40297e-79
NZ_CP009239.1|WP_013619761.1|131589_133422_-|30S-ribosomal-protein-S1	gnl|CDD|235775	PRK06299, rpsA, 30S ribosomal protein S1; Reviewed.	0
NZ_CP009239.1|WP_013619772.1|143556_144045_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl|CDD|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	2.07245e-79
NZ_CP009239.1|WP_013619760.1|130839_131379_-|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR	gnl|CDD|235365	PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR.	5.85142e-54
NZ_CP009239.1|WP_013619764.1|134879_137324_-|endopeptidase-La	gnl|CDD|223542	COG0466, Lon, ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP009239.1|WP_038504437.1|141916_142726_-|M48-family-metallopeptidase	gnl|CDD|320690	cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	6.01658e-91
NZ_CP009239.1|WP_038504443.1|146047_147439_+|dihydrolipoyl-dehydrogenase	gnl|CDD|235798	PRK06416, PRK06416, dihydrolipoamide dehydrogenase; Reviewed.	0
NZ_CP009239.1|WP_013619759.1|129902_130829_-|aspartate-carbamoyltransferase-catalytic-subunit	gnl|CDD|234849	PRK00856, pyrB, aspartate carbamoyltransferase catalytic subunit.	3.50114e-179

Protein sequences

>NZ_CP009239.1|WP_038504435.1|138625_139702_+|hypothetical-protein
MKTLHYKIITLLLLTIPFLSTANNDKGKYTKEKTIKKNFTVNANALLKVNNKYGNLNITSWDQNRIEIEVHIKTSGNNKEKVQRKLDNITVNFEGSSSTVSAKTNIAKSSSWGWGNSNNVNMQINYTIKLPVKNNIDLTNDYGSITLDRVDGHATINCDYGRLDIGELRGRNNNLNFDYTSKSEIDYVNSAKINADYSGFTITKAGNLILNTDYTSASIINAQDIDYTSDYGSISVNQAKNIKGSGDYISIKLGKVNGNVNLDADYGSIKISELTENCGNVIINADYTGVKVGYNNNYNFKFNLKSSYGGISGVDNCNLSLKEVKNSQKNYKGSCGSENSNNFVNITTEYGSISIHKN
>NZ_CP009239.1|WP_034644547.1|138096_138645_+|hypothetical-protein
MKNNIDIDNLFKELKGSFDTQEPSTTHTANFIEKLNTSNKRHNKRSWRPFAIAASIAFLCAIGFSYFYQKQTTNEQIAEIAPEITETKFYFASLINNQVNELKKETSPSTKKIIDDTLLQLTKLENDYKKLEQNLVNGGNTKLILSAIITNYQTRIDLVKDVMEQIDTIKNLKNYNDENFTL
>NZ_CP009239.1|WP_013619765.1|137542_138100_+|RNA-polymerase-sigma-factor
MSQQKEHINTLLLQCKEGKQSAQLEIYNRYYKAMHNTAYRIVKHSAEAEDIMQESFLSAFTKLHTYKGEVAFGAWLKRIVINNSIYQYRKQQKNTEVALDDIMYRVKDNDSSTIDNGETQLKAQKVMDAMKQLKDNYRISLTLHLIEGYDYEEISEIMNISYANCRTTISRAKESLRKQLTSACI
>NZ_CP009239.1|WP_013619764.1|134879_137324_-|endopeptidase-La
MRDSEFDNLALQGINEEAELIPLLTPEDEEEMSKEQLPEMLPILPLRNTVLFPGVVVPITAGRDASIHLIKDANEGSKVIGVVAQKDEQTENPGIDDIHTLGTVARILRVLKMPDGNTTVIIQGKKRFEVAEVLTEKPYMTATVREASEVRAEEDTPEFKAIIESIKDMALKVISESPNIPSEASFAIKNIESNSFLINFVSSNLRLPVKDKQELLEIENLKERALATLKFMNVEMQKLQLKNDIQSKVRTDMDRQQREYFLHQQMRTIQEELGGGATAEDELTELREKAKDKKFTKKEREYFNKELSKMQRMNPQVAEYAIQRNYLDFFVSLPWGEYSTDKFDLKAAQKILDRDHYGLEDVKKRIIEYLAVLKLRNDMKSPILCLYGPPGTGKTSLGKSIAEALGRSYVRMSLGGLRDESEIRGHRKTYIGAMPGRVLKNIKKAEHSNPVFVLDEIDKLSNSHQGDPSSAMLEVLDPEQNNEFYDNFLEVGYDLSKVMFIATANNLGAIQPALRDRMEIINVSGYTIEEKVEIAKRHLLPKQLKEHGLKPKDLKIGKAQLEKIVEGYTRESGVRTLDKQIAKMVRYAAKSIATEEEYEVKVTNEIVEKVLGPARLERDKYENNDVAGVVTGLAWTSVGGDILFIESILSKGKGAMNITGNLGKVMKESATIALEYIKSNADYFGIKDDIFDKYNVHIHVPEGATPKDGPSAGVTMLTSLVSLFTQRKVKKSLAMTGEITLRGKVLPVGGIKEKILAAKRARIKEIILCEDNRKDILEIKEEYLKGLTFHYVTDMSQVIDIAVTNQKVKNPKKI
>NZ_CP009239.1|WP_038504432.1|134132_134825_-|(d)CMP-kinase
MKKITIAIDGYSSTGKSTIAKQLAKALGYVYVDTGAMYRAVTLYAIRKGFVSETSEDFESLIAALPSISLKFVHNEDLGFSEMYLNDENVEKEIRTLEVSKQVSKVAAVKEVRTKLVEMQKAMGKEKGIVMDGRDIGSVVFPDAEFKVFMTASPETRAHRRYKELLDRGDDVTYEEVLKNVRSRDYIDSNRKESPLILAEDAIEFDNSDMGLIEQFERMHNYALRIIEKQ
>NZ_CP009239.1|WP_013619762.1|133694_134075_+|LysM-peptidoglycan-binding-domain-containing-protein
MSVKAKYQSVLDLGEKLAIKDGDVTEESGVLKIKGQAATQYEKNLIWDKIKEIGGDSPADVKANITVADESVYHRHTVQGGESLSKIAKHYYGDPMKYKQIFEANTNLLKNPDVIHPDQVLVIPNL
>NZ_CP009239.1|WP_013619761.1|131589_133422_-|30S-ribosomal-protein-S1
MAEEKNNAQVEESTQAPEVKTATPKQDPKEFLASFDWDKYEEGIERVDDSKLEEFEAMVAENFVDTADEEVVTGKVVHLTEREAIIDINAKSEGVISLNEFRYNPDLKVGDNVEVLIDIREDKSGQLVLSHRKARTIKAWDRVNNACEKEEIVNGFVKCRTKGGMIVDVFGIEAFLPGSQIDVKPIRDYDQYVGKNMEFKVVKINQEFKNVVVSHKALIEADIEEQKKEIIGQLEKGQVLEGVVKNITSYGVFIDLGGVDGLIHITDLSWSRINHPNEVVELDQKMNVVILDFDDNKSRIQLGLKQLEKHPWEALSEDMKVGDKVKGKVVVIADYGAFIEVAEGVEGLVHVSEMSWSTHLRSAQDFVKVGDEIEAQILTLDRDDRKMSLGIKQLTPDPWTDITSKYPVHSRHKGIVRNFTNFGVFVEMEEGIDGLIYISDLSWTKKIKHPSEFVTVGETLEVEVLELDVDARKLSLGHKQTTENPWDKYETEFALDSVHKGTVDEIVDKGAIVNFNEDIAAFVPTRHLEKEDGKKIAKGEEAEFKIIEFNKEFKRVVASHTAIFREEEQRNVKAAVKRQSAAADEAKPTLGDANEALQALKDKMDAANKK
>NZ_CP009239.1|WP_013619760.1|130839_131379_-|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR
MSKKVLLSSKEIQIILHRLACQLLENHTDFKDTVLIGLQPRGTYLAKRLTTILTQEYGVKEINLGSLDITFYRDDFRRGEKTLEASKTHINFLVEDKKVVFIDDVLYTGRSIRSALTAIQSFGRPAEIELLTLIDRRFSRHLPIQPNYRGRQVDAINEEKVQVLWQENDGQDIVYLINE
>NZ_CP009239.1|WP_013619759.1|129902_130829_-|aspartate-carbamoyltransferase-catalytic-subunit
MSELSVNHLLGIKYLNKNDINLIFETADHFKEVINRSIKKVPSLRDITIANIFFENSTRTKLSFELAEKRLSADVINFSASQSSVKKGETLIDTVNNILSMKVDMVVMRHPNPGAGVFLSKHVKAAIVNAGDGAHEHPTQALLDSYSIREKLGDVGGKNVVIVGDILHSRVALSNILALKLQGANVKVCGPKTLIPKHIESLGVTVETDLRKALNWCDVANMLRVQNERMDISYFPSTREYTQQFGVNKALLQSLDKEIVIMHPGPINRGVEITSDVADSNQSIILDQVENGVAVRMAVLYLLASKIK
>NZ_CP009239.1|WP_013619758.1|129563_129896_-|hypothetical-protein
MVFDKDGTTTIVDQENISLAKFLENLNNAYEKIKNDNIIVNLFSFTALTSSDVLEFLDLSNTHRGSNKSFVLVTNKVSYDDVPEEICVVPTIKEARDIIEMEEIERDLGI
>NZ_CP009239.1|WP_013619769.1|140512_141832_-|MFS-transporter-permease
MTSIALVKGSKKLLNAWAFYDWANSVYSLVIASAIFPIFYGALFRAANIEKVTVFGGEIARAPLISYTTSLAFVFIAIITPLISGVADYLGNKRMFMKFFCYLGGVSCIGLYWFSLENIYFGLVCFFMGLVGFWVSFAINNSYLPDVAHPEQMDAISAKGFSMGYAGSVLLLLFNLLMVMRPEIFGIETDTNGIAELKAMKYSFVTVGIWWIIFSQYTFYYLPKGNKQEGDRSNVILNGFKELKGVWGQLGSQVKLKRYLIAFFVYSMAVQTVMLIATYFGEEEIAWGTDKERTTGLIVSILVIQIVAILGALVTAAASKKFGNVKTLAVVNILWVVICVYAFFMVTPIDFYIGAGCVGLVMGGIQALSRSTYSKFLPNTKDTTSFFSFYDVAEKIGIVIGTFLYGFVAQVTGSMRNAIVFLAIFFIAGVVLLLRVNKK
>NZ_CP009239.1|WP_038504437.1|141916_142726_-|M48-family-metallopeptidase
MRKIFLVLTIFIAVSACKTNPFTGKKTLNIYPNSSIFPTAFAQYDQFLNENKTITGTSEAKMITSVGQRIASAAERWLTANGYPGYLKDYKWEYNLVDDATVNAWCMPGGKIVFYTGILPICQDETGIAVVMGHEVAHALADHGAQRMSAGQLQQIGAVAGNVLIKDEGTKNTFNQAYGIGSQVGVMLPFSRGHETEADRIGLQIMAIAGYNPDEAAELWKRMKANSGGQSQPEFMSTHPSNDTRINNLTQWAPAAKEEAKKFGVTSFK
>NZ_CP009239.1|WP_034644550.1|142898_143432_+|hypothetical-protein
MKKITLAVAAIFAIILTACSGSDGIDGVDGLDGVNITGSIYEVSGTFSDENNYELTFEFPNTVEVFESDVVLVYILWEQLDGTDGQPIDVWRLMPQTRLLDQGTLIYNYDHTFVDARFFLDSDFDLSTLQSADTDNQVFRVAILPAEAVNGKLDTGNINDVMGILDTKEENIIHVSL
>NZ_CP009239.1|WP_013619772.1|143556_144045_+|peptide-methionine-(R)-S-oxide-reductase-MsrB
MYKKLLILSVVALFLSCKGNSQKTKEATKKQTLAKVEKTDAEWKAQLTPLQYNVLRKAGTERAFSSELLNIKEKGIYSCAACNTPLFKSEHKFKSGTGWPSFDRTIEGNVAFDVDYKIGYKRTEEHCAVCGGHLGHVFNDGPKTTGERHCINGAALKFTPTK
>NZ_CP009239.1|WP_013619773.1|144044_144455_+|peptide-methionine-(R)-S-oxide-reductase-MsrB
MSKKYTVEKTEEEWKALLPEQSYNVLRNKGTEYPHTGEFNLHFKDGSYNCKGCNAKLFEADHKFESGCGWPSFDEAVEGAIEYIKDTSHGMTRVETVCANCGGHLGHVFDDGPQETTGQRYCINSASLNFNPSLKK
>NZ_CP009239.1|WP_034644551.1|144457_144985_+|DUF1572-domain-containing-protein
MSFVDDYKESMLFEFNRNKTMAEKTFDQLTNEDLHWTYGEADNSIAIIVKHMVGNMLSRWTNFFTEDGEKEWRNRESEFVAPYQNKEEMLLHWNKGWDCLFTAIDNINEDNFNTKIKIRAVEHSVMAAVSRQLAHYAGHIAQIAYVGRMLKGKKWQSLSIPAGKSEEFNKKMFGK
>NZ_CP009239.1|WP_038504440.1|144988_145891_-|MBL-fold-metallo-hydrolase
MMKTTKFAFLLPFLMFAAILQSQSSDVKIQVDKLTPQMYMLTGQGGNIGVFVGEEYVLMIDDQFSRLSTKIKQAIKSITTKPIVYLLNTHMHGDHTGGNANFNNQTTTIIAHQKVRERLVNENEKALLSKKIDSVTANKKLPEITFSDTMLLYDADETIMAIHVHNAHTDGDAQIYFSKNNVLHMGDTYFSGKYPYIDLNRGGSVGGYINALKKAAILANEDTKIIPGHGKLSNKKELESYILMLETIYVNVKKEIGAGKSLEQVIANKQITANYDATYAWSFISAEKIRETFYKSLMNK
>NZ_CP009239.1|WP_038504443.1|146047_147439_+|dihydrolipoyl-dehydrogenase
MSNFDVIVLGSGPGGYVTAIRASQLGLKTAIVEKESLGGVCLNWGCIPTKALIKSAQVFEYLKHAGDYGLNAENVDKDFGAIIKRSRGVAEGMSKGVQFLMKKNKIEVIKGYGTLKAGKKIAVKDADGKETEYSADHIVVATGARSRELPSLPQDGKKIIGYREAMSLPEQPKKMVVVGSGAIGMEFAYFYNSIGTEVTVVEYLPSVVPVEDQDISKQLERSFKKAGIKVMTSSEVTKVDTSGNGVSVYVKTSKGEEIIQADVVLSAVGIKTNIENIGLENVGIATDRDKIMVNDYYQTNIPGYYAIGDVTPGPALAHVASAEGILCVEKIAGMHVEPIDYGNIPGCTYCIPEVASVGLTEKQAKEKGFDLKIGKFPFSASGKAKASGTPDGFVKVIFDAKYDEWLGCHMIGAGVTDMIAEAVVARKLETTGHEILKAIHPHPTMSEAVMEAVADAYDEVIHL
>NZ_CP009239.1|WP_013619777.1|147523_147814_+|DUF3817-domain-containing-protein
MIKAFRLIAILEGISYLLLFGVGMPLKYMADIKAPNIYIGNAHGVLFIAYAILAFFVCRHLKWGIKRYAILFIASLLPFGTFYIEEKYFSPKALKA
>NZ_CP009239.1|WP_038504446.1|147821_148550_-|diphthine--ammonia-ligase
MHKTYFNWSSGKDSALALYKMQRSNAYKVDRLVTSVNSTFNRVSMHGLRLPLLEAQAKAIGLPLQTIMLNADVSMSSYNEVMKTTMQGLITEGYTHAVFGDIFLEDLKKYREDKLKEVGVKGVFPLWKQDTKVLLKELVQLGFKAITVCVNAKLLDESFVGREVDESFFNDLPENVDPCGENGEFHTFVYDGPIFKQPVPFTVGEKVKKGYAPTTNKDDNCFKKDEDTTWDTSFWYCDLLPK

Crispr_ID: NZ_CP009239_2

• CRISPR_ID: NZ_CP009239_2
• CRISPR_location: 629913-629990
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP009239_2

Consensus_repeat	Method
GATGTTGATGCTAATGAAACTGC	CRISPRCasFinder

spacers of NZ_CP009239_2

>2.1|629936|31|NZ_CP009239|CRISPRCasFinder
TGCAACTAATGCAATTGCTGCTGTGCAAACT

CRISPR arrays and Neighbor proteins around NZ_CP009239_2

CRISPR arrays

The CRISPR arrays of NZ_CP009239_2

>merge|NZ_CP009239|2|629913-629990|CRISPRCasFinder
GATGTTGATGCCAACGAAACTGCTGCAACTAATGCAATTGCTGCTGTGCAAACTGATGTTGACGCTAACGAAGCTGAT

>NZ_CP009239|2|2|629913-629990|CRISPRCasFinder
GATGTTGATGCCAACGAAACTGC	TGCAACTAATGCAATTGCTGCTGTGCAAACT
GATGTTGACGCTAACGAAGCTGAT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|366181
NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl|CDD|235463
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	unknown	unknown	gnl|CDD|179990
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|293786
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	unknown	unknown	gnl|CDD|341067
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	unknown	unknown	gnl|CDD|320692
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	unknown	unknown	gnl|CDD|350622
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	unknown	unknown	gnl|CDD|378853
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl|CDD|369777
NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	unknown	unknown	gnl|CDD|235576

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	9.20431e-09
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	7.69315e-25
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	4.60817e-13
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	7.45336e-06
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	gnl|CDD|350622	cd14847, DD-carboxypeptidase_like, Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B. This family of uncharacterized proteins similar to D-Ala-D-Ala carboxypeptidase pdcA (Myxococcus-type) are zinc-binding enzymes that belong to the peptidase M15 subfamily B. The enzyme D-Ala-D-Ala carbozypeptidase catalyzes carboxypeptidation reactions involved in bacterial cell wall metabolism.	5.22512e-69
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	gnl|CDD|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.18372e-12
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	gnl|CDD|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	5.55002e-14
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl|CDD|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.86242e-11
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	gnl|CDD|179990	PRK05282, PRK05282, dipeptidase PepE.	2.81069e-107
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	1.4723e-19
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	gnl|CDD|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	2.83452e-129
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.50206e-09
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	gnl|CDD|320692	cd07333, M48C_bepA_like, Peptidase M48C Ste24p bepA-like, integral membrane protein. This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture.	4.59785e-54
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	gnl|CDD|378853	pfam12412, DUF3667, Protein of unknown function (DUF3667). This domain family is found in bacteria and eukaryotes, and is approximately 50 amino acids in length. There is a single completely conserved residue P that may be functionally important.	4.87085e-10
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	gnl|CDD|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	6.39647e-21
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	gnl|CDD|235576	PRK05716, PRK05716, methionine aminopeptidase; Validated.	5.88682e-126

Protein sequences

>NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKNLLYIFLCCSSVAVAQNAMYNNGSIRIHDTGTLGLHTNLINDAPFEDNLGTLGFYGQVTTSVTGAFIPVFYDVEMYKPFSAAILETSITATNALNLVDGDFVTYRNNPLENLKLTQNAFTVGESNLSKVDGYMLVEQKQNFFFTVGDSGYIRPLTLQSQSENVTAKCAYFFEDPNLPSTFTTSFNTNNKEKEVRAVSTTEFWDIDSSLPSTVSISWNNRSNIANLVDEYYQVGIAGWHRTQRRWVNLGSVDPIGDLNQGAVTSETFVPNDYEVITLAKMAVATELLDLDNYYVSPNGDGINDNLVIPELEESPNNRLRIYDRNGLKVFEKDNYNGEFNGYSNTNNTIYQRNAGLPSGIYFYLVFLDDLQLEYQGFLYLTDTGN
>NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein
MKKLIFGLFLSTCLFTSIQAQVKIGENPENLHFNSVLELESTSKALVITRMSTLQMNAITPLNGAVIYNTDTRCLHYYNDTEWINLCEAENAGNINLVDNGDDTYTFTNAAGNDITFETPAFTSNHTGSGGVGFSSGIKITDDGNTVNIEVDQIHGNSILNKTIGRTKIADDAIGVDELGDTSVNTNNLIDESVTPVKIQPSATPNQVLKTNATGTNVEWGTLDATNIAGQDLTVDASLEFTGSTTGVGALLETVGISVADGGITNAKLAADAVSTDKIADETILSEDILDGTIATQDIADNAITAVKINADVAGSGLTKNATTGALDVDVAALTGDGNITSTDLNVTGGANAALNDVTLEINPSAVGANELADDAVTTTKIVDANVTTVKIADDAIDNTKVADDAVQTENILDGTIATLDIANDAVTAVKINTDVAGSGLTKNITTGALDVDVTALTGDGNITSTDLNVGGDTNALLGDVTLEINPSAVGANEIADGAVTTTKIADANITLTKLADGTTLGQLMQWDGTNWVLVDAAALTTAETDGIIGNEVTGPTDGTLAVSGTGTVADPLTLDVSAGGIDTAELADNAVTTVKIADTNVTRDKIANAAIDDNKLDKATISLSGFAVPTGDLSIGSQKLTNVSDPTDAQDAATKFYVDTEISDAAAAGATALALKEDTANKSPNVNLGTSDDAFPTQNAVKTYVDTEVSALGNLETRDMTQTAPTRTYDLNGNDFAFTGSGNVGIGTSSPTSKLQVSGEIRSESFASSQGTANTPAYSFYTGGDTNTGMYRPAADEIGFSVGGTQALKIEEDSGDTNVTVNGAFSTRIRNIDTGTTAVLEVDEHTVIFSGLVTNVTFPASASLGQVLILKNLTGGNIAITPAVSYIPSASPTPISTLPVGVTQLQYDGTNWQQIN
>NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE
MKNLLLASTSTLFGENYLEYLLDDVALFFKDVDTITFIPFARPGGISHDNYTAIAAKAFAKIDKKIVGLHTYPTAQEGINQSQAFFCGGGNTFLLVQQLYAQNAMQHLQEHITNGKPYMGTSAGSNIAGVSMHTTNDMPIVYPPSFATMQLVPFNINAHYLDPDPNSKHNGETRETRLKEFHVFNTTPVVGLREGSFLLVNNNTISLKGKHTARIFEPQKAPYESKTIQF
>NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein
MKNNLLALFLLLTTVSLFAQENDRTLLRGTVIYRDINVPNLDVINVTAEDATLTDKDGDFEINVKIGDQLVFTSFNYQIKIVFITEDILKKNRLVVDVNEKVTELDEVVVSPEDQEKFVELKNEEFKEVEYEIDRTTTVTNIAQSQIERGMENGINFVNIFKALTKSKKKKDPNAKVPEIKLSRVLRQVYEDDFFVKDLGIPQDKIDNFLQYCDDKIPSQTLLKKSNEFQLIDFLVTHSKEYKKL
>NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein
MRRYILFLSFLSVCFYANAQQVYYKSVKGAVVSNTQEVNGVYVINTTSGQATITNANGYFVMPAKEKDTLLFSAVQFKKKQLIVTKAILAKKNNIVYLEETLEELNEVVLDNRTFVTAKSLGLPNADAVVLPQSERLLHDADHGPMFGGLSVNVNKLLNAISGRTKMLKKRVARDRKYLESQQMRNSYADSVFVKDLNIPKNRIEEFMLYCEYDSEFNSIAKEKNSFIIWDFLTRKSIAFLKEDKELKIAKQDNK
>NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein
MKYICTLLLLLVAAQNTSAQTKIETLKGRIVSNTQDVVGVYVLNKTTNKGTITSKTGNFSIPVSLKDTIMFSAVQFKNKKIVVTQKILDYKSFLVNLDETLEELNEVVLDNRTLITAKSLGLPNADVEVLPLAKRELFAANNGDNYLSLDPLLNFLSGRTKMLKDRIKRDDLYARSKELRTRFVDSIFSKNLKIPASRIEEFMLYCEYDPRFKGITENKNELVVWDFLRQKSELFLKFK
>NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein
MTRFQLLLFFIMLSQINIAQNKKVETLKGRVVSSKQEVVGVYVLNRSKKKATITNPNGDFSVPVSLHDTLFISAVQFKNREIIITKKILDYNTFIINLDETLEELDEVVLDNRTLITAKKLGLPGADVKLLDIDERAYDTATNWSPSDTVFSIDPILNYLLGNTAKYKARAMRNKRYKAGQFLYKNYLDSTFVKELKIPEHRVQEFVLYCEQDEDFDAFSKQTSEIIIKAFFKMKSKTFLVLNDE
>NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein
MSKLLLFSILVFITFTTVAQQKQVDLKGTVTSTTEEVVGVYVLNRTTEKGTITNLNGYFSIPVRVKDTLEFSAVQFANKVVVVTETMLKTNNYIVPLYESVTTLNEVVVKPFNLSGDLSTDLNNLPLKPVVTGRTLGLPNQNVKILSSDERALYSSMSGGPILSLINAINGQTKLLKKRVERNHRYQKTMRVKRYYADSLFVNELKIEKDKIDLFMWYCEFKDDFQAVINTKDQLKIWAYLRKMSVEFRSKK
>NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein
MLKKRFLLLLLPLFAFVAIHKYYVSVTSVKYSDKEHTLQITSRVFIDDFDELLKQRYGIKSNLATKNENPLAEDYIKKYVKQKFHIYVNGEEVEITYLGKEYDTDNMVLYLEVQNIYDKDLKTVEVESTVLTDIYEEQKNIVHLKFLKNKKSVVLTRVNNKGMLKF
>NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase
MNKINYYLAAVLFLFATVMVQAQEQTEKQAGHTNQSKFRQMYQEFSTPNTYRSASGAPGPDYYQQQANYKMDIELDDKNAKIYGEETITYVNNSPDDLEFLWVQLDQNVREKGNKSALRNSSALQGAMPVGQFAGSHMKGAEFDGGFKIQHIKDANGKDLPYTINQTMMRVDLPTPLKSKSEVSFSIKWWYNIPDHTVSRARSGYEFFEKDGNRAYVIAQFFPRMAVYNDVEGWQNHQFWGSGEFALPFGDYEVNITVPADHVLDATGVLQNRKEVFSKEMMKRYDKAKKSFDKPVVIVTQKEAEAAEKGFSKDKKTWKFVAKNVRDYGFATSRKFIWDMQNVKLPSGKTAMAVSLYPKEGNPLWEEYSTKAVAHTLRSYSNHTFDYPYPKAISVHAKQQGMEYPMICWNYGRPNEKGEYSDRTKYGMISVIIHEVGHNFFPMIVNSDERQWGWMDEGLDTFMQYMAEQEFGEAYPEAIAPNAKYPSRRGEPSKIVPYMAGDQNFMAPIMSNPENVYQLGANAYGKPATALNILRETVMGRELFDHAFKTYSHRWMFKHPTPEDFFRTMEDASAVDLDYYWRGWFYTTDYVDMGVKGVKKYQVSNKPPKQIRDIMEQRNLKMSDLPPMVFLADMDSEDFDASLKGKNPSDVSTTLKEYMMDNLTPAERAAVKEPKFFYEVTFNKPGGIPMPLIVEYTYADGSKENVTYPAEVWRMSDKEIKKVISSQKELVGIVVDPKAETADIDTTNNTWPAKETKSGFDKFKGNLKK
>NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein
MKKIIFKLMLLAPIVISYGQIDPNLLLGLTTATSAEISGITGSLEGSILYNTDEKRIYLYNSSLWQKIPDITDLLPATYTPGSILYTNSSGEPEEDNNQIYWNSTNNRLGIGTNTPTNKVQVTGAIRSAGLLNSDGNQGEPSFRFNGDTDTGMYRTATNELNFSVGNKEAIRIDKYSSTNSQVLISERLGIGFNLPEDLAYSGEDAHSTLDVKGSVSTAIDVTSGDLALDETHHTIILGGAHNITLPDASTCKGRIYIIKNPILFEIGITASISTYKSLLGLDVNLIISQKTIWLQSDGTDWQQIQ
>NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKHILFYISLSVSCILTSQNVVHNTGNLKIFNDGQIGFHIDLTNDGNFDQNEGLAGFYSDDTRTISGAFKPVFNDMEIVVTNDLFLDVAVGITNNNNFILGDVVTPRNATDINLDFINYAFYNGDGNLTKVDGYAAVTDKYNFSFPVGDADKIRPLYLDSETNNNTAKSAYFYEDPNSPSTFTKTFNTDNFADILTAVSTYEFWHLEADTNSKITLTWDDDSSIDSFTDTIEDLRIVGWNKTLNIWENLGNTDITGNFSSGSITSDTFVPNNYDIITFGSSLSAISTNFENYFVSPNNDGVNDFLYFKEVSLSPKNNNLRIYSRWGRIVYDKDAYNNTFGGIANVSGVVKAGNALPDGVYFYILNLKDVNIIHQGYIYLGKQNQ
>NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase
MKDQKELTFKLISAIETYPVRHPVLRAGKPLSSCEFSGDNLKTTFHIGAYQNNQLIGVASLLQVKNTSILNVFAYQLRGMAIANEHQGKGLGKKIINYAETILKEKGVLLLWMNARVSAIPFYTKCGYTKSGSIFDIQKVGPHVVMFKKLN
>NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase
MQRRSFILKTGIIGAAAITAPQLIFAQEQEEEVTYSIEELMGKADIDLYGKGINLRKEAHDAFKKMKVAAYSAGIDLKIVSSYRNYYRQEGIWERKYLKYTDDQKMKPLNAIDKIIEYSTIPGTSRHHWGTDIDIIDGYQKTSGDVLVPKKFEEGGPFEDLKKWMDENANDFGFYLVYTNNKKRRGFKYEPWHYSYAPISKPMLEQFRGKNIMRLVKEQQLLGGEHFTAGFLKSYIVNNILDINPELL
>NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease
MRRGNWKIRILIGLAIVAFAYIQRCSNKEENPYTGRVQNINMDANQEIAIGLQSAPQMAQQHGGLYPDQKLQNFVDAVGNKLVQNSIAKDTPYKYEFHLLADEKTINAFALPGGQIFITYALFSKLNEAQLAGVLGHEIGHVIGRHSAERIADSNFWQTLSTGASVGADMGGVVNGIGQKTLLTNGRGDELESDELGVLFMIQSGYNPEEMIAVMKILKAAAGPNRQPEFQSTHPDPENRIEKIKEAIEKYKNEK
>NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein
MKKTILVFAAALVVATTVVKANVNAVLPNYKVVNVALETVNPFCMAILKGDVETVRKLIEFGEDVNKKSNGMTPAIFAARYNKVEILEILVANGADIRIKCDKGRTIMKHAELSNAKETIAFLEQVAKEKKLARKNKRKRK
>NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MNKKVILMILDGWGKSPDPKISAIENANTPFIDGLYTKYANANLLTDGMNVGLPEGQMGNSEVGHMNLGAGRIVYQDLAKINLAVKENTLKDEEVIKNAFKYAKENNKAVHFLGLLSNGGVHSHTSHLKGLITAAESYGVENSYIHAFTDGRDVDPKSGKSYINDIITFCKDKNTKLASVIGRYYAMDRDKRWERVKLAYDLLVNNAGTKTNNVEQAIQDSYDNDVTDEFVKPIVVTDKNGDPTAKIQENDVVIFFNFRTDRGRELTEMLSQEMFHEYNTHPLKLYYVTMTNYNEAYKNVHVIYDKANIEETLGEVLSKAGKKQIRIAETEKYPHVTFFFNGGREVPFDGEQRILCPSPKVATYDLQPEMSAFDIRDAIIPELNKAEADFVCLNFANPDMVGHTGDMQAAIKACETVDSCAEAVITAGLKNDYTTIVIADHGNCETMVNPDGSPNTAHTTNPVPLILVDKELKQINDGVLGDIAPTILKLIGVKQPELMTQKSLV
>NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase
MVKIKTPEEIEIMRESALMVSKTLGLIAKEIKPGVTTLQLDKIAEEFIRDNGGIPGFLGLYDFPNTLCMSPNQQVVHGIPNNKPLENGEIISVDCGVLKNGYYGDHAYTFEVGEVDPETKKLLDITKQSLYVGIKEFKAGNRVGDVGFAIQQFCEAQGYGVVRELVGHGLGKKMHEGPEMPNYGKRGRGKKFVEGMVVAIEPMINQGTRKIVQHSDGWTITTLDNKPSAHFEHDVAIVNGKPQLLSTFDYIYEALGIESNEEDEFRVK
>NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein
MNCKTCNTGITNTHKYCSNCGAKIVLDRISLKGAWQEFIGPFFSWDNNFWKTFFNLFTKPKEVLEAYIGGARKKYFQPFSYLVVYATIALIINKIFPSTEVADFTNGIKSGLGDANPKAPKEALESINIIYQFYSNYYNLIIISSIPAYSLLTYLTFKKRDHNYSEHLVFNAYIQANLGYILIASQLIFFNLIGLSKGLISSAFILISAIYGLYVFIKLYQLTFKQTLYAFFRYAGYIILAFITLMILSIGVGILYAMTIKTS
>NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase
MKKLFKTILNTIPRPLLIKLSYVSRPILTFFMRGKTYVDPIDGKGFKKFLPYGYEKQRDNVLSPSTLSLERHRLLWLYLQSETDFFTADLKVLHFAPEQAFYKRFRKMKNLEYTTTDLESPLADVKADICNLPFKDNSYDVILCNHVLEHIPDDTKAMQEMYRVLKPGGWGVFQIPQDLSRENTFEDDTITDKKERARIFGQYDHVRIYGKDYFAKLRKIGFTVEEVNYTKKLPPQDVKKYCLAQGEIIPVVKK

Crispr_ID: NZ_CP009239_3

• CRISPR_ID: NZ_CP009239_3
• CRISPR_location: 630288-630365
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP009239_3

Consensus_repeat	Method
GATGTTGATGCTAATGAAACTGC	CRISPRCasFinder

spacers of NZ_CP009239_3

>3.1|630311|31|NZ_CP009239|CRISPRCasFinder
GGCAACTAACGCAATTGCTGCGGTACAAGCA

CRISPR arrays and Neighbor proteins around NZ_CP009239_3

CRISPR arrays

The CRISPR arrays of NZ_CP009239_3

>merge|NZ_CP009239|3|630288-630365|CRISPRCasFinder
GATGTTGATGCTAATGAAACTGCGGCAACTAACGCAATTGCTGCGGTACAAGCAGATGTTGACGCTAATGAAACTGCA

>NZ_CP009239|3|3|630288-630365|CRISPRCasFinder
GATGTTGATGCTAATGAAACTGC	GGCAACTAACGCAATTGCTGCGGTACAAGCA
GATGTTGACGCTAATGAAACTGCA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|366181
NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl|CDD|235463
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	unknown	unknown	gnl|CDD|179990
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|293786
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	unknown	unknown	gnl|CDD|341067
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	unknown	unknown	gnl|CDD|320692
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	unknown	unknown	gnl|CDD|350622
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	unknown	unknown	gnl|CDD|378853
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl|CDD|369777
NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	unknown	unknown	gnl|CDD|235576

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	9.20431e-09
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	7.69315e-25
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	4.60817e-13
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	7.45336e-06
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	gnl|CDD|350622	cd14847, DD-carboxypeptidase_like, Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B. This family of uncharacterized proteins similar to D-Ala-D-Ala carboxypeptidase pdcA (Myxococcus-type) are zinc-binding enzymes that belong to the peptidase M15 subfamily B. The enzyme D-Ala-D-Ala carbozypeptidase catalyzes carboxypeptidation reactions involved in bacterial cell wall metabolism.	5.22512e-69
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	gnl|CDD|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.18372e-12
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	gnl|CDD|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	5.55002e-14
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl|CDD|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.86242e-11
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	gnl|CDD|179990	PRK05282, PRK05282, dipeptidase PepE.	2.81069e-107
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	1.4723e-19
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	gnl|CDD|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	2.83452e-129
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.50206e-09
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	gnl|CDD|320692	cd07333, M48C_bepA_like, Peptidase M48C Ste24p bepA-like, integral membrane protein. This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture.	4.59785e-54
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	gnl|CDD|378853	pfam12412, DUF3667, Protein of unknown function (DUF3667). This domain family is found in bacteria and eukaryotes, and is approximately 50 amino acids in length. There is a single completely conserved residue P that may be functionally important.	4.87085e-10
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	gnl|CDD|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	6.39647e-21
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	gnl|CDD|235576	PRK05716, PRK05716, methionine aminopeptidase; Validated.	5.88682e-126

Protein sequences

>NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKNLLYIFLCCSSVAVAQNAMYNNGSIRIHDTGTLGLHTNLINDAPFEDNLGTLGFYGQVTTSVTGAFIPVFYDVEMYKPFSAAILETSITATNALNLVDGDFVTYRNNPLENLKLTQNAFTVGESNLSKVDGYMLVEQKQNFFFTVGDSGYIRPLTLQSQSENVTAKCAYFFEDPNLPSTFTTSFNTNNKEKEVRAVSTTEFWDIDSSLPSTVSISWNNRSNIANLVDEYYQVGIAGWHRTQRRWVNLGSVDPIGDLNQGAVTSETFVPNDYEVITLAKMAVATELLDLDNYYVSPNGDGINDNLVIPELEESPNNRLRIYDRNGLKVFEKDNYNGEFNGYSNTNNTIYQRNAGLPSGIYFYLVFLDDLQLEYQGFLYLTDTGN
>NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein
MKKLIFGLFLSTCLFTSIQAQVKIGENPENLHFNSVLELESTSKALVITRMSTLQMNAITPLNGAVIYNTDTRCLHYYNDTEWINLCEAENAGNINLVDNGDDTYTFTNAAGNDITFETPAFTSNHTGSGGVGFSSGIKITDDGNTVNIEVDQIHGNSILNKTIGRTKIADDAIGVDELGDTSVNTNNLIDESVTPVKIQPSATPNQVLKTNATGTNVEWGTLDATNIAGQDLTVDASLEFTGSTTGVGALLETVGISVADGGITNAKLAADAVSTDKIADETILSEDILDGTIATQDIADNAITAVKINADVAGSGLTKNATTGALDVDVAALTGDGNITSTDLNVTGGANAALNDVTLEINPSAVGANELADDAVTTTKIVDANVTTVKIADDAIDNTKVADDAVQTENILDGTIATLDIANDAVTAVKINTDVAGSGLTKNITTGALDVDVTALTGDGNITSTDLNVGGDTNALLGDVTLEINPSAVGANEIADGAVTTTKIADANITLTKLADGTTLGQLMQWDGTNWVLVDAAALTTAETDGIIGNEVTGPTDGTLAVSGTGTVADPLTLDVSAGGIDTAELADNAVTTVKIADTNVTRDKIANAAIDDNKLDKATISLSGFAVPTGDLSIGSQKLTNVSDPTDAQDAATKFYVDTEISDAAAAGATALALKEDTANKSPNVNLGTSDDAFPTQNAVKTYVDTEVSALGNLETRDMTQTAPTRTYDLNGNDFAFTGSGNVGIGTSSPTSKLQVSGEIRSESFASSQGTANTPAYSFYTGGDTNTGMYRPAADEIGFSVGGTQALKIEEDSGDTNVTVNGAFSTRIRNIDTGTTAVLEVDEHTVIFSGLVTNVTFPASASLGQVLILKNLTGGNIAITPAVSYIPSASPTPISTLPVGVTQLQYDGTNWQQIN
>NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE
MKNLLLASTSTLFGENYLEYLLDDVALFFKDVDTITFIPFARPGGISHDNYTAIAAKAFAKIDKKIVGLHTYPTAQEGINQSQAFFCGGGNTFLLVQQLYAQNAMQHLQEHITNGKPYMGTSAGSNIAGVSMHTTNDMPIVYPPSFATMQLVPFNINAHYLDPDPNSKHNGETRETRLKEFHVFNTTPVVGLREGSFLLVNNNTISLKGKHTARIFEPQKAPYESKTIQF
>NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein
MKNNLLALFLLLTTVSLFAQENDRTLLRGTVIYRDINVPNLDVINVTAEDATLTDKDGDFEINVKIGDQLVFTSFNYQIKIVFITEDILKKNRLVVDVNEKVTELDEVVVSPEDQEKFVELKNEEFKEVEYEIDRTTTVTNIAQSQIERGMENGINFVNIFKALTKSKKKKDPNAKVPEIKLSRVLRQVYEDDFFVKDLGIPQDKIDNFLQYCDDKIPSQTLLKKSNEFQLIDFLVTHSKEYKKL
>NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein
MRRYILFLSFLSVCFYANAQQVYYKSVKGAVVSNTQEVNGVYVINTTSGQATITNANGYFVMPAKEKDTLLFSAVQFKKKQLIVTKAILAKKNNIVYLEETLEELNEVVLDNRTFVTAKSLGLPNADAVVLPQSERLLHDADHGPMFGGLSVNVNKLLNAISGRTKMLKKRVARDRKYLESQQMRNSYADSVFVKDLNIPKNRIEEFMLYCEYDSEFNSIAKEKNSFIIWDFLTRKSIAFLKEDKELKIAKQDNK
>NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein
MKYICTLLLLLVAAQNTSAQTKIETLKGRIVSNTQDVVGVYVLNKTTNKGTITSKTGNFSIPVSLKDTIMFSAVQFKNKKIVVTQKILDYKSFLVNLDETLEELNEVVLDNRTLITAKSLGLPNADVEVLPLAKRELFAANNGDNYLSLDPLLNFLSGRTKMLKDRIKRDDLYARSKELRTRFVDSIFSKNLKIPASRIEEFMLYCEYDPRFKGITENKNELVVWDFLRQKSELFLKFK
>NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein
MTRFQLLLFFIMLSQINIAQNKKVETLKGRVVSSKQEVVGVYVLNRSKKKATITNPNGDFSVPVSLHDTLFISAVQFKNREIIITKKILDYNTFIINLDETLEELDEVVLDNRTLITAKKLGLPGADVKLLDIDERAYDTATNWSPSDTVFSIDPILNYLLGNTAKYKARAMRNKRYKAGQFLYKNYLDSTFVKELKIPEHRVQEFVLYCEQDEDFDAFSKQTSEIIIKAFFKMKSKTFLVLNDE
>NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein
MSKLLLFSILVFITFTTVAQQKQVDLKGTVTSTTEEVVGVYVLNRTTEKGTITNLNGYFSIPVRVKDTLEFSAVQFANKVVVVTETMLKTNNYIVPLYESVTTLNEVVVKPFNLSGDLSTDLNNLPLKPVVTGRTLGLPNQNVKILSSDERALYSSMSGGPILSLINAINGQTKLLKKRVERNHRYQKTMRVKRYYADSLFVNELKIEKDKIDLFMWYCEFKDDFQAVINTKDQLKIWAYLRKMSVEFRSKK
>NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein
MLKKRFLLLLLPLFAFVAIHKYYVSVTSVKYSDKEHTLQITSRVFIDDFDELLKQRYGIKSNLATKNENPLAEDYIKKYVKQKFHIYVNGEEVEITYLGKEYDTDNMVLYLEVQNIYDKDLKTVEVESTVLTDIYEEQKNIVHLKFLKNKKSVVLTRVNNKGMLKF
>NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase
MNKINYYLAAVLFLFATVMVQAQEQTEKQAGHTNQSKFRQMYQEFSTPNTYRSASGAPGPDYYQQQANYKMDIELDDKNAKIYGEETITYVNNSPDDLEFLWVQLDQNVREKGNKSALRNSSALQGAMPVGQFAGSHMKGAEFDGGFKIQHIKDANGKDLPYTINQTMMRVDLPTPLKSKSEVSFSIKWWYNIPDHTVSRARSGYEFFEKDGNRAYVIAQFFPRMAVYNDVEGWQNHQFWGSGEFALPFGDYEVNITVPADHVLDATGVLQNRKEVFSKEMMKRYDKAKKSFDKPVVIVTQKEAEAAEKGFSKDKKTWKFVAKNVRDYGFATSRKFIWDMQNVKLPSGKTAMAVSLYPKEGNPLWEEYSTKAVAHTLRSYSNHTFDYPYPKAISVHAKQQGMEYPMICWNYGRPNEKGEYSDRTKYGMISVIIHEVGHNFFPMIVNSDERQWGWMDEGLDTFMQYMAEQEFGEAYPEAIAPNAKYPSRRGEPSKIVPYMAGDQNFMAPIMSNPENVYQLGANAYGKPATALNILRETVMGRELFDHAFKTYSHRWMFKHPTPEDFFRTMEDASAVDLDYYWRGWFYTTDYVDMGVKGVKKYQVSNKPPKQIRDIMEQRNLKMSDLPPMVFLADMDSEDFDASLKGKNPSDVSTTLKEYMMDNLTPAERAAVKEPKFFYEVTFNKPGGIPMPLIVEYTYADGSKENVTYPAEVWRMSDKEIKKVISSQKELVGIVVDPKAETADIDTTNNTWPAKETKSGFDKFKGNLKK
>NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein
MKKIIFKLMLLAPIVISYGQIDPNLLLGLTTATSAEISGITGSLEGSILYNTDEKRIYLYNSSLWQKIPDITDLLPATYTPGSILYTNSSGEPEEDNNQIYWNSTNNRLGIGTNTPTNKVQVTGAIRSAGLLNSDGNQGEPSFRFNGDTDTGMYRTATNELNFSVGNKEAIRIDKYSSTNSQVLISERLGIGFNLPEDLAYSGEDAHSTLDVKGSVSTAIDVTSGDLALDETHHTIILGGAHNITLPDASTCKGRIYIIKNPILFEIGITASISTYKSLLGLDVNLIISQKTIWLQSDGTDWQQIQ
>NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKHILFYISLSVSCILTSQNVVHNTGNLKIFNDGQIGFHIDLTNDGNFDQNEGLAGFYSDDTRTISGAFKPVFNDMEIVVTNDLFLDVAVGITNNNNFILGDVVTPRNATDINLDFINYAFYNGDGNLTKVDGYAAVTDKYNFSFPVGDADKIRPLYLDSETNNNTAKSAYFYEDPNSPSTFTKTFNTDNFADILTAVSTYEFWHLEADTNSKITLTWDDDSSIDSFTDTIEDLRIVGWNKTLNIWENLGNTDITGNFSSGSITSDTFVPNNYDIITFGSSLSAISTNFENYFVSPNNDGVNDFLYFKEVSLSPKNNNLRIYSRWGRIVYDKDAYNNTFGGIANVSGVVKAGNALPDGVYFYILNLKDVNIIHQGYIYLGKQNQ
>NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase
MKDQKELTFKLISAIETYPVRHPVLRAGKPLSSCEFSGDNLKTTFHIGAYQNNQLIGVASLLQVKNTSILNVFAYQLRGMAIANEHQGKGLGKKIINYAETILKEKGVLLLWMNARVSAIPFYTKCGYTKSGSIFDIQKVGPHVVMFKKLN
>NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase
MQRRSFILKTGIIGAAAITAPQLIFAQEQEEEVTYSIEELMGKADIDLYGKGINLRKEAHDAFKKMKVAAYSAGIDLKIVSSYRNYYRQEGIWERKYLKYTDDQKMKPLNAIDKIIEYSTIPGTSRHHWGTDIDIIDGYQKTSGDVLVPKKFEEGGPFEDLKKWMDENANDFGFYLVYTNNKKRRGFKYEPWHYSYAPISKPMLEQFRGKNIMRLVKEQQLLGGEHFTAGFLKSYIVNNILDINPELL
>NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease
MRRGNWKIRILIGLAIVAFAYIQRCSNKEENPYTGRVQNINMDANQEIAIGLQSAPQMAQQHGGLYPDQKLQNFVDAVGNKLVQNSIAKDTPYKYEFHLLADEKTINAFALPGGQIFITYALFSKLNEAQLAGVLGHEIGHVIGRHSAERIADSNFWQTLSTGASVGADMGGVVNGIGQKTLLTNGRGDELESDELGVLFMIQSGYNPEEMIAVMKILKAAAGPNRQPEFQSTHPDPENRIEKIKEAIEKYKNEK
>NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein
MKKTILVFAAALVVATTVVKANVNAVLPNYKVVNVALETVNPFCMAILKGDVETVRKLIEFGEDVNKKSNGMTPAIFAARYNKVEILEILVANGADIRIKCDKGRTIMKHAELSNAKETIAFLEQVAKEKKLARKNKRKRK
>NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MNKKVILMILDGWGKSPDPKISAIENANTPFIDGLYTKYANANLLTDGMNVGLPEGQMGNSEVGHMNLGAGRIVYQDLAKINLAVKENTLKDEEVIKNAFKYAKENNKAVHFLGLLSNGGVHSHTSHLKGLITAAESYGVENSYIHAFTDGRDVDPKSGKSYINDIITFCKDKNTKLASVIGRYYAMDRDKRWERVKLAYDLLVNNAGTKTNNVEQAIQDSYDNDVTDEFVKPIVVTDKNGDPTAKIQENDVVIFFNFRTDRGRELTEMLSQEMFHEYNTHPLKLYYVTMTNYNEAYKNVHVIYDKANIEETLGEVLSKAGKKQIRIAETEKYPHVTFFFNGGREVPFDGEQRILCPSPKVATYDLQPEMSAFDIRDAIIPELNKAEADFVCLNFANPDMVGHTGDMQAAIKACETVDSCAEAVITAGLKNDYTTIVIADHGNCETMVNPDGSPNTAHTTNPVPLILVDKELKQINDGVLGDIAPTILKLIGVKQPELMTQKSLV
>NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase
MVKIKTPEEIEIMRESALMVSKTLGLIAKEIKPGVTTLQLDKIAEEFIRDNGGIPGFLGLYDFPNTLCMSPNQQVVHGIPNNKPLENGEIISVDCGVLKNGYYGDHAYTFEVGEVDPETKKLLDITKQSLYVGIKEFKAGNRVGDVGFAIQQFCEAQGYGVVRELVGHGLGKKMHEGPEMPNYGKRGRGKKFVEGMVVAIEPMINQGTRKIVQHSDGWTITTLDNKPSAHFEHDVAIVNGKPQLLSTFDYIYEALGIESNEEDEFRVK
>NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein
MNCKTCNTGITNTHKYCSNCGAKIVLDRISLKGAWQEFIGPFFSWDNNFWKTFFNLFTKPKEVLEAYIGGARKKYFQPFSYLVVYATIALIINKIFPSTEVADFTNGIKSGLGDANPKAPKEALESINIIYQFYSNYYNLIIISSIPAYSLLTYLTFKKRDHNYSEHLVFNAYIQANLGYILIASQLIFFNLIGLSKGLISSAFILISAIYGLYVFIKLYQLTFKQTLYAFFRYAGYIILAFITLMILSIGVGILYAMTIKTS
>NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase
MKKLFKTILNTIPRPLLIKLSYVSRPILTFFMRGKTYVDPIDGKGFKKFLPYGYEKQRDNVLSPSTLSLERHRLLWLYLQSETDFFTADLKVLHFAPEQAFYKRFRKMKNLEYTTTDLESPLADVKADICNLPFKDNSYDVILCNHVLEHIPDDTKAMQEMYRVLKPGGWGVFQIPQDLSRENTFEDDTITDKKERARIFGQYDHVRIYGKDYFAKLRKIGFTVEEVNYTKKLPPQDVKKYCLAQGEIIPVVKK

Crispr_ID: NZ_CP009239_4

• CRISPR_ID: NZ_CP009239_4
• CRISPR_location: 630687-630769
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP009239_4

Consensus_repeat	Method
GATGTTGATGCTAATGAAACTGC	CRISPRCasFinder

spacers of NZ_CP009239_4

>4.1|630710|37|NZ_CP009239|CRISPRCasFinder
TGCAACTAACGCTATTACAGCTTTACAAAATGATAAA

CRISPR arrays and Neighbor proteins around NZ_CP009239_4

CRISPR arrays

The CRISPR arrays of NZ_CP009239_4

>merge|NZ_CP009239|4|630687-630769|CRISPRCasFinder
GATGTTGATGCCAACGAAACTGCTGCAACTAACGCTATTACAGCTTTACAAAATGATAAAGAAGATGCTGCTAATAAATCTAC

>NZ_CP009239|4|4|630687-630769|CRISPRCasFinder
GATGTTGATGCCAACGAAACTGC	TGCAACTAACGCTATTACAGCTTTACAAAATGATAAA
GAAGATGCTGCTAATAAATCTAC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|366181
NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl|CDD|235463
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	unknown	unknown	gnl|CDD|179990
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|293786
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl|CDD|372639
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	unknown	unknown	gnl|CDD|341067
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	unknown	unknown	gnl|CDD|274948
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	unknown	unknown	gnl|CDD|320692
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	unknown	unknown	gnl|CDD|350622
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	unknown	unknown	gnl|CDD|378853
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl|CDD|369777
NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	unknown	unknown	gnl|CDD|235576

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	9.20431e-09
NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	7.69315e-25
NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	4.60817e-13
NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	7.45336e-06
NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase	gnl|CDD|350622	cd14847, DD-carboxypeptidase_like, Uncharacterized proteins of the MEROPS peptidase family M15, subfamily B. This family of uncharacterized proteins similar to D-Ala-D-Ala carboxypeptidase pdcA (Myxococcus-type) are zinc-binding enzymes that belong to the peptidase M15 subfamily B. The enzyme D-Ala-D-Ala carbozypeptidase catalyzes carboxypeptidation reactions involved in bacterial cell wall metabolism.	5.22512e-69
NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase	gnl|CDD|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.18372e-12
NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein	gnl|CDD|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	5.55002e-14
NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl|CDD|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.86242e-11
NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE	gnl|CDD|179990	PRK05282, PRK05282, dipeptidase PepE.	2.81069e-107
NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein	gnl|CDD|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	1.4723e-19
NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase	gnl|CDD|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	2.83452e-129
NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein	gnl|CDD|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	2.50206e-09
NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease	gnl|CDD|320692	cd07333, M48C_bepA_like, Peptidase M48C Ste24p bepA-like, integral membrane protein. This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture.	4.59785e-54
NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein	gnl|CDD|378853	pfam12412, DUF3667, Protein of unknown function (DUF3667). This domain family is found in bacteria and eukaryotes, and is approximately 50 amino acids in length. There is a single completely conserved residue P that may be functionally important.	4.87085e-10
NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase	gnl|CDD|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	6.39647e-21
NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase	gnl|CDD|235576	PRK05716, PRK05716, methionine aminopeptidase; Validated.	5.88682e-126

Protein sequences

>NZ_CP009239.1|WP_038504750.1|624114_625272_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKNLLYIFLCCSSVAVAQNAMYNNGSIRIHDTGTLGLHTNLINDAPFEDNLGTLGFYGQVTTSVTGAFIPVFYDVEMYKPFSAAILETSITATNALNLVDGDFVTYRNNPLENLKLTQNAFTVGESNLSKVDGYMLVEQKQNFFFTVGDSGYIRPLTLQSQSENVTAKCAYFFEDPNLPSTFTTSFNTNNKEKEVRAVSTTEFWDIDSSLPSTVSISWNNRSNIANLVDEYYQVGIAGWHRTQRRWVNLGSVDPIGDLNQGAVTSETFVPNDYEVITLAKMAVATELLDLDNYYVSPNGDGINDNLVIPELEESPNNRLRIYDRNGLKVFEKDNYNGEFNGYSNTNNTIYQRNAGLPSGIYFYLVFLDDLQLEYQGFLYLTDTGN
>NZ_CP009239.1|WP_038504748.1|621359_624113_+|hypothetical-protein
MKKLIFGLFLSTCLFTSIQAQVKIGENPENLHFNSVLELESTSKALVITRMSTLQMNAITPLNGAVIYNTDTRCLHYYNDTEWINLCEAENAGNINLVDNGDDTYTFTNAAGNDITFETPAFTSNHTGSGGVGFSSGIKITDDGNTVNIEVDQIHGNSILNKTIGRTKIADDAIGVDELGDTSVNTNNLIDESVTPVKIQPSATPNQVLKTNATGTNVEWGTLDATNIAGQDLTVDASLEFTGSTTGVGALLETVGISVADGGITNAKLAADAVSTDKIADETILSEDILDGTIATQDIADNAITAVKINADVAGSGLTKNATTGALDVDVAALTGDGNITSTDLNVTGGANAALNDVTLEINPSAVGANELADDAVTTTKIVDANVTTVKIADDAIDNTKVADDAVQTENILDGTIATLDIANDAVTAVKINTDVAGSGLTKNITTGALDVDVTALTGDGNITSTDLNVGGDTNALLGDVTLEINPSAVGANEIADGAVTTTKIADANITLTKLADGTTLGQLMQWDGTNWVLVDAAALTTAETDGIIGNEVTGPTDGTLAVSGTGTVADPLTLDVSAGGIDTAELADNAVTTVKIADTNVTRDKIANAAIDDNKLDKATISLSGFAVPTGDLSIGSQKLTNVSDPTDAQDAATKFYVDTEISDAAAAGATALALKEDTANKSPNVNLGTSDDAFPTQNAVKTYVDTEVSALGNLETRDMTQTAPTRTYDLNGNDFAFTGSGNVGIGTSSPTSKLQVSGEIRSESFASSQGTANTPAYSFYTGGDTNTGMYRPAADEIGFSVGGTQALKIEEDSGDTNVTVNGAFSTRIRNIDTGTTAVLEVDEHTVIFSGLVTNVTFPASASLGQVLILKNLTGGNIAITPAVSYIPSASPTPISTLPVGVTQLQYDGTNWQQIN
>NZ_CP009239.1|WP_034646268.1|620537_621230_+|dipeptidase-PepE
MKNLLLASTSTLFGENYLEYLLDDVALFFKDVDTITFIPFARPGGISHDNYTAIAAKAFAKIDKKIVGLHTYPTAQEGINQSQAFFCGGGNTFLLVQQLYAQNAMQHLQEHITNGKPYMGTSAGSNIAGVSMHTTNDMPIVYPPSFATMQLVPFNINAHYLDPDPNSKHNGETRETRLKEFHVFNTTPVVGLREGSFLLVNNNTISLKGKHTARIFEPQKAPYESKTIQF
>NZ_CP009239.1|WP_013620190.1|619652_620390_-|hypothetical-protein
MKNNLLALFLLLTTVSLFAQENDRTLLRGTVIYRDINVPNLDVINVTAEDATLTDKDGDFEINVKIGDQLVFTSFNYQIKIVFITEDILKKNRLVVDVNEKVTELDEVVVSPEDQEKFVELKNEEFKEVEYEIDRTTTVTNIAQSQIERGMENGINFVNIFKALTKSKKKKDPNAKVPEIKLSRVLRQVYEDDFFVKDLGIPQDKIDNFLQYCDDKIPSQTLLKKSNEFQLIDFLVTHSKEYKKL
>NZ_CP009239.1|WP_051456106.1|618881_619649_-|hypothetical-protein
MRRYILFLSFLSVCFYANAQQVYYKSVKGAVVSNTQEVNGVYVINTTSGQATITNANGYFVMPAKEKDTLLFSAVQFKKKQLIVTKAILAKKNNIVYLEETLEELNEVVLDNRTFVTAKSLGLPNADAVVLPQSERLLHDADHGPMFGGLSVNVNKLLNAISGRTKMLKKRVARDRKYLESQQMRNSYADSVFVKDLNIPKNRIEEFMLYCEYDSEFNSIAKEKNSFIIWDFLTRKSIAFLKEDKELKIAKQDNK
>NZ_CP009239.1|WP_081901737.1|618145_618865_-|hypothetical-protein
MKYICTLLLLLVAAQNTSAQTKIETLKGRIVSNTQDVVGVYVLNKTTNKGTITSKTGNFSIPVSLKDTIMFSAVQFKNKKIVVTQKILDYKSFLVNLDETLEELNEVVLDNRTLITAKSLGLPNADVEVLPLAKRELFAANNGDNYLSLDPLLNFLSGRTKMLKDRIKRDDLYARSKELRTRFVDSIFSKNLKIPASRIEEFMLYCEYDPRFKGITENKNELVVWDFLRQKSELFLKFK
>NZ_CP009239.1|WP_034646266.1|617400_618138_-|hypothetical-protein
MTRFQLLLFFIMLSQINIAQNKKVETLKGRVVSSKQEVVGVYVLNRSKKKATITNPNGDFSVPVSLHDTLFISAVQFKNREIIITKKILDYNTFIINLDETLEELDEVVLDNRTLITAKKLGLPGADVKLLDIDERAYDTATNWSPSDTVFSIDPILNYLLGNTAKYKARAMRNKRYKAGQFLYKNYLDSTFVKELKIPEHRVQEFVLYCEQDEDFDAFSKQTSEIIIKAFFKMKSKTFLVLNDE
>NZ_CP009239.1|WP_034646265.1|616642_617401_-|hypothetical-protein
MSKLLLFSILVFITFTTVAQQKQVDLKGTVTSTTEEVVGVYVLNRTTEKGTITNLNGYFSIPVRVKDTLEFSAVQFANKVVVVTETMLKTNNYIVPLYESVTTLNEVVVKPFNLSGDLSTDLNNLPLKPVVTGRTLGLPNQNVKILSSDERALYSSMSGGPILSLINAINGQTKLLKKRVERNHRYQKTMRVKRYYADSLFVNELKIEKDKIDLFMWYCEFKDDFQAVINTKDQLKIWAYLRKMSVEFRSKK
>NZ_CP009239.1|WP_034646277.1|616058_616559_-|hypothetical-protein
MLKKRFLLLLLPLFAFVAIHKYYVSVTSVKYSDKEHTLQITSRVFIDDFDELLKQRYGIKSNLATKNENPLAEDYIKKYVKQKFHIYVNGEEVEITYLGKEYDTDNMVLYLEVQNIYDKDLKTVEVESTVLTDIYEEQKNIVHLKFLKNKKSVVLTRVNNKGMLKF
>NZ_CP009239.1|WP_038504745.1|613689_615999_-|M1-family-metallopeptidase
MNKINYYLAAVLFLFATVMVQAQEQTEKQAGHTNQSKFRQMYQEFSTPNTYRSASGAPGPDYYQQQANYKMDIELDDKNAKIYGEETITYVNNSPDDLEFLWVQLDQNVREKGNKSALRNSSALQGAMPVGQFAGSHMKGAEFDGGFKIQHIKDANGKDLPYTINQTMMRVDLPTPLKSKSEVSFSIKWWYNIPDHTVSRARSGYEFFEKDGNRAYVIAQFFPRMAVYNDVEGWQNHQFWGSGEFALPFGDYEVNITVPADHVLDATGVLQNRKEVFSKEMMKRYDKAKKSFDKPVVIVTQKEAEAAEKGFSKDKKTWKFVAKNVRDYGFATSRKFIWDMQNVKLPSGKTAMAVSLYPKEGNPLWEEYSTKAVAHTLRSYSNHTFDYPYPKAISVHAKQQGMEYPMICWNYGRPNEKGEYSDRTKYGMISVIIHEVGHNFFPMIVNSDERQWGWMDEGLDTFMQYMAEQEFGEAYPEAIAPNAKYPSRRGEPSKIVPYMAGDQNFMAPIMSNPENVYQLGANAYGKPATALNILRETVMGRELFDHAFKTYSHRWMFKHPTPEDFFRTMEDASAVDLDYYWRGWFYTTDYVDMGVKGVKKYQVSNKPPKQIRDIMEQRNLKMSDLPPMVFLADMDSEDFDASLKGKNPSDVSTTLKEYMMDNLTPAERAAVKEPKFFYEVTFNKPGGIPMPLIVEYTYADGSKENVTYPAEVWRMSDKEIKKVISSQKELVGIVVDPKAETADIDTTNNTWPAKETKSGFDKFKGNLKK
>NZ_CP009239.1|WP_038504756.1|632235_633156_+|hypothetical-protein
MKKIIFKLMLLAPIVISYGQIDPNLLLGLTTATSAEISGITGSLEGSILYNTDEKRIYLYNSSLWQKIPDITDLLPATYTPGSILYTNSSGEPEEDNNQIYWNSTNNRLGIGTNTPTNKVQVTGAIRSAGLLNSDGNQGEPSFRFNGDTDTGMYRTATNELNFSVGNKEAIRIDKYSSTNSQVLISERLGIGFNLPEDLAYSGEDAHSTLDVKGSVSTAIDVTSGDLALDETHHTIILGGAHNITLPDASTCKGRIYIIKNPILFEIGITASISTYKSLLGLDVNLIISQKTIWLQSDGTDWQQIQ
>NZ_CP009239.1|WP_013620196.1|633158_634313_+|gliding-motility-associated-C-terminal-domain-containing-protein
MKHILFYISLSVSCILTSQNVVHNTGNLKIFNDGQIGFHIDLTNDGNFDQNEGLAGFYSDDTRTISGAFKPVFNDMEIVVTNDLFLDVAVGITNNNNFILGDVVTPRNATDINLDFINYAFYNGDGNLTKVDGYAAVTDKYNFSFPVGDADKIRPLYLDSETNNNTAKSAYFYEDPNSPSTFTKTFNTDNFADILTAVSTYEFWHLEADTNSKITLTWDDDSSIDSFTDTIEDLRIVGWNKTLNIWENLGNTDITGNFSSGSITSDTFVPNNYDIITFGSSLSAISTNFENYFVSPNNDGVNDFLYFKEVSLSPKNNNLRIYSRWGRIVYDKDAYNNTFGGIANVSGVVKAGNALPDGVYFYILNLKDVNIIHQGYIYLGKQNQ
>NZ_CP009239.1|WP_013620197.1|634344_634800_+|GNAT-family-N-acetyltransferase
MKDQKELTFKLISAIETYPVRHPVLRAGKPLSSCEFSGDNLKTTFHIGAYQNNQLIGVASLLQVKNTSILNVFAYQLRGMAIANEHQGKGLGKKIINYAETILKEKGVLLLWMNARVSAIPFYTKCGYTKSGSIFDIQKVGPHVVMFKKLN
>NZ_CP009239.1|WP_013620198.1|634805_635552_+|M15-family-metallopeptidase
MQRRSFILKTGIIGAAAITAPQLIFAQEQEEEVTYSIEELMGKADIDLYGKGINLRKEAHDAFKKMKVAAYSAGIDLKIVSSYRNYYRQEGIWERKYLKYTDDQKMKPLNAIDKIIEYSTIPGTSRHHWGTDIDIIDGYQKTSGDVLVPKKFEEGGPFEDLKKWMDENANDFGFYLVYTNNKKRRGFKYEPWHYSYAPISKPMLEQFRGKNIMRLVKEQQLLGGEHFTAGFLKSYIVNNILDINPELL
>NZ_CP009239.1|WP_013620199.1|635596_636364_+|M48-family-metalloprotease
MRRGNWKIRILIGLAIVAFAYIQRCSNKEENPYTGRVQNINMDANQEIAIGLQSAPQMAQQHGGLYPDQKLQNFVDAVGNKLVQNSIAKDTPYKYEFHLLADEKTINAFALPGGQIFITYALFSKLNEAQLAGVLGHEIGHVIGRHSAERIADSNFWQTLSTGASVGADMGGVVNGIGQKTLLTNGRGDELESDELGVLFMIQSGYNPEEMIAVMKILKAAAGPNRQPEFQSTHPDPENRIEKIKEAIEKYKNEK
>NZ_CP009239.1|WP_013620201.1|636757_637183_-|ankyrin-repeat-domain-containing-protein
MKKTILVFAAALVVATTVVKANVNAVLPNYKVVNVALETVNPFCMAILKGDVETVRKLIEFGEDVNKKSNGMTPAIFAARYNKVEILEILVANGADIRIKCDKGRTIMKHAELSNAKETIAFLEQVAKEKKLARKNKRKRK
>NZ_CP009239.1|WP_013620202.1|637422_638940_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MNKKVILMILDGWGKSPDPKISAIENANTPFIDGLYTKYANANLLTDGMNVGLPEGQMGNSEVGHMNLGAGRIVYQDLAKINLAVKENTLKDEEVIKNAFKYAKENNKAVHFLGLLSNGGVHSHTSHLKGLITAAESYGVENSYIHAFTDGRDVDPKSGKSYINDIITFCKDKNTKLASVIGRYYAMDRDKRWERVKLAYDLLVNNAGTKTNNVEQAIQDSYDNDVTDEFVKPIVVTDKNGDPTAKIQENDVVIFFNFRTDRGRELTEMLSQEMFHEYNTHPLKLYYVTMTNYNEAYKNVHVIYDKANIEETLGEVLSKAGKKQIRIAETEKYPHVTFFFNGGREVPFDGEQRILCPSPKVATYDLQPEMSAFDIRDAIIPELNKAEADFVCLNFANPDMVGHTGDMQAAIKACETVDSCAEAVITAGLKNDYTTIVIADHGNCETMVNPDGSPNTAHTTNPVPLILVDKELKQINDGVLGDIAPTILKLIGVKQPELMTQKSLV
>NZ_CP009239.1|WP_013620203.1|638993_639800_+|type-I-methionyl-aminopeptidase
MVKIKTPEEIEIMRESALMVSKTLGLIAKEIKPGVTTLQLDKIAEEFIRDNGGIPGFLGLYDFPNTLCMSPNQQVVHGIPNNKPLENGEIISVDCGVLKNGYYGDHAYTFEVGEVDPETKKLLDITKQSLYVGIKEFKAGNRVGDVGFAIQQFCEAQGYGVVRELVGHGLGKKMHEGPEMPNYGKRGRGKKFVEGMVVAIEPMINQGTRKIVQHSDGWTITTLDNKPSAHFEHDVAIVNGKPQLLSTFDYIYEALGIESNEEDEFRVK
>NZ_CP009239.1|WP_013620204.1|639823_640615_+|DUF3667-domain-containing-protein
MNCKTCNTGITNTHKYCSNCGAKIVLDRISLKGAWQEFIGPFFSWDNNFWKTFFNLFTKPKEVLEAYIGGARKKYFQPFSYLVVYATIALIINKIFPSTEVADFTNGIKSGLGDANPKAPKEALESINIIYQFYSNYYNLIIISSIPAYSLLTYLTFKKRDHNYSEHLVFNAYIQANLGYILIASQLIFFNLIGLSKGLISSAFILISAIYGLYVFIKLYQLTFKQTLYAFFRYAGYIILAFITLMILSIGVGILYAMTIKTS
>NZ_CP009239.1|WP_038504760.1|640694_641459_+|class-I-SAM-dependent-methyltransferase
MKKLFKTILNTIPRPLLIKLSYVSRPILTFFMRGKTYVDPIDGKGFKKFLPYGYEKQRDNVLSPSTLSLERHRLLWLYLQSETDFFTADLKVLHFAPEQAFYKRFRKMKNLEYTTTDLESPLADVKADICNLPFKDNSYDVILCNHVLEHIPDDTKAMQEMYRVLKPGGWGVFQIPQDLSRENTFEDDTITDKKERARIFGQYDHVRIYGKDYFAKLRKIGFTVEEVNYTKKLPPQDVKKYCLAQGEIIPVVKK

Crispr_ID: NZ_CP009239_6

• CRISPR_ID: NZ_CP009239_6
• CRISPR_location: 2639189-2639292
• CRISPR_type: Unclear
• Repeat_type: NA
• Spacer_info: 1 spacers
• Cas_protein_info: cas3

Consensus repeat of NZ_CP009239_6

Consensus_repeat	Method
GTTGGTAAATCTGGTTGGTGAATAAA	CRISPRCasFinder

spacers of NZ_CP009239_6

>6.1|2639215|52|NZ_CP009239|CRISPRCasFinder
AACATTGTCGTTATAGTATTTACAATAGTTGACAAGATGAAAAAAATAACAG

CRISPR arrays and Neighbor proteins around NZ_CP009239_6

CRISPR arrays

The CRISPR arrays of NZ_CP009239_6

>merge|NZ_CP009239|6|2639189-2639292|CRISPRCasFinder
GTTGGTAAATCTGGTTGGTGAATAAAAACATTGTCGTTATAGTATTTACAATAGTTGACAAGATGAAAAAAATAACAGGTTGGTAAATCTGGTTAGTGAATAAA

>NZ_CP009239|6|6|2639189-2639292|CRISPRCasFinder
GTTGGTAAATCTGGTTGGTGAATAAA	AACATTGTCGTTATAGTATTTACAATAGTTGACAAGATGAAAAAAATAACAG
GTTGGTAAATCTGGTTAGTGAATAAA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein	unknown	unknown	gnl|CDD|225876
NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|378935
NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase	unknown	unknown	gnl|CDD|223288
NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter	unknown	unknown	gnl|CDD|223604
NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein	unknown	unknown	gnl|CDD|378161
NZ_CP009239.1|WP_013621954.1|2652742_2652895_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl|CDD|238045
NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein	unknown	unknown	gnl|CDD|275263
NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase	unknown	unknown	gnl|CDD|177922
NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase	unknown	unknown	gnl|CDD|223288
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	cas3	cd09710_cas3_CAS-I-D	gnl|CDD|350681
NZ_CP009239.1|WP_038506331.1|2637501_2638896_+|ArsR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|225420
NZ_CP009239.1|WP_038506323.1|2625366_2625744_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase	unknown	unknown	gnl|CDD|271185
NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase	unknown	unknown	gnl|CDD|235028
NZ_CP009239.1|WP_038506321.1|2624360_2625377_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein	unknown	unknown	gnl|CDD|274377
NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase	unknown	unknown	gnl|CDD|350769
NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein	unknown	unknown	gnl|CDD|236153
NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein	unknown	unknown	gnl|CDD|377831

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	cas3	cd09710_cas3_CAS-I-D	1.4e-15	51.8	0.0

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein	gnl|CDD|225876	COG3339, COG3339, Uncharacterized conserved protein [Function unknown].	0.000217355
NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase	gnl|CDD|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	7.51867e-95
NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase	gnl|CDD|223288	COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].	3.71348e-15
NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter	gnl|CDD|223604	COG0530, ECM27, Ca2+/Na+ antiporter [Inorganic ion transport and metabolism].	8.97616e-61
NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein	gnl|CDD|378161	pfam09357, RteC, RteC protein. Human colonic Bacteroides species harbor a family of large conjugative transposons, called tetracycline resistance (Tcr) elements. Activities of these elements are enhanced by pregrowth of bacteria in medium containing tetracycline, indicating that at least some Tcr element genes are regulated by tetracycline. An insertional disruption in the rteC gene abolished self-transfer of the Tcr element to Bacteroides recipients, indicating that the gene was essential for self-transfer.	1.28167e-85
NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator	gnl|CDD|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	8.75739e-08
NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein	gnl|CDD|275263	TIGR04470, hypothetical_protein_ALIPUT_00462, radical SAM mobile pair protein B. Members of this family are the downstream member (B) of a pair of tandem-encoded radical SAM enzymes. Most of these radical SAM gene pairs have an additional upstream regulatory gene in the MarR family. Examples of high sequence identity (over 96 percent) from cassettes in several Treponema species of the oral cavity to those in multiple Firmicutes in the gut microbiome suggest recent lateral gene transfer, as might be expected for antibiotic resistance genes. The function is unknown.	3.53888e-25
NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase	gnl|CDD|177922	PLN02284, PLN02284, glutamine synthetase.	2.17817e-132
NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase	gnl|CDD|223288	COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].	1.10534e-15
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	gnl|CDD|350681	cd17923, DEXHc_Hrq1-like, DEAH-box helicase domain of Hrq1 and similar proteins. Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	6.00052e-55
NZ_CP009239.1|WP_038506331.1|2637501_2638896_+|ArsR-family-transcriptional-regulator	gnl|CDD|225420	COG2865, COG2865, Predicted transcriptional regulator containing an HTH domain and an uncharacterized domain shared with the mammalian protein Schlafen [Transcription].	6.75232e-100
NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein	gnl|CDD|236153	PRK08116, PRK08116, hypothetical protein; Validated.	3.54437e-06
NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase	gnl|CDD|271185	cd01185, INTN1_C_like, Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain. IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. 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.	7.82123e-57
NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein	gnl|CDD|274377	TIGR02987, m6_adenine_and_m5_cytosine_DNA_methyltransferase, type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family. Members of this family are the m6-adenine DNA methyltransferase protein, or domain of a fusion protein that also carries m5 cytosine methyltransferase activity, of type II restriction systems of the Alw26I/Eco31I/Esp3I family. A methyltransferase of this family is alway accompanied by a type II restriction endonuclease from the Alw26I/Eco31I/Esp3I family (TIGR02986) and by an adenine-specific modification methyltransferase. Members of this family are unusual in that regions of similarity to homologs outside this family are circularly permuted. [DNA metabolism, Restriction/modification].	0.00243691
NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase	gnl|CDD|350769	cd18011, DEXDc_RapA, DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	1.4507e-50
NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|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.	2.18442e-09
NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein	gnl|CDD|377831	pfam07411, DUF1508, Domain of unknown function (DUF1508). This family represents a series of bacterial domains of unknown function of around 50 residues in length. Members of this family are often found as tandem repeats and in some cases represent the whole protein. All member proteins are described as being hypothetical.	2.66547e-20

Protein sequences

>NZ_CP009239.1|WP_038506331.1|2637501_2638896_+|ArsR-family-transcriptional-regulator
MITDKDIKSIAASGEGYNAEFKVRLPKKIKEVTEEICAFANASGGTLLLGVDDDNVIQGCTIDNAKRSAIQNSIREIKPSLNCDIYAVDVDGKEVWVIEVPSGTQKPYALSGAIYVRIGPNSQKVTEIEEMRDFFQQADRIYFDETPCPAFDIATGIHTDNLNEFKAEAGLSSTVPNEQIFKNLKLQDQKNAFKNGAVLFFGKEPQQYIDTALIRCVAFDGKDKRYIVDDKKFTGPLYVQYKEAIQWLKNKLDVRYAIEGSTGPREEIWEIPQTAFKEVIVNALAHRDYYDRGATITIELFDDRVEIANPGGLVSAVSSKDFGKRSHSRNPLVFGLFARMRMVEQIGSGIGRIKDLMKENDLQPPHFSFDGMFTVTLRRPFDFEKWISRWEKHLTKTRITILRAVHNNPKMTKTVIADLASIGSTALDNNIEHLKDLGLLDRVGTKGGRWILNYINPEVGESGW
>NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein
MIEFLENIGDYFSQHFFDEDFPKKVFDKSGYGADHIKEFTSKISPLSEKYYKFKNDYLSLRRTKDKVKRVHDFHTELLQALGYINGVRAYDEPVVMDDKKIIPVRYRFNKNDKPYLYIMEMQPMIQVGDVDADGLYEQSYIKDDWEKVLPNSWDGYDIRPEVIKEALSELFLLPEEERPVYLIMLAGPKIFLIQYEKWKFDSYLLFDLEELFTVTKTASNKNLLALFYALLAKKQFISETESVLVGLEEDAHKASYGVTVTLKSAVIYAVEALANEAIYYKSSQAKTLEAKKEIVTLLDNDNFARELKDECLEMVYRLLFLFYAESRADLEILPIKDSTYQKGYSLEMLRDLEMVPLTTDSSRNGYFFSESLWKLFDFLHTGSDLKDGFQMRPLDSPLFDNASLKQLKGIQFRNKILQEIVVRLSLSERTKNKGRGRISYANLGINQLGSVYESLLSYSGFFAREDLIEVKNAKDKNGTDGTFLVPKTRRDDFKETEILKDPEHPEQDVIIPKGHFVYRLNGRDRKNSASYYTPEVLTQTTVKYTLKGIIERLKAQQAIVDGVLTGEACADEILKLKILEPAMGAAAFHNEVINQLAVAYLELKENEEQAAGRKRITPGDYKDELQKVKAYIAANNVYGVDLNPTAVELGKLSLWLNCMHKNMETPFFAHRLGAGNAVVGAWLKVYNDKDCLEEFPVLANGKIGKKPIPKPWWDKAPKRVMWNKRGTLSRKRNQIYHFLLPDDNMVPSYGIKLLKNELTEVEQKAFKDWRSDFKKPLTRVELNRLQKISSVIDYLLEEHYKQQMGMVKDTASVYQVYGQPNPQTTTKAYNEKERLTDARKDRNAPYFKLKMILDYWCSLWFWDVRDIRLLPNRTEWYNEVESILQIDTNELLADGTPQDIKEQIRKKARAGTLFDTSDRIEKIEQLALQHRFFHNELEFIEVFYERGGFDVIVGNPPWISIGFDESGILSEYFPEVEIRRYNASKVKKMVLEKLNGNQHLEDVLFNESIAATSTQEFMGASQNYKLLSGQKNNLYKCVLSNSIEVLNLDGFAGLVHPEGIYDDPRGRNLRKDLFQRLVYHFQFKNELMLFSEIDHHNYFGINIYSGEKSSISFFNINNLFHPSTIDLSFQHSGVGLPSGIKSYDENENKLVWNILPHKSRIVEIDILSLMTLSTLFENSDKWQSAKLVSIHTREILSVLRKLADFEGKVADEKHKIVIGYDQAQAVKDGLLVQCTKYPKIDDYELILSGPHFFVANPFYKTPREICTLNSHYDVIDLLEAKESAQRTNFIPSVIKNKKREEDQFSKENKWLNSYKIAFSRMMSLTGERTMQCAILPPKVAHINSINSITFEKDERLLELSALASSIVLDFYMKSLGSGNLKDSMMKNLPLKVPVKYQKHLSLRTLILNCLSDNYKDLWERNWNDDFKKDTWSKEDARLKPFKELTEEWIWETPLRNWFERRQALVEIDVITAMALGLSLEELILMYNVQFPVLQQNEDDTWYDTTGNIVFTVSKGLVGVGLDRGDWNSIKDLKAGETYEHTITKSELYQGKTVTYHAPFTKCDRVEDYKTAWAHFESIFKTKEAVV
>NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase
MNNDTLTQQTKKVTPGIRISLRGEDFIVTNRERDIIDVEGISELVYGQSFKFDLRLEKNYKVIKPEETELKADTSAHYRQTKLFLETTFRNSSHYSEHIEIAHKAAIRGANYQFESTIKALKLPQPKILIADAVGLGKTVQVGIFLAELIRRGKGKKVLVVTPKSILAQFQQEIWARFAIPLVRLDSQGIAKIKIEIPSNKNPFDYYDKVIVSIDTLKNNAKFRHYLERVKWDVVAIDECHTVANVASQRGGLAKFLSERTEAMVLTSATPHNGKRENFANLIGMLDPTAIPFNGEFTKEAIQPLYVRRFKKDVEDEVGDAFRDRVTSKIDCPLNQDEEEALRIIQEFKKVAQEDSDGDHNFGALLFSIGLFKAYMSSPKACLETVIKRIEKNVDEEGVIEHLEELRDVLQKIVDEKSDSKYNQLKFKLDQMGWKGKKNDERIIIFAERRATLNELEKNLTEDFGLNPKAVVQFNGSLTDTQQQDILEDFSKEDSEIRLFLASDAGSQGVNLHYFCNQMFNYDIPWSIITLDQRNGRIDRFGQKQTPYIYYLISDSKSEDVQGDIRIVEKLKEKEEEVHKSLGDAGSVMGFYDQQQETKLVEKAIATGDDSLLDTKNKDAVDDDWLSSLMEDTATTKEEIKKDEGFASFYPDDFTYYATLIDELKAEDERLIPRITIDRADKVIEIEQFEELSSKGVLYDMPKEAFPQKNETFNLTTDSGIVERSIIRARKKQNEWPNFQLLYDLNPIAKWMQYKLLAQVDRGKALVARLREPLPKNTAWFVFQGITSNQQGKPMFSKTFVIGKSFDGASVGNLETFNEFLNQFRLNDRLTELETTNEQLDKIKSLLPEAVKRGEQLYKYTLQGGLEDELEDRLESYQEKLESWLTASEAQMELKFGDETSGSFHKKKRQREVNYVKEQMDEFYNEFFQLENEPFLRVLAVFFNA
>NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator
MIGERIRTLREANDILLRQLAAKLDMDQALLSKMERGERSFRKEDIDALAKIFKQSKKELLTLWLADKILKTVGSEKFSKEALRLAIENV
>NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein
MDQLNLFSEEEVKREKLGKTAIEYKAASSILTPASGFMADYDYTLNPYSGCSFGCTYCYAAFFSRNKEKMDGWGDWLTVKENALSLLKKKRKRPLIDKTIYLSSVTDPYQPVEKELELTRSILKELLDFHKVRLVIQTRSALVTRDIDLLQKYETLQVNMTVTTDSEKVRKVFEPFCTGNKQRIKAITEMHNAGIQSCITMTPLLPIENPVQFADDLLATGIKRFIIQPFHKDKGKFVRGTRNEALKILNEFNWSDEEYNRVLTVMREKIPNLGIGKTGFAPI
>NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase
MYNNYLDWLENQRSILDELFARAGFTFYEKHKHLDNFSFDANETQKECYLLGTDRDLCYDRFTIGLSYSLWYQGKRTNAFISYFAKLLYEAREENEITLLDLGAGTGAVQLAISLCKIGLDQLFGKSPKITIINIDTSPFMLDYNRSYLWPEFIKSYEIAKDIKTIYSVNSWEQTDTSNFNNFWITASYLFDQSDNVQHLSDNLSKLVETFEPRFIICNTSKRKSYLMNKASVPIKNQNYEVLSIDMKHLFTGSLPSTLAVRRKIKEECGVQYNGMPVWRENWMSSIILRLATPGLSIPIESPSVDLFTPPLTVRRDIILSPEQKKAAEDDGRPTVIYGPAGCGKTVVITERIINILKNSSEKPIEEISILVTTFNKGLVSVIKSWLKELLSREKFKFIDRGDSLRVGESTKDTITIMHFDVLPTRLWSKISDAPTPFKNDKIQFDNYHLSVAARAINTIKKKYGITTNVYDHVLNDRYVIDEYHYVIYGQDIAEASIYAKARIKGRKRLERDGNSRKYLFESVVLYLELLGLNSSFVKRRHQFYKELKKSNKSFGFSHLIVDEFQDCTQTDYNIFYELLKNPNNLIICGDFAQAIHLGNVANIPRLSQEDMGRRKFIQLVGSYRLPYRISECLQNFSKNIVTEEDDIKNPLSPFKGAPPGARPILIKASNSKEMALKIKNAVSSYHQYDIFNFNVVPYDNILILEKDAELRNELALFRRGLSYDETILKVKGLEKKCVVWTARKNIEFSERIRHYVYTILTRTSGILIIALFGEECKEYKDIINEFDPERVIIWDQDTKNYLDENYKL
>NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein
MKTTSFKKFKFEDLLLNNTRDYQNKHSELIRSAPYIYQLLTSLLDVTDLSVANRSKIFTSIGYFLVPKDLYSEDEHGAIGYIDDILLAIFVIKEVETEIGFEQIERLYNQDLNNLDELLNSGIYDNAIKDYDELFQEVLEFVGFY
>NZ_CP009239.1|WP_038506323.1|2625366_2625744_-|hypothetical-protein
MEDKKSEQNILEKAINYISKLSSSKKEKLMTILKQVNKVQSSNLTTKEKAKEIKRIMWSDQSTNSKLFIGAFLGAVTGLFIFGTGGIGIVALGTGVGVWVWLATAAGGAFISSLIQNYEKKENED
>NZ_CP009239.1|WP_038506321.1|2624360_2625377_-|hypothetical-protein
MKINSINEITQAIKNFDIAALKELLDDNKPYQDVPKSLFLEKLEKKFNQARRDDCHSFDDVFFGICGSCNKGCEGMTFLSNSGHYLDLFIESKDGEFANDIYVCNKLTNFTDLEKSIDLGFSFRKDEYYNFKPTSKYLIIKKKYNELLNQISEIEKPIKVDKLLNWYYNNFNYLSETINGFGPFECFDYNLYNDAYSLVSKVERVFEITQVKEQAIESLVDYHNCSTERERLIWFFKNQENLYGSIYFEFSEKWKTDSIIFYEQEQVELELDITGYEYVIDYFLILDNLYDELIEKYKPIPVHFEGSKNGSIECSLENYLRLHNKYIDVVKKYGRKGY
>NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein
MSKFEVYQDARSEYRFRLKADNGQKILASEGYSAKAGCMNGIESVRKNSQDDKRYERLKASNGKHYFNLKASNGQVIGTSEMYESSSGMENGIASVTSNAPKATIEEV
>NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase
MLPLLQANEIKQAVVDYLRSTFNFEDPLLDQSFEDFLLSEQKGMFKGPYMQLRLPFDKIATDGDRDAFAKALYVKPPFDPYHHQFLSFLKLSTRNGHKPEPVILTTGTGSGKTESFLFPLLDYCYQHRDKPGIKAIILYPMNALATDQARRIAEEINDFNDGELKGKIRAGLFIGEGKDKDGIRATRMSEDRIIEDRKTLVDAPPDILLTNFKMLDFALLQARFHNLWSHNFKNTDLLKFIVLDELHTYDGAKGSDVANLIRRLKLKLKLSKDQIVPVGTSATMGGGDQGKLELVDFFSKVFGVKVTTDAVIEEQRLEPDEFFDDDIEEPVIDVNQIQKCAFEENDTYDSYLERQLVFWGYAGLSPKDLGDALKKNKWFFDLLKITKSDVVEIKPKLKRWREKIGLELDDKEIHLLFGSLLALITYAKEQSGSKQFPFLYLQITYWLRSLSKIVRKLQPTAAFEWESDMNPNDPVKSLPPYFCRECGGSGWIGVKKEQNAHFEDDLSRTRQQLMAHSQNKNLYFISSLEDRKYQEVYASDYTHSGDAIDGYLHPHSLSIYDNYESNDYFKILGTRIVDGNRIDKICPHCNSRNTLALIGTGVPTLESIATAQVLATATDPTKDGQRKLLAFTNGVQDAAHQAGFIENRNFRFGMRHAIQAVLKDVKEPITLPQVYERFIEHWKEHSDDEETGNLDAYYYKFFPPDCEARLEISDYRNKDGKLSSVFDKEFSNRISWEIWSEFSYSAMIGRTLEKTGASATYFDTAVMSEVYDQMKYWLDENKLGTAIDKEPFLKFLNGFLHRLRTKGGVDHKYLKKYRTERTNSYLIGHRGNVNKQYFLMKNFGPSSRLPKFLALASGANTRAFDVVQTTTKDNWFSAYFKKCFQEIIQEETVLINDFYAQLLDYLDANKILDKRVAAGITNYGLSENSIYLSPNVVHYECSHCGNQINTGEAQASLVSGMKCLQYRCKGQYEAAENTQLDYYRMVYNRGRSLRIFAKDHTGLIDRNEREKLEYDFKRQPKQDSTNVLVATSTLEMGIDIGDLNVTFNSSLPPETANYLQRIGRAGRSSGTSMILNLAGRDAHDLYYFQDPQDMMSGQIKTPSCYLEAKDILKRHFMAFCFDHWASMDPEENNIPPMVRVLRLKSLKPGDPNFLFQKIATHIENNKTLLYDLFVEQYKEQLGDNSKSLASIFEDLSSGRFINRLTCLHKNLLDEIEYYQGKIKLVNKRLKALPETGNETVILKNEKRALSSAIYNINRRNVIEYLTNVGVLPNYAFPETGVTLNAQIKRKKEVDGKTEYKYEDFSEIVRPSSSALTELAPANIFYSQGHKLKSEGLEIKSQEDYEEHRFCSNCNHVKKEIDVEENEQSQCPVCGHGSWSSLNNRKFLVKLQGVLSVNDKERSKITDSSDDRERHFYQKSVHIKINQSSSQGAHVLKRVPFGIEFFQDVDYLEINTGIREEGFFGTREIEINGEKHPQVGFVVCKTCGKSTERSLSARELNNRDRAYHFPYCSNREVLYDDQSDDVFNEIYLYRKFNTEALSILLPIEDFRSEERIALFKAGLQLGLKEYFKGRPDHILIRENEIFNKTTNRKDRYLVFYETIPGGTGYLSKLFDTTVFTKILEKAYERIAYCSCKQEGKDGCYRCIYTYGNQYERTILSRTEAEELFSNILEKTDEWNSIESLQNVSTFGNNEESDLEWKFKGLLEEFANKFSGSTFESDNEMGLKIYKLKLAYYGNEIVYKVYPQNLNRWLFGIEKKTRPDFVLKCVGLTKNGKKFTLDELETIKDIVIYLDGYEYHASENHSDRFPKDLEIRNSIINSGRYNQWVFTWSDFAESIFNDKDAIGLKQDEKFIVGKFFLKHSSFKEYDFRDVYYNNNATRFFQLLINPITVVDNKNWSSLAVFSFQSKMMGVSYSPESVDQIIETRSIKDIEKGSLKLTNYIHTDDLQLKDEASFGLFIRPEDFKLKGYGYYKAVPFWDKENWALFWRFYNLTQFHNIEVYSFDKEIKKEVSIIQGAVSEKTLLNFSEELHDIVKLFAKNGFDFNTDTDFDLMDNDVILASAELGSHDKKIVVSPFDSESEKIFITNGYQVFTPDNFKLEK
>NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase
MNNAIKLFIHDSFFDAFSVLPRKIQKKTREFMKKFKEDPKSSAINYEKINTFKDQSLRTVRIDQKYRAIIQAPEEGNGFHLLWVDNHDEAMDWAKNKVFEWNASTQSFQMYDRPKNQTKPVSTNVTVKDAASLYTSYSDDQLTSIGVPKDLIGLVKSIERVEHLESYASNLPSDVYEYLYYLSEGISLEDILEEIEAGKVSDDNTLSPNAQKNVYVLTDDAELENILSGDFEKWKLFLHPSQRSIAYGEFKGPLKVTGSAGTGKTVCALHRAKYLSQKLESFDKPILFTTFTKSLTQYLSTVTEKFSIPDSEIVISNIDKLIFELAREFKVIDESSGMINSSQELELWKEIIEFNPSTFDEKFLQDEYNDVILANSVKSVNEYYKTSRVGRSVRIGRQDKTQIWELCEEFIKSKESNYTKFELCNLLIAYFSSISEKPFSHIICDEIQDFSNLELSLLRVLVNEKEDDLFLVGDPFQNIYGRRINFSKSGIHIRGRRSRKLKVNYRTTEEIKKRAVSILLNTEYDDFDGEKETNTGYVSLMHGSDPTYKVFASPEAEDQYISEQIETLLLDDSVNPSDICIASRTNRLVDESKKLLNEIQQKFSDIKATIRSNDSIVVSTFHNLKGHEFKHLFVRGFSKDYVPFRHPGFDIYSDIQKKEYLKKEKSLYYVVFSRAIQTLIITGVGEKSDWIV
>NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein
MKQSETIFNPKAPHILIEGATQFELGSFNGKAINYDFPKILNYLDAKGKLCFGKNFKIYKEDHELLLELASYFIQDHEYCKKLNIDTKKGILLSGPVGCGKTTLMRLLPHLVPHKKTYNFIPCRNIVFGFNGIGFKMIEDYSDNKAYCFDDLGVEHIGRHYGKDCNVMGEILISRYEVFKQKDILTHITTNLNAVEIEERYGERVRSRMRSMFNLLSFDSNTKDKRG
>NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|helix-turn-helix-domain-containing-protein
MPTSILTTDDLYDFKLELLRELKKLLQDKAPTAIKKYLKSAEVMEMLQISPGTLQNLRINGTLPYTKIGGIILYEYEEILRILQENKVAS
>NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein
MNFKSNLCNTFPKSLNVTKKQIIKIEESNLRNLSVLNDGLNLSVQTLNKLRKNLRTKDNFFTQEEEISFFKYDKPFINGRIKFFSKVRRFIAEKPNASITKQIKYVHSTIDKLEKHKMRNLEFFQYTRQCNNTLDHIYFVRGKDNLDFPVDTSHYFTDPEFSTSHDNLAAQVIGYDLLSNYYDLELEYLNKKKENVIIEEVSPAILNGLSWTASKTDLVEIIYALHSAGAIRNGQAELSKMAEVCATLFDLNLNNFYKTYAEIKNREKDTTKFLDHLKRSLEKRIDLDNAK
>NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase
MRSTHTFSILFWADQKNAINGEVLIYARITVDKKRANISLKRRVPQNLWDPKKKKLRGNSHQAQSANQYLDQIYTQLFQIYQDLKFKGELITAQLIKAQYTGEADNKGKSLKNIFEYHSKKITNTLASGSIRNFGITENYVFKFLEQKRKTTDIYLNQLNFEFLSHFELFLSEVWPTGHPKALGNNTRMKHIQRLRKVVTLAYHLEWIDKDPFVRWKMTYDKTNREFLSEQELKKLENKVFISERLDRVRDLFVFSCYTGISYVDIMNLTPNHLVLGIDGGYWIMTKRQKTNTTVKVPLLGQALDIVNKYKDHPVTAVNNSLLPVLTNEKLNMFLKEVANFVGINKNLTFHMARHTFATTVTLSNGVPIETVSKLLGHSKIATTQIYARVLENKVSADMNALKNVLLNKSKDSTVAKNSKASS
>NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase
MNFKEYIRDVQDFPKQGIVFKDITPLLNNAEILEKTTDALLNLVKEQKIDKVVGMESRGFFFATLLATKLKAGFVPVRKKGKLPFNVLSKPYSLEYGEDALEIHTDAIKKGDKVLIHDDVLATGGTAKAVCELIEELGGEVVQCNFLIELDFLNGKDKIANYNVDSLLHY
>NZ_CP009239.1|WP_013621954.1|2652742_2652895_-|hypothetical-protein
MKKALFRFLAKINRLLLPSYSKKQLDLSKASKLQLAIIGWRYYVTTNAID
>NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter
MLNLVYIIIGLVFLIMGGNWLLKSSVALSLRLQIPKIVVGMTVVSFATSAPELIVSIKAALEGSPDLALGNVVGSNIANLGLVLGVIVMLGSIDVRKSFYTTDWPILMLASLVFFGFIYFDGVIKFYEGVIMVALLIVYIVYLIKFQKTAVEDEAPEDDVPLPTFKMLLFLALGGLGLWGGSELLVSGATGLARFYNVSERVIGVTVVSVGTSIPELAASIIAVIKKEKAISLGNLIGSNIFNIFAVLGITALITPLNVVDNTLLSNDILWMLGFAIILLPLVFFPKGLRLGWRDGIVLLSGYIAFVYFTI
>NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase
MSKSKLEYIWLDGYTPTANLRSKTKVEDDFSGKLEDCPIWSFDGSSTQQAEGGSSDCLLKPVAIYPDPARKDGYLVMTEVLNADGTPHLSNSRAGIDDEDNDFWFGFEQEYFIMDKNTQLPLGFPVGGYPGPQGMYYCSVGGKNTHGRDFVEEHADLCIAAGLNFEGINQEVASGQWEFQLFAKGAKKAGDEIWIARYLLDRLTEQYGYYIEYHPKPVKGDWNGSGMHANFSNTILRTCGSKETYEKICEAFRPVTKEHIAVYGEFNDQRLTGEHETAAITDFSYGISDRGASIRIPIITVEKGWKGWLEDRRPASNGDPYKIAGRIIKTVKSAKI

Crispr_ID: NZ_CP009239_5

• CRISPR_ID: NZ_CP009239_5
• CRISPR_location: 2638876-2639079
• CRISPR_type: Unclear
• Repeat_type: NA
• Spacer_info: 2 spacers
• Cas_protein_info: cas3

Consensus repeat of NZ_CP009239_5

Consensus_repeat	Method
GTTGGTAAATCTGGTTGGTGAATAAA	CRISPRCasFinder

spacers of NZ_CP009239_5

>5.1|2638902|63|NZ_CP009239|CRISPRCasFinder
TAGATTATAACCAAATCTTAAATTATTGATAATAAAATAGTTAATAAACAGACTATTTAAAAG
>5.2|2638991|62|NZ_CP009239|CRISPRCasFinder
TGAATTTGAATTGCTCATAAACCGCTGTAAACACTTTTTTTACGATTAATTAGGTTTTTTAG

CRISPR arrays and Neighbor proteins around NZ_CP009239_5

CRISPR arrays

The CRISPR arrays of NZ_CP009239_5

>merge|NZ_CP009239|5|2638876-2639079|CRISPRCasFinder
GTGGGTGAATCAGGTTGGTAAATAAATAGATTATAACCAAATCTTAAATTATTGATAATAAAATAGTTAATAAACAGACTATTTAAAAGGTTGGTGAATCAGGTGGGTAAATAAATGAATTTGAATTGCTCATAAACCGCTGTAAACACTTTTTTTACGATTAATTAGGTTTTTTAGGTGGGTAAATTGGGTGGGTGAATAATT

>NZ_CP009239|5|5|2638876-2639079|CRISPRCasFinder
GTGGGTGAATCAGGTTGGTAAATAAA	TAGATTATAACCAAATCTTAAATTATTGATAATAAAATAGTTAATAAACAGACTATTTAAAAG
GTTGGTGAATCAGGTGGGTAAATAAA	TGAATTTGAATTGCTCATAAACCGCTGTAAACACTTTTTTTACGATTAATTAGGTTTTTTAG
GTGGGTAAATTGGGTGGGTGAATAATT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein	unknown	unknown	gnl|CDD|225876
NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|378935
NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase	unknown	unknown	gnl|CDD|223288
NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter	unknown	unknown	gnl|CDD|223604
NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein	unknown	unknown	gnl|CDD|378161
NZ_CP009239.1|WP_013621954.1|2652742_2652895_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl|CDD|238045
NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein	unknown	unknown	gnl|CDD|275263
NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase	unknown	unknown	gnl|CDD|177922
NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase	unknown	unknown	gnl|CDD|223288
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	cas3	cd09710_cas3_CAS-I-D	gnl|CDD|350681
NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase	unknown	unknown	gnl|CDD|271185
NZ_CP009239.1|WP_038506323.1|2625366_2625744_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase	unknown	unknown	gnl|CDD|235028
NZ_CP009239.1|WP_038506321.1|2624360_2625377_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein	unknown	unknown	gnl|CDD|274377
NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase	unknown	unknown	gnl|CDD|350769
NZ_CP009239.1|WP_013621935.1|2622224_2622482_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein	unknown	unknown	gnl|CDD|236153
NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein	unknown	unknown	gnl|CDD|377831

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	cas3	cd09710_cas3_CAS-I-D	1.4e-15	51.8	0.0

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein	gnl|CDD|225876	COG3339, COG3339, Uncharacterized conserved protein [Function unknown].	0.000217355
NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase	gnl|CDD|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	7.51867e-95
NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase	gnl|CDD|223288	COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].	3.71348e-15
NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter	gnl|CDD|223604	COG0530, ECM27, Ca2+/Na+ antiporter [Inorganic ion transport and metabolism].	8.97616e-61
NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein	gnl|CDD|378161	pfam09357, RteC, RteC protein. Human colonic Bacteroides species harbor a family of large conjugative transposons, called tetracycline resistance (Tcr) elements. Activities of these elements are enhanced by pregrowth of bacteria in medium containing tetracycline, indicating that at least some Tcr element genes are regulated by tetracycline. An insertional disruption in the rteC gene abolished self-transfer of the Tcr element to Bacteroides recipients, indicating that the gene was essential for self-transfer.	1.28167e-85
NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator	gnl|CDD|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	8.75739e-08
NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein	gnl|CDD|275263	TIGR04470, hypothetical_protein_ALIPUT_00462, radical SAM mobile pair protein B. Members of this family are the downstream member (B) of a pair of tandem-encoded radical SAM enzymes. Most of these radical SAM gene pairs have an additional upstream regulatory gene in the MarR family. Examples of high sequence identity (over 96 percent) from cassettes in several Treponema species of the oral cavity to those in multiple Firmicutes in the gut microbiome suggest recent lateral gene transfer, as might be expected for antibiotic resistance genes. The function is unknown.	3.53888e-25
NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase	gnl|CDD|177922	PLN02284, PLN02284, glutamine synthetase.	2.17817e-132
NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase	gnl|CDD|223288	COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].	1.10534e-15
NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase	gnl|CDD|350681	cd17923, DEXHc_Hrq1-like, DEAH-box helicase domain of Hrq1 and similar proteins. Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	6.00052e-55
NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase	gnl|CDD|271185	cd01185, INTN1_C_like, Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain. IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. 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.	7.82123e-57
NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein	gnl|CDD|236153	PRK08116, PRK08116, hypothetical protein; Validated.	3.54437e-06
NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein	gnl|CDD|274377	TIGR02987, m6_adenine_and_m5_cytosine_DNA_methyltransferase, type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family. Members of this family are the m6-adenine DNA methyltransferase protein, or domain of a fusion protein that also carries m5 cytosine methyltransferase activity, of type II restriction systems of the Alw26I/Eco31I/Esp3I family. A methyltransferase of this family is alway accompanied by a type II restriction endonuclease from the Alw26I/Eco31I/Esp3I family (TIGR02986) and by an adenine-specific modification methyltransferase. Members of this family are unusual in that regions of similarity to homologs outside this family are circularly permuted. [DNA metabolism, Restriction/modification].	0.00243691
NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase	gnl|CDD|350769	cd18011, DEXDc_RapA, DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	1.4507e-50
NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|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.	2.18442e-09
NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein	gnl|CDD|377831	pfam07411, DUF1508, Domain of unknown function (DUF1508). This family represents a series of bacterial domains of unknown function of around 50 residues in length. Members of this family are often found as tandem repeats and in some cases represent the whole protein. All member proteins are described as being hypothetical.	2.66547e-20

Protein sequences

>NZ_CP009239.1|WP_038506329.1|2632744_2637505_+|hypothetical-protein
MIEFLENIGDYFSQHFFDEDFPKKVFDKSGYGADHIKEFTSKISPLSEKYYKFKNDYLSLRRTKDKVKRVHDFHTELLQALGYINGVRAYDEPVVMDDKKIIPVRYRFNKNDKPYLYIMEMQPMIQVGDVDADGLYEQSYIKDDWEKVLPNSWDGYDIRPEVIKEALSELFLLPEEERPVYLIMLAGPKIFLIQYEKWKFDSYLLFDLEELFTVTKTASNKNLLALFYALLAKKQFISETESVLVGLEEDAHKASYGVTVTLKSAVIYAVEALANEAIYYKSSQAKTLEAKKEIVTLLDNDNFARELKDECLEMVYRLLFLFYAESRADLEILPIKDSTYQKGYSLEMLRDLEMVPLTTDSSRNGYFFSESLWKLFDFLHTGSDLKDGFQMRPLDSPLFDNASLKQLKGIQFRNKILQEIVVRLSLSERTKNKGRGRISYANLGINQLGSVYESLLSYSGFFAREDLIEVKNAKDKNGTDGTFLVPKTRRDDFKETEILKDPEHPEQDVIIPKGHFVYRLNGRDRKNSASYYTPEVLTQTTVKYTLKGIIERLKAQQAIVDGVLTGEACADEILKLKILEPAMGAAAFHNEVINQLAVAYLELKENEEQAAGRKRITPGDYKDELQKVKAYIAANNVYGVDLNPTAVELGKLSLWLNCMHKNMETPFFAHRLGAGNAVVGAWLKVYNDKDCLEEFPVLANGKIGKKPIPKPWWDKAPKRVMWNKRGTLSRKRNQIYHFLLPDDNMVPSYGIKLLKNELTEVEQKAFKDWRSDFKKPLTRVELNRLQKISSVIDYLLEEHYKQQMGMVKDTASVYQVYGQPNPQTTTKAYNEKERLTDARKDRNAPYFKLKMILDYWCSLWFWDVRDIRLLPNRTEWYNEVESILQIDTNELLADGTPQDIKEQIRKKARAGTLFDTSDRIEKIEQLALQHRFFHNELEFIEVFYERGGFDVIVGNPPWISIGFDESGILSEYFPEVEIRRYNASKVKKMVLEKLNGNQHLEDVLFNESIAATSTQEFMGASQNYKLLSGQKNNLYKCVLSNSIEVLNLDGFAGLVHPEGIYDDPRGRNLRKDLFQRLVYHFQFKNELMLFSEIDHHNYFGINIYSGEKSSISFFNINNLFHPSTIDLSFQHSGVGLPSGIKSYDENENKLVWNILPHKSRIVEIDILSLMTLSTLFENSDKWQSAKLVSIHTREILSVLRKLADFEGKVADEKHKIVIGYDQAQAVKDGLLVQCTKYPKIDDYELILSGPHFFVANPFYKTPREICTLNSHYDVIDLLEAKESAQRTNFIPSVIKNKKREEDQFSKENKWLNSYKIAFSRMMSLTGERTMQCAILPPKVAHINSINSITFEKDERLLELSALASSIVLDFYMKSLGSGNLKDSMMKNLPLKVPVKYQKHLSLRTLILNCLSDNYKDLWERNWNDDFKKDTWSKEDARLKPFKELTEEWIWETPLRNWFERRQALVEIDVITAMALGLSLEELILMYNVQFPVLQQNEDDTWYDTTGNIVFTVSKGLVGVGLDRGDWNSIKDLKAGETYEHTITKSELYQGKTVTYHAPFTKCDRVEDYKTAWAHFESIFKTKEAVV
>NZ_CP009239.1|WP_051983485.1|2629900_2632738_+|DEAD/DEAH-box-helicase
MNNDTLTQQTKKVTPGIRISLRGEDFIVTNRERDIIDVEGISELVYGQSFKFDLRLEKNYKVIKPEETELKADTSAHYRQTKLFLETTFRNSSHYSEHIEIAHKAAIRGANYQFESTIKALKLPQPKILIADAVGLGKTVQVGIFLAELIRRGKGKKVLVVTPKSILAQFQQEIWARFAIPLVRLDSQGIAKIKIEIPSNKNPFDYYDKVIVSIDTLKNNAKFRHYLERVKWDVVAIDECHTVANVASQRGGLAKFLSERTEAMVLTSATPHNGKRENFANLIGMLDPTAIPFNGEFTKEAIQPLYVRRFKKDVEDEVGDAFRDRVTSKIDCPLNQDEEEALRIIQEFKKVAQEDSDGDHNFGALLFSIGLFKAYMSSPKACLETVIKRIEKNVDEEGVIEHLEELRDVLQKIVDEKSDSKYNQLKFKLDQMGWKGKKNDERIIIFAERRATLNELEKNLTEDFGLNPKAVVQFNGSLTDTQQQDILEDFSKEDSEIRLFLASDAGSQGVNLHYFCNQMFNYDIPWSIITLDQRNGRIDRFGQKQTPYIYYLISDSKSEDVQGDIRIVEKLKEKEEEVHKSLGDAGSVMGFYDQQQETKLVEKAIATGDDSLLDTKNKDAVDDDWLSSLMEDTATTKEEIKKDEGFASFYPDDFTYYATLIDELKAEDERLIPRITIDRADKVIEIEQFEELSSKGVLYDMPKEAFPQKNETFNLTTDSGIVERSIIRARKKQNEWPNFQLLYDLNPIAKWMQYKLLAQVDRGKALVARLREPLPKNTAWFVFQGITSNQQGKPMFSKTFVIGKSFDGASVGNLETFNEFLNQFRLNDRLTELETTNEQLDKIKSLLPEAVKRGEQLYKYTLQGGLEDELEDRLESYQEKLESWLTASEAQMELKFGDETSGSFHKKKRQREVNYVKEQMDEFYNEFFQLENEPFLRVLAVFFNA
>NZ_CP009239.1|WP_013621942.1|2629609_2629882_+|helix-turn-helix-transcriptional-regulator
MIGERIRTLREANDILLRQLAAKLDMDQALLSKMERGERSFRKEDIDALAKIFKQSKKELLTLWLADKILKTVGSEKFSKEALRLAIENV
>NZ_CP009239.1|WP_038506326.1|2628603_2629455_-|radical-SAM-protein
MDQLNLFSEEEVKREKLGKTAIEYKAASSILTPASGFMADYDYTLNPYSGCSFGCTYCYAAFFSRNKEKMDGWGDWLTVKENALSLLKKKRKRPLIDKTIYLSSVTDPYQPVEKELELTRSILKELLDFHKVRLVIQTRSALVTRDIDLLQKYETLQVNMTVTTDSEKVRKVFEPFCTGNKQRIKAITEMHNAGIQSCITMTPLLPIENPVQFADDLLATGIKRFIIQPFHKDKGKFVRGTRNEALKILNEFNWSDEEYNRVLTVMREKIPNLGIGKTGFAPI
>NZ_CP009239.1|WP_038506325.1|2626172_2628602_-|ATP-dependent-helicase
MYNNYLDWLENQRSILDELFARAGFTFYEKHKHLDNFSFDANETQKECYLLGTDRDLCYDRFTIGLSYSLWYQGKRTNAFISYFAKLLYEAREENEITLLDLGAGTGAVQLAISLCKIGLDQLFGKSPKITIINIDTSPFMLDYNRSYLWPEFIKSYEIAKDIKTIYSVNSWEQTDTSNFNNFWITASYLFDQSDNVQHLSDNLSKLVETFEPRFIICNTSKRKSYLMNKASVPIKNQNYEVLSIDMKHLFTGSLPSTLAVRRKIKEECGVQYNGMPVWRENWMSSIILRLATPGLSIPIESPSVDLFTPPLTVRRDIILSPEQKKAAEDDGRPTVIYGPAGCGKTVVITERIINILKNSSEKPIEEISILVTTFNKGLVSVIKSWLKELLSREKFKFIDRGDSLRVGESTKDTITIMHFDVLPTRLWSKISDAPTPFKNDKIQFDNYHLSVAARAINTIKKKYGITTNVYDHVLNDRYVIDEYHYVIYGQDIAEASIYAKARIKGRKRLERDGNSRKYLFESVVLYLELLGLNSSFVKRRHQFYKELKKSNKSFGFSHLIVDEFQDCTQTDYNIFYELLKNPNNLIICGDFAQAIHLGNVANIPRLSQEDMGRRKFIQLVGSYRLPYRISECLQNFSKNIVTEEDDIKNPLSPFKGAPPGARPILIKASNSKEMALKIKNAVSSYHQYDIFNFNVVPYDNILILEKDAELRNELALFRRGLSYDETILKVKGLEKKCVVWTARKNIEFSERIRHYVYTILTRTSGILIIALFGEECKEYKDIINEFDPERVIIWDQDTKNYLDENYKL
>NZ_CP009239.1|WP_013621939.1|2625754_2626192_-|DUF1232-domain-containing-protein
MKTTSFKKFKFEDLLLNNTRDYQNKHSELIRSAPYIYQLLTSLLDVTDLSVANRSKIFTSIGYFLVPKDLYSEDEHGAIGYIDDILLAIFVIKEVETEIGFEQIERLYNQDLNNLDELLNSGIYDNAIKDYDELFQEVLEFVGFY
>NZ_CP009239.1|WP_038506323.1|2625366_2625744_-|hypothetical-protein
MEDKKSEQNILEKAINYISKLSSSKKEKLMTILKQVNKVQSSNLTTKEKAKEIKRIMWSDQSTNSKLFIGAFLGAVTGLFIFGTGGIGIVALGTGVGVWVWLATAAGGAFISSLIQNYEKKENED
>NZ_CP009239.1|WP_038506321.1|2624360_2625377_-|hypothetical-protein
MKINSINEITQAIKNFDIAALKELLDDNKPYQDVPKSLFLEKLEKKFNQARRDDCHSFDDVFFGICGSCNKGCEGMTFLSNSGHYLDLFIESKDGEFANDIYVCNKLTNFTDLEKSIDLGFSFRKDEYYNFKPTSKYLIIKKKYNELLNQISEIEKPIKVDKLLNWYYNNFNYLSETINGFGPFECFDYNLYNDAYSLVSKVERVFEITQVKEQAIESLVDYHNCSTERERLIWFFKNQENLYGSIYFEFSEKWKTDSIIFYEQEQVELELDITGYEYVIDYFLILDNLYDELIEKYKPIPVHFEGSKNGSIECSLENYLRLHNKYIDVVKKYGRKGY
>NZ_CP009239.1|WP_013621936.1|2623086_2623413_+|YegP-family-protein
MSKFEVYQDARSEYRFRLKADNGQKILASEGYSAKAGCMNGIESVRKNSQDDKRYERLKASNGKHYFNLKASNGQVIGTSEMYESSSGMENGIASVTSNAPKATIEEV
>NZ_CP009239.1|WP_013621935.1|2622224_2622482_+|hypothetical-protein
MNIVERYKKPTPKFFRTLRNIGIALATAGGAIIAAPISLPAVLVTVATYMTVAGTVATAVSQAVTIDEKTEIPKIDGKDSASNIK
>NZ_CP009239.1|WP_038506332.1|2639324_2645630_+|DEAD/DEAH-box-helicase
MLPLLQANEIKQAVVDYLRSTFNFEDPLLDQSFEDFLLSEQKGMFKGPYMQLRLPFDKIATDGDRDAFAKALYVKPPFDPYHHQFLSFLKLSTRNGHKPEPVILTTGTGSGKTESFLFPLLDYCYQHRDKPGIKAIILYPMNALATDQARRIAEEINDFNDGELKGKIRAGLFIGEGKDKDGIRATRMSEDRIIEDRKTLVDAPPDILLTNFKMLDFALLQARFHNLWSHNFKNTDLLKFIVLDELHTYDGAKGSDVANLIRRLKLKLKLSKDQIVPVGTSATMGGGDQGKLELVDFFSKVFGVKVTTDAVIEEQRLEPDEFFDDDIEEPVIDVNQIQKCAFEENDTYDSYLERQLVFWGYAGLSPKDLGDALKKNKWFFDLLKITKSDVVEIKPKLKRWREKIGLELDDKEIHLLFGSLLALITYAKEQSGSKQFPFLYLQITYWLRSLSKIVRKLQPTAAFEWESDMNPNDPVKSLPPYFCRECGGSGWIGVKKEQNAHFEDDLSRTRQQLMAHSQNKNLYFISSLEDRKYQEVYASDYTHSGDAIDGYLHPHSLSIYDNYESNDYFKILGTRIVDGNRIDKICPHCNSRNTLALIGTGVPTLESIATAQVLATATDPTKDGQRKLLAFTNGVQDAAHQAGFIENRNFRFGMRHAIQAVLKDVKEPITLPQVYERFIEHWKEHSDDEETGNLDAYYYKFFPPDCEARLEISDYRNKDGKLSSVFDKEFSNRISWEIWSEFSYSAMIGRTLEKTGASATYFDTAVMSEVYDQMKYWLDENKLGTAIDKEPFLKFLNGFLHRLRTKGGVDHKYLKKYRTERTNSYLIGHRGNVNKQYFLMKNFGPSSRLPKFLALASGANTRAFDVVQTTTKDNWFSAYFKKCFQEIIQEETVLINDFYAQLLDYLDANKILDKRVAAGITNYGLSENSIYLSPNVVHYECSHCGNQINTGEAQASLVSGMKCLQYRCKGQYEAAENTQLDYYRMVYNRGRSLRIFAKDHTGLIDRNEREKLEYDFKRQPKQDSTNVLVATSTLEMGIDIGDLNVTFNSSLPPETANYLQRIGRAGRSSGTSMILNLAGRDAHDLYYFQDPQDMMSGQIKTPSCYLEAKDILKRHFMAFCFDHWASMDPEENNIPPMVRVLRLKSLKPGDPNFLFQKIATHIENNKTLLYDLFVEQYKEQLGDNSKSLASIFEDLSSGRFINRLTCLHKNLLDEIEYYQGKIKLVNKRLKALPETGNETVILKNEKRALSSAIYNINRRNVIEYLTNVGVLPNYAFPETGVTLNAQIKRKKEVDGKTEYKYEDFSEIVRPSSSALTELAPANIFYSQGHKLKSEGLEIKSQEDYEEHRFCSNCNHVKKEIDVEENEQSQCPVCGHGSWSSLNNRKFLVKLQGVLSVNDKERSKITDSSDDRERHFYQKSVHIKINQSSSQGAHVLKRVPFGIEFFQDVDYLEINTGIREEGFFGTREIEINGEKHPQVGFVVCKTCGKSTERSLSARELNNRDRAYHFPYCSNREVLYDDQSDDVFNEIYLYRKFNTEALSILLPIEDFRSEERIALFKAGLQLGLKEYFKGRPDHILIRENEIFNKTTNRKDRYLVFYETIPGGTGYLSKLFDTTVFTKILEKAYERIAYCSCKQEGKDGCYRCIYTYGNQYERTILSRTEAEELFSNILEKTDEWNSIESLQNVSTFGNNEESDLEWKFKGLLEEFANKFSGSTFESDNEMGLKIYKLKLAYYGNEIVYKVYPQNLNRWLFGIEKKTRPDFVLKCVGLTKNGKKFTLDELETIKDIVIYLDGYEYHASENHSDRFPKDLEIRNSIINSGRYNQWVFTWSDFAESIFNDKDAIGLKQDEKFIVGKFFLKHSSFKEYDFRDVYYNNNATRFFQLLINPITVVDNKNWSSLAVFSFQSKMMGVSYSPESVDQIIETRSIKDIEKGSLKLTNYIHTDDLQLKDEASFGLFIRPEDFKLKGYGYYKAVPFWDKENWALFWRFYNLTQFHNIEVYSFDKEIKKEVSIIQGAVSEKTLLNFSEELHDIVKLFAKNGFDFNTDTDFDLMDNDVILASAELGSHDKKIVVSPFDSESEKIFITNGYQVFTPDNFKLEK
>NZ_CP009239.1|WP_013621947.1|2645631_2647710_+|AAA-family-ATPase
MNNAIKLFIHDSFFDAFSVLPRKIQKKTREFMKKFKEDPKSSAINYEKINTFKDQSLRTVRIDQKYRAIIQAPEEGNGFHLLWVDNHDEAMDWAKNKVFEWNASTQSFQMYDRPKNQTKPVSTNVTVKDAASLYTSYSDDQLTSIGVPKDLIGLVKSIERVEHLESYASNLPSDVYEYLYYLSEGISLEDILEEIEAGKVSDDNTLSPNAQKNVYVLTDDAELENILSGDFEKWKLFLHPSQRSIAYGEFKGPLKVTGSAGTGKTVCALHRAKYLSQKLESFDKPILFTTFTKSLTQYLSTVTEKFSIPDSEIVISNIDKLIFELAREFKVIDESSGMINSSQELELWKEIIEFNPSTFDEKFLQDEYNDVILANSVKSVNEYYKTSRVGRSVRIGRQDKTQIWELCEEFIKSKESNYTKFELCNLLIAYFSSISEKPFSHIICDEIQDFSNLELSLLRVLVNEKEDDLFLVGDPFQNIYGRRINFSKSGIHIRGRRSRKLKVNYRTTEEIKKRAVSILLNTEYDDFDGEKETNTGYVSLMHGSDPTYKVFASPEAEDQYISEQIETLLLDDSVNPSDICIASRTNRLVDESKKLLNEIQQKFSDIKATIRSNDSIVVSTFHNLKGHEFKHLFVRGFSKDYVPFRHPGFDIYSDIQKKEYLKKEKSLYYVVFSRAIQTLIITGVGEKSDWIV
>NZ_CP009239.1|WP_013621948.1|2647790_2648474_-|ATP-binding-protein
MKQSETIFNPKAPHILIEGATQFELGSFNGKAINYDFPKILNYLDAKGKLCFGKNFKIYKEDHELLLELASYFIQDHEYCKKLNIDTKKGILLSGPVGCGKTTLMRLLPHLVPHKKTYNFIPCRNIVFGFNGIGFKMIEDYSDNKAYCFDDLGVEHIGRHYGKDCNVMGEILISRYEVFKQKDILTHITTNLNAVEIEERYGERVRSRMRSMFNLLSFDSNTKDKRG
>NZ_CP009239.1|WP_013621950.1|2649177_2649450_-|helix-turn-helix-domain-containing-protein
MPTSILTTDDLYDFKLELLRELKKLLQDKAPTAIKKYLKSAEVMEMLQISPGTLQNLRINGTLPYTKIGGIILYEYEEILRILQENKVAS
>NZ_CP009239.1|WP_148228905.1|2649630_2650506_-|hypothetical-protein
MNFKSNLCNTFPKSLNVTKKQIIKIEESNLRNLSVLNDGLNLSVQTLNKLRKNLRTKDNFFTQEEEISFFKYDKPFINGRIKFFSKVRRFIAEKPNASITKQIKYVHSTIDKLEKHKMRNLEFFQYTRQCNNTLDHIYFVRGKDNLDFPVDTSHYFTDPEFSTSHDNLAAQVIGYDLLSNYYDLELEYLNKKKENVIIEEVSPAILNGLSWTASKTDLVEIIYALHSAGAIRNGQAELSKMAEVCATLFDLNLNNFYKTYAEIKNREKDTTKFLDHLKRSLEKRIDLDNAK
>NZ_CP009239.1|WP_013621952.1|2650573_2651845_-|site-specific-integrase
MRSTHTFSILFWADQKNAINGEVLIYARITVDKKRANISLKRRVPQNLWDPKKKKLRGNSHQAQSANQYLDQIYTQLFQIYQDLKFKGELITAQLIKAQYTGEADNKGKSLKNIFEYHSKKITNTLASGSIRNFGITENYVFKFLEQKRKTTDIYLNQLNFEFLSHFELFLSEVWPTGHPKALGNNTRMKHIQRLRKVVTLAYHLEWIDKDPFVRWKMTYDKTNREFLSEQELKKLENKVFISERLDRVRDLFVFSCYTGISYVDIMNLTPNHLVLGIDGGYWIMTKRQKTNTTVKVPLLGQALDIVNKYKDHPVTAVNNSLLPVLTNEKLNMFLKEVANFVGINKNLTFHMARHTFATTVTLSNGVPIETVSKLLGHSKIATTQIYARVLENKVSADMNALKNVLLNKSKDSTVAKNSKASS
>NZ_CP009239.1|WP_013621953.1|2652233_2652746_+|adenine-phosphoribosyltransferase
MNFKEYIRDVQDFPKQGIVFKDITPLLNNAEILEKTTDALLNLVKEQKIDKVVGMESRGFFFATLLATKLKAGFVPVRKKGKLPFNVLSKPYSLEYGEDALEIHTDAIKKGDKVLIHDDVLATGGTAKAVCELIEELGGEVVQCNFLIELDFLNGKDKIANYNVDSLLHY
>NZ_CP009239.1|WP_013621954.1|2652742_2652895_-|hypothetical-protein
MKKALFRFLAKINRLLLPSYSKKQLDLSKASKLQLAIIGWRYYVTTNAID
>NZ_CP009239.1|WP_013621955.1|2653470_2654406_+|calcium/sodium-antiporter
MLNLVYIIIGLVFLIMGGNWLLKSSVALSLRLQIPKIVVGMTVVSFATSAPELIVSIKAALEGSPDLALGNVVGSNIANLGLVLGVIVMLGSIDVRKSFYTTDWPILMLASLVFFGFIYFDGVIKFYEGVIMVALLIVYIVYLIKFQKTAVEDEAPEDDVPLPTFKMLLFLALGGLGLWGGSELLVSGATGLARFYNVSERVIGVTVVSVGTSIPELAASIIAVIKKEKAISLGNLIGSNIFNIFAVLGITALITPLNVVDNTLLSNDILWMLGFAIILLPLVFFPKGLRLGWRDGIVLLSGYIAFVYFTI
>NZ_CP009239.1|WP_013621956.1|2654493_2655504_-|glutamine-synthetase
MSKSKLEYIWLDGYTPTANLRSKTKVEDDFSGKLEDCPIWSFDGSSTQQAEGGSSDCLLKPVAIYPDPARKDGYLVMTEVLNADGTPHLSNSRAGIDDEDNDFWFGFEQEYFIMDKNTQLPLGFPVGGYPGPQGMYYCSVGGKNTHGRDFVEEHADLCIAAGLNFEGINQEVASGQWEFQLFAKGAKKAGDEIWIARYLLDRLTEQYGYYIEYHPKPVKGDWNGSGMHANFSNTILRTCGSKETYEKICEAFRPVTKEHIAVYGEFNDQRLTGEHETAAITDFSYGISDRGASIRIPIITVEKGWKGWLEDRRPASNGDPYKIAGRIIKTVKSAKI

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP009239_2	2.1|629936|31|NZ_CP009239|CRISPRCasFinder	629936-629966	31	MN693371	Marine virus AFVG_25M511, complete genome	9467-9497	6	0.806
NZ_CP009239_2	2.1|629936|31|NZ_CP009239|CRISPRCasFinder	629936-629966	31	NC_019516	Cyanophage S-TIM5, complete genome	47389-47419	6	0.806
NZ_CP009239_2	2.1|629936|31|NZ_CP009239|CRISPRCasFinder	629936-629966	31	MK368614	Vibrio phage 2 TSL-2019, complete genome	70688-70718	7	0.774
NZ_CP009239_1	1.5|140319|30|NZ_CP009239|CRISPRCasFinder	140319-140348	30	NZ_CP014680	Kozakia baliensis strain DSM 14400 plasmid pKB14400_6	1794-1823	8	0.733
NZ_CP009239_2	2.1|629936|31|NZ_CP009239|CRISPRCasFinder	629936-629966	31	CP013001	Bacillus thuringiensis strain XL6 plasmid, complete sequence	130206-130236	8	0.742
NZ_CP009239_2	2.1|629936|31|NZ_CP009239|CRISPRCasFinder	629936-629966	31	NC_011775	Bacillus cereus G9842 plasmid pG9842_209, complete sequence	192809-192839	8	0.742
NZ_CP009239_1	1.2|140145|33|NZ_CP009239|CRISPRCasFinder	140145-140177	33	NZ_CP012100	Bacillus thuringiensis strain HS18-1 plasmid pHS18-1, complete sequence	10309-10341	9	0.727
NZ_CP009239_1	1.2|140145|33|NZ_CP009239|CRISPRCasFinder	140145-140177	33	MF417897	Uncultured Caudovirales phage clone 9F_6, partial genome	2201-2233	11	0.667

1. spacer 2.1|629936|31|NZ_CP009239|CRISPRCasFinder matches to MN693371 (Marine virus AFVG_25M511, complete genome) position: , mismatch: 6, identity: 0.806

tgcaactaatgcaattgctgct-gtgcaaact	CRISPR spacer
tgcaactaatgtaaatgctgctggtgcagta-	Protospacer
***********.** ******* *****.   

2. spacer 2.1|629936|31|NZ_CP009239|CRISPRCasFinder matches to NC_019516 (Cyanophage S-TIM5, complete genome) position: , mismatch: 6, identity: 0.806

tgcaactaatgcaattgctgctgtgcaaact-	CRISPR spacer
tggaactgatgcaattgctgctg-gtgaccta	Protospacer
** ****.*************** *..* ** 

3. spacer 2.1|629936|31|NZ_CP009239|CRISPRCasFinder matches to MK368614 (Vibrio phage 2 TSL-2019, complete genome) position: , mismatch: 7, identity: 0.774

tgcaactaatgcaattgctgctgtgcaaact	CRISPR spacer
accaactagtgcaattactgctgtgcacaac	Protospacer
  ******.*******.********** * .

4. spacer 1.5|140319|30|NZ_CP009239|CRISPRCasFinder matches to NZ_CP014680 (Kozakia baliensis strain DSM 14400 plasmid pKB14400_6) position: , mismatch: 8, identity: 0.733

ggtaactgcaaaagaaactatagacgctag	CRISPR spacer
atttattgcaaaagaaactatagaggcatc	Protospacer
. * *.****************** **   

5. spacer 2.1|629936|31|NZ_CP009239|CRISPRCasFinder matches to CP013001 (Bacillus thuringiensis strain XL6 plasmid, complete sequence) position: , mismatch: 8, identity: 0.742

tgcaactaatgcaattgctgctgtgcaaact	CRISPR spacer
agcaactactgcaattgctgcagttcctgca	Protospacer
 ******* ************ ** *  .* 

6. spacer 2.1|629936|31|NZ_CP009239|CRISPRCasFinder matches to NC_011775 (Bacillus cereus G9842 plasmid pG9842_209, complete sequence) position: , mismatch: 8, identity: 0.742

tgcaactaatgcaattgctgctgtgcaaact	CRISPR spacer
agcaactactgcaattgctgcagttcctgca	Protospacer
 ******* ************ ** *  .* 

7. spacer 1.2|140145|33|NZ_CP009239|CRISPRCasFinder matches to NZ_CP012100 (Bacillus thuringiensis strain HS18-1 plasmid pHS18-1, complete sequence) position: , mismatch: 9, identity: 0.727

cctaaaagttaaaacaaaagaactaaaagctag	CRISPR spacer
tattaaagttaaaagaaaaaaactaaaagactt	Protospacer
. * ********** ****.********* .  

8. spacer 1.2|140145|33|NZ_CP009239|CRISPRCasFinder matches to MF417897 (Uncultured Caudovirales phage clone 9F_6, partial genome) position: , mismatch: 11, identity: 0.667

cctaaaagttaaaacaaaagaactaaaagctag	CRISPR spacer
aagtaaggttaaaacaaaagaagtaaaaagccc	Protospacer
    **.*************** *****. .