CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	1 crisprs	NA	0	6	1	0
NZ_CP015516	Enterococcus hirae strain R17, complete genome	3 crisprs	DEDDh,cas2,DinG,cas3,csa3,cas14j,csn2,cas1,cas9	0	10	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP015517_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP015517_1

13773-13998

Orphan

Consensus_repeat	Method
TTAGGGGAAAAAGAGAAAAAGAGA	CRISPRCasFinder
GAGAAAAAGAGAAAAAGAGAAA	PILER-CR

3 spacers

The CRISPR arrays of NZ_CP015517_1

>merge|NZ_CP015517|1|13773-13998|CRISPRCasFinder,PILER-CR
TTAGGGGAAAAAGAGAAAAAGAGAAAATACCCCTTGAATATTGTTGTTGTTTAATAATTATAACTAGGAGAAAAGTCTCTTAGGAGAAAAAGAGAAAAAGAGACTTTTCTCTTTTTGGAATCGCAATACAACAGCTCTTTAGATAAAAGAGAAAAAGAGAAAAAGAGAAATTTCTCTTAATTTATTAATATACTTTTCCAAAAAGAGAAAAAGAGAAAAAGAGAAA

>NZ_CP015517|1|1|13773-13988|CRISPRCasFinder
TTAGGGGAAAAAGAGAAAAAGAGA	AAATACCCCTTGAATATTGTTGTTGTTTAATAATTATAACTAGGAGAAAAGTCTC
TTAGGAGAAAAAGAGAAAAAGAGA	CTTTTCTCTTTTTGGAATCGCAATACAACAGCT
CTTTAGATAAAAGAGAAAAAGAGA	AAAAGAGAAATTTCTCTTAATTTATTAATATA
CTTTTCCAAAAAGAGAAAAAGAGA

>NZ_CP015517|1|1|13779-13998|PILER-CR
GAAAAAGAGAAAAAGAGAAAAT	ACCCCTTGAATATTGTTGTTGTTTAATAATTATAACTAGGAGAAAAGTCTCTTAGGA
GAAAAAGAGAAAAAGAGACTTT	TCTCTTTTTGGAATCGCAATACAACAGCTCTTTAGATAAAAGA
GAAAAAGAGAAAAAGAGAAATT	TCTCTTAATTTATTAATATACTTTTCCAAAAAGA
GAAAAAGAGAAAAAGAGAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP015517.1\|WP_002354485.1\|20491_21178_-\|IS6-like-element-IS1216-family-transposase	unknown	unknown	gnl\|CDD\|225853
NZ_CP015517.1\|WP_010706226.1\|17937_18537_-\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271192
NZ_CP015517.1\|WP_001574272.1\|21974_22976_+\|peptidase-P60	unknown	unknown	gnl\|CDD\|372680
NZ_CP015517.1\|WP_063627746.1\|10205_10547_-\|DUF5406-domain-containing-protein	unknown	unknown	gnl\|CDD\|379975
NZ_CP015517.1\|WP_010726525.1\|15507_15801_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_010726527.1\|14137_15094_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379293
NZ_CP015517.1\|WP_063627742.1\|6357_8334_-\|isopeptide-forming-domain-containing-fimbrial-protein	unknown	unknown	gnl\|CDD\|374637
NZ_CP015517.1\|WP_063627743.1\|8386_9058_-\|class-A-sortase	unknown	unknown	gnl\|CDD\|320680
NZ_CP015517.1\|WP_063627747.1\|18739_20398_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275009
NZ_CP015517.1\|WP_010776886.1\|11453_11786_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_010726526.1\|15106_15415_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_063627744.1\|9143_9383_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_033651474.1\|10560_10863_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_001224319.1\|22972_23905_+\|conjugal-transfer-protein	unknown	unknown	gnl\|CDD\|372237
NZ_CP015517.1\|WP_104888407.1\|9897_10122_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015517.1\|WP_010726524.1\|16089_16785_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379492
NZ_CP015517.1\|WP_063627745.1\|9449_9689_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380482
NZ_CP015517.1\|WP_010726528.1\|12621_13668_-\|replication-initiator-protein-A	unknown	unknown	gnl\|CDD\|369151
NZ_CP015517.1\|WP_010706225.1\|16975_17875_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379523
NZ_CP015517.1\|WP_063627741.1\|5590_6343_-\|class-C-sortase	unknown	unknown	gnl\|CDD\|320676

Protein	Function_ID	Function_description	E-value
NZ_CP015517.1\|WP_063627742.1\|6357_8334_-\|isopeptide-forming-domain-containing-fimbrial-protein	gnl\|CDD\|374637	pfam16569, GramPos_pilinBB, Gram-positive pilin backbone subunit 2, Cna-B-like domain. GramPos_pilinBB is one of the major backbone units of Gram-positive pili, such as those from S.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three transthyretin-like, CnaB, domains along with a crucial N-terminal domain, D1. The three Cna-B like domains are stabilized by internal Lys-Asn isopeptdie bonds, Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base.	8.20336e-31
NZ_CP015517.1\|WP_001574272.1\|21974_22976_+\|peptidase-P60	gnl\|CDD\|372680	pfam13702, Lysozyme_like, Lysozyme-like.	7.72157e-80
NZ_CP015517.1\|WP_063627746.1\|10205_10547_-\|DUF5406-domain-containing-protein	gnl\|CDD\|379975	pfam17400, DUF5406, Family of unknown function (DUF5406). This is a family of unknown function found in Bacteria.	1.02861e-48
NZ_CP015517.1\|WP_010726527.1\|14137_15094_+\|AAA-family-ATPase	gnl\|CDD\|379293	pfam13614, AAA_31, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	2.19781e-28
NZ_CP015517.1\|WP_010706226.1\|17937_18537_-\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271192	cd01192, INT_C_like_3, Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain. Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction 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. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.	2.00454e-55
NZ_CP015517.1\|WP_063627743.1\|8386_9058_-\|class-A-sortase	gnl\|CDD\|320680	cd06165, Sortase_A, Sortase domain found in class A sortases. Class A sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They perform a housekeeping role in the cell as members of this group are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class A sortases recognize a canonical LPXTG motif, X can be any amino acid), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase A protein from Staphylococcus aureus (named Sa-SrtA) cleaves the amide bond between threonine and glycine residues of the canonical LPXTG motif in a wide range of protein substrates with diverse functions that can promote bacterial adhesion, nutrient acquisition, host cell invasion, and immune evasion. Next, it catalyzes a transpeptidation reaction by which the proteins are covalently linked to the peptidoglycan precursor lipid II. SrtA is therefore affects the ability of a pathogen to establish successful infection. SrtA contains an N-terminal hydrophobic segment, a linker region and an extra-cellular C-terminal catalytic domain. The hydrophobic segment functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. The catalytic domain contains the catalytic TLXTC signature sequence where X is usually a valine, isoleucine or a threonine. The gene encoding SrtA is generally not located in the same gene cluster as its substrates while the gene encoding SrtB is usually clustered in the same locus as its substrate.	2.20911e-45
NZ_CP015517.1\|WP_063627747.1\|18739_20398_-\|hypothetical-protein	gnl\|CDD\|275009	TIGR04141, conserved_hypothetical_protein, sporadically distributed protein, TIGR04141 family. This model describes a sporadically distributed conserved hypothetical protein in which complete members average over 500 amino acids in length, although matching sequences frequently are truncated or broken into tandem ORFs. Regular co-clustering with known markers of mobility (integrases, transposases, phage proteins, restriction enzymes, etc.) suggests this family also is part of the mobilome. The function is unknown.	8.65131e-40
NZ_CP015517.1\|WP_002354485.1\|20491_21178_-\|IS6-like-element-IS1216-family-transposase	gnl\|CDD\|225853	COG3316, COG3316, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	2.80773e-92
NZ_CP015517.1\|WP_001224319.1\|22972_23905_+\|conjugal-transfer-protein	gnl\|CDD\|372237	pfam12642, TpcC, Conjugative transposon protein TcpC. This family of proteins are annotated as conjugative transposon protein TcpC. The transfer clostridial plasmid (tcp) locus is part of some conjugative antibiotic resistance and virulence plasmids. TcpC was one of five genes whose products had low-level sequence identity to Tn916 proteins, having similarity to ORF13 homologs from Tn916, Tn5397, and CW459tet. This family of proteins is found in bacteria. Proteins in this family are typically between 302 and 351 amino acids in length.	1.73847e-74
NZ_CP015517.1\|WP_010726524.1\|16089_16785_-\|hypothetical-protein	gnl\|CDD\|379492	pfam14163, SieB, Super-infection exclusion protein B. This family includes superinfection exclusion proteins. These proteins prevent the growth of superinfecting phage which are insensitive to repression. It aborts lytic development of superinfecting phage.	9.30885e-11
NZ_CP015517.1\|WP_063627745.1\|9449_9689_-\|hypothetical-protein	gnl\|CDD\|380482	cd01540, PBP1_arabinose_binding, periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.	0.00924334
NZ_CP015517.1\|WP_010726528.1\|12621_13668_-\|replication-initiator-protein-A	gnl\|CDD\|369151	pfam06970, RepA_N, Replication initiator protein A (RepA) N-terminus. This of family of predicted proteins represents the N-terminus (approximately 80 residues) of replication initiator protein A (RepA), a DNA replication initiator in plasmids. Most proteins in this family are bacterial, but archaeal and eukaryotic members are also included.	1.1661e-30
NZ_CP015517.1\|WP_010706225.1\|16975_17875_-\|hypothetical-protein	gnl\|CDD\|379523	pfam14253, AbiH, Bacteriophage abortive infection AbiH. This family of proteins confers resistance to bacteriophage.	6.44529e-44
NZ_CP015517.1\|WP_063627741.1\|5590_6343_-\|class-C-sortase	gnl\|CDD\|320676	cd05827, Sortase_C, Sortase domain found in class C sortases. Class C sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They function as pilin polymerases responsible for the assembly of pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. First, one or more class C sortases form the long thin shaft of the pilus through linking together pilin subunits via isopeptide bonds. The base of the pilus is then anchored to the cell wall by a housekeeping sortase or, in some cases, the class C sortase itself. Depending upon the organism both the number and type of sortase enzymes involved varies, and in some cases, accessory factors appear to be needed. In three-component spaA pilus from Corynebacterium diphtheriae, the prototypical class C sortase (named Cd-SrtA) catalyzes polymerization of the SpaA-type pilus, consisting of the shaft pilin SpaA, tip pilin SpaC and minor pilin SpaB. The pilus shaft is then attached to the cell wall by a housekeeping class E sortase, Cd-SrtF. In the absence of Cd-SrtF, Cd-SrtA attaches the pilus to the cell wall, albeit at a reduced rate. Cd-SrtA can recognize two distinct sorting signals (LPLTG in SpaA and SpaC, and LAFTG in SpaB) and it can employ lysine residues that originate from different proteins (either Lys190 within the pilin motif of SpaA or Lys139 in SpaB). However, Cd-SrtA cannot be able to polymerize the major pilin subunit SpaH, even though it contains LPLTG motif. In two-component pili of prototypical Bacillus cereus, the class C sortase (named Bc-SrtD) cleaves related sorting signals within a major pilin protein BcpA (LPVTG) and a minor tip pilin BcpB (IPNTG), and catalyzes a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif). Unlike the SpaA pilus in C. diphtheriae, in B. cereus Bc-SrtD is unable to covalently attach the pilus to the cell wall without the help of the housekeeping sortase.	6.38956e-61

>NZ_CP015517.1|WP_010726528.1|12621_13668_-|replication-initiator-protein-A
MQEFNFITAQETYRALYYQLPKVLFTSPLYKDMSNDSKIAYAMLQDRCEASIENNWIDEQNRIFFIFTRAELMDILGCKENKISKIKKELKSKNLLFEQRTPPKKLPNGEWLNFPNRLYLGKLEVTAEDVFVHTKDKAKEPNSESGKNKPSKEPLKQKDSYGRGKNPLSNKKASNQFSFESGKKGDNLFYSSSTLDTNRHNIDTETDQLQNQVLLDNFVEIMKEDSINTFLPEKVLSLIKTFSNTYEEAQQTVTTIHNAKHKAEGLEKTVVVYEELESYGIDADKGLYMTLLKAYQKQKTEKVNNLQNLIFVYVKNWFIEKAIAAKLANEQKETFNELPTVNTENWLE
>NZ_CP015517.1|WP_010776886.1|11453_11786_-|hypothetical-protein
MSYTGILSLEDIYHYGKRCTATEKITKKLSTGQNKTVVQCKKYIIQKDKVSEEMIYYVGKQKQIILKDPIPLKELYPAIKHVYDQNGVLIGRRKNGVLRCTAKGMGRLIS
>NZ_CP015517.1|WP_033651474.1|10560_10863_-|hypothetical-protein
MIQKFAKMSKTAWIEKLENDLNVMRLAPKNFKREIAEKETILSVLNAIDDNCPVKISFSDITTIIEGILYGEVDEEISSTKDLLEFLNKNKDRFVVLTYY
>NZ_CP015517.1|WP_063627746.1|10205_10547_-|DUF5406-domain-containing-protein
MKNYDPNMRRGTHTIKVSFQRWEYKGFVTFRRGGNCKGLDVLVLDEDDLYDQTLTDNPIGFGLLPEDDEGNEWFKMTLTNDNGDELSVEDTWSYLSDYIVSVEIIDFVADKKE
>NZ_CP015517.1|WP_104888407.1|9897_10122_-|hypothetical-protein
MCRFYEQLVAGIEDHEEFIRCLHELNTNEAMQESAKTISEETLQPIGMEEATKDIFTIIDEQKSCVLSIDSTLV
>NZ_CP015517.1|WP_063627745.1|9449_9689_-|hypothetical-protein
MARSALEAMDMDTLTKGRYVQLLARGYSPKDVFKALSKGTDMEKERLRKEFDYWRTHNGIKELKPARPVIKRKKKITQD
>NZ_CP015517.1|WP_063627744.1|9143_9383_-|hypothetical-protein
MNLKKIENRKKVSKEMEEKLLKTMKQKHLKRLSVMQYINDMQITGKEKACLLGSMKNFEQLRRTYVKTSSNCQLLLEVS
>NZ_CP015517.1|WP_063627743.1|8386_9058_-|class-A-sortase
MRKWLFGFLGVALIVFCSVFGYISYQKHEGEVFKQNIEKKMPVDQINTHAKSYKDNAANVNNDLSLGQMLSIQKEAIEMGVNKQVFAQIQIPVLGLTLPIFKGANQYTLSLGAATYFYEDAEMGKGNYVLAGHNMEMPGVLFSDIQKLSVGEVMDLVSNDGVYRYKVTRKFIVPEYFKLIDGVPEESSFLSLPKKGEKPLLTLFTCVYTSQGKERYVVQGELQ
>NZ_CP015517.1|WP_063627742.1|6357_8334_-|isopeptide-forming-domain-containing-fimbrial-protein
MAINRYVKKAGMFFGMLGIIAGCFQGSHVYADDVTQKTPPEKVNITVHKLMYDQGTQLNADIDGIKNDGYTHDQYPTGVTKYNKADYGDVEFTLGNITDQVLPREDSDLTNAKVDEIVKDVEDKGSNSEYVKNATNKITSAVDENGEITFANQPAYVNSKGNVYVIYESKSAAGLVKQKAKPMVVLAPMTDNTGSGFLKDIHLYPKNIVSKLSFELTKFGDDGTEQSKQTPLKGAKFELYKGEPGKGTKLGDLVSDDQGKLTATDLTLGKYYFVEIPSDVVVGPDQEPTADQYLLGADARNDAHNKLTFEITNDGVTSDLKASYVNYKAPIIDKTVTNGTGAEHSFQIGDAVNYQGTIHIPTDIAGGADGITVNGVKSETSPYSVFKWGDTAGQGLSYVAAKANIKVTNKDGSVVLKENTDYKIQNSENGFVIDFIVNNGQVSDTVASLHGQDLQMTYNMYVNDSAAVANPLTNSVDFVYNNNPFNQEEHHEKTKADVVTYGAKFLKVDSGLFGTGIKATPLEGAEFAAKNAEGKYYGGLVDTDKDGVKEAVWVDDVANAAILKSDKEGHFEITGLTEGEYSLEETKAPENYQKLTKEISFKVDKDSYKEENRITIKNNQKASVPMTGSNGFQTYVLVSCLLLGAGALSAVVYFKKKA
>NZ_CP015517.1|WP_063627741.1|5590_6343_-|class-C-sortase
MIIRKPKKKRIMGKWIIAFWLLSAAGVLLLMPAEASVAKYQQNQQIVAIDRTGTAASTDSSLDVAKIELGDPVGILTIPSISLKLPIYDGTSDKILENGVGITEGTGDITGGNGKNPLIAGHSGLYKDNLFDDLPSVKKGEKFYIKVDGEQHAYQIDRIEEVQKDELQRNFVTYLEPNPNEDRVTLMTCTPKGINTHRFLVYGKRVSFTKSELKDEENKKQKLSWKWLLGSTVFLSVMIIGSLFVYKKKK
>NZ_CP015517.1|WP_010726527.1|14137_15094_+|AAA-family-ATPase
MKRKGTTIINANQKGGVGKTTSTTEEALVATLPNPQFNKKVLIIDWDIQANATSLIGKTFNKNFPATIYQSIKDYSNGDKEALTKATVKLTDNLYMIAGGRDMADFGDLLEDLYPKENDPMYKKKRTFHFSNILETIKYDYDYIWIDVGPSTDIKVDNAMVCADYFVITQETKTYSFEGSLDIINEYLQTLIDDFGSDFKGEVLGLLPFLLQPKRELHESIIKNTKEAFGENFTFNAIVNNQKRLEEYPEYGVSVVDYHDRKVFALFADIFTEIEERIQLFEQYGDIPEDYVYSPKYLNGNKLTKLSRELDLAQFELA
>NZ_CP015517.1|WP_010726526.1|15106_15415_+|hypothetical-protein
MALTKREKKERPKVERIVETSRVNNEDNVASTEQNKKEWTAKDRRTIKIDPDIKSLIEIFSDFDGTKEYETVRQMAEFYLKNNYDERAQRIITNIQKEKFIN
>NZ_CP015517.1|WP_010726525.1|15507_15801_-|hypothetical-protein
MSINTFVYSHPINVYIIKYLGITVEQFCELYAYPQGTVASWITRQRRIKSLPASFIYDLSLASSMNMTDVYEKLLVLENEYDQFTSKQNKKEKKHIS
>NZ_CP015517.1|WP_010726524.1|16089_16785_-|hypothetical-protein
MGDITKIKDLPANITTALEAIVKFSKYLVIPTAVTTFFPDSWLQHMNLLSIKNSTFGMWISVAFWICISVVIIDMLQKLLTILFSIYNSKKLKRDLAKNMESLTKTEKDIVYKIFIYDNYRFNVLEDAAVKKLKNQDIIFHSNMGNQITGFSCGLQPMAREYLNENPNYLEEHAKLCKKSLVTELDKLEKSMSDLYQFDYDSMTKRETIEQLEKKLEEYNNFLENYNNDSK
>NZ_CP015517.1|WP_010706225.1|16975_17875_-|hypothetical-protein
MSTLYIIGNGFDLSHGLKTSYTDFSKWVEKNHSEIFDKIDTMINENNEVRSTADDKIGWFDFESSLHELIQSPVFEDHVEESKDYLIGYGHEDWSDSAHHDFQNVVYDYVVSLKKLQQLFKEWIRKEIQTTIEHKIPKYQFSSDVLFFTFNYTNVLEILYKQPKENIYHIHGSYDDIIVGHSENFDNFIGDPYDENADVRESEAARIVGDLHDSLNKNVPLQIKKFESTVFFEKLADVYEVQVIGHSYNRYDLPYFSLLNNAFSSNTRWVLNYRTDNDLTNLKSMVCQLKIINYEQHQI
>NZ_CP015517.1|WP_010706226.1|17937_18537_-|tyrosine-type-recombinase/integrase
MKTVEPIRDKKKIDAMKAILASGKYGQRNLVLFSIGINTAYRISDLRQLKLADVLEISRGRVVVKDRLAMKEQKTAKHNSVYISNKLRKTILEYVQQEFPEELLRQDFDGYLFPSRKGTNEPLNRQSLWRIIHDAGTAIGLKDIGPHSMRKTFGYFLYKQGTKTEIIQSLLNHSSQRETLRYIGITQEDKDTAVKSLDL
>NZ_CP015517.1|WP_063627747.1|18739_20398_-|hypothetical-protein
MRKNHNVTGKIFVLQEKQAEVRWLENVNSFSEKQIDFTTPNILNKPLIIIKTTSSSIYAISYSYGYTLLNREHVVPDFGLNIARKELKLHTIKRVKNTNFSDTLYVSNFSSNNKINLNEISTSQSIPNIVDEILGEMTIRFTDGNNNIKELNIFASSKDSIKINGNFSIEEDLVPILKQLGNTYRQRRSDRTFLDKEILAVSSRKKEYLNKHFDDYLSNLMVTFKKNSNEFKVNNLDKLFLDIPLNKVKFNIEDLEIRVHSIFRPGEYLNFFDNTQEEIFSKIFSFFLKNNVQEFVDKLKSINVSIKNRNSDSSKDTSIGNLFSCLYMELNHDSEKYILYQGDWLSVNKNVWRETRDFVNSISSEAHGIDFNEFNNEDADEGDYNIKISKLDSNKGLICVDKENFGNQNLDGGFPLYEINGRSQIEPCDILKVNENSAFFCHVKRGTATSGLSHLLSQARASCILIKKSEDFVNHINSVIKTELSESEAIFLNETNLKRSKIILGIIIPEKKVHFKNSKVFPVLFSLNLVALVNALSLEGFEVSLVKIPDKK
>NZ_CP015517.1|WP_002354485.1|20491_21178_-|IS6-like-element-IS1216-family-transposase
MTMNHFKGKQFQQDVIIVAVGYYLRYNLSYREVQEILYDRGINVSHTTIYRWVQEYGKLLYQIWKKKNKKSFYSWKMDETYIKIKGKWHYLYRAIDADGLTLDIWLRKKRDTQAAYAFLKRLVKQFDEPKVVVTDKAPSITSAFKKLKEYGFYQGTEHRTIKYLNNLIEQDHRPVKRRNKFYRSLRTASTTIKGMEAIRGLYKKTRKEGTLFGFSVCTEIKVLLGIPA
>NZ_CP015517.1|WP_001574272.1|21974_22976_+|peptidase-P60
MKLKALVIGGSGLFLMVFSLLLFVAILFSDEQDSGISNIHYGGVNVSAEVLAHKPMVEKYAKEYGVEEYVNILLAIIQVESGGTAEDVMQSSESLGLPPNSLSTEESIKQGVKYFSELLASSERLSVDLESVIQSYNYGGGFLGYVANRGNKYTFELAQSFSKEYSGGEKVSYPNPIAIPINGGWRYNYGNMFYVQLVTQYLVTTEFDDDTVQAIMDEALKYEGWRYVYGGASPTTSFDCSGLTQWTYGKAGINLPRTAQQQYDVTQHIPLSEAQAGDLVFFHSTYNAGSYITHVGIYLGNNRMFHAGDPIGYADLTSPYWQQHLVGAGRIKQ
>NZ_CP015517.1|WP_001224319.1|22972_23905_+|conjugal-transfer-protein
MRKEDLMMKFRKNQNKEKQIPKEKKPRVYKVNPHKKVVIALWVLLGLSFSFAIFKHFTAIDTHTIHETTIIEKEYVDTHHVENFVENFAKVYYSWEQSDKSIDNRMESLKGYLTDELQALNVDTVRKDIPVSSSVRGFQIWTVEPTGDNEFNVTYSVDQLITEGENTKTVHSAYIVSVYVDGSGNMVLVKNPTITNIPKKSSYKPKAIESEGTVDSITTNEINEFLTTFFKLYPTATASELSYYVNDGILKPIGKEYIFQELVNPIHNRKDNQVTVSLTVEYIDQQTKATQVSQFDLVLEKNGSNWKIVK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP015517_1	1.1\|13797\|55\|NZ_CP015517\|CRISPRCasFinder	13797-13851	55	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	58015-58069	0	1.0
NZ_CP015517_1	1.1\|13797\|55\|NZ_CP015517\|CRISPRCasFinder	13797-13851	55	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13797-13851	0	1.0
NZ_CP015517_1	1.2\|13876\|33\|NZ_CP015517\|CRISPRCasFinder	13876-13908	33	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13876-13908	0	1.0
NZ_CP015517_1	1.2\|13876\|33\|NZ_CP015517\|CRISPRCasFinder	13876-13908	33	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	57958-57990	0	1.0
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	57902-57933	0	1.0
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13933-13964	0	1.0
NZ_CP015517_1	1.4\|13801\|57\|NZ_CP015517\|PILER-CR	13801-13857	57	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	58011-58067	0	1.0
NZ_CP015517_1	1.4\|13801\|57\|NZ_CP015517\|PILER-CR	13801-13857	57	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13799-13855	0	1.0
NZ_CP015517_1	1.5\|13880\|43\|NZ_CP015517\|PILER-CR	13880-13922	43	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	57946-57988	0	1.0
NZ_CP015517_1	1.5\|13880\|43\|NZ_CP015517\|PILER-CR	13880-13922	43	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13878-13920	0	1.0
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	NZ_CP011283	Enterococcus faecium strain E39 plasmid p2, complete sequence	57890-57923	0	1.0
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	NZ_CP015517	Enterococcus hirae strain R17 plasmid, complete sequence	13943-13976	0	1.0
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	AP014354	Uncultured Mediterranean phage uvMED isolate uvMED-GF-U-MedDCM-OCT-S39-C41, * SEQUENCING IN PROGRESS *	27009-27040	8	0.75
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	JN638751	Bacillus phage G, complete genome	18610-18641	8	0.75
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	NC_016982	Lactococcus garvieae 21881 plasmid pGL5 complete sequence	56937-56970	8	0.765
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NC_006872	Clostridium perfringens plasmid pBCNF5603 DNA, complete sequence	8508-8539	9	0.719
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NC_010180	Bacillus mycoides KBAB4 plasmid pBWB401, complete sequence	159069-159100	9	0.719
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	CP016196	Bacillus thuringiensis serovar coreanensis strain ST7 plasmid pST7-2, complete sequence	12828-12859	9	0.719
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	NC_015417	Clostridium botulinum BKT015925 plasmid p1BKT015925, complete sequence	90108-90141	9	0.735
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	AB012112	Clostridium botulinum D phage gene for ORF-22, HA3, HA2, HA1, NTNH, NTX, complete and partial sequence	6451-6484	9	0.735
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	ACSJ01000015	Clostridium phage D-1873 CLG.Contig168, whole genome shotgun sequence	12197-12230	9	0.735
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	NC_007581	Clostridium phage c-st, complete genome	74358-74391	9	0.735
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	X72793	Clostridium botulinum C phage BONT/C1, ANTP-139, ANTP-33, ANTP-17, ANTP-70 genes and ORF-22	6725-6758	9	0.735
NZ_CP015517_1	1.6\|13945\|34\|NZ_CP015517\|PILER-CR	13945-13978	34	AP008983	Clostridium phage c-st genomic DNA, complete genome	74358-74391	9	0.735
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NZ_BK010451	Paeniclostridium sordellii strain SSCC37615 plasmid pCSTC2, complete sequence	7639-7670	10	0.688
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NZ_LR214986	Mycoplasma cynos strain NCTC10142 plasmid 13	168553-168584	10	0.688
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	NC_029119	Staphylococcus phage SPbeta-like, complete genome	76686-76717	10	0.688
NZ_CP015517_1	1.3\|13933\|32\|NZ_CP015517\|CRISPRCasFinder	13933-13964	32	KT895374	Bacillus phage vB_BpuM-BpSp, complete genome	5551-5582	11	0.656

1. spacer 1.1|13797|55|NZ_CP015517|CRISPRCasFinder matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

aaataccccttgaatattgttgttgtttaataattataactaggagaaaagtctc	CRISPR spacer
aaataccccttgaatattgttgttgtttaataattataactaggagaaaagtctc	Protospacer
*******************************************************

2. spacer 1.1|13797|55|NZ_CP015517|CRISPRCasFinder matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

aaataccccttgaatattgttgttgtttaataattataactaggagaaaagtctc	CRISPR spacer
aaataccccttgaatattgttgttgtttaataattataactaggagaaaagtctc	Protospacer
*******************************************************

3. spacer 1.2|13876|33|NZ_CP015517|CRISPRCasFinder matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

cttttctctttttggaatcgcaatacaacagct	CRISPR spacer
cttttctctttttggaatcgcaatacaacagct	Protospacer
*********************************

4. spacer 1.2|13876|33|NZ_CP015517|CRISPRCasFinder matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

cttttctctttttggaatcgcaatacaacagct	CRISPR spacer
cttttctctttttggaatcgcaatacaacagct	Protospacer
*********************************

5. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
aaaagagaaatttctcttaatttattaatata	Protospacer
********************************

6. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
aaaagagaaatttctcttaatttattaatata	Protospacer
********************************

7. spacer 1.4|13801|57|NZ_CP015517|PILER-CR matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

ataccccttgaatattgttgttgtttaataattataactaggagaaaagtctcttag	CRISPR spacer
ataccccttgaatattgttgttgtttaataattataactaggagaaaagtctcttag	Protospacer
*********************************************************

8. spacer 1.4|13801|57|NZ_CP015517|PILER-CR matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

ataccccttgaatattgttgttgtttaataattataactaggagaaaagtctcttag	CRISPR spacer
ataccccttgaatattgttgttgtttaataattataactaggagaaaagtctcttag	Protospacer
*********************************************************

9. spacer 1.5|13880|43|NZ_CP015517|PILER-CR matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

tttctctttttggaatcgcaatacaacagctctttagataaaa	CRISPR spacer
tttctctttttggaatcgcaatacaacagctctttagataaaa	Protospacer
*******************************************

10. spacer 1.5|13880|43|NZ_CP015517|PILER-CR matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

tttctctttttggaatcgcaatacaacagctctttagataaaa	CRISPR spacer
tttctctttttggaatcgcaatacaacagctctttagataaaa	Protospacer
*******************************************

11. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to NZ_CP011283 (Enterococcus faecium strain E39 plasmid p2, complete sequence) position: , mismatch: 0, identity: 1.0

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
tttctcttaatttattaatatacttttccaaaaa	Protospacer
**********************************

12. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to NZ_CP015517 (Enterococcus hirae strain R17 plasmid, complete sequence) position: , mismatch: 0, identity: 1.0

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
tttctcttaatttattaatatacttttccaaaaa	Protospacer
**********************************

13. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to AP014354 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-U-MedDCM-OCT-S39-C41, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.75

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
gaaagaaaaatttatcttaatttatggcatta	Protospacer
.*****.****** *********** .   **

14. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to JN638751 (Bacillus phage G, complete genome) position: , mismatch: 8, identity: 0.75

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
gatttagaagtttctcttaatttattgatttc	Protospacer
.*   ****.****************.** *

15. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to NC_016982 (Lactococcus garvieae 21881 plasmid pGL5 complete sequence) position: , mismatch: 8, identity: 0.765

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
tattttcttctttttaaatatacttttccaaaaa	Protospacer
* *.*..*  *** * ******************

16. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NC_006872 (Clostridium perfringens plasmid pBCNF5603 DNA, complete sequence) position: , mismatch: 9, identity: 0.719

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
cctattggaatttcttttaatttatttatatc	Protospacer
   *  *.*******.********** ****

17. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NC_010180 (Bacillus mycoides KBAB4 plasmid pBWB401, complete sequence) position: , mismatch: 9, identity: 0.719

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
tataccatcatttccgttaatttattaatata	Protospacer
 * *  .  *****. ****************

18. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to CP016196 (Bacillus thuringiensis serovar coreanensis strain ST7 plasmid pST7-2, complete sequence) position: , mismatch: 9, identity: 0.719

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
cagcttaagatttcaattaatttattaatata	Protospacer
 *.   .*.*****  ****************

19. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to NC_015417 (Clostridium botulinum BKT015925 plasmid p1BKT015925, complete sequence) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

20. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to AB012112 (Clostridium botulinum D phage gene for ORF-22, HA3, HA2, HA1, NTNH, NTX, complete and partial sequence) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

21. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to ACSJ01000015 (Clostridium phage D-1873 CLG.Contig168, whole genome shotgun sequence) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

22. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to NC_007581 (Clostridium phage c-st, complete genome) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

23. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to X72793 (Clostridium botulinum C phage BONT/C1, ANTP-139, ANTP-33, ANTP-17, ANTP-70 genes and ORF-22) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

24. spacer 1.6|13945|34|NZ_CP015517|PILER-CR matches to AP008983 (Clostridium phage c-st genomic DNA, complete genome) position: , mismatch: 9, identity: 0.735

tttctcttaatttattaatatacttttccaaaaa	CRISPR spacer
taatatttatattattaatatacttttccatata	Protospacer
*  . .***  ******************* * *

25. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NZ_BK010451 (Paeniclostridium sordellii strain SSCC37615 plasmid pCSTC2, complete sequence) position: , mismatch: 10, identity: 0.688

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
tcttcttgaatttctcttaatttataaacata	Protospacer
       .***************** **.***

26. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NZ_LR214986 (Mycoplasma cynos strain NCTC10142 plasmid 13) position: , mismatch: 10, identity: 0.688

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
tagtttctaatttcttttaatttattgatatt	Protospacer
 *.     *******.**********.****

27. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to NC_029119 (Staphylococcus phage SPbeta-like, complete genome) position: , mismatch: 10, identity: 0.688

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
tccattcctatttctcctaatttattaattta	Protospacer
   *     *******.************ **

28. spacer 1.3|13933|32|NZ_CP015517|CRISPRCasFinder matches to KT895374 (Bacillus phage vB_BpuM-BpSp, complete genome) position: , mismatch: 11, identity: 0.656

aaaagagaaatttctcttaatttattaatata	CRISPR spacer
tcttctaaaatttcccttaattcattaataat	Protospacer
      .*******.*******.*******

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

28638 : 42001

Streptococcus_phage(60.0%)

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_002354485.1\|28638_29325_-\|transposase	IS6-like element IS1216 family transposase	A0A1X9I6C6	Streptococcus_phage	2.0e-127	99.6
WP_100249774.1\|30137_30248_-	hypothetical protein	E4ZFP9	Streptococcus_phage	1.9e-08	88.6
WP_002321849.1\|30252_30990_-	23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(B)	E4ZFQ0	Streptococcus_phage	3.7e-135	100.0
WP_001814874.1\|31114_31198_-	23S rRNA methyltransferase attenuation leader peptide	NA	NA	NA	NA
WP_002379942.1\|31419_32106_+\|transposase	IS6-like element ISEnfa1 family transposase	A0A1X9I6C6	Streptococcus_phage	4.8e-113	88.5
WP_000242080.1\|32302_33133_-	undecaprenyl-diphosphate phosphatase	NA	NA	NA	NA
WP_000933358.1\|33132_33882_-	ABC transporter permease subunit	NA	NA	NA	NA
WP_002346952.1\|33874_34792_-	ATP-binding cassette domain-containing protein	A0A2H4PQG7	Staphylococcus_phage	4.6e-42	43.2
WP_000395511.1\|34974_35589_-	helix-turn-helix transcriptional regulator	A0A139ZPI6	Marinitoga_camini_virus	5.5e-07	46.8
WP_000384569.1\|35578_35776_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_001808810.1\|35941_36106_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_002379942.1\|36138_36825_+\|transposase	IS6-like element ISEnfa1 family transposase	A0A1X9I6C6	Streptococcus_phage	4.8e-113	88.5
WP_002321813.1\|36935_37196_-	hypothetical protein	A0A0S2MYI8	Enterococcus_phage	3.4e-11	51.4
WP_002325539.1\|37561_38047_-	single-stranded DNA-binding protein	Q938M7	Temperate_phage	7.5e-44	60.5
WP_063627749.1\|38049_38949_-	nucleotidyl transferase AbiEii/AbiGii toxin family protein	NA	NA	NA	NA
WP_002330563.1\|38964_39558_-	amino acid ABC transporter substrate-binding protein	NA	NA	NA	NA
WP_063627750.1\|39796_42001_-	type IA DNA topoisomerase	A0A1X9I6W8	Streptococcus_phage	1.6e-117	51.3

Anti-CRISPR protein detection

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

2. NZ_CP015516

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP015516_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP015516_1

415104-415231

Orphan

Consensus_repeat	Method
TGAATCACTAAGAACGAAGTGAGTAGATGATGAACAATACTTGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP015516_1

>merge|NZ_CP015516|1|415104-415231|CRISPRCasFinder
TGAATCACTAAGAACGAAGTGAGTAGATGATGAACAATACTTGGCGAACAGAGTGAGCGAAGTTCCCTCTCAAGCGAAGCATGATGAATCACTAAGAACGAAGTGAGTAGATGATGAACAATACTTGG

>NZ_CP015516|1|1|415104-415231|CRISPRCasFinder
TGAATCACTAAGAACGAAGTGAGTAGATGATGAACAATACTTGG	CGAACAGAGTGAGCGAAGTTCCCTCTCAAGCGAAGCATGA
TGAATCACTAAGAACGAAGTGAGTAGATGATGAACAATACTTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP015516.1\|WP_063626533.1\|416356_416572_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223456
NZ_CP015516.1\|WP_063626535.1\|420404_420731_+\|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin	unknown	unknown	gnl\|CDD\|367091
NZ_CP015516.1\|WP_063626528.1\|405745_406630_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|283645
NZ_CP015516.1\|WP_010720158.1\|404686_404857_+\|preprotein-translocase-subunit-SecE	unknown	unknown	gnl\|CDD\|376355
NZ_CP015516.1\|WP_010720092.1\|417728_418406_+\|TVP38/TMEM64-family-protein	unknown	unknown	gnl\|CDD\|223475
NZ_CP015516.1\|WP_063626536.1\|421072_422602_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP015516.1\|WP_010720091.1\|418582_419767_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
NZ_CP015516.1\|WP_010720157.1\|404956_405502_+\|transcription-termination/antitermination-protein-NusG	unknown	unknown	gnl\|CDD\|180161
NZ_CP015516.1\|WP_010720152.1\|412488_413157_-\|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-beta	unknown	unknown	gnl\|CDD\|224674
NZ_CP015516.1\|WP_063626532.1\|411608_412475_-\|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-alpha	unknown	unknown	gnl\|CDD\|129801
NZ_CP015516.1\|WP_010720086.1\|423878_424592_+\|MgtC/SapB-family-protein	unknown	unknown	gnl\|CDD\|224204
NZ_CP015516.1\|WP_010720151.1\|413687_414110_+\|50S-ribosomal-protein-L11	unknown	unknown	gnl\|CDD\|234661
NZ_CP015516.1\|WP_063626537.1\|423031_423733_+\|glucosamine-6-phosphate-deaminase	unknown	unknown	gnl\|CDD\|238693
NZ_CP015516.1\|WP_010720150.1\|414213_414903_+\|50S-ribosomal-protein-L1	unknown	unknown	gnl\|CDD\|180071
NZ_CP015516.1\|WP_063626534.1\|420170_420404_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_063626530.1\|408236_409217_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_063626529.1\|407049_408030_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_063626531.1\|409236_411282_-\|EndoU-domain-containing-protein	unknown	unknown	gnl\|CDD\|373068
NZ_CP015516.1\|WP_010720148.1\|415842_416211_+\|50S-ribosomal-protein-L7/L12	unknown	unknown	gnl\|CDD\|234671
NZ_CP015516.1\|WP_010720149.1\|415286_415790_+\|50S-ribosomal-protein-L10	unknown	unknown	gnl\|CDD\|234632

Protein	Function_ID	Function_description	E-value
NZ_CP015516.1\|WP_063626533.1\|416356_416572_+\|hypothetical-protein	gnl\|CDD\|223456	COG0379, NadA, Quinolinate synthase [Coenzyme metabolism].	0.00357289
NZ_CP015516.1\|WP_063626535.1\|420404_420731_+\|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin	gnl\|CDD\|367091	pfam02452, PemK_toxin, PemK-like, MazF-like toxin of type II toxin-antitoxin system. PemK is a growth inhibitor in E. coli known to bind to the promoter region of the Pem operon, auto-regulating synthesis. This family represents the toxin molecule of a typical bacterial toxin-antitoxin system pairing. The family includes a number of different toxins, such as MazF, Kid, PemK, ChpA, ChpB and ChpAK.	4.06075e-22
NZ_CP015516.1\|WP_063626528.1\|405745_406630_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|283645	pfam06028, DUF915, Alpha/beta hydrolase of unknown function (DUF915). This family consists of several bacterial proteins of unknown function. Members of this family have an alpha/beta hydrolase fold.	1.10774e-77
NZ_CP015516.1\|WP_010720158.1\|404686_404857_+\|preprotein-translocase-subunit-SecE	gnl\|CDD\|376355	pfam00584, SecE, SecE/Sec61-gamma subunits of protein translocation complex. SecE is part of the SecYEG complex in bacteria which translocates proteins from the cytoplasm. In eukaryotes the complex, made from Sec61-gamma and Sec61-alpha translocates protein from the cytoplasm to the ER. Archaea have a similar complex.	4.32122e-12
NZ_CP015516.1\|WP_010720092.1\|417728_418406_+\|TVP38/TMEM64-family-protein	gnl\|CDD\|223475	COG0398, COG0398, Uncharacterized conserved protein [Function unknown].	5.75433e-13
NZ_CP015516.1\|WP_063626536.1\|421072_422602_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	3.47859e-168
NZ_CP015516.1\|WP_010720157.1\|404956_405502_+\|transcription-termination/antitermination-protein-NusG	gnl\|CDD\|180161	PRK05609, nusG, transcription antitermination protein NusG; Validated.	4.49583e-84
NZ_CP015516.1\|WP_010720152.1\|412488_413157_-\|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-beta	gnl\|CDD\|224674	COG1760, SdaA, L-serine deaminase [Amino acid transport and metabolism].	3.8878e-76
NZ_CP015516.1\|WP_063626532.1\|411608_412475_-\|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-alpha	gnl\|CDD\|129801	TIGR00718, Probable_L-serine_dehydratase_alpha_chain, L-serine dehydratase, iron-sulfur-dependent, alpha subunit. This enzyme is also called serine deaminase. L-serine dehydratase converts serine into pyruvate in the gluconeogenesis pathway from serine. This model describes the alpha chain of an iron-sulfur-dependent L-serine dehydratase, found in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of alpha chains from the homologous region of single chain forms such as found in Escherichia coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis].	1.09646e-100
NZ_CP015516.1\|WP_010720086.1\|423878_424592_+\|MgtC/SapB-family-protein	gnl\|CDD\|224204	COG1285, SapB, Uncharacterized membrane protein [Function unknown].	1.09669e-47
NZ_CP015516.1\|WP_010720151.1\|413687_414110_+\|50S-ribosomal-protein-L11	gnl\|CDD\|234661	PRK00140, rplK, 50S ribosomal protein L11; Validated.	9.72997e-95
NZ_CP015516.1\|WP_063626537.1\|423031_423733_+\|glucosamine-6-phosphate-deaminase	gnl\|CDD\|238693	cd01399, GlcN6P_deaminase, GlcN6P_deaminase: Glucosamine-6-phosphate (GlcN6P) deaminase subfamily; GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium. The reaction is an aldo-keto isomerization coupled with an amination or deamination. It is the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate (GlcNAc6P). GlcN6P deaminase is a hexameric enzyme that is allosterically activated by GlcNAc6P.	7.31862e-115
NZ_CP015516.1\|WP_010720150.1\|414213_414903_+\|50S-ribosomal-protein-L1	gnl\|CDD\|180071	PRK05424, rplA, 50S ribosomal protein L1; Validated.	1.55211e-146
NZ_CP015516.1\|WP_010720091.1\|418582_419767_+\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like 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.	4.9779e-70
NZ_CP015516.1\|WP_063626531.1\|409236_411282_-\|EndoU-domain-containing-protein	gnl\|CDD\|373068	pfam14436, EndoU_bacteria, Bacterial EndoU nuclease. This is a bacterial virion of EndoU nuclease. It is found at C-terminal region of polymorphic toxin proteins.	2.25856e-14
NZ_CP015516.1\|WP_010720148.1\|415842_416211_+\|50S-ribosomal-protein-L7/L12	gnl\|CDD\|234671	PRK00157, rplL, 50S ribosomal protein L7/L12; Reviewed.	9.48622e-45
NZ_CP015516.1\|WP_010720149.1\|415286_415790_+\|50S-ribosomal-protein-L10	gnl\|CDD\|234632	PRK00099, rplJ, 50S ribosomal protein L10; Reviewed.	2.17032e-67

>NZ_CP015516.1|WP_010720150.1|414213_414903_+|50S-ribosomal-protein-L1
MAKKSKKMQDALKKVDSSKVYPVAEAVALAKETNIAKFDATVEVAYRLNVDPKKADQQIRGAVVLPNGTGKTQTVLVFAKGDKAKEAEAAGADFVGDDDMVQKIQNGWFDFDVVVATPDMMATVGRLGRVLGPKGLMPNPKTGTVTMDVTKAVNEVKAGKVTYRVDKAGNIHVPIGKVSFDNEKLVENFATIHDVLVKAKPSAAKGQYMKNITVTTTFGPGIHVDQASF
>NZ_CP015516.1|WP_010720151.1|413687_414110_+|50S-ribosomal-protein-L11
MAKKVEKIVKLQIPAGKATPAPPVGPALGQAGINIMGFTKEFNARTADQAGLIIPVVISVYEDRSFTFVTKTPPAAVLLKKAAKIDKGSGEPNKTKVAKVSSDQVKEIAELKMEDLNAADIEAAMRMVEGTARSMGITVE
>NZ_CP015516.1|WP_010720152.1|412488_413157_-|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-beta
MKELRYRSVFDIIGPVMIGPSSSHTAGAARIGKIVRSIFGEQPDSVDIYLYESFAKTYRGHGTDIALVGGLLGMEPDDERLADSLQLAYEAGMEVLFVPKGEKAEHPNSVKLLLKKGKRKLSVTGISIGGGNIQISELNGFKISLSMGTPTFIIVHQDVPGMIAKVTNILSETNTNIGTMTVTRESKGENAIMIIEVDDPQVDDTISKLTQLPKIDSVNYFD
>NZ_CP015516.1|WP_063626532.1|411608_412475_-|L-serine-ammonia-lyase,-iron-sulfur-dependent,-subunit-alpha
MFFSIEELVRQAENYPSVAELMIAVEMEMSGRPREQIIAIMEKNLSVMEQSITEGNEGVTSVTGITGGDAQKLARYLKEADFLSGETILSAVRNAIAVNEVNAKMGLICATPTAGSAGVVPGVLMAVRDRLSLTHEQQIEFLFTAGAFGLVIANNASISGAEGGCQAEVGSASAMAAAALVCAKNGTPHQAAQAIAITLKNMMGLICDPVAGLVEVPCVKRNALGSSQAFISADMALAGIESVIPPDEVVAAMYQVGRQMPAIFKETAEGGLAVTPTAKRLTAELLNH
>NZ_CP015516.1|WP_063626531.1|409236_411282_-|EndoU-domain-containing-protein
MKNKKLTWGCWWLVLYLLLTTILPPSIIAFATDHTLHSASREAPVTFTLPNALSSPEEPQKITEIEKLKFEKDPSSLSSQRNVFDNLILNDYLDLMYGPAFLPLSTRFNLAPIAPIIQAVTLAEFTTPYLKPGAQETALSQAYRLTQKKLLRHTLAVFDEIIDHPENPTDLDEFSKMEMASWIALQNQFIDYLNVSPDLSGYQLIKTKEKLTFRPKTTDGQSLLVYLENSINNYYPGNIKIPPRIGSLQEITFVPSMWTDKQVNATFAFTAYDHEKQTYNNYSSNTINIAIETDFDTFLNQMDTPETVLQFFLNHATVQIGAIPPTDVDTVNRTGKDITGAMIKERDQLISQFPETFYTNFFRIVAQANGQDLVLNREGAFVYRGTQTVVPMEQITIGYNQQVIYSLRKVQKFFGIYATYYALADGLYDEERTDALPKTLNDDTVNVLEEIGGNVLKNLPNYENTELRIKQSEMKIEPLDVLLVAMCLPWSEMRSLLTTVERGELIGAVEVEEAQAKTILAAEEEILLKGCPNKGIVEKIQPTKYFKRKTLNHLAGEVKPGKDGVPNLSGAHSRHPDFYRKESGIIYEPIGEVKKGMPYEAKVKYAGKYKEANSTVFPDDWDAEKIMKEVEQIISETTFNGTGNKPFSGKASNGLFEIQGHVNIKENGKITISTVYPLVKK
>NZ_CP015516.1|WP_063626530.1|408236_409217_+|hypothetical-protein
MRVFFPDPQRRPQKAIQEMTVKLTKKFQAIDERLTLEHFDDFVDYGPEVFPQLAPLYWDPRVPNHPMEHFVYYEYVLRLNGFPIYVITPYSEVIDKTYTRKGRDKDPFWSLMRRIDPEILSLIHDYQIQNLHYWRDLYSVTQFQAEINKINSRVSLIPEKTNNEARTLLFIDPKQRDPEFVRRTTEQMAQELAELDPHLSVVYHEDFIDFGPEDGLFLSECPFDPEEDDSDDPRAGLADTEYTVYYEDTILYASTPYSLGYGYHGDYFRGGIPSTEYLGLSQELTAEILKILHTFKIYNKYYWRHLYTPAEFQTEIRRYQKSWDLE
>NZ_CP015516.1|WP_063626529.1|407049_408030_+|hypothetical-protein
MRVFFPDPQRRPQKDIQEMTAKLTKQFQAIDERLTLEHFYDFVDYGPEVFPQLAPLYWDPRVPNHPMEHFVYYEYVLRLNGFPIYVITPYSEVIDKTYTRKGRDKDPFWSLMRRIDPEILSLIHDYQIQNLHYWRDLYSVTQFQAEINKINSRVSLIPEKTNNEARTLLFIDPKQRDPEFVRRTTEQMAQELAELDPHLSVVYHEDFIDFGPEDGLFLSECPFDPEEDDPDDPRAGLADTEYTVYYEDTILYASTPYSLGYGYHGDYFRGGIPSREYLGLSQEFTAEILRIMNKFSLYNYYYWRHLYTPADFQTEIRRYQKSWDLE
>NZ_CP015516.1|WP_063626528.1|405745_406630_+|alpha/beta-fold-hydrolase
MKNWRKSGIVGFLLMVSVLFISGCQTKETSQSSEAAKTVETTQATKEKETQSTTPTLFFHGYSGTVNSFKGMIQRLESSESGKKELTLTVDVNGNVQAEGELSKEADNPMIQVLFVDNKNNEWNQTEWIKDCLSYLQQTYGINQVNLVGHSMGGVSGLRYLATYGQDQTLPKVDKFVAIAAPFNDFEENNGQSISDELANGPAIASSRYQDYQRLIGNVPTTTQILLIAGQVSETDLSDGTVPLSSALAVYALLKQHGNQVEEKVITGENVTHSMLHEDKEVDALTRQFLWNID
>NZ_CP015516.1|WP_010720157.1|404956_405502_+|transcription-termination/antitermination-protein-NusG
MESFEKNWYVLHTYSGYENKVKANIESRAQSMKMADFIFRVVVPEETEKEVKNGKEKEIVHKTFPGYVLVEMIMTDASWYVVRNTPGVTGFVGSHGAGSKPAPLLPEEVSHILRSIGMSLRQTDLEIEVGEVIKIIEGAFAGLEGQVTEVDEEKEKLKVNIDMFGRETSTELDFEQVDKID
>NZ_CP015516.1|WP_010720158.1|404686_404857_+|preprotein-translocase-subunit-SecE
MKFIKSVKDEMKQVTWPSGKQLRKDTLVVIETSIIFGVMFFVMDTAIQSLFAYLLK
>NZ_CP015516.1|WP_010720149.1|415286_415790_+|50S-ribosomal-protein-L10
MSEAIIAKKAAIVDEVSEKFTAAASVVVVDYRGLTVDEVTRLRKQLRDANVEMKVIKNSILSRAAKKAGLEGLDEVFTGPTAVAFSNEDVVAPAKIMDEFAKEAKALEIKGGIIEGKVSSLEEITALAKLPNREGLLSMLLSVLQAPVRNVAYAVKAVADKEDGDAA
>NZ_CP015516.1|WP_010720148.1|415842_416211_+|50S-ribosomal-protein-L7/L12
MAMNIENIVAELKEATILELNDLVKAIEEEFGVSAAAPVAAVAAGGAAAAEEQTEFTVELTAAGDQKVKVIKAVREATGLGLKEAKAVVDGAPAPVKEGVSKEEAEELKAKLEEVGASVTVK
>NZ_CP015516.1|WP_063626533.1|416356_416572_+|hypothetical-protein
MELYKMLSPADIQFLKTKLNVIIQDRNYTDDEVVQIYDKIEDFHILQSFDENYNLSEDGRHALDILYLDIW
>NZ_CP015516.1|WP_010720092.1|417728_418406_+|TVP38/TMEM64-family-protein
MKTKKLRVFLIIIGLLLILFIGYRLYLEYQTDIQMFLDPKTSRQALLDQIRSHGFRTALFLILLISVMCAVPGIPTSVIGVLVGLSYGPLLGTLINVSGNAFGNMLSIFLMQHLKLFDHSKKSNRWVTAIRNMKHPKIGVMVGYMVPVIPSSVINFAAMTLNLQIRDIILSIVIGVIPSSILYACGGEALFHGYSKTALLLVASVLILTLLVVIIYKDRRKRHVK
>NZ_CP015516.1|WP_010720091.1|418582_419767_+|MFS-transporter
MDKNEKTTLTSSLILLLSITCGVVVANMYYIQPIGTKVATSLSVSTSAIGILTMLTQLGYALGLLFLVPLGDVVDRPKLIIRMAALSAISLLAAFFAPSFTLFACASFLIGLLSIVPQIIIPYGAVLAGPKARGKVMGTLLSGLLVGILLSRTVSGIVASLFSWRMIYLFALVLVAILTGLLYWKMPRTQIKTTSSVSYLDSLKSLPYLVKTQRLLREASISGFFMFGTFSIFWSTLIFYISSPVYHWGTFEAGILAIFGLSGAVAAPIVGRLSDSYSERKIVGMGLAMQTLSFVALLVAGSHLVVLLVAIILLDVGNQFGQVANQTRVQGLGEAASNRNNTVFMFMYFIGGATGSLLGTTMWQQFGWLGVTLTGLAFQLCAYICQYIIFQKRS
>NZ_CP015516.1|WP_063626534.1|420170_420404_+|hypothetical-protein
METVARKIGNSVGAIFPKDISPKVGELFTILKVGEAYILKPKKEDIFKNEKAWEGFRESITAEESEWESMKLEGEEY
>NZ_CP015516.1|WP_063626535.1|420404_420731_+|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin
MKYPKQKDIIWIDFDPSKGKEIRKRRPALVVSRDEFNERTGFCLVCPITSTKRNFATYIEIKDPQKIVGEVATHQLRSVDYTTRNIEKIEQCDLLTWIEVVEVIGMFI
>NZ_CP015516.1|WP_063626536.1|421072_422602_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MSLLTLTNITQQFGDKILYENVQLQVNAGEHLGLIGQNGAGKSTLIKIITGEILPDDGQVHWQKNIHRGYLDQYVAVDETLTIEEFLKTAYSDEFKKEALITQLYQEYSETMEEALLEKAGKLQTELDQGVFYQIDTLVAEMSSGLGIDVLGLSTPLKKLSGGQRSKVILAKLLLENPDVLILDEPTNHLDDQHIQWLTQFLQSFEGAYIVISHDQEFLDKITTHIADIEFGKITKYTGHLKQALRQKEQNRESYLRQFHAQQKHIEKTEAYIRKYKAGSRSTMAKSRQKQLDKIERLTPPASTAKPIFDFPYSPIVTTLAVETTDLVIGYDRPLLLPINLTIRFGEKVAIRGFNGIGKSTLLKTLIGEIEQLAGEYHFPDNTAINYFSQDLIWEKPLETPLQYLGAQFPKATVKELRRQLAKSGLVNQLASEPLSTLSGGEQTKVKLAQLTMNQGNLLILDEPTNHIDHETKDSLQTGIKHFPGTVIIVSHEQEFYQDLVDRVIEIEG
>NZ_CP015516.1|WP_063626537.1|423031_423733_+|glucosamine-6-phosphate-deaminase
MEIIRVKNAEEGGKKAFEFIKKGMENGAKVLGLATGSTPITLYKEMTSSDLDFSDMTSVNLDEYVGLGGSDDQSYRHFMNSQLFDKKPFKESYVPDGKAADLEAACQEYDEILEQHPIDIQILGIGQNGHIGFNEPGAPFDGTTSVVDLTESTINANKRFFEKAEDVPTKAVSMGIGSILKGKEIVLLAYGENKADAIKGMIQGPMTTDLPASALQEHDNVIVIIDDAAGSKL
>NZ_CP015516.1|WP_010720086.1|423878_424592_+|MgtC/SapB-family-protein
MDEMILSVPEIILRLGIALIFGGAIGFERQYKNRPAGMRTHILVCMGACIIALIQVEIASKALRDALEYPELVGTIRSDEARLIAQVVSGVGFLGAGTIIVTKQSVTGLTTAASLWAIAGLGIAIGMGFYWIAIISFIGIVIALTVVKKIIHVPTTKKLEIQYIHRKETKDFLTEYFEQRGIIIEDVNFDVDFVEDYRVYKNIYTIDLPKDMTYADVIEELSVHKNIMKLHLVSVAQ

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Crispr_ID: NZ_CP015516_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP015516_2

1349472-1349772

Orphan

II-A,II-B

Consensus_repeat	Method
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC	PILER-CR
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	CRISPRCasFinder
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	CRT

4 spacers

The CRISPR arrays of NZ_CP015516_2

>merge|NZ_CP015516|2|1349472-1349772|PILER-CR,CRISPRCasFinder,CRT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACTAAACTTGTGTAGGGCGTGGCTTTGATCCTGTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACAGGGACTTACTGGGATAAGTATCCTCTTGAGTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACATTGTAAACGGAGAGCTGTTTGGGGCGACGGTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACAAAATGAATGAGACGGAAAAATGCGCTACAGTTTTAGAGCTATGTTGTTTTGAATGTTTCTGAACTA

>NZ_CP015516|2|1|1349472-1349705|PILER-CR
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC	TAAACTTGTGTAGGGCGTGGCTTTGATCCT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC	AGGGACTTACTGGGATAAGTATCCTCTTGA
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC	ATTGTAAACGGAGAGCTGTTTGGGGCGACG
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC

>NZ_CP015516|2|2|1349472-1349772|CRISPRCasFinder
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACT	AAACTTGTGTAGGGCGTGGCTTTGATCCT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	GGGACTTACTGGGATAAGTATCCTCTTGA
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	TTGTAAACGGAGAGCTGTTTGGGGCGACG
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	AAATGAATGAGACGGAAAAATGCGCTACA
GTTTTAGAGCTATGTTGTTTTGAATGTTTCTGAACTA

>NZ_CP015516|2|1|1349472-1349772|CRT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACT	AAACTTGTGTAGGGCGTGGCTTTGATCCT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	GGGACTTACTGGGATAAGTATCCTCTTGA
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	TTGTAAACGGAGAGCTGTTTGGGGCGACG
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAACA	AAATGAATGAGACGGAAAAATGCGCTACA
GTTTTAGAGCTATGTTGTTTTGAATGTTTCTGAACTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP015516.1\|WP_063627090.1\|1357177_1357990_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|270318
NZ_CP015516.1\|WP_063627088.1\|1355775_1356498_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213225
NZ_CP015516.1\|WP_063627083.1\|1348651_1349287_+\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234771
NZ_CP015516.1\|WP_063627078.1\|1340510_1341791_+\|dihydroorotase	unknown	unknown	gnl\|CDD\|236479
NZ_CP015516.1\|WP_063627081.1\|1347012_1347942_+\|dihydroorotate-dehydrogenase	unknown	unknown	gnl\|CDD\|235982
NZ_CP015516.1\|WP_063627092.1\|1361198_1362239_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380548
NZ_CP015516.1\|WP_010737550.1\|1358286_1359996_-\|fibronectin/fibrinogen-binding-protein	unknown	unknown	gnl\|CDD\|336217
NZ_CP015516.1\|WP_063627079.1\|1342875_1346061_+\|carbamoyl-phosphate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|235393
NZ_CP015516.1\|WP_010719216.1\|1338269_1339553_+\|uracil-transporter	unknown	unknown	gnl\|CDD\|236744
NZ_CP015516.1\|WP_063627084.1\|1350683_1351388_+\|carbonic-anhydrase-family-protein	unknown	unknown	gnl\|CDD\|239398
NZ_CP015516.1\|WP_034697869.1\|1341796_1342873_+\|carbamoyl-phosphate-synthase-small-subunit	unknown	unknown	gnl\|CDD\|237139
NZ_CP015516.1\|WP_063627086.1\|1353431_1354664_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_010719207.1\|1350010_1350652_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|378993
NZ_CP015516.1\|WP_063627080.1\|1346239_1347016_+\|dihydroorotate-dehydrogenase-electron-transfer-subunit	unknown	unknown	gnl\|CDD\|99814
NZ_CP015516.1\|WP_063627091.1\|1360198_1360843_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_063627082.1\|1347938_1348655_+\|orotidine-5'-phosphate-decarboxylase	unknown	unknown	gnl\|CDD\|234695
NZ_CP015516.1\|WP_010719215.1\|1339565_1340492_+\|aspartate-carbamoyltransferase-catalytic-subunit	unknown	unknown	gnl\|CDD\|234849
NZ_CP015516.1\|WP_063627085.1\|1351384_1352293_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656
NZ_CP015516.1\|WP_063627089.1\|1356494_1357166_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224922
NZ_CP015516.1\|WP_010719217.1\|1337716_1338256_+\|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR	unknown	unknown	gnl\|CDD\|235365

Protein	Function_ID	Function_description	E-value
NZ_CP015516.1\|WP_063627090.1\|1357177_1357990_+\|hypothetical-protein	gnl\|CDD\|270318	cd13600, PBP2_lipoprotein_like_1, Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; the type 2 periplasmic binding protein fold. This subgroup shares significant sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.	1.02289e-95
NZ_CP015516.1\|WP_063627088.1\|1355775_1356498_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213225	cd03258, ABC_MetN_methionine_transporter, ATP-binding cassette domain of methionine transporter. MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	2.40353e-107
NZ_CP015516.1\|WP_063627083.1\|1348651_1349287_+\|orotate-phosphoribosyltransferase	gnl\|CDD\|234771	PRK00455, pyrE, orotate phosphoribosyltransferase; Validated.	8.01052e-83
NZ_CP015516.1\|WP_063627078.1\|1340510_1341791_+\|dihydroorotase	gnl\|CDD\|236479	PRK09357, pyrC, dihydroorotase; Validated.	0
NZ_CP015516.1\|WP_063627081.1\|1347012_1347942_+\|dihydroorotate-dehydrogenase	gnl\|CDD\|235982	PRK07259, PRK07259, dihydroorotate dehydrogenase.	0
NZ_CP015516.1\|WP_063627092.1\|1361198_1362239_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|380548	cd06325, PBP1_ABC_unchar_transporter, type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.	1.22731e-113
NZ_CP015516.1\|WP_010737550.1\|1358286_1359996_-\|fibronectin/fibrinogen-binding-protein	gnl\|CDD\|336217	pfam05833, FbpA, Fibronectin-binding protein A N-terminus (FbpA). This family consists of the N-terminal region of the prokaryotic fibronectin-binding protein. Fibronectin binding is considered to be an important virulence factor in streptococcal infections. Fibronectin is a dimeric glycoprotein that is present in a soluble form in plasma and extracellular fluids; it is also present in a fibrillar form on cell surfaces. Both the soluble and cellular forms of fibronectin may be incorporated into the extracellular tissue matrix. While fibronectin has critical roles in eukaryotic cellular processes, such as adhesion, migration and differentiation, it is also a substrate for the attachment of bacteria. The binding of pathogenic Streptococcus pyogenes and Staphylococcus aureus to epithelial cells via fibronectin facilitates their internalisation and systemic spread within the host.	0
NZ_CP015516.1\|WP_063627079.1\|1342875_1346061_+\|carbamoyl-phosphate-synthase-large-subunit	gnl\|CDD\|235393	PRK05294, carB, carbamoyl-phosphate synthase large subunit.	0
NZ_CP015516.1\|WP_010719216.1\|1338269_1339553_+\|uracil-transporter	gnl\|CDD\|236744	PRK10720, PRK10720, uracil transporter; Provisional.	6.38797e-148
NZ_CP015516.1\|WP_063627084.1\|1350683_1351388_+\|carbonic-anhydrase-family-protein	gnl\|CDD\|239398	cd03124, alpha_CA_prokaryotic_like, Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.	3.18911e-65
NZ_CP015516.1\|WP_034697869.1\|1341796_1342873_+\|carbamoyl-phosphate-synthase-small-subunit	gnl\|CDD\|237139	PRK12564, PRK12564, carbamoyl-phosphate synthase small subunit.	0
NZ_CP015516.1\|WP_010719207.1\|1350010_1350652_+\|HD-domain-containing-protein	gnl\|CDD\|378993	pfam12917, HD_2, HD containing hydrolase-like enzyme. This is a family of bacterial and archaeal hydrolases.	6.69905e-57
NZ_CP015516.1\|WP_063627080.1\|1346239_1347016_+\|dihydroorotate-dehydrogenase-electron-transfer-subunit	gnl\|CDD\|99814	cd06218, DHOD_e_trans, FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.	2.13591e-105
NZ_CP015516.1\|WP_063627082.1\|1347938_1348655_+\|orotidine-5'-phosphate-decarboxylase	gnl\|CDD\|234695	PRK00230, PRK00230, orotidine-5'-phosphate decarboxylase.	1.48823e-127
NZ_CP015516.1\|WP_010719215.1\|1339565_1340492_+\|aspartate-carbamoyltransferase-catalytic-subunit	gnl\|CDD\|234849	PRK00856, pyrB, aspartate carbamoyltransferase catalytic subunit.	1.32084e-168
NZ_CP015516.1\|WP_063627085.1\|1351384_1352293_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	2.92695e-41
NZ_CP015516.1\|WP_063627089.1\|1356494_1357166_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224922	COG2011, AbcD, ABC-type metal ion transport system, permease component [Inorganic ion transport and metabolism].	1.85321e-62
NZ_CP015516.1\|WP_010719217.1\|1337716_1338256_+\|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR	gnl\|CDD\|235365	PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR.	2.34565e-97

>NZ_CP015516.1|WP_063627083.1|1348651_1349287_+|orotate-phosphoribosyltransferase
MNTIEKNIAKDLLAIEAVFLSPNEPFTWASGLKSPIYCDNRITMSYPKVRKAIAQGLAEKIKQAFPDVEVIAGTATAGIPHAAWVAEILDLPMVYIRSKAKDHGKGNQIEGRIFEGQKMVVIEDLISTGQSVLEATEAAKREGANVLGVAAIFMYELPAGEENFAKAELPLFTLTNYSVLIETALAEKYIDEAELALLKEWKKNPADWLKQ
>NZ_CP015516.1|WP_063627082.1|1347938_1348655_+|orotidine-5'-phosphate-decarboxylase
MNQRPIIALDFSTWQEVEQFMQLFPEEEKLFVKIGMELFYQEGPIIVRWLKDAGHEVFLDLKLHDIPNTVEKAMRGLAKLGVDITCVHAAGGIKMMQAALRGLEEGTPAGKKRPLLLAITQLTSTSEADMHHDQLIQVPLEESVIHYAKCAEAAGLDGVVSSALEVSGIKTATRQDFICLSPGIRPEGSVAGDQTRIVTPAQARGIGSTFIVVGRPITQAKDPYQAYQTIKEEWSRSI
>NZ_CP015516.1|WP_063627081.1|1347012_1347942_+|dihydroorotate-dehydrogenase
MSNPLAIKLPGLELKNPIMPASGCFGFGKEYGKYYDLNQLGSIMVKATTPHARFGNPTPRVAETPSGMLNAIGLQNPGLEVVMNELLPELAVYPDLPIIANVAGACEEDYVEVCRKIGEAPNVKAIELNISCPNVKHGGIAFGTDPDVAFQLTQAVKKVASVPVYVKLSPNVTDIVPIAQAIESGGADGFTMINTLLGMRIDLKTRQPILANQTGGLSGPAIKPVAIRLIHQVAAVSELPIIGMGGVQTVDDVLEMFMAGASAVAVGTANFTDPYICPKLIEELPVRMAELGIESLQQLIKEVREERMK
>NZ_CP015516.1|WP_063627080.1|1346239_1347016_+|dihydroorotate-dehydrogenase-electron-transfer-subunit
MKQEVMTIIQQTQLAPRIYELTLKGELVKEMSIPGQFLHIRVPRADLLLRRPISIHSIDQQNHTCQIIYRIEGEGTKEFSTLKAGDSLDVLGPLGNGFDLSGLSTGDEVFIVGGGIGIPPLYELAKQLNMRGVKVTNFLGFASKEVMYHEAKFHELGETRVATDDGTYGIHGNVGNLLMSTHKQPKAVFACGANGLLKTVEQLFVAHPNVQLSLESRMACGIGACYACVCHRPDDETGTKSVKVCDEGPIFKVGEVVL
>NZ_CP015516.1|WP_063627079.1|1342875_1346061_+|carbamoyl-phosphate-synthase-large-subunit
MPKRTDIKKIMVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDQEIADQVYIEPITLEFVSRILRKERPDALLPTLGGQTGLNMAMELAESGILDELGIELLGTKLSAIDQAEDRDLFKKLMEELNQPIPESEIVTTVEEAVEFANKIGYPIIVRPAFTLGGTGGGMCKNEEELRVIAENGLSLSPVTQCLIERSIAGFKEIEYEVMRDSADNAIVVCNMENFDPVGIHTGDSIVFAPSQTLSDHEYQLLRDASLAIIRALKIEGGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIALGLTLDEMKNPVTGTTYAEFEPALDYVVAKIPRWPFDKFENGERVLGTQMKATGEVMAIGRNIEESLLKAVRSLEIGTHHLELPELNMIDDSELIEKVVRAQDDRLFYVAEAIRRGYPIEELAELTKIDLFFLDKLLHIVELETELLEHPQDANVLRTVKQNGFTDQKIAELWKTEAKQIRELREKSDIKPVYKMVDTCAAEFASQTPYFYSSYEVENESERSAKDSVLVLGSGPIRIGQGVEFDYATVHSVKAIQQAGYEAIIMNSNPETVSTDFSISDKLYFEPLTFEDVMNVIELEQPIGVIVQFGGQTAINLAEPLVQAGVKILGTTIEDLDRAENRDLFEQALRSLEVPQPLGDTATSKEEAVGIASKIGYPVLVRPSYVLGGRAMEIVENQQDLEDYMEHAVKASPEHPVLIDRYLLGSECEVDAICDGETVLIPGIMEHIERAGVHSGDSMAVYPPQALSAEIKQTIEDYTIRLARGLNCIGMMNIQFVIHDNQVYVIEVNPRASRTVPFLSKVTGIPMAQIATKAILGEKLSDLGFTNGLYPESNAVHVKAPVFSFTKLQQVDTYLGPEMKSTGEVMGSDQNLDKALYKAFEASGLRLPDYGAVLFTIADETKEEALALAKRFSEIGYSLLATKHTAAYFEKNGLIVTPVAKISEKATEKNVVELIREGKAQVVVNTIDKDRGNASKDGFIIRREAVEHGIPLFTSLDTADAIIRVMESRAFSTQAI
>NZ_CP015516.1|WP_034697869.1|1341796_1342873_+|carbamoyl-phosphate-synthase-small-subunit
MERLLILEDGTVFKGKAFGANNNVFGEIVFTTSMTGYQETITDQSFNGQIITFTYPMVGNYGVNRDDYESIAPTCKGVVVKEHARVASNWRSQMTLDEFLKRKGIPGISGVDTRALTRKIRQVGTMKASIVDAGDSFEHAFDQLKATVLATNQVQQVSTSKPYPSPGTGKNVAVIDFGLKHSILRELSKRNCNLTVLPYNTDAKTILSLAPDGVMLTNGPGDPKDVPEAIEMIREIQGKIPIFGICLGHQLFALANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEKTVDPDQLLITHVEVNDGTVEGIRHRHYPAFSVQFHPDAAPGPHDALHLFDEFMEMMDAGEEK
>NZ_CP015516.1|WP_063627078.1|1340510_1341791_+|dihydroorotase
MKTLIKNGQINTRKNETTPAEIWIENGKIKAIGEGFSEAEFDEVFDAKGQLITPGLVDVHVHLREPGFTYKETIAAGTKAAARGGFTTVCAMPNLNPVPDTPEKLKQVYDLIKRDAVVKVLQYAPITENLRSEVLVDQEAMIKAGAFAFTNDGVGVQTAGTMYQAMKEAAKNNKALVAHTEDESLLFGGVMHAGDKAKELGLPGILSVTESSQIARDLLLAEATGVHYHVCHVSTKESVRVIRDAKKAGIHVTAEVSPHHLILIDEDIPEDFGFWKMNPPLRGKEDREALIEGLLDGTIDCIATDHAPHGLEEKSKSFLESPFGIVGSETAFQLIYTHFVETNRFTLEQVINWMATKPAEIFQLEAGTLTVGAPADVAVFDIEHSSTIDKKDFLSKGENTPFVGWNVKGETLGTFVDGKLVWHKGE
>NZ_CP015516.1|WP_010719215.1|1339565_1340492_+|aspartate-carbamoyltransferase-catalytic-subunit
MIIKSERISLKHLLTVEALTDQEVMGLIRRGQEFKQGANWTPQKPQYFATNLFFENSTRTHKSFDVAEKKLGLEVIEFEASTSSVQKGETLYDTVLTMSALGVDVAVIRHGDENYYDELIQSKTIQCSIINGGDGSGQHPTQCLLDLMTIYEEFGYFEGLKVAIVGDITHSRVAKSNMQMLKRLGAQVFFSGPREWYDEEFEVYGHYLPLDELLEQVDVMMMLRVQHERHDGKESFSKEAYHQEYGLTVERAKKLQKHAIIMHPAPVNRDVELADSLVEGLQSRIVQQMSNGVFVRMAILEAVLNGKA
>NZ_CP015516.1|WP_010719216.1|1338269_1339553_+|uracil-transporter
MSEQKKFHNHDAVLDIHDRPKTGHWIGLSLQHLFTMFGATVLVPILVGIDPGIALVSSGLGTLVYLFTTKGKIPAYLGSSFAFIAAMQMLMKTDGYPAIAQGAVTTGLVYLIVAWIIKKIGSAWLDKILPPIVVGPVIMVIGLGLAANAATNAMYNQGNYDFKYIAVALITLALTIFFNMWLKGFLGLIPILLGIICGYLVALLFGIVDTKPIADAAWFALPNFEIPFVQYEPKLYLGAITTMAPIAFVTMTEHIGHLMVLNKLTKRNFFEEPGLHKTLMGDGLAQIVAAFVGGPPVTSYGENIGVLAITRVHSVFVIGGAAVFAVILGFVGKLSALILSIPGPVISGISFILFGVIAASGMKILIENKIDFDKKKNLLIASVILVVGIGGLVFEVGTFTLSAMALATVLGIILNLILPETSRSEEK
>NZ_CP015516.1|WP_010719217.1|1337716_1338256_+|bifunctional-pyr-operon-transcriptional-regulator/uracil-phosphoribosyltransferase-PyrR
MQAKEVVDQVTMKRALTRITYEIIERNQTIQDVVLIGIKTRGIYIASRVADRLKQLEGIEVPVGELDITLYRDDKKETPAEAELHSSDIPVSLEGKEVILIDDVLYTGRTIRAAMDAVMDYGRPRKISLAVLVDRGHRELPIRADYVGKNIPTAKTEEILVEMQELDGKDRIMILKEEE
>NZ_CP015516.1|WP_010719207.1|1350010_1350652_+|HD-domain-containing-protein
MGLNEFILGLNNLEKITRAPGFFKFTEHTVAAHSYRVASIAQVLGDIEEVHGQAIDWKLLYEKALNHDYTERFIGDIKTPVKYANKELRGMLQTVEEKMTDEFINQEIPEEFQEVYRRRLFEGKDDTVEGELLAISDKVDLLYESFEEIIKNNPEKVYKEMFIEAVTTIKGFEHRPSVKYFFNEIFPELLNQEFYGKEDFLATVSTIVKNSQQ
>NZ_CP015516.1|WP_063627084.1|1350683_1351388_+|carbonic-anhydrase-family-protein
MKKNMDVEWGYTGERGPEHWAELCDWFAKGAAFELQSPIPLTTCEPAKDQSDTIAFHYQKQRFTDKEFKNTIHLVPYDQLSYVEFKGQKYYLTDIHFHMPSEHLINGNQEDIEFHFVHMNAKKENLVVGVMFQLTTDEGWLYDRDNGDSWDVEKHEHWTNPMVLFPEQKSHYHYVGSLTTPPTSGPIQWFVMDQVQKLNKDFLIPFKGQYAQPNNRPLQPLKNRPISYFVRDHQ
>NZ_CP015516.1|WP_063627085.1|1351384_1352293_+|LysR-family-transcriptional-regulator
MNFQQLKYVIAVANNGSFREAAKKLYVAQPSLSAGIKELETELGITLFTRTNRGAYLTEEGQEFIKRAERILLQLESLENYYLTNEKRESFSIASQHYDFLGPLTAKLISSFKSEIKQFRIIETTTANVIEEVKDQHSEIGILYMNEHNQAGIKRYLEQGELVAHSLGEFQTHIFLRQGHPLSEKKEIFKEELLPYPQVRFTQDGNNFPYFYEDLIESPDQETVIYTSDRGTLMNIVLETDAYASGSGLVIGEIKEYLRLIPLANSPQNELYVIYSAKRQLSEIAQKFMESLTVLLSQIKTN
>NZ_CP015516.1|WP_063627086.1|1353431_1354664_+|hypothetical-protein
MRLDKMIVTFINALSIASGIGGARALPSLDNQNQGRGLGKVLDLENRNETTRLSDKTYSHKKLHSKHRNKGNLKHLDKIQDDVSRQPYSAKKFLHKKIKNLIKQEETDFKKLKEGISTESSIEVNQLQTNLRRVQNFCSKFRKLRNDIVIEYGKMTQQKVNLRKHKIKNKKMLKECYKEIKVLSTNKKHIDYLISNCKDMVNQLQESIESKKTHSVSTSKSTMTTSHTEQPTTTSHTEQPTTTSRTEQPTISLQETERILIRSKKLISQFNEGTQQINAFRRQEKELLLLLQNQNRTQFENPRNISDVKVDLNEINRNIIPKLESEKFHIKAEIIKEVNHINSLEGQGKISPFEAKKFLNEYNKLNINFAKERNKRDISLKQNLSKKLESIVLNNSEKPIAQNTTISMTR
>NZ_CP015516.1|WP_063627088.1|1355775_1356498_+|ATP-binding-cassette-domain-containing-protein
MIELINVTKSYEGTQAVKNIHLTIEPGEIIGIVGKSGSGKSTLLRLLNLMEEPSSGEILIDSVAVQKLNKKEKRQQKQKMGMIFQNHNLLDNLKVYENVELPLKLQKKKNREKIDYLLNFVGMAHKAAVYPVKLSGGEKQRVSIARALTRDPEILLCDEATSSLDEENTESVIRLLHKVHEEFQPTIFFVSHELETVKSLCQRILVMENGELIGELRNHPQRYTEENLTYFKKIKRSLAQ
>NZ_CP015516.1|WP_063627089.1|1356494_1357166_+|ABC-transporter-permease-subunit
MIHSQSMMEYWPALLTSLEETGIMMAISMGVCVVGGLPLGLGLFLTNPKVRGHYPWIYWTLNFLVTVIRSFPYLLFVIALIPVTRAVLGKAFGPIPASVPLSIIAITIFARLVEQVLLDVSDETYALANSLGTNRFQYIWHFLLVEARSGLVLAYTTTTVSMVSYSTVMGVIGGGGIGDFAVRVGYQRYEYGVMYVAIVIMIVLVFILQMLGNFVAQTLDKRK
>NZ_CP015516.1|WP_063627090.1|1357177_1357990_+|hypothetical-protein
MKKFYLIGFAMIAILTLAACEGHSADKDKKEIKVAVQLESSKDILEIAKKEAEKQGYTIDIMEVSDNVAYNDAVQHDEADANFAQHEPFMAMFNQEKKADLVAVQPIYYFAGGFYSKNYKNADQLPKNAKVGIPSDPTNEGRALAILNKNGVIKLKDNMGFNGTVADIVDNPKNLQFERIDLLNLVKAYDEKDIAMVFCYPAYLEPAGLSTKDAILLEDEAASKHYALQLVTREGEKDSEKINVLKKAMTTKEVAEYIKKNSKGANIPAF
>NZ_CP015516.1|WP_010737550.1|1358286_1359996_-|fibronectin/fibrinogen-binding-protein
MSFDGVFTHAMINELRETLLSGRISKIHQPYENEVVLVIRSRGKNQRLLLSAHPSYARIQITQIDYQNPDTPPNFVMMLRKHLDGAILESIEQIENDRVIHFHFTKRDELGDLQNIILIVELMGRHSTIILVNKESGKILDAIKHIGSSQNTYRSLLPGVDYIAPPEQNQLNPFSQEKEKVFHRLSQMDLTPKGIQQQFQGIGFDTAQELVARLTERPNEKMLVWQEFFTAIDTQLSPSLYEVAEKEYFTPINYRFFDSNTQQKKMYPTLSALLDAFYQEKAEKDRAKQQGGELIRKIENELKRNRNKLKKREQTLKDSENAEDYRRDGELLTTFMAQVPRGANEVTLPNYYEEDRPITIKLDPALTPNQNAQKYFHRYQKLKNAVKLIGKQIEEAKNEIDYLESVLSQLEIAGPMDIEVIKEELTAEGYLKKKSSKKQKRKKPSQPDQYLSTDGTLILVGKNNLQNDQLSLKTAKKTDYWLHAKNIPGSHVIIKSDQPSDETITEAAELAAYFSKYRHSAQVPVDLVQVKHLRKPNGAKPGYVIYENQKTIIVTPEEEKINKMKQMTN
>NZ_CP015516.1|WP_063627091.1|1360198_1360843_+|hypothetical-protein
MWKEISETIKVKYHHFLADFDTHPQRYFMRLLFVFLVSLVITITMFVFPKDIREAQVESLVYAEINSLKLKPLNINEASQTIEESKAISVLFSVPSGEMYQALMDIFHDPKKMAELNRPIYFYPLVYQVNELEQRYDLKQEHLTVIFFQNGKETNRLVYNANQLSDFPTQLIPELNRLPLANIKKLEEELGKETQTTSTNTQLGTDLNAGNKTE
>NZ_CP015516.1|WP_063627092.1|1361198_1362239_+|ABC-transporter-substrate-binding-protein
MKNKRLITVVALIMLYLVGTFIYEKITPASTESKPKETDQTVSVGVLQYVSHPALDEIYRGIKDGLQQSGLEEGKNLTISFQNGQADQSKLATMSQQLVQADPDVLVGIATPAAQSLANVTNTIPLVLGAVTDPVGAGLVNSLKEPGGNITGVSDQPPVEAQIKLGAELLPNAKKVGILYASSEDNSKYQVSQAEKAIQKAGLTSVKYAVPSTNEIAQTVQVMSQQVDFIYVPLDNTIANAMQTVVKEADKAKIPVIPSVDSMVEQGGLATIGINQYDLGVQSGKMAAMLALGKEKPATTPVYVFDKGDVIINEKQAEKLGITIPDSIKQEAKNVSEEPKDEGDEQ

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Crispr_ID: NZ_CP015516_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP015516_3

2602307-2602727

TypeII

II-A,II-B

Consensus_repeat	Method
TGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	CRISPRCasFinder
GTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	CRT
GTTTTAGAGCTATGTTGTTTTGAATGCTTCCAAAAC	PILER-CR

5 spacers

csn2,cas2,cas1,cas9

The CRISPR arrays of NZ_CP015516_3

>merge|NZ_CP015516|3|2602307-2602727|CRISPRCasFinder,CRT,PILER-CR
ACATCTTCATTCATTCAAAACAACATAACTCTAAAGCTACCTCTTATCATAGTTGATGAGGTCAGCACTCAAAATAACACAAAACTAAAACAGCGATCGAGTAAAGCACAACGCTTCTACATTTTGGAAACATTCAAAACAACATAGCTCTAAAACTATTTGCTAGCTTTATATCAAAGTATTCCTGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAACCCGCTTGTTCAATATGTCTTCTGGTGCAATGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAACTTATAAATAAGGTTGTATAAGGAGTGTGTAGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAACAATGCCGCATTTCAAGATAAATCCAAGCGGAGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC

>NZ_CP015516|3|3|2602307-2602727|CRISPRCasFinder
ACATCTTCATTCATTCAAAACAACATAACTCTAAAGC	TACCTCTTATCATAGTTGATGAGGTCAGCACTCAAAATAACACAAAACTAAAACAGCGATCGAGTAAAGCACAACGCTTCTA
CATTTTGGAAACATTCAAAACAACATAGCTCTAAAAC	TATTTGCTAGCTTTATATCAAAGTATTCC
TGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	CCGCTTGTTCAATATGTCTTCTGGTGCAA
TGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	TTATAAATAAGGTTGTATAAGGAGTGTGT
AGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	AATGCCGCATTTCAAGATAAATCCAAGCGG
AGTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC

>NZ_CP015516|3|2|2602427-2602727|CRT
ATTTTGGAAACATTCAAAACAACATAGCTCTAAAAC	TATTTGCTAGCTTTATATCAAAGTATTCCT
GTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	CCGCTTGTTCAATATGTCTTCTGGTGCAAT
GTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	TTATAAATAAGGTTGTATAAGGAGTGTGTA
GTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC	AATGCCGCATTTCAAGATAAATCCAAGCGGA
GTTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC

>NZ_CP015516|3|2|2602428-2602727|PILER-CR
TTTTGGAAACATTCAAAACAACATAGCTCTAAAACT	ATTTGCTAGCTTTATATCAAAGTATTCCTG
TTTTGGAAGCATTCAAAACAACATAGCTCTAAAACC	CGCTTGTTCAATATGTCTTCTGGTGCAATG
TTTTGGAAGCATTCAAAACAACATAGCTCTAAAACT	TATAAATAAGGTTGTATAAGGAGTGTGTAG
TTTTGGAAGCATTCAAAACAACATAGCTCTAAAACA	ATGCCGCATTTCAAGATAAATCCAAGCGGAG
TTTTGGAAGCATTCAAAACAACATAGCTCTAAAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP015516.1\|WP_063627732.1\|2611370_2612216_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_010720999.1\|2613666_2613984_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372928
NZ_CP015516.1\|WP_010721000.1\|2614276_2614744_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|173926
NZ_CP015516.1\|WP_010737013.1\|2588581_2589034_-\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP015516.1\|WP_010720982.1\|2589129_2589729_-\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|240029
NZ_CP015516.1\|WP_063627606.1\|2595565_2596996_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|163525
NZ_CP015516.1\|WP_010720992.1\|2603492_2603837_-\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP015516.1\|WP_053766205.1\|2602843_2603503_-\|type-II-A-CRISPR-associated-protein-Csn2	csn2	cd09758_csn2_CAS-II-A	gnl\|CDD\|213408
NZ_CP015516.1\|WP_063627605.1\|2594229_2595549_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|224038
NZ_CP015516.1\|WP_010720996.1\|2609548_2611243_+\|oleate-hydratase	unknown	unknown	gnl\|CDD\|237575
NZ_CP015516.1\|WP_063627604.1\|2591576_2594120_-\|HAD-IC-family-P-type-ATPase	unknown	unknown	gnl\|CDD\|319775
NZ_CP015516.1\|WP_053766204.1\|2603833_2604700_-\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|187851
NZ_CP015516.1\|WP_063627607.1\|2597311_2599144_-\|tyrosine-decarboxylase	unknown	unknown	gnl\|CDD\|163523
NZ_CP015516.1\|WP_010720995.1\|2609366_2609495_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP015516.1\|WP_010737002.1\|2612505_2613639_+\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176243
NZ_CP015516.1\|WP_063627610.1\|2604681_2608692_-\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	COG3513_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|374653
NZ_CP015516.1\|WP_063627603.1\|2589984_2591439_+\|HTH-domain-containing-protein	unknown	unknown	gnl\|CDD\|375760
NZ_CP015516.1\|WP_063627609.1\|2601304_2601664_-\|DUF1622-domain-containing-protein	unknown	unknown	gnl\|CDD\|377914
NZ_CP015516.1\|WP_063627608.1\|2599639_2601070_+\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|311953
NZ_CP015516.1\|WP_010720990.1\|2601653_2602025_-\|DUF1622-domain-containing-protein	unknown	unknown	gnl\|CDD\|377914

Protein	Function_ID	Function_description	E-value
NZ_CP015516.1\|WP_010720999.1\|2613666_2613984_+\|hypothetical-protein	gnl\|CDD\|372928	pfam14145, YrhK, YrhK-like protein. The YrhK-like protein family includes the B. subtilis YrhK protein, which is functionally uncharacterized. Its expression is under the control of the motility sigma factor sigma-D. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length.	1.03168e-14
NZ_CP015516.1\|WP_010721000.1\|2614276_2614744_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|173926	cd04301, NAT_SF, N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.	6.49402e-07
NZ_CP015516.1\|WP_010737013.1\|2588581_2589034_-\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	4.65046e-18
NZ_CP015516.1\|WP_010720982.1\|2589129_2589729_-\|NUDIX-hydrolase	gnl\|CDD\|240029	cd04672, Nudix_Hydrolase_14, Members of the Nudix hydrolase superfamily catalyze 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 and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases 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 & "house-cleaning" enzymes. Substrate specificity is used to define 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.	5.88022e-62
NZ_CP015516.1\|WP_063627606.1\|2595565_2596996_-\|amino-acid-permease	gnl\|CDD\|163525	TIGR03813, put_Glu_GABA_T, putative glutamate/gamma-aminobutyrate antiporter. Members of this protein family are putative putative glutamate/gamma-aminobutyrate antiporters. Each member of the seed alignment is found adjacent to a glutamate decarboxylase, which converts glutamate (Glu) to gamma-aminobutyrate (GABA). However, the majority belong to genome contexts with a glutaminase (converts Gln to Glu) as well as the decarboxylase that converts Glu to GABA. The specificity of the transporter remains uncertain.	4.27821e-52
NZ_CP015516.1\|WP_010720992.1\|2603492_2603837_-\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.80036e-43
NZ_CP015516.1\|WP_053766205.1\|2602843_2603503_-\|type-II-A-CRISPR-associated-protein-Csn2	gnl\|CDD\|213408	cd09758, Csn2, CRISPR/Cas system-associated protein Csn2. Csn2 is a Nmeni subtype-specific Cas protein, which may function in the adaptation process which mediates the incorporation of foreign nucleic acids into the microbial host genome. Csn 2 may interact directly with double-stranded DNA. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA. Csn2 has been predicted to be a functional analog of Cas4 based on anti-correlated phyletic patterns; also known as SPy1049 family.	1.26064e-112
NZ_CP015516.1\|WP_063627605.1\|2594229_2595549_-\|amino-acid-permease	gnl\|CDD\|224038	COG1113, AnsP, Gamma-aminobutyrate permease and related permeases [Amino acid transport and metabolism].	4.98859e-124
NZ_CP015516.1\|WP_010720996.1\|2609548_2611243_+\|oleate-hydratase	gnl\|CDD\|237575	PRK13977, PRK13977, myosin-cross-reactive antigen; Provisional.	0
NZ_CP015516.1\|WP_063627604.1\|2591576_2594120_-\|HAD-IC-family-P-type-ATPase	gnl\|CDD\|319775	cd02080, P-type_ATPase_cation, P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase. This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
NZ_CP015516.1\|WP_053766204.1\|2603833_2604700_-\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|187851	cd09720, Cas1_II, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer intergration. Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain.	8.73092e-122
NZ_CP015516.1\|WP_063627607.1\|2597311_2599144_-\|tyrosine-decarboxylase	gnl\|CDD\|163523	TIGR03811, tyrosine_decarboxylase, tyrosine decarboxylase, Enterococcus type. This model represents tyrosine decarboxylases in the family of the Enterococcus faecalis enzyme Tdc. These enzymes often are encoded next to tyrosine/tyramine antiporter, together comprising a system in which tyrosine decarboxylation can protect against exposure to acid conditions. This clade differs from the archaeal tyrosine decarboxylases associated with methanofuran biosynthesis. [Cellular processes, Adaptations to atypical conditions].	0
NZ_CP015516.1\|WP_010737002.1\|2612505_2613639_+\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176243	cd08283, FDH_like_1, Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.	3.95764e-174
NZ_CP015516.1\|WP_063627610.1\|2604681_2608692_-\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|374653	pfam16592, Cas9_REC, REC lobe of CRISPR-associated endonuclease Cas9. The REC lobe of Cas9 - the CRISPR-associated endonuclease Cas9 - includes the REC1 and REC2 domains. REC1 forms an elongated, alpha-helical structure consisting of 25 alpha helices and two beta-sheets, whereas REC2 inserted within REC1 adopts a six-helix bundle structure. The REC lobe and the NUC lobe of Cas9 fold to present a positively charged groove at their interface which accommodates the negatively charged sgRNA:target DNA heteroduplex. CRISPR (clustered regularly interspaced short palindromic repeat)-Cas system occurs naturally in bacteria as a defense against invasion by phages or other mobile genetic elements. Cas9 is targeted to specific genomic locations by sgRNAs or single guide RNAs, in order to complex with invading DNA in order to cleave it and render it inactive.	0
NZ_CP015516.1\|WP_063627603.1\|2589984_2591439_+\|HTH-domain-containing-protein	gnl\|CDD\|375760	pfam18333, ssDNA_DBD, Non-canonical single-stranded DNA-binding domain. This domain is found in ThermoDBP, a non-canonical single-stranded DNA-binding protein in Thermoproteales. Single-stranded DNA-binding proteins are needed for DNA metabolism, sequestering and protecting transiently formed ssDNA during DNA replication and recombination, detecting DNA damage and recruiting repair proteins. The outer edge of the ssDNA-binding cleft, formed by this domain, has a strongly positive electrostatic surface potential because of the conserved basic residues R49, K54, R65, R80, R86, R90, K97, and R112.	1.9434e-16
NZ_CP015516.1\|WP_063627609.1\|2601304_2601664_-\|DUF1622-domain-containing-protein	gnl\|CDD\|377914	pfam07784, DUF1622, Protein of unknown function (DUF1622). This is a family of 14 highly conserved sequences, from hypothetical proteins expressed by both bacterial and archaeal species.	3.47366e-21
NZ_CP015516.1\|WP_063627608.1\|2599639_2601070_+\|DNA-binding-protein	gnl\|CDD\|311953	pfam08280, HTH_Mga, M protein trans-acting positive regulator (MGA) HTH domain. Mga is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions.	0.00184945
NZ_CP015516.1\|WP_010720990.1\|2601653_2602025_-\|DUF1622-domain-containing-protein	gnl\|CDD\|377914	pfam07784, DUF1622, Protein of unknown function (DUF1622). This is a family of 14 highly conserved sequences, from hypothetical proteins expressed by both bacterial and archaeal species.	4.39167e-21

>NZ_CP015516.1|WP_010720990.1|2601653_2602025_-|DUF1622-domain-containing-protein
MFDTNLITYLDWLIAILNIASIIILLVGIFLVLKNLFDWHPLKKDYEQRNFRNAEVRKLLASYILLSLEVLVVADIIESVIKPTWTDILKLAVIIIIRTIISYFLNLETQDKKQVKVGTHNGN
>NZ_CP015516.1|WP_063627609.1|2601304_2601664_-|DUF1622-domain-containing-protein
MEINLIEKLAPYLEQLVIVLDVFAILIILWGAWLAIKDFLYFSFTERRIKAERINQNNAIKKMLGGYILLSLEVLISAGIIESIIKPTLEDVFQLAALVVIRTIISFFLNKEIGSDARQ
>NZ_CP015516.1|WP_063627608.1|2599639_2601070_+|DNA-binding-protein
MFEDYLEKNILRQLFLCGQFYHKKEIDLDELSHLLQVCKTTLLNDIKAIRTELKDEIIYSQREKDTCSLYFDPTIPRFRLIQKLARPSLFLKTCQLYLENEPDYLQLTEIEYISVSKAYSLKKQVLAYFEDCDIQIQHHSPRFREIERRLLLLNVTYRTGTLKIPTLPADYFLAIDEFIESVTFNSRRIYDKDNREILRIGLLISYLSQKKHPLSIEQDFIAELQKRPIYQYVMDAWHTTKLKHYYQENEVYFALILFNLSDYGFNSYQAIEEDFCHLHQVFIEDSQSIKQLITQFESYFNRKFIGNRAFERALIRLMRTAWDNYQLFVPEKFYLLSPEQQSLLAEIQPLFNQWLAQLPYRLRLKINCLDAFVIELSGILRINKTKLHVRIVTNSDVKYLIYREALESVTTFDMEVDPVVYQHLDEAIKSAAQQENTRILCEKTLYTPEAEQFPTIVPVSVDTIEKSIVWAVQAVR
>NZ_CP015516.1|WP_063627607.1|2597311_2599144_-|tyrosine-decarboxylase
MKDMDIKAVFIGDKSENGAFYKMQLNKMVDEHLGWRENYLPGDVAAISEADKQAPRYIATREHMVEVLDEVSQRMRAGSIPWHSAGRYWGQMNAETLMPALLAYNFAMLWNPNNVALESSMATSQMEAEVGQDFADLFNMTGGWGHITADGSIANLEGLWYARCIKSIPLAVKEVYPEKVKDKTDWELLNLSVEEILEMVGTFSDEELDAVKAASSRSGKHLQELGKWLVPQTKHYSWMKALDICGIGLDQMIAIPVQEDYRMDVAILEKTIRELAAQKIPVLGVVAVVGTTEEGQVDSVDKIVELREKLYKEGIYFYLHVDAAYGGYARALFLNEAGEFVPYESLPDFFEEHHVFNYDVSIDQSVYDGFKAISEADSVTIDPHKMGYVPYAAGGIVIKHKEMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNITGYGQLIGASIEAAQRFRAFLEQLSFTIKGKTIEVYPLNHPDFNMVNWVFKVKGCTDLKTINELNEKMFNRSSYMEGDVYSEHFITSHTTFMKEEYGDSPLPFIERIGLSKEEWQKEQKVTLLRAAIMTPYLNDDKIFEFYTQGITKAMEKTLNEII
>NZ_CP015516.1|WP_063627606.1|2595565_2596996_-|amino-acid-permease
MTDSKTSQITTLTFIGMTCALVASVRNIPDVAATGWTMLFYMLVAVLFYAFPISLISGEFAGMFPQKGGPELWVSNSLGRKWGFVVSWLLWVQMFPGMVMVASALAPLLGNMIDNVPLGLNSKFTLIVILVVYWIITLLNLKFDMAKIGGKIGVWLGLYIPLAIMLLLGIFSWIKVGIQPHATLGHFSWAKLIPDAETAKSFVYFAPIMFIFTGIEMSSVYITRLKNPVKTYTKGIFAALIFLFFVNTLNALVVANVVPKGQMELNNIAQSISIYCQILGLPHIIVNIFSLLVFVGVAVQLSAWASGPAKTVTASARKGAYPPKFNFWKTNQFDVSKSVILTQSTIISIFALFYLLIPGVNQAFLMLVNSTTVIYCIVYVIMGIAILKLRKAKPELARPFRIGKKGGKGDLGAWIVVLVLFAAIGCSVGLTMQAGTLINFIAVTLISLILFIAPLCIDKIRKPSWEQEVQQKLNQE
>NZ_CP015516.1|WP_063627605.1|2594229_2595549_-|amino-acid-permease
MERTTMKKTLTNRNIQMIALGGAIGTGLFLGSAKAIKLAGPAVLLTYFVCGLAIYGLMYAMGELFLSNNEFQSIGDFIQYYLGERWAFLVNWTYWLCWMGAGLTELTAIGLYIRFWLPALSPLISGIFALIALVIINVVAVRWFGELESLFSTIKIFGILLFILLGIGVCFLYFKSPRIGVRENFDQLQTIFPFGLTGLVAAFPMVLFSFAGVEMIGLTVGETADPQKNLKKAIQCLPARILFFYIGTIVAVLLVVPWQSLDLKESPLVTMLQFIHCSKGAGVINLIILVASLSSTNSAIYSTSRILYNTAKEKNLSKWFLTLSSRGVPLHGILFTGGMFLLGLCLHFFVSDSRILFQLLAGMTTISFLFVWSAILFAHLKLTKSQLKKWKDRLILCFFGLVGISLFFEPTTRVIPVVSVVWFGALNLIYQRIRQTSPK
>NZ_CP015516.1|WP_063627604.1|2591576_2594120_-|HAD-IC-family-P-type-ATPase
MVWYKETAQEVMKTLKTTPDGLNQDERISRLKENGYNHIEVKKKVSPLRKFLKHLTELLMIILLVASLLKFFTGEVIEGSIILAVVLVNSFVGYWQERKAEEALNGLEKLLGQNAVIFTEGIKELVPAKELVPGDLLALKAGDVVPADVRLIEVHDFMVEEAALTGESEAVEKTSKRLTTTVSTGDQKNLAFSGTLVQTGTAIGVVIETGDTTEIGKINQALQSVQQQTTPLVKKINQLNKQIFRGILFLSLFLLFFTTFRYGLEMNFLFSTIIALIVSMIPEGLPAVLTMILSLGVNEMAKEQAIIKGLPSVETLGSMTVICSDKTGTLTKNEMSVVETVTDQEETMLAIMKNCQEIQTKANQNVAELTGNPTELALLRYTAKASLPLEPVKGKIPFSSSYKYMATMHDKQEHAIVYVKGAPEVLLAKANLTPKQVGKWQEEAMKLAQKGQRVLGFAYKTLAPDQELGHDQLNELTFVGIAGIIDPPKESAIRAVKECQNAGISVKMITGDHKDTAQAIAEQIGLKHTKNVLEGIDIDRLSDEELAKQVKSVDVFARTTPEHKLRIVDALQKNEEIVGMTGDGVNDAPALKRADVGIAMGIKGSEVSKQAADMVLGDDNFHTIAKAVKEGRRILDNLQKTINFFLPTALAQGLVIIWALLVNQPLPLTPVQILWVNMVTTITLSYALGFEKAGKDTMSRSPRDPKQGILTRYSVFRIFYVSLLIMIPAYLLAMSFEGQALQQTMLLQNIVAAQAVYMINCRELLDPSLNRSLFENKALFLSLGMLVLLQAGVIYLPIAQQLIGTTSLSLTEQLPILLNILLLFVIVEIEKRISKMIAKKRNAELPT
>NZ_CP015516.1|WP_063627603.1|2589984_2591439_+|HTH-domain-containing-protein
MYSLMKKIITEKDIKRQVSLVELLLNHSQITVNELAEAVNTTERTIFSDLQTIKTQLPKGWLINSDQSGIQLKNEQNLLTNELWEIFLTQSISVQLLKELLTIKEVATPTFLARNGLSYETLNRHVKKLNQQLVVYELQIEQNRHRLSFSGEEETIRLFYHRLLMPFTHNNYFFEDYSIHESHYFRFLKRLRQAELAVDTEEVFGICWFFINTIRIKAGCRIPTSLFSTQDQLFLLYAPELEKLYRTEGVYLKDKEAAFAFSCFLDSWNYNNSYPPMILDILHRHPAETNIREFVNRLSESLAIKELEQTNLPENLILLLLKYYESPLLIEQTTKQYHYYLKEYEQEYPELYPYKFALLQQVKESTSMVKKVTNETYFFYLLSLLIQQTLLAVQPYQATIYFIFQGEPSWKAFLQQELNAYLGKRVILEPIELSQLSDITIKKNDLLVSNIPIDTPPMPVIYLSTIPTKNELDRLSDLSLRSYL
>NZ_CP015516.1|WP_010720982.1|2589129_2589729_-|NUDIX-hydrolase
METRLNDYRRLLAIAQAGLLYGKDVFDKERYEELQEISLKLLSEVGLETKEEWTSLIEAHEGYPTPKVDVRAWIKQDEKILLIEDTKTQEWSLPGGFAEVGLSPKENIRKEVKEETGLEVEVGQLLAIFDTNLRTDIPQAFQYYKIVFSCAILSGTFVANHETSNMKFFHLNDLPKLSLKRTTKEQLLILEKATLPYCD
>NZ_CP015516.1|WP_010737013.1|2588581_2589034_-|winged-helix-turn-helix-transcriptional-regulator
MDEIIREIGAIARALDSISNIEFQEVDLTRGQYLYLVRICEHPGIIQEKLAEMINVDRTTTARAVKKLIAKDLIKSMPDKKNKKIKKLYPTDRGKKVYPFILREHHYSNQVAVKGLSQQEVLQLHTLLQKVRKNVSEDWHYIKKGNKRIY
>NZ_CP015516.1|WP_053766205.1|2602843_2603503_-|type-II-A-CRISPR-associated-protein-Csn2
MNLNFSLLEQPISFEKTLIFVIEDVEVFSKVVHGVYQYGENSMLKFFNDKLQLLKPSELMVVTDILSFDSQAPTTLKLIYADLEQQLNENIELKSRIDQLTTKVQEWISEELLEHELDLVCKEMSMVELFKALKIRITTQPESIFQKIMEILQIYKYLVKKKYLVFINVGAYLTITEMAELQEYISLCHMPVLFIEPRKIKGLKQTVLDQDYFLCEEMW
>NZ_CP015516.1|WP_010720992.1|2603492_2603837_-|CRISPR-associated-endonuclease-Cas2
MSYRYMRMLLMFDLPTETSDDRKVYRRFRKFLLSEGFIMHQFSVYSKLLLNGTANQAMLGRLKAHHPKKGLVTLLTVTEKQFSRMVYLCGEKDLSPANSDERVIFLGEDVEDEP
>NZ_CP015516.1|WP_053766204.1|2603833_2604700_-|type-II-CRISPR-associated-endonuclease-Cas1
MGWRTVVINTHSKLTYANNHLVFKNAQQTEKIHLSEIDILILETTDITITTMLLKRLTDEKILVIFCDDKRLPSSQLFSYYGRHDSSLQLSKQIQWESDLKGVVWTTIIAQKIHNQCRFLQENDFVEKASALSKLSEELETFDPTNREGHAARIYFQTLFGNQFTREESNEINAGLDYGYTLLMSLFAREIVKNGCMTQFGLKHANQFNDFNLASDLMEPFRPLVDQIVYTYRDQPFPIIKRRLFDLVSQKYLYGKKEMFLTNIVTDYTNKTIKTLNNEGKGVPYFGI
>NZ_CP015516.1|WP_063627610.1|2604681_2608692_-|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MTKDYTIGLDIGTNSVGWAVLTDDYQLMKRKMSVHGNTEKKKIKKNFWGARLFDEGQTAEFRRTKRTNRRRLARRKYRLSKLQDLFAEELCKQDDCFFVRLEESFLVPEEKQYKPASIFPTLEEEKEYYQKYPTIYHLRQKLVDSTEKEDLRLVYLALAHLLKYRGHFLFEGYLDTENTSIEESFRVFLEQYGKQSDQPLIVHQPVLTILTDKLSKTKKVEEILKYYPTEKINSFFAQCLKLIVGNQANFKRIFDLEAEVKLQFSKETYEEDLESLLEKIGDEYLDIFLQAKKVHDAILLSEIISSTVKHTQAKLSSGMVERYERHKADLAKFKQFVKENVPQKATVFFKDTTKNGYAGYIKGKTTQEEFYKFVKKELSGVVGSEPFLEKIDQETFLLKQRTYTNGVIPHQVHLIELKAIIDQQKQHYPFLEEAGPKIIALFKFRIPYYVGPLAKEQEASSFAWIERKTAEKIHPWNFSEVVDIEKSAMRFIQRMTKQDTYLPTEKVLPKNSLLYQKYMIFNELTKVSYKDERGVKQYFSGDEKQQIFKQLFQKERGKITVKKLQNFLYTHYHIENAHIFGIEKAFNASYSTYHDFMKLAKTNQKSMQEWLEQPEMEPIFEDIVKILTIFEDRQMIKHQLSKYQEVFGEKLLKEFARKHYTGWGRFSAKLIHGIRDRKTNKTILDYLINDDDVPANRNRNLMQLINDEHLSFKEEIAKATVFSKHKSLVDVIQDLPGSPAIKKGIWQSLKIVEELIAIIGYKPKNIVIEMARENQKTHRTKPRLKALENGLKQIGSTLLKEQPTDNKALQKERLYLYYLQNGRDIYTGEPLDIENLHQYEVDHIIPRSFIVDNSIDNKVLVASKQNQKKRDDVPNKQIVNEQRIFWNQLKEAKLISPKKYAYLTKIELTPEDKARFIQRQLVETRQITKHVANILHQSFHQEEEGTDCDGVQIITLKATLTSQFRQTFGLYKVREINPHHHAHDAYLNGFIANVLLKRYPKLAPEFVYGKYVKYSLARENKATAKKEFYSNILKFLESDEPFCDENGEIYWEKSYHLPRIKKVLSSHQVNVVKKVEQQKGGFYKETVNSKEKPDKLIERKNNWDVTKYGGFGSPVIAYAIAFVYAKGKTQKKTRAIEGITIMEQAAFEKDPTTFLKDKGFPQVTEFIKLPKYTLFEFDNGRRRFLASHKESQKGNPFILSDQLVTLLYHAQHYDKITYQESFDYVNTHLSDFSAILTEVLAFAEKYTLADKNIERIQELYEENKYGEISMIAQSFLQLLQFNAIGAPADFKFFGVTIPRKRYTSLTEIWDATIIYQSVTGLYETRIRMGDLWAGEQ
>NZ_CP015516.1|WP_010720995.1|2609366_2609495_+|hypothetical-protein
MSKKWIKLGIGLGILTLGAVYLGKKTGLLEDDRHLYDEFESI
>NZ_CP015516.1|WP_010720996.1|2609548_2611243_+|oleate-hydratase
MRKSKAIMIGAGIANMAAAVYLIQEGNWRGDQITFYSLDDHGSNDGAPTDTVVDEYWNKNHPLENKKGYIARGGRMLNYRTYVDLMDLLSRIPSVTEPGMTAAEDTRDFDAKHRTFDKARLMEGGKGIIDGGKLGFNNKDRLLLTKLIAMPDSEEEKLDNVTIEEYFKDDPHFFETNFWFMWETTFAFRTRSSAQELRRYMHQMIYEFTQIEHLVGVNRTRYNQYESIMLPLINYLKDQGCQIILNRRVVDWEFKETPMQDEITVTGLKMINTLTNEEEHVVVDGDTGVLFTNGSITDSATLGDYDTPAVENMDYGAASSLWKKASERFYNLGNPDKFFADRDASEWVSFTLTTKDHLLLNEITRITTQVPGNALNSFISTTPITPLGQKDVNMSIVVHHQPHFTSQKPNETVIWGYFLYPRRRGEFVDKQYIKMTGKEMLEELIGQLSKVDPGPENIRTKETEIFDSVVNNIPVYMPYASALFNNRAKSDRPKVIPQHSTNLAFTGEFVEQPYQMIFTEQSAVRSGEIAAFHFAGIPMSRLVKTPRYDKDIPTLMRAAKKMFE
>NZ_CP015516.1|WP_063627732.1|2611370_2612216_-|hypothetical-protein
MVTFACSVTLFVIISVGIIQVTFFDQAYLLGQIEKTKYSELILAEAAQNFRKENTEESEFSEVVATALSPSFVEEALRPFIQHTYEETNYELRDSNEVSEKIAQAVATIATKKQLTIDKEEKNKIETMIFIYMYHFQSALGDRYLTIFIENIVSARKIVVPLFYICLGLLVFWLVYLYRLINKTPFSFPRYGMFILGTTGSMFCVLAGLLYIQDVLHNIAFHSQATLQLMTHYVQDLLMYPAIIGGILLFCAVLFGGGSKLLQKRQSKKWLKTGSSTLKKA
>NZ_CP015516.1|WP_010737002.1|2612505_2613639_+|alcohol-dehydrogenase-catalytic-domain-containing-protein
MKAVTWQGNQKMEIRNVDDPKIVEPTDAIIRITATAICGSDLHLYHHGEAVLEKGYVVGHEPMGIVEEVGPAVKKLKKGQRVVIPFNISCGHCHFCTHEMESQCDRSNPDQLYGGLFGFGRLNGNHWGGQAEYLRVPFADSTSFIVPDNDLADEKVLFLSDILPTAYWSVQNANVKKGDTVVVLGSGPVGLFAQKFAAMAGAERVIAVDPVQHRIDKAARYNHVETYLLEDTQSAGKELYELAKGGADVIIDCVGMDGLEPVKEKAKNLVSLQSGTISPIQMAAQAVKKFGTVQITGVYMTPASSYPLQEFFMRDITVKHGQAPIVHLMPKIYEMIAAGLFDPTQIITHAMPLADAARAYEIFDKKEDKNIKVVLKP
>NZ_CP015516.1|WP_010720999.1|2613666_2613984_+|hypothetical-protein
MPEIKRKSHEIDIGKEEDIEIAGQRFRLYFQNRYTLLSLAVDLLTGIFYIFGSVALLTDIPDRYSTYCYLVGAIFLTARPILKIVRNVFIYDEKKKQKKSEKKNE
>NZ_CP015516.1|WP_010721000.1|2614276_2614744_-|GNAT-family-N-acetyltransferase
MKGYELVKIRERPEWLEQAAQWFTSKWHLPLSFYQESMEDSLQSSNAVPQWYIVVTSEQKIIAGAGVIANDFHDRPDLTPNVCALFVEKEYRNQGIAKEILSFIREDMGALGISQLYVATDHTGFYERYEWEYLTTVQDNEGIPVYLYQLAIFTT

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP015516_3	3.3\|2602529\|29\|NZ_CP015516\|CRISPRCasFinder	2602529-2602557	29	MG788324	Lactobacillus phage PM411, complete genome	67569-67597	5	0.828
NZ_CP015516_3	3.4\|2602595\|29\|NZ_CP015516\|CRISPRCasFinder	2602595-2602623	29	NZ_CP029750	Staphylococcus aureus strain Smith plasmid pSS41, complete sequence	30324-30352	5	0.828
NZ_CP015516_3	3.7\|2602529\|30\|NZ_CP015516\|CRT	2602529-2602558	30	MG788324	Lactobacillus phage PM411, complete genome	67568-67597	5	0.833
NZ_CP015516_3	3.8\|2602595\|30\|NZ_CP015516\|CRT	2602595-2602624	30	NZ_CP029750	Staphylococcus aureus strain Smith plasmid pSS41, complete sequence	30323-30352	5	0.833
NZ_CP015516_3	3.11\|2602530\|30\|NZ_CP015516\|PILER-CR	2602530-2602559	30	MG788324	Lactobacillus phage PM411, complete genome	67568-67597	5	0.833
NZ_CP015516_3	3.12\|2602596\|30\|NZ_CP015516\|PILER-CR	2602596-2602625	30	NZ_CP029750	Staphylococcus aureus strain Smith plasmid pSS41, complete sequence	30323-30352	5	0.833
NZ_CP015516_3	3.7\|2602529\|30\|NZ_CP015516\|CRT	2602529-2602558	30	NZ_CP025589	Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence	15693-15722	6	0.8
NZ_CP015516_3	3.7\|2602529\|30\|NZ_CP015516\|CRT	2602529-2602558	30	NZ_CP025589	Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence	49700-49729	6	0.8
NZ_CP015516_3	3.11\|2602530\|30\|NZ_CP015516\|PILER-CR	2602530-2602559	30	NZ_CP025589	Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence	15693-15722	6	0.8
NZ_CP015516_3	3.11\|2602530\|30\|NZ_CP015516\|PILER-CR	2602530-2602559	30	NZ_CP025589	Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence	49700-49729	6	0.8
NZ_CP015516_2	2.4\|1349509\|29\|NZ_CP015516\|CRISPRCasFinder,CRT	1349509-1349537	29	NC_013533	Enterococcus faecalis plasmid pBEE99, complete sequence	54452-54480	7	0.759
NZ_CP015516_2	2.5\|1349575\|29\|NZ_CP015516\|CRISPRCasFinder,CRT	1349575-1349603	29	CP001772	Spirosoma linguale DSM 74 plasmid pSLIN03, complete sequence	16716-16744	7	0.759
NZ_CP015516_3	3.4\|2602595\|29\|NZ_CP015516\|CRISPRCasFinder	2602595-2602623	29	MN694522	Marine virus AFVG_250M345, complete genome	34790-34818	7	0.759
NZ_CP015516_2	2.1\|1349508\|30\|NZ_CP015516\|PILER-CR	1349508-1349537	30	NC_013533	Enterococcus faecalis plasmid pBEE99, complete sequence	54451-54480	8	0.733
NZ_CP015516_2	2.2\|1349574\|30\|NZ_CP015516\|PILER-CR	1349574-1349603	30	CP001772	Spirosoma linguale DSM 74 plasmid pSLIN03, complete sequence	16715-16744	8	0.733
NZ_CP015516_2	2.4\|1349509\|29\|NZ_CP015516\|CRISPRCasFinder,CRT	1349509-1349537	29	NZ_CP022300	Acinetobacter johnsonii strain IC001 plasmid pIC001B, complete sequence	18905-18933	8	0.724
NZ_CP015516_3	3.8\|2602595\|30\|NZ_CP015516\|CRT	2602595-2602624	30	MN694522	Marine virus AFVG_250M345, complete genome	34789-34818	8	0.733
NZ_CP015516_3	3.12\|2602596\|30\|NZ_CP015516\|PILER-CR	2602596-2602625	30	MN694522	Marine virus AFVG_250M345, complete genome	34789-34818	8	0.733
NZ_CP015516_2	2.1\|1349508\|30\|NZ_CP015516\|PILER-CR	1349508-1349537	30	NZ_CP022300	Acinetobacter johnsonii strain IC001 plasmid pIC001B, complete sequence	18905-18934	9	0.7

1. spacer 3.3|2602529|29|NZ_CP015516|CRISPRCasFinder matches to MG788324 (Lactobacillus phage PM411, complete genome) position: , mismatch: 5, identity: 0.828

ccgcttgttcaatatgtcttctggtgcaa	CRISPR spacer
ctcctaatttaatatgtcttctggtgcaa	Protospacer
*. ** .**.*******************

2. spacer 3.4|2602595|29|NZ_CP015516|CRISPRCasFinder matches to NZ_CP029750 (Staphylococcus aureus strain Smith plasmid pSS41, complete sequence) position: , mismatch: 5, identity: 0.828

ttataaataaggttgtataaggagtgtgt-	CRISPR spacer
ttataaataatgttgtgtaagga-tatgga	Protospacer
********** *****.****** *.**

3. spacer 3.7|2602529|30|NZ_CP015516|CRT matches to MG788324 (Lactobacillus phage PM411, complete genome) position: , mismatch: 5, identity: 0.833

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgcaat	Protospacer
*. ** .**.********************

4. spacer 3.8|2602595|30|NZ_CP015516|CRT matches to NZ_CP029750 (Staphylococcus aureus strain Smith plasmid pSS41, complete sequence) position: , mismatch: 5, identity: 0.833

ttataaataaggttgtataaggagtgtgta-	CRISPR spacer
ttataaataatgttgtgtaagga-tatggat	Protospacer
********** *****.****** *.** *

5. spacer 3.11|2602530|30|NZ_CP015516|PILER-CR matches to MG788324 (Lactobacillus phage PM411, complete genome) position: , mismatch: 5, identity: 0.833

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgcaat	Protospacer
*. ** .**.********************

6. spacer 3.12|2602596|30|NZ_CP015516|PILER-CR matches to NZ_CP029750 (Staphylococcus aureus strain Smith plasmid pSS41, complete sequence) position: , mismatch: 5, identity: 0.833

ttataaataaggttgtataaggagtgtgta-	CRISPR spacer
ttataaataatgttgtgtaagga-tatggat	Protospacer
********** *****.****** *.** *

7. spacer 3.7|2602529|30|NZ_CP015516|CRT matches to NZ_CP025589 (Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.8

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgctat	Protospacer
*. ** .**.***************** **

8. spacer 3.7|2602529|30|NZ_CP015516|CRT matches to NZ_CP025589 (Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.8

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgctat	Protospacer
*. ** .**.***************** **

9. spacer 3.11|2602530|30|NZ_CP015516|PILER-CR matches to NZ_CP025589 (Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.8

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgctat	Protospacer
*. ** .**.***************** **

10. spacer 3.11|2602530|30|NZ_CP015516|PILER-CR matches to NZ_CP025589 (Lactobacillus plantarum strain KC3 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.8

ccgcttgttcaatatgtcttctggtgcaat	CRISPR spacer
ctcctaatttaatatgtcttctggtgctat	Protospacer
*. ** .**.***************** **

11. spacer 2.4|1349509|29|NZ_CP015516|CRISPRCasFinder,CRT matches to NC_013533 (Enterococcus faecalis plasmid pBEE99, complete sequence) position: , mismatch: 7, identity: 0.759

aaacttgtgtagggcgtggctttgatcct	CRISPR spacer
tagaatgtgtagagcgtggcttagatccc	Protospacer
 *.  *******.********* *****.

12. spacer 2.5|1349575|29|NZ_CP015516|CRISPRCasFinder,CRT matches to CP001772 (Spirosoma linguale DSM 74 plasmid pSLIN03, complete sequence) position: , mismatch: 7, identity: 0.759

gggacttactgggataagtatcctcttga	CRISPR spacer
gatacttacggcgataagtatcctctctc	Protospacer
*. ****** * **************.

13. spacer 3.4|2602595|29|NZ_CP015516|CRISPRCasFinder matches to MN694522 (Marine virus AFVG_250M345, complete genome) position: , mismatch: 7, identity: 0.759

ttataaataaggttgtataaggagtgtgt	CRISPR spacer
ttaaaaaaaaggttgtataaggaaagaaa	Protospacer
*** *** ***************. * .

14. spacer 2.1|1349508|30|NZ_CP015516|PILER-CR matches to NC_013533 (Enterococcus faecalis plasmid pBEE99, complete sequence) position: , mismatch: 8, identity: 0.733

taaacttgtgtagggcgtggctttgatcct	CRISPR spacer
gtagaatgtgtagagcgtggcttagatccc	Protospacer
  *.  *******.********* *****.

15. spacer 2.2|1349574|30|NZ_CP015516|PILER-CR matches to CP001772 (Spirosoma linguale DSM 74 plasmid pSLIN03, complete sequence) position: , mismatch: 8, identity: 0.733

agggacttactgggataagtatcctcttga	CRISPR spacer
tgatacttacggcgataagtatcctctctc	Protospacer
 *. ****** * **************.

16. spacer 2.4|1349509|29|NZ_CP015516|CRISPRCasFinder,CRT matches to NZ_CP022300 (Acinetobacter johnsonii strain IC001 plasmid pIC001B, complete sequence) position: , mismatch: 8, identity: 0.724

aaacttgtgtagggcgtggctttgatcct	CRISPR spacer
ctgatggtgtagcgcgtggctttgatctc	Protospacer
  . * ****** **************..

17. spacer 3.8|2602595|30|NZ_CP015516|CRT matches to MN694522 (Marine virus AFVG_250M345, complete genome) position: , mismatch: 8, identity: 0.733

ttataaataaggttgtataaggagtgtgta	CRISPR spacer
ttaaaaaaaaggttgtataaggaaagaaat	Protospacer
*** *** ***************. * .

18. spacer 3.12|2602596|30|NZ_CP015516|PILER-CR matches to MN694522 (Marine virus AFVG_250M345, complete genome) position: , mismatch: 8, identity: 0.733

ttataaataaggttgtataaggagtgtgta	CRISPR spacer
ttaaaaaaaaggttgtataaggaaagaaat	Protospacer
*** *** ***************. * .

19. spacer 2.1|1349508|30|NZ_CP015516|PILER-CR matches to NZ_CP022300 (Acinetobacter johnsonii strain IC001 plasmid pIC001B, complete sequence) position: , mismatch: 9, identity: 0.7

taaacttgtgtagggcgtggctttgatcct	CRISPR spacer
actgatggtgtagcgcgtggctttgatctc	Protospacer
   . * ****** **************..

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1157895 : 1166955

Prochlorococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_063626987.1\|1157895_1159203_+	adenylosuccinate lyase	A0A2H4UUU6	Bodo_saltans_virus	4.7e-16	27.7
WP_010737435.1\|1159359_1159737_-	hypothetical protein	NA	NA	NA	NA
WP_063626988.1\|1159998_1160715_+	phosphoribosylaminoimidazolesuccinocarboxamide synthase	E3SPA9	Prochlorococcus_phage	3.7e-47	41.9
WP_010737437.1\|1160729_1160984_+	phosphoribosylformylglycinamidine synthase subunit PurS	NA	NA	NA	NA
WP_063626989.1\|1160985_1161657_+	phosphoribosylformylglycinamidine synthase subunit PurQ	NA	NA	NA	NA
WP_063626991.1\|1161658_1163881_+	phosphoribosylformylglycinamidine synthase subunit PurL	A6N228	Microbacterium_phage	4.0e-148	41.6
WP_063626993.1\|1163865_1165308_+	amidophosphoribosyltransferase	A0A0M3SGR2	Mollivirus	1.1e-50	32.9
WP_063626995.1\|1165321_1166365_+	phosphoribosylformylglycinamidine cyclo-ligase	Q58MH8	Prochlorococcus_phage	8.3e-64	43.2
WP_010719379.1\|1166361_1166955_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	1.2e-24	34.6

DBSCAN-SWA_2

1774608 : 1828924

Enterococcus_phage(23.53%)

head,terminase,protease,integrase,tail

attL 1788511:1788526|attR 1803269:1803284

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_063627259.1\|1774608_1775307_-\|protease	rhomboid family intramembrane serine protease	NA	NA	NA	NA
WP_010737802.1\|1775320_1775866_-	5-formyltetrahydrofolate cyclo-ligase	NA	NA	NA	NA
WP_010718839.1\|1776227_1777223_-	iron ABC transporter permease	NA	NA	NA	NA
WP_014834567.1\|1777219_1778209_-	iron ABC transporter permease	NA	NA	NA	NA
WP_080292474.1\|1778205_1779021_-	ABC transporter ATP-binding protein	A0A1V0SE00	Indivirus	3.2e-15	31.2
WP_010718836.1\|1779181_1780138_+	ABC transporter substrate-binding protein	NA	NA	NA	NA
WP_063627260.1\|1780216_1780720_-	dihydrofolate reductase	A0A076GDN3	Bacillus_phage	1.3e-19	38.6
WP_002296119.1\|1780888_1781038_-	50S ribosomal protein L33	NA	NA	NA	NA
WP_053766725.1\|1781259_1781706_+	DUF2188 domain-containing protein	NA	NA	NA	NA
WP_063627261.1\|1781814_1783710_-	asparagine synthase (glutamine-hydrolyzing)	F2Y2L7	Organic_Lake_phycodnavirus	3.2e-21	26.5
WP_010718832.1\|1784299_1785247_+	glycosyltransferase family 2 protein	V5USA4	Oenococcus_phage	6.1e-82	50.2
WP_063627262.1\|1785325_1786690_-	hypothetical protein	V9QKK6	Oenococcus_phage	1.1e-07	22.4
WP_063627263.1\|1786974_1787175_-	hypothetical protein	NA	NA	NA	NA
WP_081248822.1\|1787459_1787984_+	helix-turn-helix transcriptional regulator	Q9MBT4	Staphylococcus_prophage	1.2e-18	45.9
WP_063627265.1\|1788097_1788454_+	helix-turn-helix transcriptional regulator	E9LUS8	Lactobacillus_phage	7.7e-22	52.3
1788511:1788526	attL	NA	NA	NA	NA
WP_155727585.1\|1788745_1789276_+	helix-turn-helix domain-containing protein	A0A1S5SFG5	Streptococcus_phage	3.6e-23	46.4
WP_063627266.1\|1789293_1789776_+	hypothetical protein	A1BTY5	Staphylococcus_virus	6.2e-14	33.8
WP_063627267.1\|1789879_1790080_+	hypothetical protein	A0A097BY73	Enterococcus_phage	1.2e-24	87.9
WP_063627268.1\|1790100_1790973_+	LysM peptidoglycan-binding domain-containing protein	NA	NA	NA	NA
WP_063627269.1\|1791135_1792296_+\|integrase	site-specific integrase	A0A1S5S7K9	Streptococcus_phage	4.7e-60	36.5
WP_010737811.1\|1792675_1793242_-	TetR/AcrR family transcriptional regulator	NA	NA	NA	NA
WP_063627270.1\|1793496_1794825_+	DUF1576 domain-containing protein	NA	NA	NA	NA
WP_010718770.1\|1794787_1795129_+	hypothetical protein	NA	NA	NA	NA
WP_010737813.1\|1795542_1796139_+	TVP38/TMEM64 family protein	M1Q152	Streptococcus_phage	4.3e-33	41.7
WP_063627271.1\|1796231_1798034_+	glycerophosphodiester phosphodiesterase	A0A173GBD0	Staphylococcus_phage	2.2e-11	27.6
WP_010737815.1\|1798257_1798476_-	hypothetical protein	NA	NA	NA	NA
WP_063627272.1\|1799173_1800958_-	hypothetical protein	NA	NA	NA	NA
WP_063627713.1\|1801424_1802276_+	hypothetical protein	NA	NA	NA	NA
WP_010737819.1\|1802806_1803079_+	hypothetical protein	NA	NA	NA	NA
WP_010718761.1\|1803292_1803706_-	DUF4231 domain-containing protein	NA	NA	NA	NA
1803269:1803284	attR	NA	NA	NA	NA
WP_063627273.1\|1804788_1806339_-	hypothetical protein	NA	NA	NA	NA
WP_063627274.1\|1806372_1807389_-	hypothetical protein	NA	NA	NA	NA
WP_063627275.1\|1807640_1808621_-	hypothetical protein	A0A1G5SA77	Enterococcus_phage	3.9e-55	63.2
WP_063627276.1\|1808604_1808892_-	hypothetical protein	NA	NA	NA	NA
WP_010719480.1\|1808933_1809215_-	hypothetical protein	NA	NA	NA	NA
WP_063627277.1\|1809371_1809725_-	hypothetical protein	NA	NA	NA	NA
WP_063627278.1\|1810264_1810624_-	hypothetical protein	NA	NA	NA	NA
WP_063627279.1\|1813038_1815750_-	peptidoglycan DD-metalloendopeptidase family protein	Q9AZX5	Lactococcus_phage	7.3e-213	44.1
WP_034867692.1\|1815746_1816487_-\|tail	tail protein	NA	NA	NA	NA
WP_063627714.1\|1816476_1819266_-	tape measure protein	I7A9A7	Enterococcus_phage	2.4e-70	48.5
WP_063627280.1\|1819507_1819849_-	hypothetical protein	NA	NA	NA	NA
WP_063627281.1\|1819848_1820466_-\|tail	phage tail protein	NA	NA	NA	NA
WP_010752291.1\|1820466_1820844_-	hypothetical protein	NA	NA	NA	NA
WP_063627282.1\|1821235_1821607_-	hypothetical protein	NA	NA	NA	NA
WP_002304501.1\|1821606_1821948_-	hypothetical protein	NA	NA	NA	NA
WP_002311614.1\|1821959_1822175_-	hypothetical protein	NA	NA	NA	NA
WP_063627283.1\|1822197_1823088_-	hypothetical protein	NA	NA	NA	NA
WP_063627284.1\|1823102_1823717_-	DUF4355 domain-containing protein	NA	NA	NA	NA
WP_081248824.1\|1823719_1823911_-	hypothetical protein	NA	NA	NA	NA
WP_063627285.1\|1823849_1824167_-	hypothetical protein	NA	NA	NA	NA
WP_063627715.1\|1824168_1825047_-\|head	phage head morphogenesis protein	NA	NA	NA	NA
WP_063627286.1\|1828090_1828924_-\|terminase	small subunit of terminase	D2J000	Enterococcus_phage	2.0e-81	66.1

DBSCAN-SWA_3

2160724 : 2168441

Streptococcus_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_002328071.1\|2160724_2160985_-	hypothetical protein	A0A0S2MYI8	Enterococcus_phage	6.9e-12	52.6
WP_010718684.1\|2161129_2161996_-	16S rRNA (cytidine(1402)-2'-O)-methyltransferase	M1PLC5	Streptococcus_phage	8.6e-91	63.0
WP_010718685.1\|2162537_2162882_-	DNA replication initiation control protein YabA	M1PFV3	Streptococcus_phage	2.9e-18	41.4
WP_010738041.1\|2162874_2163699_-	stage 0 sporulation family protein	NA	NA	NA	NA
WP_010718687.1\|2163734_2164676_-	DNA polymerase III subunit delta'	M1NSC1	Streptococcus_phage	3.4e-32	32.3
WP_010718688.1\|2164684_2165014_-	hypothetical protein	NA	NA	NA	NA
WP_010718689.1\|2165028_2165673_-	dTMP kinase	M1PSC7	Streptococcus_phage	3.5e-57	52.2
WP_010718690.1\|2165736_2166333_-	recombination protein RecR	NA	NA	NA	NA
WP_010718691.1\|2166356_2166668_-	YbaB/EbfC family nucleoid-associated protein	NA	NA	NA	NA
WP_034699015.1\|2166692_2168441_-	DNA polymerase III subunit gamma/tau	A0A1U9WR94	Streptococcus_virus	9.3e-52	41.9

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_CP015517

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP015516

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection