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_CP041029	Riemerella anatipestifer strain WJ4 chromosome, complete genome	2 crisprs	cas3,RT,DEDDh,cas2,cas1,cas9,WYL	1	6	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP041029_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP041029_1

326675-326745

Orphan

Consensus_repeat	Method
AAGGTTTAAAGTTCAAATATTCAAGG	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_CP041029_1

>merge|NZ_CP041029|1|326675-326745|CRISPRCasFinder
AAGGTTTAAAGTTCAAATATTCAAGGGGTAAGGGTTCAAGAGTTCAAAGTTTAAAGTTCAAATATTCAAGG

>NZ_CP041029|1|1|326675-326745|CRISPRCasFinder
AAGGTTTAAAGTTCAAATATTCAAGG	GGTAAGGGTTCAAGAGTTC
AAAGTTTAAAGTTCAAATATTCAAGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP041029.1\|WP_004918929.1\|322309_323674_-\|signal-recognition-particle-protein	unknown	unknown	gnl\|CDD\|236780
NZ_CP041029.1\|WP_038694348.1\|330219_331734_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	unknown	unknown	gnl\|CDD\|234854
NZ_CP041029.1\|WP_014938677.1\|319050_319674_+\|PorT-family-protein	unknown	unknown	gnl\|CDD\|372635
NZ_CP041029.1\|WP_014938669.1\|324432_325278_-\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	unknown	unknown	gnl\|CDD\|236467
NZ_CP041029.1\|WP_014938663.1\|331771_334597_-\|excinuclease-ABC-subunit-UvrA	unknown	unknown	gnl\|CDD\|234734
NZ_CP041029.1\|WP_014938658.1\|341298_341553_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_014938670.1\|323740_324436_-\|RNA-methyltransferase	unknown	unknown	gnl\|CDD\|349965
NZ_CP041029.1\|WP_014938671.1\|321616_322234_+\|protein-tyrosine-phosphatase	unknown	unknown	gnl\|CDD\|319973
NZ_CP041029.1\|WP_014938660.1\|338745_340839_+\|toprim-domain-containing-protein	unknown	unknown	gnl\|CDD\|227832
NZ_CP041029.1\|WP_014938665.1\|328879_329263_+\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|375718
NZ_CP041029.1\|WP_127919815.1\|341557_343066_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|274043
NZ_CP041029.1\|WP_014938675.1\|320128_320518_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_014938672.1\|321126_321597_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_004918915.1\|334720_335665_-\|SPFH-domain-containing-protein	unknown	unknown	gnl\|CDD\|259805
NZ_CP041029.1\|WP_014938668.1\|325277_326036_-\|peroxide-stress-protein-YaaA	unknown	unknown	gnl\|CDD\|234999
NZ_CP041029.1\|WP_014938659.1\|340857_341073_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_038694124.1\|338330_338729_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_014938676.1\|319681_320107_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|369706
NZ_CP041029.1\|WP_014938673.1\|320738_321071_+\|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|238042
NZ_CP041029.1\|WP_038694347.1\|335992_337774_+\|30S-ribosomal-protein-S1	unknown	unknown	gnl\|CDD\|235775

Protein	Function_ID	Function_description	E-value
NZ_CP041029.1\|WP_004918929.1\|322309_323674_-\|signal-recognition-particle-protein	gnl\|CDD\|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP041029.1\|WP_038694348.1\|330219_331734_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	gnl\|CDD\|234854	PRK00881, purH, bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional.	0
NZ_CP041029.1\|WP_014938677.1\|319050_319674_+\|PorT-family-protein	gnl\|CDD\|372635	pfam13568, OMP_b-brl_2, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	2.2956e-11
NZ_CP041029.1\|WP_014938669.1\|324432_325278_-\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	gnl\|CDD\|236467	PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional.	2.22066e-91
NZ_CP041029.1\|WP_004918915.1\|334720_335665_-\|SPFH-domain-containing-protein	gnl\|CDD\|259805	cd03407, SPFH_like_u4, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.	1.04006e-136
NZ_CP041029.1\|WP_014938670.1\|323740_324436_-\|RNA-methyltransferase	gnl\|CDD\|349965	cd18092, SpoU-like_TrmH, SAM-dependent tRNA methylase related to TrmH. TrmH catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of the ribose of the universally conserved guanosine 18 (G18) position in tRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	5.22244e-64
NZ_CP041029.1\|WP_014938671.1\|321616_322234_+\|protein-tyrosine-phosphatase	gnl\|CDD\|319973	cd16345, LMWP_ArsC, Arsenate reductase of the LMWP family. Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).	3.54904e-14
NZ_CP041029.1\|WP_014938660.1\|338745_340839_+\|toprim-domain-containing-protein	gnl\|CDD\|227832	COG5545, COG5545, Predicted P-loop ATPase and inactivated derivatives [General function prediction only].	3.46678e-17
NZ_CP041029.1\|WP_014938665.1\|328879_329263_+\|DNA-binding-protein	gnl\|CDD\|375718	pfam18291, HU-HIG, HU domain fused to wHTH, Ig, or Glycine-rich motif. Rapidly-diverging family of HU domains predominantly observed in the bacteroidetes lineage with a predicted role in recognition and possible interception of the DNA of parasitic elements, a counter-conflict strategy preventing incorporation of these elements into the host genome.	1.77568e-39
NZ_CP041029.1\|WP_014938663.1\|331771_334597_-\|excinuclease-ABC-subunit-UvrA	gnl\|CDD\|234734	PRK00349, uvrA, excinuclease ABC subunit UvrA.	0
NZ_CP041029.1\|WP_038694347.1\|335992_337774_+\|30S-ribosomal-protein-S1	gnl\|CDD\|235775	PRK06299, rpsA, 30S ribosomal protein S1; Reviewed.	0
NZ_CP041029.1\|WP_014938668.1\|325277_326036_-\|peroxide-stress-protein-YaaA	gnl\|CDD\|234999	PRK02101, PRK02101, peroxide stress protein YaaA.	1.13133e-107
NZ_CP041029.1\|WP_014938676.1\|319681_320107_+\|hypothetical-protein	gnl\|CDD\|369706	pfam08139, LPAM_1, Prokaryotic membrane lipoprotein lipid attachment site. In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.	0.00184218
NZ_CP041029.1\|WP_014938673.1\|320738_321071_+\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	9.16634e-15
NZ_CP041029.1\|WP_127919815.1\|341557_343066_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|274043	TIGR02225, Tyrosine_recombinase_XerD, tyrosine recombinase XerD. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerD, one of two closely related chromosomal proteins along with XerC (TIGR02224). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and with homologs of XerD on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerD, as some apparent XerD examples score below the trusted and noise cutoff scores. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	7.82164e-35

>NZ_CP041029.1|WP_014938668.1|325277_326036_-|peroxide-stress-protein-YaaA
MLILSSPAKLMNISLKSDMLKLTEPQFIEDSAFIQSFLKEKTPQYLSDLMEISSKLADENWERNQNWSTSPSEEESNAALYTFTGEVYRGLDAPTLDKKAVDYLQKHYRILSGLYGLLKPSDRIMLYRLEMGRPFQFDKYKNLYSFWKSKITAALNEELKDDDILLNLASTEYFKSVDTKKLKAKVIDVKFYEYKNGKLKTIVVYTKHARGLLIRFCAETNAKTLDDIKAFNYEGYLIDEERSKDNQLVFVR
>NZ_CP041029.1|WP_014938669.1|324432_325278_-|peptide-chain-release-factor-N(5)-glutamine-methyltransferase
MKLLELHSIFKQELSELYNSSEISCLWEIFGEHYLGLDKIGLRQSENTQLPSQPIVQYTEAINQLKSGKPYQQILGEAEFFGMKFCVNQHVLIPRPETEELLDYAIKTISKEFSKTEIKILDIGTGSGVIPIVLKKHFPNARIASIDFSKEALTIAKKNAERHHTEIEFILDDYLNYTLPTHYDVIISNPPYIDIEEVSEISDTVKNFEPHLALFSPCADPLVFYRKIATDAKQYLNNGGFLFLEINQKLGAETLALYKDFSDAQLIKDLSNNDRMIIAKK
>NZ_CP041029.1|WP_014938670.1|323740_324436_-|RNA-methyltransferase
MKPELTNNLEDLEKTFQYLAQFLTEERLQKINHYAEESSDFILPVMEDVYQYRNAAAIVRSVEACAFHKVVALEKDNIFDPNLSVTKGADTWVEVEKMPRNKASLEKIKERGYKIVAVSPENNAMMLPDYKVETPIALVFGTEWEGVSDELLDFADETLAIPMYGFTKSFNVSVAAAICMYELKQKLLNSTIDYKLSPDEKWHTKIRWAVNSIRSGEEIYHKFLRENFNNP
>NZ_CP041029.1|WP_004918929.1|322309_323674_-|signal-recognition-particle-protein
MFNSLQDKLDKALHNLSGRGKITEINVAETVKEIRRALVDADVNYKVAKDLTKRVQEKALGQNVLTSLTPGQLMTKIVHDELVELMGGSQEGINLSGKPTVILIAGLQGSGKTTFSGKLANYLKKKRAKNPLLVACDVYRPAAIDQLKVLGSQTGIPVYTEEENKNPSTIAENAVNFAKANKHDVVIVDTAGRLAIDEQMMNEIKSVHYFIKPTETLFVVDSMTGQDAVNTAKAFNDALNFDGVVLTKLDGDTRGGAALTIRSVVNKPIKFISTGEKMEALDLFYPERMADRILGMGDVVSLVERAQEQFDEEEAKKLQKKIAKNEFGFDDFLKQIQQIKKMGNMKDLLGMLPGVGKAIKDVDIDDNSFKHIEAIIHSMTPEERRRPSIIDVNRKKRIAKGSGRKLEEVNQLMKQFDQMGKMMKMMQGPQGKQLMAMMGKMGGGMPGMGGLFGR
>NZ_CP041029.1|WP_014938671.1|321616_322234_+|protein-tyrosine-phosphatase
MPLLSKIQNFIEKLEVNSISEERKKILQPLIDFITEKQRKGEFIRLNFICTHNSRRSHLCQIWAKTMAYYFGIYNVECYSAGTEATALFPKIAETLHNVGFSIKVLSKEENNPIYAIKYSDNEMPIIGFSKTLDHLFNPKVNFAAVMTCSQADNNCPSVLGAEKRFSIAYEDPKVSDNTPKQSFVYAERNLQIATEMLYVFQSIK
>NZ_CP041029.1|WP_014938672.1|321126_321597_+|hypothetical-protein
MKLSEFKKVLATLSRIDFQTPNGDFIPPHFHITEVGQITKDFIDCGGIVRKEKWVNFQLWTATDYDHRLTPEKLLDIIALSEKQLQLTDEEIEVEYQEESIQKFGLDFQGNHFVLTTKQTDCLAPDKCGIPTEKPKLKLSELQNKTNCCDPNSGCC
>NZ_CP041029.1|WP_014938673.1|320738_321071_+|winged-helix-turn-helix-transcriptional-regulator
MKRNLEPIDYTEDVELLADFAKALAHPTRIAILSYLEQQNSCFTGDLVDIFPLAQSTISQHLKELKRVGLIKGELNPPKIKYCIDEEKWNLAKSLFFNFFDKKTQSSCCD
>NZ_CP041029.1|WP_014938675.1|320128_320518_+|hypothetical-protein
MKYLVLGLSLLCLTTLFSCKNNDDDIEFVNQNSTPLEGVWKLQNIPSGSRLTFEKQNWKLESGTVRITGTFTLSGNTINAVVINRSGSGSSALQPDAFTGNIAIEGNKATFTNFSGNWYAVFSTWYQKQ
>NZ_CP041029.1|WP_014938676.1|319681_320107_+|hypothetical-protein
MRKILFLFVAIALLQNCSRDRENETSNPIKKSQFFNPPSWIRGKWGHGNVVVFKFTNDDFFTSSISHKGLLESTRSAGGTAVVDEDISNSHYDFTIKIGNPGGSGPVSEGEYQFRRVSSTKIEWVNNPAGNDDSYYLTKIQ
>NZ_CP041029.1|WP_014938677.1|319050_319674_+|PorT-family-protein
MKKVLLLAAAITANFYSAQTDSYGLKAGLNISSLSTNFKNEYNSFYSVELDSRSKVGVYLGAYIERKYTEKSSLNAEALLSFQGARLSLTQKISVPSYGYGSSNYDKTVVTNVNFTQLNIPVYYKYKTNERFAVHGGGYLGLTLSSDANGVTLENNTFDLGLIAGASYTINDKFSAEARYNLGLLNLDKSNEFKNRTFQLGISYQLK
>NZ_CP041029.1|WP_014938665.1|328879_329263_+|DNA-binding-protein
MPVKFKVIERGQPGVSGGGDKKWYATPVSSGEKTLTDLTKDIEKISTVSGADIRAVLYALVDVMQSSLASGQIVRLGELGSLRVSFSSEGKATEKEVTASAIKQAKVIFTPAKGIKDTLATLTYEKA
>NZ_CP041029.1|WP_038694348.1|330219_331734_-|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase
MKKRALISVSDKTNLVEFATFLEQHNYQLISTGGTFKHLKEAGLSPIQIDEVTEFPEMLDGRVKTLHPKVHGGLLAVRSNPEHMSTVKDHGIELIDMVIVNLYPFFENVNKNISLDEKVEFIDIGGPSMLRSAAKNFNAVTVVTDVKDYAKVQAEISEAGDTTLETKKTLAGKVFNLTSAYDAAISKMLLEEEYPEYLNASYQKVADLRYGENPHQSAAYYVSTTENGAMKDFEQLGGKELSFNNLRDMDLCWKVVNEFKNEKACCAVKHSTPCGVAIGETALDTYKKAFECDPVSIFGGIVAMNYTVDKDTAEELNKTFLEIVMATDFDAEALEVLSKKKNLRIIKIKNPVSDRQVWVKIDGGMLVQNADDQFSDDIKTVTEVQPTEEQTKALLFSQRIVKYVKSNAIVVTNGTQALGVGGGQVNRIWATQQAIERAKEKFSGDLVLASDAFFPFRDVVDTCAKEGIKAIIQPGGSMRDDESIQAANEHNIPMLFTGMRHFFH
>NZ_CP041029.1|WP_014938663.1|331771_334597_-|excinuclease-ABC-subunit-UvrA
MMKNRDFIEVYGAREHNLKNIDVKIPRNELVVITGLSGSGKSSLAFDTIFAEGQRRYIETFSAYARQFLGGLERPDVDKIEGLSPVIAIEQKTTNKNPRSTVGTVTELYDFLRLLFARVSTAYSLETGKKLQSYTEEQILETIKEQYQNEKVLLLAPLVKARKGHYHELFVQLAKKGYSQARIDGTLQDIEYDLKLDRYKTHDIEVVIDRWIIGETASEARMQKSLSTALQMGGGVVMVQKYNSEEFQYFSKDLMDTATGQALPLPEPNTFSFNSPKGSCPHCKGLGTVKKINPDYLVTEPTLPFQSALLPLETYKFSKWALSQIKSILELFELSLLTPFNKIPKEALDYIYYGCEKEFVKDLKHAGISKKTKINFEGLIPHLEKVIEDKENYGATQVEREFTVEEICTDCNGTRLKPESLAFKIEGKTIAEVNAMSLLDLKDWLSEIKNSFSEKNKIIAHEILKEIETRLGFLLDVGLEYLSLSRSSKTLSGGESQRIRLATQIGSQLVNVLYILDEPSIGLHQRDNERLINSLKSLRDLGNSVLVVEHDKDMILEADEVLDIGPKAGKYGGKVLWQGSPKDLIKADTITADYLTGRRKIEIPEKRREGNGNSIVLKGATGNNLKNVTLKIPLGKMVVVTGISGSGKSSLINGTLYPILNRHFYRAVQEPLPYKKIEGIEHIDKIVDVDQTPIGRTPRSNPATYTGVFSDIRTLFANLPESKIRGYKAGRFSFNVKGGRCETCQGGGLKVIEMNFLPDVYVHCETCNGKRFNRETLEVRYKGKSISDVLDMTIDEAVEFFQPIPKIYSKVKTLQEVGLGYITLGQQSTTLSGGEAQRVKLATELSKKQTGKTLYILDEPTTGLHFEDVKILMEVIQKLVDLGNSFIIIEHNMDVIKLADHIIDVGPEGGKNGGSIIAEGTPEEIIKNKKSITGKFLKKEM
>NZ_CP041029.1|WP_004918915.1|334720_335665_-|SPFH-domain-containing-protein
MITTFSFILGSLGAVLFVGIIFLSFFGLWFIVKQQTSVIIERLGKFHSVRGPGFHLKIPFVDQIAGRISLKIQQLDVVVETKTKDDVFVKIKVSTQYLVIGEKVYDAFYKLDNPHAQITSYIFDVVRAEVPKLRLDDVFEKKDDIAIAVKSELQEAMNDYGYDIIKTLVTDIDPDEQVKQAMNRINASEREKIAAQYEGDAQRILIVEKAKAEAESKRLQGQGIADQRREIAKGLEESVNVLNKVGINSQEASALIVVTQHYDTLSSIGSTNKSNLILLPNTPNAAGDMLNNLVTSFSTASIIGEEIKKKNKEA
>NZ_CP041029.1|WP_038694347.1|335992_337774_+|30S-ribosomal-protein-S1
MSEQTKQQEEVLLNQNVAPENFDWDSFESGLNAEDRNEKKELEEIYKGSLSDLAEDDVIVGKVVRLTDKEAIVDIDFKSEGVISLNEFRYNPSLKVGDEVEVMVDRREDKTGQLQLSHKKARTLKAWDKVNQYHESGEVVNGFVKSRTKGGMIVDVFGIEAFLPGSQIDVKPIKDYDQYVGKTMEFKVVKINPEFKNVVVSHKALIEADIEDQKKEIIAQLEKGQVLEGTVKNITSYGVFIDLGGVDGLVHITDLSWSRVNHPTEILEDGQTVKVVILDFDEDKTRIQLGMKQLEAHPWDALDENLKVGDKVKGKVVVLADYGAFVEVAPGVEGLIHVSEMSWSTHLRSAGDFVKVGDEVEAQVLTLDKEERKISLGMKQLSEDPWANIQDKYPLGSKHSGTVRNFTNFGVFLELEEGIDGLIYISDLSWTKKIKHPSEFCSVGDKLDVVVLELDVDARRLSLGHKQLTENPWDKFETKYAEGTVHTGVASDVFDKGAQVKFEDVEVEAFCPARLLEKEDGSKIKKGDEAEFKVIEFNKEFKRVVVSHTGLFREEEKKNVKEAATKSSASEEKTTLGDIDALAELKKKMEEGK
>NZ_CP041029.1|WP_038694124.1|338330_338729_+|hypothetical-protein
MVNFGITLSNLSTYIQVSNRNRIEREKLAISLQEQLSSEINTIDAEILDLQRDSIALAYEYQNITLLEELNTIKLKQYEQNQINLEEKIRHQMNLNNSKNTFEIRKINYINRRNKLINKLKKPSKSTDFLGL
>NZ_CP041029.1|WP_014938660.1|338745_340839_+|toprim-domain-containing-protein
MDKNTILQQTNQIEIYNFYYGSHFQPYTKISSPFSEDQNPSFKVFKNGTFKCFSTGKQGDVWQFVADIKGLDCKTQFAEVLKTISNDMGVILQQQQKNSSHQSISKNTDNHHFKYYDKPYTSQSLEFWTQGNWKVTKAILEKYNVKNLDKYEYFNSKKNTIQKIKLYSGIVGFIYKVNSNAEIYIPAQGKNKKIFYNNLQFSDIFGYEQLKEKEDYIIITAGKKDCLILNANGFPAVSFRSESGFIKEEEILKLKQKTDNIYICYDNDKTGLETALKLCNSYSIKQIILPEKYNDIADYFLVYDKSHYQKLIDEIRELEEAETKKDTQNTIFHITEEYLSTYYKFRYNTIALDIEYCKKTTHEWKSLNENSLYLELQKKGIKISINNLIAILKSEFVPHYNPIQEYFENLPKWDGKTDYISNLANYVYPLDREKFNHHFKKWAVRTVKCALLERYFNKQAFVLVHKAQNSGKSSFCRFLCPPELSQYLAEDISNDKDARILLCKNFLINLDELSSLAKKEINTLKSYFSKDQINERLPYDRKNSILPRICSFIGSTNRDTFLDDETGSVRWLCFQITGINWNYRQECNIDLFWSQAYALAFDNNFNSEMTLEEIQDNEDRNKKYQILSTEQELIASNYKPAQENEGVFVTSTDVLIRLSELGVRLSSVQIGKAFNALGFERKKHKTKQTYGYWVKVL
>NZ_CP041029.1|WP_014938659.1|340857_341073_+|hypothetical-protein
MKQVEIKNEVEYIDGVREALSYILEVIDKDTDYLYHEKEIIKKIIHSEIWKNISEKEFNHFLNQLQQQKNK
>NZ_CP041029.1|WP_014938658.1|341298_341553_+|hypothetical-protein
MKSKITLLTAAVLLLTTCNHYQLTQEDRALLKKYPETYLSHNGYSHLVRARRLEIADSIQKAHQQDLSQEFKEEQYQNNTPEDL
>NZ_CP041029.1|WP_127919815.1|341557_343066_+|tyrosine-type-recombinase/integrase
MMTIDYISKEESLLLIEKCKNPKYKCIILLMLDCGFRVSETVTLRLKNFDFQKRTITVKSLKKKNENYRTIPISDRLYRAIAHYLEQTKIPITQPENYLFPSYTHKGHLCRKTVWKVLKAYGKKLGIQNLHPHTLRHTFATHHLNNGTKLEEIKTMLGHSSYDTTLIYAQIPTEQLSKKIEAVTTQKRNFWVRIQQKFFPPKKTKLINLSFNKNYFTIGRNEELSKLNVNAELGINTIIIGDIGTGKTHLLENLKTNKKILKFEDDRMAKKSLMYMMLHLLKGDKENMLSLLYGDIGIEAVEKKIQRESALFICDKIMTIVEPKEYILLIDNITDITTASKRIIERLKDTFVIICAARYIKNSNTSFLWNFEKIDLKNLSRENAIKFIQQNSFGLEVESWEDFRNHIYQQTNGNPRAMAEMIDRYRKEPFLTLDIVKNIKHSGALPEIDFTFIIVVFLGIITALRYASRELDEPALRMIGSIGLILLIISRPLFKELKRKFI

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Crispr_ID: NZ_CP041029_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP041029_2

971960-972775

TypeII

Consensus_repeat	Method
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	CRISPRCasFinder
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	PILER-CR

10 spacers

cas2,cas1,cas9

The CRISPR arrays of NZ_CP041029_2

>merge|NZ_CP041029|2|971960-972775|CRISPRCasFinder,PILER-CR
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACCTATTTTGTTTTTTAAGTGTGAATTGTGCGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTTCTACAAAGTCTAGCCACGCACCCATAGCGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACATATCACGAAAATTTAAAGTTTAGCGACACGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACAGCCTCTAACTCATACGCACAGGCACAGGCGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACCGACAACTTTTTTTGGGTGGCGCCGCCAGAGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTTTCGTACATAAATTACGCCTCGTGCGTGTGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTCTTTATACTAAGAGCATTTAGCAACAATAGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTATTTTCCAAACAGGCGATTTGGCGGGTTAGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTTTATCGCTAAAATTATTAAGGGCAGGAAAGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAACTGGCTTGTTCTGATACAGACGCATTTCTAAGTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC

>NZ_CP041029|2|2|971960-972775|CRISPRCasFinder
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	CTATTTTGTTTTTTAAGTGTGAATTGTGC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTCTACAAAGTCTAGCCACGCACCCATAGC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	ATATCACGAAAATTTAAAGTTTAGCGACAC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	AGCCTCTAACTCATACGCACAGGCACAGGC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	CGACAACTTTTTTTGGGTGGCGCCGCCAGA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTTCGTACATAAATTACGCCTCGTGCGTGT
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TCTTTATACTAAGAGCATTTAGCAACAATA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TATTTTCCAAACAGGCGATTTGGCGGGTTA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTTATCGCTAAAATTATTAAGGGCAGGAAA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TGGCTTGTTCTGATACAGACGCATTTCTAA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC

>NZ_CP041029|2|1|972036-972775|PILER-CR
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTCTACAAAGTCTAGCCACGCACCCATAGC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	ATATCACGAAAATTTAAAGTTTAGCGACAC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	AGCCTCTAACTCATACGCACAGGCACAGGC
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	CGACAACTTTTTTTGGGTGGCGCCGCCAGA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTTCGTACATAAATTACGCCTCGTGCGTGT
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TCTTTATACTAAGAGCATTTAGCAACAATA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TATTTTCCAAACAGGCGATTTGGCGGGTTA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TTTATCGCTAAAATTATTAAGGGCAGGAAA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC	TGGCTTGTTCTGATACAGACGCATTTCTAA
GTTGTGAATTGCTTTCAATTTTTACTATCTTTGTGATAGTTCGCAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP041029.1\|WP_014938038.1\|973210_974110_-\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
NZ_CP041029.1\|WP_052911821.1\|979833_980163_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|185668
NZ_CP041029.1\|WP_014938044.1\|962740_964369_-\|methylcrotonoyl-CoA-carboxylase	unknown	unknown	gnl\|CDD\|178415
NZ_CP041029.1\|WP_038693825.1\|966922_969730_+\|carboxypeptidase-regulatory-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|200604
NZ_CP041029.1\|WP_014938032.1\|981379_982126_+\|DUF3108-domain-containing-protein	unknown	unknown	gnl\|CDD\|378635
NZ_CP041029.1\|WP_004918191.1\|982703_983369_+\|DUF937-domain-containing-protein	unknown	unknown	gnl\|CDD\|368733
NZ_CP041029.1\|WP_014938030.1\|983519_984494_+\|deoxyhypusine-synthase	unknown	unknown	gnl\|CDD\|376661
NZ_CP041029.1\|WP_014938048.1\|957587_959600_-\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236054
NZ_CP041029.1\|WP_014938046.1\|960455_962264_-\|ComEC/Rec2-family-competence-protein	unknown	unknown	gnl\|CDD\|377126
NZ_CP041029.1\|WP_014938043.1\|964475_965669_-\|endonuclease	unknown	unknown	gnl\|CDD\|197338
NZ_CP041029.1\|WP_014938041.1\|969755_971159_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_004918211.1\|972882_973221_-\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP041029.1\|WP_064970014.1\|978851_979787_+\|2-nitropropane-dioxygenase	unknown	unknown	gnl\|CDD\|240081
NZ_CP041029.1\|WP_014938047.1\|959662_960331_-\|succinate-dehydrogenase-cytochrome-b-subunit	unknown	unknown	gnl\|CDD\|239578
NZ_CP041029.1\|WP_014938049.1\|956793_957564_-\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|181038
NZ_CP041029.1\|WP_014938040.1\|971508_971778_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP041029.1\|WP_014938050.1\|955625_956708_-\|DNA-polymerase-IV	unknown	unknown	gnl\|CDD\|235035
NZ_CP041029.1\|WP_140222294.1\|980168_981221_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223566
NZ_CP041029.1\|WP_004918194.1\|982155_982656_+\|DUF2480-family-protein	unknown	unknown	gnl\|CDD\|313799
NZ_CP041029.1\|WP_014938037.1\|974122_978340_-\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|375967

Protein	Function_ID	Function_description	E-value
NZ_CP041029.1\|WP_014938030.1\|983519_984494_+\|deoxyhypusine-synthase	gnl\|CDD\|376661	pfam01916, DS, Deoxyhypusine synthase. Eukaryotic initiation factor 5A (eIF-5A) contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first step in the post-translational formation of hypusine is catalyzed by the enzyme deoxyhypusine synthase (DS) EC:1.1.1.249. The modified version of eIF-5A, and DS, are required for eukaryotic cell proliferation.	4.83992e-36
NZ_CP041029.1\|WP_014938044.1\|962740_964369_-\|methylcrotonoyl-CoA-carboxylase	gnl\|CDD\|178415	PLN02820, PLN02820, 3-methylcrotonyl-CoA carboxylase, beta chain.	0
NZ_CP041029.1\|WP_014938032.1\|981379_982126_+\|DUF3108-domain-containing-protein	gnl\|CDD\|378635	pfam11306, DUF3108, Protein of unknown function (DUF3108). This is a bacterial family of putative lipoproteins. Structure 3fzx, the first structural template for this large family including several homologs in the human gut microbiome and in metagenomic datasets, folds into a beta barrel that topologically looks like a small-scale porin (such as FepA). Bacteroides fragilis glyA is a putative exported protein, and this fold is of the YmcC-like type, with a predicted signal peptide SpI cleavage site AGAMA\|QNQDC, and a Phobius server prediction of non-cytoplasmic localization for amino acids 21-236. The possibility of it being a membrane protein can be ruled out by the hydrophilic nature of the solvent exposed surface outside the barrels. Analysis of sequence conservation suggests that an area near Glu172/Trp206 is potentially interesting. These two residues are also conserved in Dali hit Structure 2in5, a hypothetical lipoprotein classified as a new YmcC-like fold in SCOP (SCOP:159271, with a 12-stranded meander beta-sheet folded into a deformed beta-barrel) despite large structural differences between the two structures, suggesting similarity in function.	1.92447e-65
NZ_CP041029.1\|WP_004918191.1\|982703_983369_+\|DUF937-domain-containing-protein	gnl\|CDD\|368733	pfam06078, DUF937, Bacterial protein of unknown function (DUF937). This family consists of several hypothetical bacterial proteins of unknown function.	9.81533e-14
NZ_CP041029.1\|WP_014938048.1\|957587_959600_-\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236054	PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	0
NZ_CP041029.1\|WP_014938046.1\|960455_962264_-\|ComEC/Rec2-family-competence-protein	gnl\|CDD\|377126	pfam03772, Competence, Competence protein. Members of this family are integral membrane proteins with 6 predicted transmembrane helices. Some members of this family have been shown to be essential for bacterial competence in uptake of extracellular DNA. These proteins may transport DNA across the cell membrane. These proteins contain a highly conserved motif in the amino terminal transmembrane region that has two histidines that may form a metal binding site.	3.21871e-54
NZ_CP041029.1\|WP_014938043.1\|964475_965669_-\|endonuclease	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	2.65668e-12
NZ_CP041029.1\|WP_052911821.1\|979833_980163_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	gnl\|CDD\|185668	PTZ00490, PTZ00490, Ferredoxin superfamily; Provisional.	7.26116e-19
NZ_CP041029.1\|WP_004918211.1\|972882_973221_-\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.87616e-22
NZ_CP041029.1\|WP_064970014.1\|978851_979787_+\|2-nitropropane-dioxygenase	gnl\|CDD\|240081	cd04730, NPD_like, 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.	2.84203e-100
NZ_CP041029.1\|WP_014938047.1\|959662_960331_-\|succinate-dehydrogenase-cytochrome-b-subunit	gnl\|CDD\|239578	cd03498, SQR_TypeB_2_TM, Succinate:quinone oxidoreductase (SQR)-like Type B subfamily 2, transmembrane subunit; composed of proteins with similarity to the SQRs of Geobacter metallireducens and Corynebacterium glutamicum. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. C. glutamicum SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) or Complex II and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The transmembrane subunit of members of this subfamily is also called Sdh cytochrome b558 subunit based on the Bacillus subtilis protein. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes. Proteins in this subfamily from G. metallireducens and G. sulfurreducens are bifunctional enzymes with SQR and QFR activities.	1.38468e-62
NZ_CP041029.1\|WP_014938049.1\|956793_957564_-\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	gnl\|CDD\|181038	PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated.	0
NZ_CP041029.1\|WP_038693825.1\|966922_969730_+\|carboxypeptidase-regulatory-like-domain-containing-protein	gnl\|CDD\|200604	cd11308, Peptidase_M14NE-CP-C_like, Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.	3.3669e-06
NZ_CP041029.1\|WP_014938038.1\|973210_974110_-\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	1.95987e-92
NZ_CP041029.1\|WP_140222294.1\|980168_981221_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|223566	COG0492, TrxB, Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones].	4.69146e-73
NZ_CP041029.1\|WP_004918194.1\|982155_982656_+\|DUF2480-family-protein	gnl\|CDD\|313799	pfam10652, DUF2480, Protein of unknown function (DUF2480). All the members of this family are uncharacterized proteins, but the environment in which they are found on the bacterial genome suggests a function as a glucose-6-phosphate isomerase (EC 5.3.1.9). This could not, however, be confirmed.	2.81272e-92
NZ_CP041029.1\|WP_014938050.1\|955625_956708_-\|DNA-polymerase-IV	gnl\|CDD\|235035	PRK02406, PRK02406, DNA polymerase IV; Validated.	0
NZ_CP041029.1\|WP_014938037.1\|974122_978340_-\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	5.53437e-54

>NZ_CP041029.1|WP_014938040.1|971508_971778_+|hypothetical-protein
MSSKSVYENEKGFKFVAKLKAEMKQKIPSLLYPETKEALSPLLLKANLEIFFQMKEFIKLIKNIFSKEPFEQDITIRFSLSLEQIIFIF
>NZ_CP041029.1|WP_014938041.1|969755_971159_+|hypothetical-protein
MKTTTYLKTSLIALSFGALTSCVHDDKFDTPAIQCSNQFSEPTTTIKDFKTLAPTPVNFVSNYTIPNGETDAPVIFEGYVISSDEGGNFYKQLTIQDNTENPTAGIQVAINKTFLYTDYPVGSRVRVRANGLSVGLDREVVKLGYVNPTGQIPEGNMRDFITGVCGGNTMDIKAITPRVVNSIAEATKDEYINTLVTIKGVQFSEADGKITYADAVNRQTVDRTLVDREDNTAVVRNSGFARFAGKTLPTESGDITVVVNKYVSGRNVTWQLYIRDLNDVKFEQERFVSSKNVLGGNAPEYNKTMTEAFDNVSTVTNFKRIADPKYINYSVFGNRFWEQKTFSGNNYIQISAFRANADVSTYFIVPAEFTGSSKLSFQTKDGYYTGDALKVYYTTKYTPGGVVNKTDLIDITSKFTLSKGNTNGYAADWVDSGEFTIPTTGKGYIFFEYVGNTTVTTTVQIDNITLK
>NZ_CP041029.1|WP_038693825.1|966922_969730_+|carboxypeptidase-regulatory-like-domain-containing-protein
MIKKLSLVSMFCLLPASYYYAQTTVYAYVKDADGKPIENAVADLREANDDVKADKIGYFQFVDLKPGHYQMVVTQPNYETKVLEFDVFENEKRKDLGIITLFSNLKNSELGVVLLDDNSSMDESSSQATLGLLQSSRDVFSNIAAFDLGFYWFRPRGIDGRRSEVMMNGISMENADNGNVDYGNWGGLNEITRYPEIAVNHSPSEYAFGGVGSVVYKNMKASEYRKGFQFTQSLTNRNYRNRTSLRYSSGMNKKGWAFTVMGARRWAQEGIQEGTFYDAYGAYLGIEKKVNDKHTLTLNLIGSPYRRSTASPNTQEVIDYNGVHYNAFWGWQDGEKRSERVRKGFQPILQLTDYWKISSRSQLWTTVSYQFGKDKASRLDWYNAQNPSPLYYRNLPSYFAGLANPSDSDIAQLEITKNRWESNDQNYTQINWDRLYLANRNREQAVYFLVNDVNDDKVWNVGTHFVHNFSDKTQLFINASYRNYLSNQYREIKDLLGAQYALNGDPFASTNQPKLSGLFNEGEENTHKKVGDKIGYDYTFRRQETKINPALKFSTGNFDIFVSALAAYITNNREGHFNHYLYKDALGKSENQDYWNFGLKGQVIYKLDGRNFLVYNSAYYSQAPYLNNLFINARVNSAIAPNIKNTIVSANDISYMVSSPFVKVRATAFLINTQNDTNVQRFFADGIKLDGVDSEGNTTSARSAFVTQVMSNVNRRNMGAELGVEVKVTPTITVNGVANYGKYIYTNNPEVYFASDAVGMFPNEKLYTSYGTSYIKNFRQGGTPQEAYSLGVKYSSPKYWWVGANWNYLGSNFLDPSPLIRSDFFVNNPVTETPYAGISEEEYKRVTAQVKLPVAYFFNINAGKSWMLGKYYVLISATVNNVLDNTKYATGGFEQTRNVNFADFRRDYDREYPNFAPRYFFTQGRNYFINLQVRF
>NZ_CP041029.1|WP_014938043.1|964475_965669_-|endonuclease
MKMKKIFSLLTLGLFLTSFSQTGKLRRMATVGFYNVENLWDTIQSADYIDGTLPPNHPRFHRSVPIDSVKYLEREDYKGEWSDSKLIGKKVVRFQGSSEEFTPKSAKNYNTSIYNQKLINAARVISELGASVTKTAPVVVGLLEVENRQVVEDLVKQPALKRYDYGVIHYNSYDYRGIDVALIYQKRRFSSTYSTKKELKIYNEEGKREYTRDLLVVSGYLDGEKVAFFVNHWPSRRGGEAVSLPKRNAAAQLLRVQMDSVRALDANTKLIAMGDFNDDPISSSLKNYLKAVGSTKELSPEYPYLNLMYPLYKKGVASLAYRDAPNLFDQIIVSENLVSPKDASYSIFRTEVYAPAYLINKEGSFKGYPFRSWDGDKFTGGYSDHFPVFTILYKEVN
>NZ_CP041029.1|WP_014938044.1|962740_964369_-|methylcrotonoyl-CoA-carboxylase
MDLQFNKNEDLNRLKLSEINQLLAKIKKGGGEKRLEKLRSEGKMTARERIDYLLDDNKDSIEIGAFAGFEMYEEHGGCPSAGVVVKIGYISGKQCIVVANDASVKAGAWFPITGKKNLRAQEIAMENRLPIIYLVDSAGVYLPMQDEIFPDKEHFGRIFRNNAKMSAMGIIQISAVMGSCVAGGAYLPIMSDEAMIVDKTGSIFLAGSYLVKAAIGESIDNETLGGATTHCSISGVTDYKAKDDKDALDRIKNIMKSIGDFEKAGFDRTESFLPKENPENIFGIIPAARSEQYDTYEIIKCLVDKSEYEEYKPDYGKSIICATARIDGWSVGIVANQRKLVKSGKGEMQFGGVIYSDSADKATRFIANCNQRKIPLVFLQDVTGFMVGSKSEHGGIIKDGAKMVNAVSNSVVPKFTIITGNSYGAGNYAMCGKAYDPRLIVAWPWADLAVMGGAQAAKVLAQIQEATLRKKGKEITEEDRNEILQEISKKYQKQTEATYAAARLWTDAIISPLDTRKWISMGIEAANHSPITEKFNLGVIQV
>NZ_CP041029.1|WP_014938046.1|960455_962264_-|ComEC/Rec2-family-competence-protein
MLNLVSCISLFIKVKKQILFSLFISFSLGVFLQDLSELSWQQSNITTTLGAISLGLIWVKADWLVRIRIWLLNIFFLCFGVFTHYLNSEKSVLPSVSKKEELVFKIEQKLNSTAKNKRYEITAFYQNQPLKAVLSVPKDLEELDYMHYYQSQLSLYPLEPSKNNYQFDYAKYQARKGVYYRAYAKDLHKAPKSELTFSEKMKQWRLELLSNIDKNEKLSQQTRAFLKGIVLADRTEVDAETNTNFRRSGLTHVLAISGSHIAIIFGVIYMLLSLIVPAKFRTGVILFSLVLIWIFTWFIGWGSSVVRSCIMLTVYFGFVLLQRKPQVLDALALAGLGILMVDTQELFSVGFQLSFSAVLGIYWFNKPIIRLFPNPRNKTQKLLLYTFTVSTAAQLGTMPIVIYYFHQYSAWSILANLLVLPLMEIVIIISFLMTIIFGLGIYWSWLSFTYDWLIKALLWLIGFFGKIEMGYFQDIPLSIWEMGVWAVGLYFLREILIRFTWRGFMKLMFSVLLFFGIKMGLDVRAYHDKEARWHYHYHTKVFSVLDKGKVYFWVSDKDNLEMLESYLIKPYVISKRAESYKVKMMSKEVDEVIFNGKRYLFQ
>NZ_CP041029.1|WP_014938047.1|959662_960331_-|succinate-dehydrogenase-cytochrome-b-subunit
MAGLTSSTIGRKYAMALSAIFLLVFLVMHLSVNMLSVFSESAFNQASYFMGYNPFVQFLMQPILIFAVFFHFVMGFVLEAKNNKARPVKYAVNGAKANSSWMSRNMIISGVVILAFLALHMYDFWVHEMTYKYIPGEGDPSDVARFWEELHEKFSNPIRVAFYVVSFVLLGLHLAHGFQSSFQSIGARHPKYTPCIMALGKWYSILIPLGFIFVAVFHFVTQ
>NZ_CP041029.1|WP_014938048.1|957587_959600_-|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit
MSILDSKIPAGPLADKWKNHKNHMNLVAPNNRDKIDVIVVGTGLAGGSAAATLAEQGYNVKAFCYQDSPRRAHSIAAQGGINAAKNYQGDGDSIYRLFYDTIKGGDYRAREANVYRLAEVSANIIDQCVSQGVPFGRDYGGQLDNRSFGGVQVKRTFYAKGQTGQQLLLGAYSAMSRQIGKGRIKMYNRHEMMELVIVDGKARGIIARNLVTGEIERHSAHAVVIASGGYGNVYFLSTNAMGSNCSAAWKIHKKGAYFANPCFVQIHPTCIPVHGTQQSKLTLMSESLRNSGRIWVPKKIEDAVAIREGKLRPENIKEEDRDYYLERRYPAFGNLVPRDVASRAAKERCDAGFGIENNETKEGVYLDFSTEIMKKGKEAALERNLHNPTEQQIYDLGKAWVEEKYGNLFQMYEKITADNPYKTPMKIYPAVHYSMGGVWVDYNLMSTIPGCFVIGEANFSDHGANRLGASALMQGLADGYFVLPYTIADYLSADIRTGQIPTDTPAFEQAEKEIQEKVNFFINNNGTHSVDYFHKKLGNVMWNKVGMARNEQGLKEAIQEIEEIRKDFWQNVRVPGEANGMNPELEKAFRVADFLELGQLMAMDALNRNESCGGHFREEYSTPDGEAQRDDENYKYAAVWEYKGEDINQEVLHKEELVYENIEVKTRSYK
>NZ_CP041029.1|WP_014938049.1|956793_957564_-|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit
MSAKKGLNLTLKIWRQKNNKSKGQFETYKISDVSPDSSFLEMLDMLNENLVNEGKEPVAFDHDCREGICGMCSLYINGRAHGPDTGITTCQLHMRMFKDGETIHIEPWRSAAFPVIKDLVVDRSAFDRIMATGGFISVNTSGNTTDANSIPVPKEDADKAMDAAACIGCGACVATCKNGSAMLFVGAKVSQYALLPQGRVEAKRRVLKMVAAMDEEGFGNCSNTGACEVECPKGISLENIARMNREFLCATLSSAE
>NZ_CP041029.1|WP_014938050.1|955625_956708_-|DNA-polymerase-IV
MEQFYRKIIHIDMDAFYASVEQRDFPELKGKPVAVGGEHRGVVAAASYEARKYGVRSAMSSVVAKKKCPQIIFVKPRFHRYKEISEQIRAIFFEYTDLVEPLSLDEAYLDVTHNKKGIDSANLIAKEIRRKIFETTGLTASAGISVNKFLAKVASDINKPNGQKTIHPTKVLSFLENLPIERFYGIGNVTANKMYQLGIYKGKDLKEKSLEYLITHFGKMGRHYYDIVRGIHRSEVKPHRIAKSVGVEHTYADDIDTEKDIDQQLIRLAQELYERAEKKQVKGKSLTLKIKYKDFSLFTRSKTQDLYFETEEEMYQIARFLWSLRPYDKAIRLLGLSLSGLDTPSHKKVYVQLKIPFKDL
>NZ_CP041029.1|WP_004918211.1|972882_973221_-|CRISPR-associated-endonuclease-Cas2
MKFNRFNAYRVMWVMVLYDLPTETKAMRKAAQLFRKRLEDDGFSLFQFSIYIRHCPSRENAEVHIKRVKSILPKHGKVAIMSITDKQFGDIEIFFARAKEEPKPTYQQLELF
>NZ_CP041029.1|WP_014938038.1|973210_974110_-|type-II-CRISPR-associated-endonuclease-Cas1
MLYRSIYIGNPAYLKLKDQQMKIICPETKAEKGSISVEDLGLLMLDHFQITISHQLIQKLMGNNVVVISCDAHHLPHGIMLPLYGHSEYSERVKYQLEASEPLKKNLWKQVVESKINNQSEVLKRLGNYYEPMLEYKEQVKSGDTTNMEGIAAQHYWKYLIAPDFLRERFGDSPNQFFNFGYSVLRSIVARAIVETGLLPVLGIFHKNKYNPYCLADDLMEPYRPFVDFLVMEWLENYPESEELTKDFKAFMLNIATLDVRIENKLRPLIVAVKTSVVSVYKCYTGEKRQLSVPEFYEV
>NZ_CP041029.1|WP_014938037.1|974122_978340_-|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKTILGLDLGTNSIGWALVKEAENSNEKSEIIKLGVRVNPLTVDEKTNFEAGRPLSTNADRTAKRSARRNLQRYKLRRKNLIDLLIKNQLIDKDTPLTEIGKNTTHQTLELRAKAARERIELEDLARVFLAINKKRGYRSSRKVNNEEEGQAVDGMAVAKKLYDENLTPGQYAYELLSKGKKYVPDFYRSDLQAEFNAIWEYQKQFYADILDDELYNALKGQGQQNSRKRFLAIKGVYTAENKGKRDDVKLRHYKWRSEAISKKINIEEVAYVLVEINNDLNKSSGYLGAISDRSKELYFNKETVGENLWKQIQKNPHTSLKNQVFYRQDYLDEFEQIWETQAQFHPQLTLALKEQIRDVIIFYQRKLKSQKGLLSFCQFESWEIERKDENGNVILNKTTQLPKRQTVGRRVAPKSSPLFQEFKIWQNINNLEVTKISEGASKNKKETETLSDDERKLLFEELNLRGNLSQKEVLQILGLKDKEYKTNFSEGLEGNRTNAALFNIYQQIAENEGYGFDWSKKSAQEIKEELKAVFPQIGIQADILDFNANLDGKEFENQASYQLWHLLYSAEEDDKINEEDQIIYGNSAVSLKKKLCEKFGFTPEYAKWIANVSLQDDYGNLSTKAMRKIIPYLIDGNDYSEACALAGYNHSNSLTKEENDNRELLDKLELLPKNSLRNPVVEKILNQMVNVVNQVIETYGKPDEVRIELARELKKSAEKRAEMTKSINEATRRNEDIKKLITKDFGIPNPTKSDVVRYRLWEELAPLAYKDVFTGKQIKKEDLFSSKIDIEHIIPKALLFDDSFSNKTLVFRETNLKKADRTAYDFIESDYNATLDDYIQRVETLYNNTKGTISKGKRNKLLMAQKNLPDGFIERDLRNSQYIAKKAKAMLYQVFKDVNVTSGSITDRLREDWDLINVMKELNFPKYKALGLTEIEERYDIGQEKTKRVEVITDWTKRNDHRHHAMNALTVAFTTSSHIQYLNYLNARKNESHKEHKNIKGIENKITHKQKDKRKFIPPMPNFREEAKKHIETILVSIKNKNKVYTKNINKTKKKSGHNTKEQLTPRGQLHKETVYGKSKRPMSKPTKINKNFSLEQAQLIINVQEKELVLRHLAQFDNNPAVAFDTKTLKKMPLLKNGEPLKEVLCFEEIFTIRKDITPDLKIEKVVDEKIKAILEQRKKDFGGNAKEAFSDLDKNPIWLNKKKGICIKRVTITGVSNAEALHHQKDHLGREILDDNGNPIPADFVSTGNNHHLAVYLDSEGKLQDNIVSFYEAVVRTSQGLPVVDKGLNKDLGWKFLFSLKQNEMFVFPNDDFDINDFDLLDDKKAELISKHLYRVQKISKVSAGNSFVRDIVFRHHLETTVKEVKELKDISYIQLKSLEGLRNIKKVRINHIGKIVQVGEY
>NZ_CP041029.1|WP_064970014.1|978851_979787_+|2-nitropropane-dioxygenase
MKNRISELFNIQYPIIQGGMVWHSGWRLASAVSNAGGLGLIGAGSMYPDVLKEHLQKCKKATNKPFGVNIPMLYPNLDEIINIIMEEQIKIVFTSAGNPKTYTETLQKEGIKVAHVVSSLKFAIKCEEAGVDAVVAEGFEAGGHNGRDETTTFCLIPNVSKHISTPLIAAGGIATGQQIKAAMMLGADGVQIGSRFAATIEASSHESFKQKIVEAKEGDTQLTLKELAPVRLLKNKFFYDLEKLYENRRDTEALKQALGRARAKKGMFEGDLDEGELEIGQVSALIDDIISVDEVFERLIKEFKETKEPFL
>NZ_CP041029.1|WP_052911821.1|979833_980163_-|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein
MADVQLKITDREGVQHDIVAPTDMSMNLMEVIRAYELAEEGTVGVCGGMAMCASCQVYVLNDVPLPEKSDEEEAMLSEAFDVKDNSRLGCQIHITEEIDGLEVEIAPYS
>NZ_CP041029.1|WP_140222294.1|980168_981221_-|FAD-dependent-oxidoreductase
MITTDLLIIGAGPTGLFAVFEAGLLKLKCHIIDALPQPGGQLAELYPKKPIFDIPGYPSVNAGELVDNLMEQIKQFQPGFTLAETAVSLEKIDDEWFEVITNKGTVHRAKAVAIAGGLGTFELRKPLLENLEKYEENGVEYFVKAPEVFRDKKIVIAGGGDSALDWSIFLSNVAKEVTLVHRRNEFRGALDSVEKVQELKNQGKINLVTPAEVVELKGANTLESIVIEREGEKTEIETDYFIPLFGLTPKLGPIANWGLEIEKNSIKVNNALDYQTNREGIYAIGDINTYPGKLKLILCGFHEATLMCQSVYNRLNPGKKYVLKYTTVSGVDGFDGSRKEAEKAVVKKID
>NZ_CP041029.1|WP_014938032.1|981379_982126_+|DUF3108-domain-containing-protein
MTLVISASLWSQITNIKSGETLTYRIHYGILNAGYATLNIKETTYKGEPHYYVKGTGKTTGAVRAFFKVEDLYESYINISTALPSFYVRNVQEGSYRQHLETVFNHSNQTLILTDKKTPSNGSKTLKSVKGIQDMLSAFYYLRSRDNSALKVGTSIKMNVWIDDEMFPFQLRIAGVETKRTKFGKVECLKIIPSVISGRVFKDQEGVTMWVTNDANHIPVELKAELAVGSLKASLDDYKNIKYNINFK
>NZ_CP041029.1|WP_004918194.1|982155_982656_+|DUF2480-family-protein
MSEIKNKVAESGLVNFDLSSLVPKGKRLGIDLKPFLFQELVLKEKDFREKVKGLELDSYKDAYVYIYNSAEAIVPLWAYFLIASQLSGVAKKVIYGDKDELELLIMHQALNDYDFSNLKDKRVLVKGCTDENIPENAYIELVEKLKPIVKSLMFGEACSNVPIFKN
>NZ_CP041029.1|WP_004918191.1|982703_983369_+|DUF937-domain-containing-protein
MSLLDLITGNPGTQVAEKAESKFGISKSQIMALLVVATPLVISYLRNKSKDEKEAEALNNALERDHDGSILDDVSQVENRQEEGNSILSHIFGDKKSTVENQLSQNTGISMDKIGPLMAMLAPVIMGYIGKQKRENNVTSGGGLSDLLGGILGQGSQEAQQGGGGNPLTDLLGSVLGGGQSQQGGGNPLNDILGSVLGGGDNKQQSGGLGGLLGGLFGGSK
>NZ_CP041029.1|WP_014938030.1|983519_984494_+|deoxyhypusine-synthase
MSKPITEFIEKYYLHFNAAALVDASKGYVAHLKDGGKMMITLAGAMSTAEMGKILAEMIRQDKVQIISCTGANLEEDLMNLVAHSHYERVPNYRDLTPQQEWDLLERGLNRVTDTCIPEEEAFRRLQKHIVEIWKEAESKGERYFPHEYMYKMLLSGVLEQYYEIPKENSWMLAAAEKNLPIVVPGWEDSTMGNIFASYCIKGELKPSTMKSGIEYMTYLANWYTKNCGGKGVGFFQIGGGIAGDFPICVVPMLYQDMEMHDIPFWSYFCQISDSTTSYGSYSGAVPNEKITWGKLDIDTPKFIVESDATICAPLMFQYVLENS

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

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP041029_1	1.1\|326701\|19\|NZ_CP041029\|CRISPRCasFinder	326701-326719	19	NZ_CP041029.1	1273088-1273106	0	1.0

1. spacer 1.1|326701|19|NZ_CP041029|CRISPRCasFinder matches to position: 1273088-1273106, mismatch: 0, identity: 1.0

ggtaagggttcaagagttc	CRISPR spacer
ggtaagggttcaagagttc	Protospacer
*******************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	NC_007103	Bacillus cereus E33L plasmid pE33L466, complete sequence	92187-92215	5	0.828
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	NZ_CP009967	Bacillus cereus E33L plasmid pBCO_1, complete sequence	229958-229986	5	0.828
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	NZ_CP053657	Bacillus cereus strain CTMA_1571 plasmid p.1, complete sequence	7349-7377	5	0.828
NZ_CP041029_2	2.8\|972545\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972545-972574	30	NZ_CP016375	Elizabethkingia anophelis strain F3201 plasmid unnamed, complete sequence	14824-14853	5	0.833
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	MN694608	Marine virus AFVG_250M55, complete genome	906-934	6	0.793
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	MN694542	Marine virus AFVG_250M54, complete genome	38140-38168	6	0.793
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	MN694156	Marine virus AFVG_250M53, complete genome	38400-38428	6	0.793
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	MN693443	Marine virus AFVG_25M490, complete genome	34252-34280	6	0.793
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	MN693132	Marine virus AFVG_25M489, complete genome	34016-34044	6	0.793
NZ_CP041029_2	2.3\|972160\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972160-972189	30	MN694345	Marine virus AFVG_250M178, complete genome	1115-1144	6	0.8
NZ_CP041029_2	2.7\|972468\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972468-972497	30	MN592897	Vibrio phage MZH0603, complete genome	30446-30475	6	0.8
NZ_CP041029_2	2.8\|972545\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972545-972574	30	CP011076	Brevibacillus laterosporus strain B9 plasmid unnamed2, complete sequence	434710-434739	6	0.8
NZ_CP041029_2	2.9\|972622\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972622-972651	30	NZ_AP017561	Pseudanabaena sp. ABRG5-3 plasmid ABRG53a, complete sequence	44364-44393	6	0.8
NZ_CP041029_2	2.9\|972622\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972622-972651	30	MN695335	Synechococcus phage B23, complete genome	188974-189003	6	0.8
NZ_CP041029_2	2.9\|972622\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972622-972651	30	MN695334	Synechococcus phage B3, complete genome	190463-190492	6	0.8
NZ_CP041029_2	2.1\|972007\|29\|NZ_CP041029\|CRISPRCasFinder	972007-972035	29	AP013655	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C24-MedDCM-OCT-S28-C120, * SEQUENCING IN PROGRESS *	9197-9225	7	0.759
NZ_CP041029_2	2.10\|972699\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972699-972728	30	MN693392	Marine virus AFVG_25M95, complete genome	32086-32115	7	0.767
NZ_CP041029_2	2.3\|972160\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972160-972189	30	NZ_CP047143	Lactobacillus sp. C25 plasmid unnamed, complete sequence	1015-1044	8	0.733
NZ_CP041029_2	2.9\|972622\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972622-972651	30	NZ_KJ645709	Enterococcus faecium strain P26 plasmid pXD5, complete sequence	48966-48995	9	0.7
NZ_CP041029_2	2.9\|972622\|30\|NZ_CP041029\|CRISPRCasFinder,PILER-CR	972622-972651	30	NZ_CP040462	Enterococcus sp. M190262 plasmid pM190262, complete sequence	98503-98532	9	0.7

1. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to NC_007103 (Bacillus cereus E33L plasmid pE33L466, complete sequence) position: , mismatch: 5, identity: 0.828

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
attttttgttttttatgtatgaattgtga	Protospacer
 * ************ **.*********

2. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to NZ_CP009967 (Bacillus cereus E33L plasmid pBCO_1, complete sequence) position: , mismatch: 5, identity: 0.828

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
attttttgttttttatgtatgaattgtga	Protospacer
 * ************ **.*********

3. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to NZ_CP053657 (Bacillus cereus strain CTMA_1571 plasmid p.1, complete sequence) position: , mismatch: 5, identity: 0.828

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
atttgttgttttttatgtatgaattgtgc	Protospacer
 * * ********** **.**********

4. spacer 2.8|972545|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to NZ_CP016375 (Elizabethkingia anophelis strain F3201 plasmid unnamed, complete sequence) position: , mismatch: 5, identity: 0.833

tattttccaaacaggcgatttggcgggtta--	CRISPR spacer
tattttccaaataggcaatttggt--gttaag	Protospacer
***********.****.******.  ****

5. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to MN694608 (Marine virus AFVG_250M55, complete genome) position: , mismatch: 6, identity: 0.793

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
atattttgtcttttaattgtgaatttttg	Protospacer
 ********.****** ******** *

6. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to MN694542 (Marine virus AFVG_250M54, complete genome) position: , mismatch: 6, identity: 0.793

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
atattttgtcttttaattgtgaatttttg	Protospacer
 ********.****** ******** *

7. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to MN694156 (Marine virus AFVG_250M53, complete genome) position: , mismatch: 6, identity: 0.793

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
atattttgtcttttaattgtgaatttttg	Protospacer
 ********.****** ******** *

8. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to MN693443 (Marine virus AFVG_25M490, complete genome) position: , mismatch: 6, identity: 0.793

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
gtcttttgttttttaactgtgaatattga	Protospacer
 * ************* *******  **

9. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to MN693132 (Marine virus AFVG_25M489, complete genome) position: , mismatch: 6, identity: 0.793

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
gtcttttgttttttaactgtgaatattga	Protospacer
 * ************* *******  **

10. spacer 2.3|972160|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to MN694345 (Marine virus AFVG_250M178, complete genome) position: , mismatch: 6, identity: 0.8

atatcacgaaaatttaaagtttagcgacac	CRISPR spacer
cactaacgaaaagttaaagtttagcgactc	Protospacer
   * ******* *************** *

11. spacer 2.7|972468|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to MN592897 (Vibrio phage MZH0603, complete genome) position: , mismatch: 6, identity: 0.8

tctttatactaagagcatttagcaacaata	CRISPR spacer
tctttatacaaagagcatttagccgctgca	Protospacer
********* ************* .* ..*

12. spacer 2.8|972545|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to CP011076 (Brevibacillus laterosporus strain B9 plasmid unnamed2, complete sequence) position: , mismatch: 6, identity: 0.8

tattttccaaacaggcgatttggcgggtta	CRISPR spacer
tttgtacaaaacaggcgatttggcgcgttg	Protospacer
* * * * ***************** ***.

13. spacer 2.9|972622|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to NZ_AP017561 (Pseudanabaena sp. ABRG5-3 plasmid ABRG53a, complete sequence) position: , mismatch: 6, identity: 0.8

tttatcgctaaaattattaagggcaggaaa	CRISPR spacer
atgatcggtaaaattattaagggcaagagc	Protospacer
 * **** *****************.**.

14. spacer 2.9|972622|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to MN695335 (Synechococcus phage B23, complete genome) position: , mismatch: 6, identity: 0.8

tttatcgct-aaaattattaagggcaggaaa	CRISPR spacer
-gaattgttcaaaattattaatggcaggaaa	Protospacer
   **.*.* *********** *********

15. spacer 2.9|972622|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to MN695334 (Synechococcus phage B3, complete genome) position: , mismatch: 6, identity: 0.8

tttatcgct-aaaattattaagggcaggaaa	CRISPR spacer
-gaattgttcaaaattattaatggcaggaaa	Protospacer
   **.*.* *********** *********

16. spacer 2.1|972007|29|NZ_CP041029|CRISPRCasFinder matches to AP013655 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C24-MedDCM-OCT-S28-C120, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 7, identity: 0.759

ctattttgttttttaagtgtgaattgtgc	CRISPR spacer
atattttgttttttaagtttgaactcaag	Protospacer
 ***************** ****.*  .

17. spacer 2.10|972699|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to MN693392 (Marine virus AFVG_25M95, complete genome) position: , mismatch: 7, identity: 0.767

tggcttgttctgatacagacgcatttctaa	CRISPR spacer
tggcttgttctgatacaggctcaagttttt	Protospacer
******************.* **  *.*

18. spacer 2.3|972160|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to NZ_CP047143 (Lactobacillus sp. C25 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.733

atatcacgaaaatttaaagtttagcgacac	CRISPR spacer
atatcacgaaatttaaaagtttaagtattt	Protospacer
*********** ** ********.  *. .

19. spacer 2.9|972622|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to NZ_KJ645709 (Enterococcus faecium strain P26 plasmid pXD5, complete sequence) position: , mismatch: 9, identity: 0.7

tttatcgctaaaattattaagggcaggaaa	CRISPR spacer
cttatcgataaaattattaaggagggattt	Protospacer
.****** **************. .*.

20. spacer 2.9|972622|30|NZ_CP041029|CRISPRCasFinder,PILER-CR matches to NZ_CP040462 (Enterococcus sp. M190262 plasmid pM190262, complete sequence) position: , mismatch: 9, identity: 0.7

tttatcgctaaaattattaagggcaggaaa	CRISPR spacer
cttatcgataaaattattaaggagggattt	Protospacer
.****** **************. .*.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

710050 : 730517

Riemerella_phage(95.65%)

portal

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_038693955.1\|710050_710482_-	hypothetical protein	F5A3A1	Riemerella_phage	3.8e-55	94.5
WP_014938300.1\|710538_710832_+	type II toxin-antitoxin system HigB family toxin	F5A3A2	Riemerella_phage	2.2e-51	99.0
WP_004917838.1\|710828_711191_+	helix-turn-helix domain-containing protein	F5A3A3	Riemerella_phage	4.7e-59	100.0
WP_140222271.1\|711193_715672_-	tape measure protein	F5A3A4	Riemerella_phage	0.0e+00	64.2
WP_038693949.1\|715857_716550_+	hypothetical protein	F5A3A6	Riemerella_phage	1.7e-110	90.0
WP_014938297.1\|716705_717539_+	DUF3800 domain-containing protein	NA	NA	NA	NA
WP_014938296.1\|717839_718025_-	hypothetical protein	F5A3A9	Riemerella_phage	5.8e-29	98.4
WP_014938295.1\|718042_718504_-	hypothetical protein	F5A3B0	Riemerella_phage	6.0e-75	97.4
WP_014938294.1\|718583_719087_-	hypothetical protein	F5A3B1	Riemerella_phage	6.0e-44	54.6
WP_014938293.1\|719115_719526_-	hypothetical protein	F5A3B2	Riemerella_phage	5.5e-72	99.3
WP_014938292.1\|719522_719966_-	hypothetical protein	F5A3B3	Riemerella_phage	9.2e-73	96.6
WP_014938291.1\|719956_720280_-	hypothetical protein	F5A3B4	Riemerella_phage	1.1e-56	97.2
WP_014938290.1\|720273_720597_-	hypothetical protein	F5A3B5	Riemerella_phage	4.5e-53	94.4
WP_014938289.1\|720596_721679_-	hypothetical protein	F5A3B6	Riemerella_phage	7.5e-201	99.4
WP_014938288.1\|721698_722070_-	hypothetical protein	F5A3B7	Riemerella_phage	5.7e-60	95.1
WP_038693946.1\|722073_722730_-	hypothetical protein	F5A3B8	Riemerella_phage	3.3e-79	95.8
WP_014614984.1\|722863_723130_+	hypothetical protein	F5A3B9	Riemerella_phage	1.2e-43	100.0
WP_038693944.1\|723173_723374_+	hypothetical protein	F5A3C0	Riemerella_phage	1.3e-10	93.9
WP_013447244.1\|723789_723993_+	hypothetical protein	F5A3C2	Riemerella_phage	1.0e-31	98.5
WP_014938283.1\|724016_724340_-	hypothetical protein	F5A3C3	Riemerella_phage	1.1e-48	93.3
WP_014614979.1\|724368_724590_-	hypothetical protein	F5A3C4	Riemerella_phage	7.1e-34	100.0
WP_014938282.1\|724594_725650_-	hypothetical protein	F5A3C5	Riemerella_phage	1.7e-197	97.7
WP_140222273.1\|725649_727008_-\|portal	phage portal protein	F5A3C6	Riemerella_phage	2.4e-244	96.6
WP_014938279.1\|728369_730517_+	DNA mismatch repair protein MutS	E3T5Q7	Cafeteria_roenbergensis_virus	1.9e-14	27.4

DBSCAN-SWA_2

895890 : 902887

Enterobacteria_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_038693867.1\|895890_896496_-	LemA family protein	A0A1X9IGG1	Lactococcus_phage	2.1e-11	31.0
WP_004918315.1\|896576_897068_+	dihydrofolate reductase	A0A0H3UYW4	Geobacillus_virus	1.3e-32	44.0
WP_004918313.1\|897078_898383_-	30S ribosomal protein S12 methylthiotransferase RimO	NA	NA	NA	NA
WP_038693865.1\|898488_899346_-	glucose-1-phosphate thymidylyltransferase RfbA	H9NC64	Sphingomonas_phage	6.5e-99	62.5
WP_038693863.1\|899350_900433_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	1.4e-85	48.4
WP_038693861.1\|900443_900989_-	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	8.7e-41	48.6
WP_038694281.1\|901021_901606_-	sugar transferase	NA	NA	NA	NA
WP_127919946.1\|901753_902887_-	aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme	A0A0P0YLZ6	Yellowstone_lake_phycodnavirus	4.8e-17	23.8

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_CP041029

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

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection