CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Prophage number
NZ_CP021275	Legionella pneumophila strain D-4040 plasmid unnamed1, complete sequence	0 crisprs	NA	0
NZ_CP021274	Legionella pneumophila strain D-4040 chromosome, complete genome	2 crisprs	csa3,DinG,cas3,PD-DExK,WYL,DEDDh	4
NZ_CP021276	Legionella pneumophila strain D-4040 plasmid unnamed2, complete sequence	0 crisprs	csa3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP021274_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP021274_1

2769394-2769561

Orphan

Consensus_repeat	Method
TAAATTTACCGCGATAACAGTAATTT	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP021274_1

>merge|NZ_CP021274|1|2769394-2769561|CRISPRCasFinder
TAAATTTACCGCGATAACAGTAATTTTATAAATTTAACATAAATAAATACACAGAAAATTAGAAAATCGAGTAAATTTACCGCCATAACAGTAATTTATAGTGAATTAATGCAAAAAAATGCAATAATAAATTTATTTTAATCATTTTTACTGCTATAACAGTAATAT

>NZ_CP021274|1|1|2769394-2769561|CRISPRCasFinder
TAAATTTACCGCGATAACAGTAATTT	TATAAATTTAACATAAATAAATACACAGAAAATTAGAAAATCGAG
TAAATTTACCGCCATAACAGTAATTT	ATAGTGAATTAATGCAAAAAAATGCAATAATAAATTTATTTTAAT
CATTTTTACTGCTATAACAGTAATAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP021274.1\|WP_080464248.1\|2775595_2776504_-\|NADP-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|176191
NZ_CP021274.1\|WP_106195121.1\|2769135_2769345_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_106184168.1\|2773494_2775336_+\|amidohydrolase	unknown	unknown	gnl\|CDD\|224490
NZ_CP021274.1\|WP_161499067.1\|2777370_2777511_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379112
NZ_CP021274.1\|WP_106195124.1\|2769582_2769810_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|213767
NZ_CP021274.1\|WP_152027455.1\|2777627_2777990_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_062728061.1\|2781479_2782637_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_062728057.1\|2772743_2773424_+\|hydrolase	unknown	unknown	gnl\|CDD\|238494
NZ_CP021274.1\|WP_106195118.1\|2767315_2768905_-\|Fic-family-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_110540214.1\|2756597_2757038_+\|IS630-family-transposase	unknown	unknown	gnl\|CDD\|315923
NZ_CP021274.1\|WP_106195112.1\|2764868_2766380_+\|Fic-family-protein	unknown	unknown	gnl\|CDD\|225718
NZ_CP021274.1\|WP_014842378.1\|2759457_2760789_+\|Na+/H+-antiporter-NhaA	unknown	unknown	gnl\|CDD\|377746
NZ_CP021274.1\|WP_014842377.1\|2758952_2759288_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|182502
NZ_CP021274.1\|WP_106195109.1\|2764097_2764373_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP021274.1\|WP_106184171.1\|2779643_2780927_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_106195115.1\|2766605_2767031_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_014842376.1\|2757647_2758658_+\|fatty-acid-desaturase	unknown	unknown	gnl\|CDD\|239584
NZ_CP021274.1\|WP_106195130.1\|2770111_2771050_+\|lpg2370-family-Dot/Icm-T4SS-effector	unknown	unknown	gnl\|CDD\|377920
NZ_CP021274.1\|WP_106195127.1\|2769806_2770115_+\|HipA-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|274416
NZ_CP021274.1\|WP_014842375.1\|2757053_2757380_+\|DUF389-domain-containing-protein	unknown	unknown	gnl\|CDD\|273024

Protein	Function_ID	Function_description	E-value
NZ_CP021274.1\|WP_080464248.1\|2775595_2776504_-\|NADP-dependent-oxidoreductase	gnl\|CDD\|176191	cd05289, MDR_like_2, alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases. Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	4.14268e-107
NZ_CP021274.1\|WP_106184168.1\|2773494_2775336_+\|amidohydrolase	gnl\|CDD\|224490	COG1574, COG1574, Predicted metal-dependent hydrolase with the TIM-barrel fold [General function prediction only].	0
NZ_CP021274.1\|WP_161499067.1\|2777370_2777511_-\|hypothetical-protein	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	3.28954e-05
NZ_CP021274.1\|WP_106195124.1\|2769582_2769810_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|213767	TIGR03070, couple_hipB, transcriptional regulator, y4mF family. Members of this family belong to a clade of helix-turn-helix DNA-binding proteins, among the larger family pfam01381 (HTH_3; Helix-turn-helix). Members are similar in sequence to the HipB protein of E. coli. Genes for members of the seed alignment for this protein family were found to be closely linked to genes encoding proteins related to HipA. The HibBA operon appears to have some features in common with toxin-antitoxin post-segregational killing systems. [Regulatory functions, DNA interactions].	5.58215e-23
NZ_CP021274.1\|WP_062728057.1\|2772743_2773424_+\|hydrolase	gnl\|CDD\|238494	cd01012, YcaC_related, YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.	1.05433e-56
NZ_CP021274.1\|WP_106195112.1\|2764868_2766380_+\|Fic-family-protein	gnl\|CDD\|225718	COG3177, COG3177, Fic family protein [Function unknown].	1.8504e-16
NZ_CP021274.1\|WP_014842378.1\|2759457_2760789_+\|Na+/H+-antiporter-NhaA	gnl\|CDD\|377746	pfam06965, Na_H_antiport_1, Na+/H+ antiporter 1. This family contains a number of bacterial Na+/H+ antiporter 1 proteins. These are integral membrane proteins that catalyze the exchange of H+ for Na+ in a manner that is highly dependent on the pH.	7.86125e-162
NZ_CP021274.1\|WP_014842377.1\|2758952_2759288_+\|hypothetical-protein	gnl\|CDD\|182502	PRK10504, PRK10504, putative transporter; Provisional.	0.00198298
NZ_CP021274.1\|WP_106195109.1\|2764097_2764373_-\|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.	0.00150731
NZ_CP021274.1\|WP_110540214.1\|2756597_2757038_+\|IS630-family-transposase	gnl\|CDD\|315923	pfam13358, DDE_3, DDE superfamily endonuclease. This family of proteins are related to pfam00665 and are probably endonucleases of the DDE superfamily. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction.	3.80681e-40
NZ_CP021274.1\|WP_014842376.1\|2757647_2758658_+\|fatty-acid-desaturase	gnl\|CDD\|239584	cd03507, Delta12-FADS-like, The Delta12 Fatty Acid Desaturase (Delta12-FADS)-like CD includes the integral-membrane enzymes, delta-12 acyl-lipid desaturases, oleate 12-hydroxylases, omega3 and omega6 fatty acid desaturases, and other related proteins, found in a wide range of organisms including higher plants, green algae, diatoms, nematodes, fungi, and bacteria. The expression of these proteins appears to be temperature dependent: decreases in temperature result in increased levels of fatty acid desaturation within membrane lipids subsequently altering cell membrane fluidity. An important enzyme for the production of polyunsaturates in plants is the oleate delta-12 desaturase (Arabidopsis FAD2) of the endoplasmic reticulum. This enzyme accepts l-acyl-2-oleoyl-sn-glycero-3-phosphocholine as substrate and requires NADH:cytochrome b oxidoreductase, cytochrome b, and oxygen for activity. FAD2 converts oleate(18:1) to linoleate (18:2) and is closely related to oleate 12-hydroxylase which catalyzes the hydroxylation of oleate to ricinoleate. Plastid-bound desaturases (Arabidopsis delta-12 desaturase (FAD6), omega-3 desaturase (FAD8), omega-6 desaturase (FAD6)), as well as, the cyanobacterial thylakoid-bound FADSs require oxygen, ferredoxin, and ferredoxin oxidoreductase for activity. As in higher plants, the cyanobacteria delta-12 (DesA) and omega-3 (DesB) FADSs desaturate oleate (18:1) to linoleate (18:2) and linoleate (18:2) to linolenate (18:3), respectively. Omega-3 (DesB/FAD8) and omega-6 (DesD/FAD6) desaturases catalyze reactions that introduce a double bond between carbons three and four, and carbons six and seven, respectively, from the methyl end of fatty acids. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXX(X)HH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homologue, stearoyl CoA desaturase. Mutation of any one of four of these histidines in the Synechocystis delta-12 acyl-lipid desaturase resulted in complete inactivity.	8.29842e-45
NZ_CP021274.1\|WP_106195130.1\|2770111_2771050_+\|lpg2370-family-Dot/Icm-T4SS-effector	gnl\|CDD\|377920	pfam07804, HipA_C, HipA-like C-terminal domain. The members of this family are similar to a region close to the C-terminus of the HipA protein expressed by various bacterial species. This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis. When expressed alone, it is toxic to bacterial cells, but it is usually tightly associated with HipB, and the HipA-HipB complex may be involved in autoregulation of the hip operon. The hip proteins may be involved in cell division control and may interact with cell division genes or their products.	4.39719e-60
NZ_CP021274.1\|WP_106195127.1\|2769806_2770115_+\|HipA-N-terminal-domain-containing-protein	gnl\|CDD\|274416	TIGR03071, couple_hipA, HipA N-terminal domain. Although Pfam models pfam07805 and pfam07804 currently are called HipA-like N-terminal domain and HipA-like C-terminal domain, respectively, those models hit the central and C-terminal regions of E. coli HipA but not the N-terminal region. This model hits the N-terminal region of HipA and its homologs, and also identifies proteins that lack match regions for pfam07804 and pfam07805.	8.53709e-44
NZ_CP021274.1\|WP_014842375.1\|2757053_2757380_+\|DUF389-domain-containing-protein	gnl\|CDD\|273024	TIGR00341, Uncharacterized_protein_MJ0678, TIGR00341 family protein. This conserved hypothetical protein is found so far only in three archaeal genomes and in Streptomyces coelicolor. It shares a hydrophobic uncharacterized domain (see TIGR00271) of about 180 residues with several eubacterial proteins, including the much longer protein sll1151 of Synechocystis PCC6803. [Hypothetical proteins, Conserved].	2.40272e-15

>NZ_CP021274.1|WP_106195121.1|2769135_2769345_+|hypothetical-protein
MKNITLLGINLAKDVFQLHHIKGADPDESRITSQRAGTRYTCIFYMIKEIYSHSILDAVIFHIRRTFNP
>NZ_CP021274.1|WP_106195118.1|2767315_2768905_-|Fic-family-protein
MKISPLYQSKLNNFKLTPKLDTPLRLIARGIHYGQISGEETELREFILAHITDPADIEAINQSDDYQTYTVIAELFGMLPSSILELSEENKRNILLAFRIFLEKNPLSLIKSIQQKTEYGDTVWTASALEKIAEVPELLQELIPELSLFISEYASKLSELELRRLVAAIHGNQVLIGLVMELYASGQFNLSHFQRNTLSEEELACSLEIYWHPEQKGNMAYFYQDFPELELWRLFMDGYQQEAGWSNYEAREKGCINQLYQAWLYTKKTMTEPLTPEYFKKIHSICAKGIIWNNTEGTYRKYGTSFGLSLRTLTFLGYIEHLTQFNNLCTLEKHGSLGFDALTSIETERLDTVIEQIIEEYESTACTHAENPQALLHAIIIFCKKLELTHPFNDCNGRLFCNLLLNRELVRHGFSPTILDNPNIIEGYTVKESMSELIRGMNSFQRLKVDGSFKTGMNTLDLIKTQTYPIPDVWNIYQLSQSIPENAAALLGQHGVFAASSEKQVRVCSETLNHGINFQNDTKSDPATY
>NZ_CP021274.1|WP_106195115.1|2766605_2767031_-|hypothetical-protein
MPLASEIAEAIAKSTGKTIMVHGAEAARQLQLTTQVPTRLVFYTDGNSRTLTIANRTVGLKHANPSRMIEPGTIAGLVITALIYLGQENVTPSTIHLIKKRIPEADFKKTIDLISRMPAWLADIFFRYQKDSCNARASKLS
>NZ_CP021274.1|WP_106195112.1|2764868_2766380_+|Fic-family-protein
MKPSEKLAQSLEILHNLQKQGKYAIQSKDISRTHRERLVENAFLEEVVKGWYVPIKPDEKKGESTTWYASFWSFCASYLNERFGEEWCLSPEQSLLLHSENWTVPKQLMIRSPNGTNRNMELPHNTALFSVQYKMPAAQDIEIKQGMRIYAIVPALIYCSPKFFSQYPTEARSVLSMFNSASDLLHYLLEEGHSWIAGRICGALQNIGKSHVAEEIKKTMESAGYQIREEDPFLTNTPIDFSATYKPAYRSRLEVMWHDMRDIVRENFPKPRLTTIDIKKYIEQVDEKYISDAYHSLSIEGYQVSPELIEKVRSEQWNPDATEQDRNQRNALAARGYWQAFQSVKKSLIEILNGENPGKIVQKEHGDWYRELFQPSVAVGLLKPTDLAGYRRSPVFIRQSKHIPPRWQIVSELMEEFFQLITQEKEPAVRVVLGHFFFVYIHPYSDGNGRIGRFLMNVMLASGHYPWTIIPVERRNEYMEALEQASVNQNIIPFTKFIASCIQ
>NZ_CP021274.1|WP_106195109.1|2764097_2764373_-|helix-turn-helix-domain-containing-protein
MPAQKPSRLHLLNEFESAPQSALFNQQTIAAVLSCSTQLLERNRWAGGGVPYLKIGRKVLYRKSDVLNFLQQQKIYYSTSDEGQLPLVENA
>NZ_CP021274.1|WP_014842378.1|2759457_2760789_+|Na+/H+-antiporter-NhaA
MPLNPQLPKELIHWVSKPLDRFIRIETSTAILLLLSTFVALIMANSPWSKSFLSIWDITLGIHLGSFEFSRSIHGWINDGLMTLFFFFVSLELKREFVFGELRKPQMAALPIIAAVGGMLVPALFYLFLQYNEAGQNGWGTVMATDTAFVIGCLALFGKLIPQSLRIFMLSLAIIDDIGAILVVAIGYSDGISWTALVISAIGFILVFLMRKLGIRSITVFFFIGSIIWVSVDASGIHPTITGVILGLMTPTGSWVNDKRLNEILNHMVSFNPGEHWSVDTDDRKALRIAEMAVRETLSPVERLEFLLHPWIGYLIMPLFALANAGVLINFSDFTNEVTIAVFLGFILGKPIGVFSFSFIADFLGLAKRPSDLNWILLACGSILTGIGFTMAIFIANLAFNENLINSARLGIMLASIFCALTGIFMLLIYKFYSENIDSSMSK
>NZ_CP021274.1|WP_014842377.1|2758952_2759288_+|hypothetical-protein
MKEKECSKISTCLWTLRFEILGVILLAIGTVLTISTGNGLGIIALFTAGVVLCLFNKFCCYICSSKQPSCPICNAPHSYHSEKSSQILEKEDNEAKQAMDNEGGNQNNRRK
>NZ_CP021274.1|WP_014842376.1|2757647_2758658_+|fatty-acid-desaturase
MVKKQINKDFQRHVYEYITPNSWRSIAEILATILLLLLGLTTLNFAMKNSIWLLFMIIVISLSLLYSRLFILQHDLGHGNLFKNRKYNNAVGVIIGIILLTPYYFWRKAHAIHHVSGGNADRRPWIGDIDLLSVKEYRKKNWWEKLLYRLYRNPFIMFCFGSIYVFMIEHRFCRKRKGFGRKEAQSVLTTNIAIIILYGSIISLLGIKFYLLAILLPQWLGGVFGIYLFYIQHNFKNRYFVSAKYWNLQDSALLGSTFYDFPQPIRWLTANIGYHHIHTLMPRIPFYRLPQCHKENVFFHIAPTFRLKDMPKMISLKLYDEKNKKMITWKEYRKLR
>NZ_CP021274.1|WP_014842375.1|2757053_2757380_+|DUF389-domain-containing-protein
MAISFTTGVSAALIGVMVSVALLPPLLVACGLLLGAGYGVLALGALYLFLMNFVCVNLSGVAMFLVQGIRPLSWWERGRAKKATLIAIGLWSITLASLIILILLLNNS
>NZ_CP021274.1|WP_110540214.1|2756597_2757038_+|IS630-family-transposase
MVYLDESGFAHSMPRTHGYSLKGHRCYGQRAWGERGRINAIGALLDNQLITVSLFEGTINAATFNSWIEQDLIPKLPATSVVVMDNAAFHKDKGMQEQLFLAGFTLEYLPPYSPDLNPIEHKWAQAKSIRRKTNCSIDELFQSHCQ
>NZ_CP021274.1|WP_106195124.1|2769582_2769810_+|helix-turn-helix-transcriptional-regulator
MRTHEIANLVHYYRKQSGLSQQELARLAGVGKTVIYDIEKGKESVRLNTLLKVLDVLNIQMKFETPFPQATDNNS
>NZ_CP021274.1|WP_106195127.1|2769806_2770115_+|HipA-N-terminal-domain-containing-protein
MRKAYVSVNGIKAGTLEELQGGKYQFTYFDDYLGAPVSLTMPLTNKVYYFDVFPPFFEGLLPEGIMLEALLRKYKIDKNDYFGQLIIVGQDVVGAVTIEEIR
>NZ_CP021274.1|WP_106195130.1|2770111_2771050_+|lpg2370-family-Dot/Icm-T4SS-effector
MKRCPITYEKISDQENYSQRGLRLLSPQLKNLSPLDLSADEQRQEAIARVGKMSIQGVQKKLSAKLKIKEGCFEIVDQNGHYILKPQSDIYPELPENEAITMTLAKTIGLEVPVHGLVYSKDNSLTYFIKRFDRIGHNKKLALEDFAQLSGEDRHTKYKSSMEKVIAVIQQFCTFPKIEFVKLFKLTLFNFLVGNEDMHLKNFSLITKDRKISISPAYDLLNSTIAQKNTKEEIALPLKGKKNNLTKSDFLKYFAVEKLGLNQNVIDGIVQEFHQVIPKWQELIDFSFLSQEMQEKYLELLDQRCKRFNFFD
>NZ_CP021274.1|WP_062728057.1|2772743_2773424_+|hydrolase
MSAATEQLLTPQNCAFVFIDHQPQMSFGVTSIDRQLLKNNVVAMAKTAKLFNIPTLLTAVETESFSGYIWPELMDVLQQDPIERTSMNSWEDKVFVDAVKKTGRKKLVIAALWTEACLIFPTLCALDEGYEVIMNIDASGGTSKEAHDAAIRRCEKHGAESISTVQLTLELQRDWSRKETYEGITNIVRDHFGAYGMGIDYAASMVHDYGQRAKYLHKVIQSQNKA
>NZ_CP021274.1|WP_106184168.1|2773494_2775336_+|amidohydrolase
MSKGYPELILYHGKVTTLDKQKSEVSAIALSDGVVTAIGNDAEILKLAGQGTQQINLQGKRVIPGLNDSHLHLIRGGLNYNMELRWDGVVRLADALMILKVQAERTPNPQWVRVVGGWSEFQFKERRMPTLAEINHAAPNTPVFILHLYDRALLNGAALKAAGITRESPDPIGGRIERDKKGNPTGMLIAEPNAMILYSTLAKGPKLPFEHQVNSTRHFMRELNRLGITSCIDAGGGFQNYPEDYQVIEKLHQEGLMTVRIAYNLFTQNPGRELADFQQWTKQINPYSGDGFYRHNGAGEMLVFSAADFEDFLQPRPDMPGKMEDELKDVVRFLVDQRWPFRLHATYNETIDRALTVFESVNKDTAFDGLRWFFDHAETVDEHNLERIKKLGGGIAVQHRMAFQGEYFVERYGKEAAQNAPPIRKMLDMGIPVGGGTDATRVASYNPFVSLYWLITGKTVGGLSLYRDNNRLEREEALRLWTQGSAYKSNEETVKGALSVGQYADLAVLSDDFMHVDDEAIKAITSVLTVVGGKIVYAAEEFKSFDPPMPPPSPEWSPVAHYGGYAAPHWHGSSCMIHGHDGKLSRCLGLNKTAHHRPNFDNPWALGCGCFAY
>NZ_CP021274.1|WP_080464248.1|2775595_2776504_-|NADP-dependent-oxidoreductase
MKLIDQPTPNPGYDEVLVRVKAASVNPVDIQTRRGDYNNLITLPARLGVDCAGIIEKVGKGVHGFQIGDEVFYVPRLLENEGSYATHHVEKATIVAKKPETISFEQAATLPLSAGTAWECLIERGRLKSGDKVLIHGGAGGVGVYAIQIAKFFGAHVVTTSGLHNKDFVEMLGADVSYDYRKESLYQELRQDYPAGFDIILDTVGQKTIENSLSLLATSGRLVSIVDMSEPQNLISGWLVNAEIHFVFTTQSAKRLAEIAKVVDAGGIKPIIERVMKLSEIVLAHDLIEAGNRKGKIVISID
>NZ_CP021274.1|WP_161499067.1|2777370_2777511_-|hypothetical-protein
MQKLIAVVHPENTSSQNVLIKCGMSHAGKINYWNKEIMKFEITNKF
>NZ_CP021274.1|WP_152027455.1|2777627_2777990_-|hypothetical-protein
MNKEFKEAANELKQCIQPLTQTPFFDSSGQHKQYKRTIFHHVMEINKCGSSEAVNNEMFHMTLKDLATIAKELPDTGEDSKLKQGLNQYVSAIQAAARPYISNPEEVEAYIGKEKGPQIK
>NZ_CP021274.1|WP_106184171.1|2779643_2780927_-|hypothetical-protein
MSIESSQYNYDALTVEENKKNIENAFSENQNEKFKVKNSTFVVFSDKGLDAKAHKEMESNWKIHLSVAPEDIGKAWDLAYPLLHDKAAQFKVVDMTRAIAAKDRNLRQLDTVKHEKEIFIQNYEKGELNLEQLKQQAGPLTYGREEWEPYATDAKTLYEFLLKKHDEKIQKCENMVKENDRIIQGMQITIYIPPGQELEMHKLAQEIEQRFQENNIKKGTIYPTDNPLGDYASYRHPGLEYQDAVAIDTYNPDNLDDPLFLASIDNKINSLKELCKKTYDLEYQTLIKDSITLLETVKQAYQNNNIPQKQAIKITEASYHVAAQPSIENVNKFKKVEYSMRDDSSVPLNVKTGMDKFLGSVYKFFGNLFNKESWKQKGDEILRKVEDTEKFKSDFKQFKSKISDFKAEKENLDVNEEKTPLMSFKQN
>NZ_CP021274.1|WP_062728061.1|2781479_2782637_+|hypothetical-protein
MYSLPLKSKSLRFFNLVFIALVLSFYLLANANAARIKRYDFGEMSSKVTKAWDQDVALYVARRFAAENGFDEKEITVKKLEAGATNHFIYLMFINNQLKFVLKGLGTEKEAEALFALQNYSKIPDIQNNPQAATVTLSKTINSYEVKNDRKTYYFAILEAAQGKELFKIMTYELLQHKDINTLKDVFYRIGQQTSELHKTIIGHDQFITPRDLVTVIHDDFHPENTFYNLETNVFSLIDNESMGDSITNPLPIIRELYGFYEVPIIRWPSEKITVDLLRDADPHDIASIYYDFVLGMASVYHDSQDAKRVLIEAIIDLNNMAIAFLKDRYSEPWMFNPSDKHEAHIVWGKLAKVADNPQLAELYINKLAIINTDLQSLSGLWLQQ

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Crispr_ID: NZ_CP021274_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP021274_2

2812251-2812795

Orphan

Consensus_repeat	Method
CGTCACTTCACTGAATTTGAGTGGAAATT	CRISPRCasFinder
GCATGACTTCACTGGATTTAAGCTGGAATG	PILER-CR
CGTCACTTCACTGAATTTGAGTGGAAATT	CRISPRCasFinder

4 spacers

The CRISPR arrays of NZ_CP021274_2

>merge|NZ_CP021274|2|2812251-2812795|CRISPRCasFinder,PILER-CR,CRISPRCasFinder
TGTTACTTCCCTTGATTTAAGTTGGAATAACCTGGACAGTATAAGCACGGTTGAATTAATGCAAGCCTTTGCTAATATACCCGCCAGCGTCACTTCACTGAATTTGAGTGGAAATTCCTTAGGCTTTAAAAACAGTGATGAATTAGTTCAGATTCTCGCAGCCATCCCTGCCAACGTCACTTCATTGAATTTGAGTGGAAATTACTTAGGAAATCAAAACGGCGCTGACTTGGCACGACTCCTTGCTACCATCCCTATCAGCGTCACTGCGCTGGATTTAAGCTGGAATGATTTAAGTAGTAAAAGTAGCTCAGAATTAGCACAAACCTTCGCAGCTATCCCTACCAATTTGACATCATTAGATTTAAGCTGGAATGCTCTATACCGTAATCCAGGTTTAACTCGAGTCTCTGCTGCTATTCTTGCTGGCATGACTTCACTGAATTTAAGCTGGAATTTCATAGGATTAAAAAGCTGTGCTGAAATAGCACATGTCTTTTCTTCTATCCCTAATCATGTAATTTCACTTAATTTGTGCCTTAATT

>NZ_CP021274|2|2|2812251-2812541|CRISPRCasFinder
TGTTACTTCCCTTGATTTAAGTTGGAATA	ACCTGGACAGTATAAGCACGGTTGAATTAATGCAAGCCTTTGCTAATATACCCGCCAG
CGTCACTTCACTGAATTTGAGTGGAAATT	CCTTAGGCTTTAAAAACAGTGATGAATTAGTTCAGATTCTCGCAGCCATCCCTGCCAA
CGTCACTTCATTGAATTTGAGTGGAAATT	ACTTAGGAAATCAAAACGGCGCTGACTTGGCACGACTCCTTGCTACCATCCCTATCAG
CGTCACTGCGCTGGATTTAAGCTGGAATGATTTAAGTAGTAAAAGTAGCTCAGAATTAGCACAAACCTTCGCAGCTATCCCTACCAATTTGACATCATTAGATTTAAGCTGGAATGCTCTATACCGTAATCCAGGTTTAACTCGAGTCTCTGCTGCTATTCTTGCTGGCATGACTTCACTGAATTTAAGCTGGAATT	TCATAGGATTAAAAAGCTGTGCTGAAATAGCACATGTCTTTTCTTCTATCCCTAATCA


>NZ_CP021274|2|1|2812511-2812708|PILER-CR
GCGTCACTGCGCTGGATTTAAGCTGGAATG	ATTTAAGTAGTAAAAGTAGCTCAGAATTAGCACAAACCTTCGCAGCTATCCCTACCA
ATTTGACATCATTAGATTTAAGCTGGAATG	CTCTATACCGTAATCCAGGTTTAACTCGAGTCTCTGCTGCTATTCTTGCTG
GCATGACTTCACTGAATTTAAGCTGGAATT

>NZ_CP021274|2|3|2812680-2812795|CRISPRCasFinder
	ACCTGGACAGTATAAGCACGGTTGAATTAATGCAAGCCTTTGCTAATATACCCGCCAG
CGTCACTTCACTGAATTTGAGTGGAAATT	CCTTAGGCTTTAAAAACAGTGATGAATTAGTTCAGATTCTCGCAGCCATCCCTGCCAA
CGTCACTTCATTGAATTTGAGTGGAAATT	ACTTAGGAAATCAAAACGGCGCTGACTTGGCACGACTCCTTGCTACCATCCCTATCAG
CGTCACTGCGCTGGATTTAAGCTGGAATGATTTAAGTAGTAAAAGTAGCTCAGAATTAGCACAAACCTTCGCAGCTATCCCTACCAATTTGACATCATTAGATTTAAGCTGGAATGCTCTATACCGTAATCCAGGTTTAACTCGAGTCTCTGCTGCTATTCTTGCTGGCATGACTTCACTGAATTTAAGCTGGAATT	TCATAGGATTAAAAAGCTGTGCTGAAATAGCACATGTCTTTTCTTCTATCCCTAATCA
TGTAATTTCACTTAATTTGTGCCTTAATT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP021274.1\|WP_106195385.1\|2810947_2811925_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238064
NZ_CP021274.1\|WP_106195142.1\|2804508_2805579_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|316372
NZ_CP021274.1\|WP_106195170.1\|2819123_2820278_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_192875949.1\|2813374_2814889_+\|serine-hydrolase	unknown	unknown	gnl\|CDD\|365903
NZ_CP021274.1\|WP_106195174.1\|2822455_2823115_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_027227434.1\|2803256_2803721_-\|bacterioferritin	unknown	unknown	gnl\|CDD\|225104
NZ_CP021274.1\|WP_106195164.1\|2817727_2818651_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_106195172.1\|2821926_2822190_-\|type-IV-secretion-protein-Dot	unknown	unknown	unknown
NZ_CP021274.1\|WP_106195167.1\|2818638_2819040_+\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|239217
NZ_CP021274.1\|WP_106195159.1\|2814865_2815786_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176155
NZ_CP021274.1\|WP_106195153.1\|2809620_2810682_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238064
NZ_CP021274.1\|WP_106195145.1\|2805953_2807153_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|366703
NZ_CP021274.1\|WP_106195390.1\|2820550_2821648_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_106195147.1\|2807207_2807780_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|275224
NZ_CP021274.1\|WP_106195176.1\|2823359_2824181_+\|DUF4116-domain-containing-protein	unknown	unknown	gnl\|CDD\|372614
NZ_CP021274.1\|WP_192875948.1\|2804021_2804381_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP021274.1\|WP_106195150.1\|2807970_2809326_-\|YdgA-family-protein	unknown	unknown	gnl\|CDD\|377603
NZ_CP021274.1\|WP_106195136.1\|2802247_2803138_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238064
NZ_CP021274.1\|WP_106195161.1\|2815917_2817432_-\|cytochrome-P450	unknown	unknown	gnl\|CDD\|365848
NZ_CP021274.1\|WP_106184181.1\|2800674_2801979_-\|Dot/Icm-T4SS-effector-SdbC	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP021274.1\|WP_106195385.1\|2810947_2811925_+\|hypothetical-protein	gnl\|CDD\|238064	cd00116, LRR_RI, Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).	1.23636e-07
NZ_CP021274.1\|WP_106195142.1\|2804508_2805579_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|316372	pfam13847, Methyltransf_31, Methyltransferase domain. This family appears to have methyltransferase activity.	4.08558e-24
NZ_CP021274.1\|WP_192875949.1\|2813374_2814889_+\|serine-hydrolase	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	4.2837e-23
NZ_CP021274.1\|WP_027227434.1\|2803256_2803721_-\|bacterioferritin	gnl\|CDD\|225104	COG2193, Bfr, Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism].	9.45818e-21
NZ_CP021274.1\|WP_106195167.1\|2818638_2819040_+\|NUDIX-hydrolase	gnl\|CDD\|239217	cd02883, Nudix_Hydrolase, Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.	2.53993e-19
NZ_CP021274.1\|WP_106195159.1\|2814865_2815786_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176155	cd08466, PBP2_LeuO, The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an activator of leucine synthesis operon, contains the type 2 periplasmic binding fold. LeuO, a LysR-type transcriptional regulator, was originally identified as an activator of the leucine synthesis operon (leuABCD). Subsequently, LeuO was found to be not a specific regulator of the leu gene but a global regulator of unrelated various genes. LeuO activates bglGFB (utilization of beta-D-glucoside) and represses cadCBA (lysine decarboxylation) and dsrA (encoding a regulatory small RNA for translational control of rpoS and hns). LeuO also regulates the yjjQ-bglJ operon which coding for a LuxR-type transcription factor. In Salmonella enterica serovar Typhi, LeuO is a positive regulator of ompS1 (encoding an outer membrane), ompS2 (encoding a pathogenicity determinant), and assT, while LeuO represses the expression of OmpX and Tpx. Both osmS1 and osmS2 influence virulence in the mouse model of Salmonella. In Vibrio cholerae, LeuO is involved in control of biofilm formation and in the stringent response. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.69343e-56
NZ_CP021274.1\|WP_106195153.1\|2809620_2810682_+\|hypothetical-protein	gnl\|CDD\|238064	cd00116, LRR_RI, Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).	1.21606e-09
NZ_CP021274.1\|WP_106195145.1\|2805953_2807153_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	2.36774e-17
NZ_CP021274.1\|WP_106195147.1\|2807207_2807780_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|275224	TIGR04431, aminoglycoside-6'-N-acetyltransferase_type_Ib, aminoglycoside N(6')-acetyltransferase, AacA4 family. Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance].	5.23235e-21
NZ_CP021274.1\|WP_106195176.1\|2823359_2824181_+\|DUF4116-domain-containing-protein	gnl\|CDD\|372614	pfam13475, DUF4116, Domain of unknown function (DUF4116).	5.15187e-06
NZ_CP021274.1\|WP_106195150.1\|2807970_2809326_-\|YdgA-family-protein	gnl\|CDD\|377603	pfam06097, DUF945, Bacterial protein of unknown function (DUF945). This family consists of several hypothetical bacterial proteins of unknown function.	9.97589e-78
NZ_CP021274.1\|WP_106195136.1\|2802247_2803138_+\|hypothetical-protein	gnl\|CDD\|238064	cd00116, LRR_RI, Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).	2.34934e-07
NZ_CP021274.1\|WP_106195161.1\|2815917_2817432_-\|cytochrome-P450	gnl\|CDD\|365848	pfam00067, p450, Cytochrome P450. Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.	1.54858e-21

>NZ_CP021274.1|WP_106195385.1|2810947_2811925_+|hypothetical-protein
MHYKLILPTGSNLVQEFTSIPPGITSLDLSWNNLDSISTVELMQAFANISASVTSLNLRGNYLGHKSNDELVQILATIPANITSLNLSANYLCSKSGAELAQLLAAIPARVTSLSLSWNGLNSKSDAELAQAFAAIPASVTSLDLSWNGLHSISSMGLVRVFAAIPVNVTSLDLSVNLLGLKSCSELVHIFPSIPNHVVSLNLYLNYLQGLSLENLVLLKGSLKYLQTVYLGYDTVKNMSKEERQALGSVFPNVQKIILTDKNGKEIHPSQSITIANLIRELSGKADAPSLLNQCILFTQKHQTNIEDLNIPQELKESIQTFNPY
>NZ_CP021274.1|WP_106195153.1|2809620_2810682_+|hypothetical-protein
MIYELILTGGCNLVQEFSSIPHGVTSLDLSVNSLCSKSTGELTQAFASLPASITSLNLGGNHLGSKSGAELAQLLAAIPASVTALDLGWNALNITNSSELAEALAAIPSGVTSLNLSHNHLGSKSGTELAQLLAAIPISVTALDLSWNDLNSKNSAGLTQALAAIPASMTSLNLSWNVLGSSGAGLAQAFATIPANVISLDLSWNLLGFKHCAELARVFSSLPNHVVSLNLCFNPLNELSIENLMPLKDSLKHVQTIYLSHSIVENMSKEQRQALGSAFPNIQKIVLVDDNYKEIHPSQSITISNLIRELSGKADAPSLLNQSILFAQKHQTNIDHLNIPEELKESILTFNPY
>NZ_CP021274.1|WP_106195150.1|2807970_2809326_-|YdgA-family-protein
MKKWIISLLLLIIIVLCSYPIIGMMALSTVKKNVDNIPKNPFLTWQLKDNHRGWFCSTAVLNLLVDLPAQENKDAQGNVKVQPALHLSLDIPMVIHHGPFIMTNNGLRFGLAWVTTRPETHYGALINYLNQTVVRYSLPAINMQGTNNGDQGNFVFVWQGLSAKLKVNPKVDKASGHVTMYGMSTKVQETDVRIGKVKVNFALNRYMDDLWLGDSSILLSSLSTITNSQPVFDLQDLSMDAWAGVNNNLLDFNLQLSLNKFLMNNNSYGPGQLKIELKKLDPKAMAKLNQLNYDYPSNQIAILAEIFNLLSKGATLSLNQELDTPQGHLSSSLNMSLTRNSFSNPGDLWQNLKGNGQFKAPIKLIKQLLLESIKSKTATPADVSQSQAKQPDSTQPVDIDADAHKQTEELLQKLVSQGVLKVEGDYYHASFTLEHTKFTVNGQPFDPALLN
>NZ_CP021274.1|WP_106195147.1|2807207_2807780_-|GNAT-family-N-acetyltransferase
MVLINISKSQVMSDFKFQPLGINDLNQLHQWFQEPIINHWYARDKNWSINDIKEKYEPRIVGTEHVPSFIVYKDDLPFGFVQFYILTDSLPDGIDGYESLLFQHYKPMDLAGIDLFIAESQGRGKGLGVELINCFINKFLTRFKAIVIDPDVNNQQAIRCYEKAGFQRTDFSRDPNHLIMIKPLLLTIGN
>NZ_CP021274.1|WP_106195145.1|2805953_2807153_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MIKSFRFTIFLFLASCLVFARDLQAFPTPSESHQDKLAYFQLEAETFYSPKPVTIEGNPYLTYEVFLTNVGDYPFSLENVEVLNGRQPHKVLFSYNQEQLRKMIYSFGGHSKHLKSDLTLRPGERGLLFFMVKFNSLGEIPKKLTHRFHLYSSKTQISEEEVRYSFLAAPAHVKTTKPLVIANPLDGKHWMAINGPSNHSLHRRARVAAHGIVYYPERYAIDFMQFGSDGHIYKENPYKNDNYYSYGANIYSVTDGKVVDVYDGLPDNTPPGRDYPVTLSNMAGNYVIIEIAKHQYALYAHLIPHSIKVTKGEFVRKNQLIAKLGNSGNSDAPHLHFHVIDKPSPLIGQGIPYVFANFSTEEYRFAGDDWESPIIYEGRLREHHHELVHENALMNFAEK
>NZ_CP021274.1|WP_106195142.1|2804508_2805579_-|class-I-SAM-dependent-methyltransferase
MKTGRFDQARSDAFAERLLSVLNDAALTLMISIGHRTGLFDVMDGLDFASSEVIAEAAGCNERYVREWLNALVVGGIVDYDAHAKTYQLPTEHAAFLTRKSSPQNMAVIAQFIPVLAYVENGIVDAFKHGGGVPYEAYHRFHEVMAEESGQTILSSLTDKILPMVDGLVDKLNQGIQVLDIGCGYGRALILMAKTYPQSQFTGYDLCDETIAHALHSAKENNIHNIHFEKMDLSVWDEQEKYDLITSFDVIHDQAKPAQVLGNVFKALKPKGTFLMQDIKTSSEVSGNVHHPLGAFIYAISCMHCMTVSLSQNGLGLGAAWGEELAEKMLVEAGFGKIEKHYLEHDIMNTYYVMRK
>NZ_CP021274.1|WP_192875948.1|2804021_2804381_+|hypothetical-protein
MSNKAKNTHLKDGDNQTKQTYSNSGSPLFFSQKQISPSSGTLETKKPQEGKQPTQEISLETTTDILLAAILQELKTQNMIELMKLKAQQEQEQEELETIEKMKEKDDARFNEIRQTMYA
>NZ_CP021274.1|WP_027227434.1|2803256_2803721_-|bacterioferritin
MKHKRSETQDIDDAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTLKIGKLLETHEHNISNILEESLEHERQSLDLYYQLLQYAENKSVLVEEFARQMIQEEEMHLGEISKMLNSPATFKD
>NZ_CP021274.1|WP_106195136.1|2802247_2803138_+|hypothetical-protein
MLYELVLTRRSNLRQEFLSIPHGITSLDLSLNELGSISNAELIQAFTNIPDSVNSLDLTHNHLCDKNGAELAQLLAAIPVHVTSLNLSSNNLDRKSGAELAQAFAAIPTNVTSLYLSCNGMGNINGAELAQALTAIPASVTSLDLGMNYFDLESSNDLSQIFTSIPPQVVSLNLSFNSLNEISFEKLVLLKDSLKHVQTVYLSFYSVKEMSKEQRKALGAVFPNVQKIILVDDYGHESQPSESVTISNLIREITGKANAPSLLNQCILFAQRHQTGCMERNIPEELKEDIRTFNSR
>NZ_CP021274.1|WP_106184181.1|2800674_2801979_-|Dot/Icm-T4SS-effector-SdbC
MPNSRVQIWLQRQIAARTFPPNREDWYVKNGFGNSEMSLEERFACFVEAIRQVDSPYHEQLSSIEFERFEIEVTLANQTTCMTEVIGFQNNSNQSSSTLNEKFKAVGKGKHVIYFTGIGTQYQDCLIDIAKAVQITGAHYYAFEYPGMKKLGGEVLEANDMVNTGIALANTLLEKGISIDDILFQGDSFGAAVAKKVSDQFKLQSNVTVRCIMNNTFSTFQAAVEGNLGMFSTLRYTVRPLLRYTGWDIRPGESYGQDTPYQIHINHTGDLTLGAGHATLAESVESNSQLEHFVDPCPEEYRIKRDTYKQWHWASLSEQGITFLETKYGRNSDGQLDTHLADLYLLKYDTGLGVYESFICKYLEDSNDYIANHPQKLSLDELPRPLESETVSLRQLIVSVLPSRPSIAGFFSRTTPVIEEVETEKQEQKSIELK
>NZ_CP021274.1|WP_192875949.1|2813374_2814889_+|serine-hydrolase
MSYMKIEELLLKDTMKKGQIPGVSIAYINNQGIISTQEIGFTDGCGLVKMSKDPTQCPFQELVLGSKNELGIGTKNTVIAFNKELYYVDQAAKMVQKIALTEANKVAYEMLHAKCTETYQLADSNEHEFIATLTGRMPPTEVKPDSVFGAASLSKPVFAYLVQKLIQTNAKNQSEASFDQFILPEKLKHFDLYTPLFHIIPLEEFNIDGMTFDLSDESVVAHSKALTARMVLSHTSGLAHGEMKFQFLPNAQEKEHGYSNVGIIYLQQVIEKLTGSDLETLAQKHVFQPCGMVHSTYGPKPCAANSLWTTAGDYANFVKHLIHDSTIENPFVPHTDMTKDKGLAGAIGIAKGNIPDTILQRVAWGLGWGLQTNDEGRVITAYHSGDMNDYRAWVVIDLQDKDKKNAVVFFANSHNGHILAEQIIPKAMQMEQAANYFFAKWGFARNFAELGGKTTRLGIKSSSCNSDSSPDTSIQDEPIEVKKETEKSDTSSIEIYTSGRTFNA
>NZ_CP021274.1|WP_106195159.1|2814865_2815786_-|LysR-family-transcriptional-regulator
MAIPFKRINLNLILHLDALLNEKSVSSAAEKVFVSQPAMSSSLKQLRELFKDPLLIPGKGEYFLSPKAKELQPQLEQVMFFIRNILQPSERFDPLQTKRSFKIALPDYVELILLPCLMSALEKLPHIVIETTIQSMADDPHLFIDENVDLAIGAINENSLSAQLKVKKLYEEEIICFASKNNPLINKPLSLEDYISNKHIAFSFNQERYSHSAEYLYKRKLVRNDMLFVKNILPAIFAVANSDAVISTAPSFLINIFAGQFNLGMQPLPFDLEPTPIYLVTHSKSQYDEGVAWLAKLVSSCIKSPS
>NZ_CP021274.1|WP_106195161.1|2815917_2817432_-|cytochrome-P450
MFGELFASSIVLGIRYYSNQAYQAVTGLLGQIERFGIGYTREFIRDPKSMIQSLTSKARSGEAGYSVVSLGYLGGNYAVITPKSQSQLTELLNQFDQEKSGRRGHASFKFFSGNDFFIISDTGHAALSSRKNLSRFLVPSRLVNPTITEVEKRVDGDADIQLRHTICGIVRAVMVENMLGIKQLPDNTYDVMASYRNDVKRWGAFPFPELLNFMPSLRQKRDVYRAFSKSILEQEFEKLVEILHTDPNPGNTNLIAASVVSLFKDENPTLSNEELLSALRSLSSEDIRKYFENPIVQSLPMILKAADNLTDAIVLCLEQIASDPDKFAMLRYEMDRSHLRIEEGIDIRTLKSLPILDAFYKESVRFDAPVAVPRYTQNGYSSDSMTIPPNTMMIFDLHALAKGEQYWTNPEEFDPTRFLQKDIEQVAEEGGMSSNNKNHTVGQFPFIPFSVGLRNCPAFAVTESLFKVTIAKFVSDYQLQLVKKDEDDSTLHITSRDKSLGLMQ
>NZ_CP021274.1|WP_106195164.1|2817727_2818651_+|hypothetical-protein
MATTQTQTSSYTKNLILNLDDYPGGVAIWGALPALFDTSNQGFDRGVHVHARLADSSKKVIDATYDRVTVIAANRIFTITEEAAVHFSMSAIFDINIISLECLRCSQPITSIGYAAVCPSRQHQCNHCGEITTTTTDCISNPIMLLKELIGDKQVKRPAVIPNRTIAIDPERYRGGIQIWGSNPSIIWTAKRLEESAIHVHAYNDSGKRVIDNTYGRVSLAGYKLDIEMIRVLQIQLALPNLALHLATVYCPHCGKEQFDQGIGAVCAHKHRVCLLCKQTFISQDVISNPAFDVLTHVSGVSSQCAH
>NZ_CP021274.1|WP_106195167.1|2818638_2819040_+|NUDIX-hydrolase
MRTLNTIFKVGALIFNEQNQLLAVHKKGKPPMEFIVPGGVMEENETDEETLRREIKEELDSDITSFQFYKQFEDKAIYEEKWLVMRTYIVTLDRVPKPANEIDQLVWLGHDYHESGYRFGSILGKQIIPDFFK
>NZ_CP021274.1|WP_106195170.1|2819123_2820278_-|hypothetical-protein
MKVLFDKTAKNNSGSGITYSSKNNEICTSSICMKSKLPSEVVTEHLHGLQSTMVDRRNPDLPDSKPLMKAAKAHAILKTGTEIDMLTATGISEDDLPSAKGAITLTSPEELTLKATWKNKNQERGVSGRDASVFGGLGVLIISPDMKVMNIPKMNALAVPASFLAKYGAELIPLEQPFTLDAVDKSSLENLYLVEYQWDADYIQDYVMNVRGGGGLFVETHPFPHVFTPLSPECRGALILGFERKDGAFDFAAFEIPFGYTMKIASNVIHGDSFFVGPYAIALTETELADSVLLKQDTPQRDIQRVAQMPTKAFAVFLFEEVRLANQINRKMMADKAHHEGFSGKRLGFFKESSPKAPTEVRHSSDADQDIHDQKFGLVPCLTK
>NZ_CP021274.1|WP_106195390.1|2820550_2821648_+|hypothetical-protein
MKKKDEQNNLTKGKENEHNTISTNTNLLFSKPPGIDAETSNHMASSIDRLKDFDRSKQNLWLKYSEDIINEFCALLPEFPKIKPKVREDIRCPEEALLTQVGCAYAFLASKRREVAKLLKHGPLRHQFGLFNKPGFASIDDFNLSKDIPSQKDKIYEHLSLLISQSNPFIEVKKNHREAEGFSIYTITFKMKPDEIEQVHIKNLNSNKPFIENDTVLTITFNDYGKNDNRTSIVIDHCPTPFAENYTNESSYFKVQFELIEPYFQACLVWEPSEGMNQFLENIGKIAYILARMQPVGRGNSAIVEWMIRGLAQTKNIELGPFNPDEKIGWDFKAFLTPQMQDYAHWFSEKAFAHSQLKNVSSLEY
>NZ_CP021274.1|WP_106195172.1|2821926_2822190_-|type-IV-secretion-protein-Dot
MKPSSEKSKEIRKKYKAPGASDEQLANSIKVASDFEYKNSSTFGWGGVYMVDRFQSIITGRAITNNTQRLLDAQTLEEEASKSNLKQ
>NZ_CP021274.1|WP_106195174.1|2822455_2823115_+|hypothetical-protein
MLTKNLNEALSAIKYVKSKLIYGSNTEQDSKKPNWEPGRIIHLRKEVHEQAVAYARSHNGKAGFDIISKLTHAALLKYGFGNCGEQAQTAFCYLQSRGVAPLDYCQTSIGEHCLIVIGRVNGSDPNDISTWGEEAVICDPWAEKAYPLSEFKKMQNPENDIRYPEMCYANGKSPKPYLAGDLISFHRKEPALKRQSLSFFKNENTDCSQSSYTPLKSPA
>NZ_CP021274.1|WP_106195176.1|2823359_2824181_+|DUF4116-domain-containing-protein
MTDSTRLKNPVSKSLNDLCQDELTVIGSYVGAWNDLWSLTFTASEMKKHLIDKQNDKLWEFFFKEYFPYLPLPTKDFYKNFMESYKSWYQTLCRVKSDPFFLMYLDKLEEDPAHLFRNDKEIIMAAIEKQPFLYKNFSREYKEDQEVILCALKGNRFIIHDVPRAVRQTFEKIADIKDDKTRIDACDKLIAELSSQRVSKIESLDLFKSQLQFLAQDTRKSTGEQTNSHPLQKSTVSIITPAGITSLVNLSLFKDTQTQDKDKDESPQTQYRN

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

146101 : 179281

Escherichia_phage(25.0%)

transposase

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_061504501.1\|146101_147223_-\|transposase	ISAs1 family transposase	NA	NA	NA	NA
WP_014844325.1\|148233_149028_-	AAA family ATPase	A0A2L1IVB6	Escherichia_phage	1.6e-75	53.9
WP_106194034.1\|151202_153218_-	M3 family metallopeptidase	A0A1V0SD92	Indivirus	6.3e-44	21.8
WP_106194037.1\|153314_154652_-	hypothetical protein	NA	NA	NA	NA
WP_192875972.1\|154910_156917_+	transketolase	NA	NA	NA	NA
WP_192875973.1\|156998_157991_+	type I glyceraldehyde-3-phosphate dehydrogenase	NA	NA	NA	NA
WP_106194045.1\|158001_159192_+	phosphoglycerate kinase	NA	NA	NA	NA
WP_106194048.1\|159175_160600_+	pyruvate kinase	NA	NA	NA	NA
WP_106194051.1\|166384_167455_-	hypothetical protein	NA	NA	NA	NA
WP_106194054.1\|167455_168148_-	activator of prop osmoprotectant transporter	NA	NA	NA	NA
WP_061504501.1\|168452_169574_+\|transposase	ISAs1 family transposase	NA	NA	NA	NA
WP_106194056.1\|170099_170858_+	PAS and helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_106194059.1\|171030_172284_+	ankyrin repeat domain-containing protein	NA	NA	NA	NA
WP_161538218.1\|172485_172839_+	hypothetical protein	NA	NA	NA	NA
WP_161520671.1\|172768_173632_+\|transposase	IS4 family transposase	NA	NA	NA	NA
WP_106194064.1\|173784_174603_+\|transposase	transposase	NA	NA	NA	NA
WP_106194067.1\|174793_175762_+	virulence protein RhuM/Fic/DOC family protein	Q9JMN3	Wolbachia_phage	8.0e-21	36.6
WP_106194069.1\|175911_176778_+\|transposase	transposase	NA	NA	NA	NA
WP_106194075.1\|177450_177882_+	hypothetical protein	NA	NA	NA	NA
WP_106194079.1\|178113_179281_-\|transposase	IS3 family transposase	A0A0P0I4A4	Acinetobacter_phage	1.5e-61	44.7

DBSCAN-SWA_2

947846 : 954728

Acinetobacter_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_062727111.1\|947846_948623_-	indole-3-glycerol phosphate synthase TrpC	A0A0P0IR83	Acinetobacter_phage	1.1e-57	48.6
WP_062727110.1\|948615_949650_-	anthranilate phosphoribosyltransferase	A0A0N7IRD9	Acinetobacter_phage	9.3e-76	47.6
WP_062727109.1\|949627_950206_-	aminodeoxychorismate/anthranilate synthase component II	A0A0P0IKJ1	Acinetobacter_phage	3.9e-55	52.6
WP_027221199.1\|950239_950965_-	LPS export ABC transporter ATP-binding protein	A0A2H4PQG7	Staphylococcus_phage	8.1e-18	25.1
WP_106183505.1\|950961_951471_-	lipopolysaccharide transport periplasmic protein LptA	NA	NA	NA	NA
WP_106183506.1\|951451_952021_-	LPS export ABC transporter periplasmic protein LptC	NA	NA	NA	NA
WP_106183507.1\|952017_952545_-	3-deoxy-manno-octulosonate-8-phosphatase KdsC	A0A140XBD6	Dickeya_phage	1.4e-27	47.7
WP_027227556.1\|953930_954728_+	ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	1.7e-21	33.8

DBSCAN-SWA_3

1341807 : 1347745

Staphylococcus_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_062727573.1\|1341807_1342881_+	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A2H4PQS8	Staphylococcus_phage	1.5e-28	27.0
WP_062727574.1\|1342865_1343480_+	riboflavin synthase	A0A2I2L4R9	Orpheovirus	4.6e-22	38.4
WP_027227759.1\|1343476_1344685_+	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	5.9e-98	48.7
WP_106183665.1\|1344692_1345160_+	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	1.9e-23	50.9
WP_028378484.1\|1345286_1346924_+	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	3.2e-155	52.5
WP_062727576.1\|1346920_1347745_+	3-deoxy-8-phosphooctulonate synthase	E3T537	Cafeteria_roenbergensis_virus	2.7e-54	44.3

DBSCAN-SWA_4

2267666 : 2277783

Bacillus_phage(16.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_062726361.1\|2267666_2269349_-	S8 family serine peptidase	A0A1B0T6A2	Bacillus_phage	6.1e-16	30.4
WP_192875931.1\|2269482_2270490_-	AraC family transcriptional regulator ligand-binding domain-containing protein	NA	NA	NA	NA
WP_106184006.1\|2270614_2271940_-	adenosylhomocysteinase	S4VPF6	Pandoravirus	6.2e-48	31.4
WP_106184007.1\|2271958_2273107_-	methionine adenosyltransferase	A0A2H4PQS6	Staphylococcus_phage	9.9e-127	58.2
WP_062726357.1\|2273310_2274423_-	glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit	R4TGJ8	Halovirus	7.2e-50	34.7
WP_027229222.1\|2274521_2275661_-	molecular chaperone DnaJ	A0A1V0SBY2	Catovirus	1.6e-23	26.7
WP_062726356.1\|2275848_2277783_-	molecular chaperone DnaK	G8DDB7	Micromonas_pusilla_virus	1.3e-147	49.6

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP021274

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection