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
NC_004917	Helicobacter hepaticus ATCC 51449, complete sequence	1 crisprs	cas3	2	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NC_004917_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_004917_1

54329-54524

Orphan

Consensus_repeat	Method
AAAGCTAAAAAATTTAATCAGCCTTTAGAAAGCTGGAATGTATCTA	PILER-CR

2 spacers

The CRISPR arrays of NC_004917_1

>merge|NC_004917|1|54329-54524|PILER-CR
AAAGCTAAAAAATTTAATCAGCCTTTAGAAAGCTGGAATGTTTCTAATGTTGCAAATATGAGAAATATGTTTGGTGAAACAGATGTATTTAATCAGCCATTAGATAAATGGGATACAAGCAATGTTACAAATATGAGTGAAATGTTTGATAAGGCTAAAAAATTTAATCAGCCTTTAGAAAGCTGGAATGTATCTA

>NC_004917|1|1|54329-54524|PILER-CR
AAAGCTAAAAAATTTAATCAGCCTTTAGAAAGCTGGAATGTTTCTA	ATGTTGCAAATATGAGAAATATGTTTGGTGAAACAGATGT
ATTTAATCAGCCATTAGATAAATGGGATACAAGCAATGTTACAAAT	ATGAGTGAAATGTTTGATAAGGCTAAAAAATTTAATCAGCCTTTAG
AAAGCTGGAATGTATCTA

Protein	Signature genes	Signature genes Name	Protein_function
NC_004917.1\|WP_011114887.1\|48103_48688_+\|GTP-cyclohydrolase-II	unknown	unknown	gnl\|CDD\|234745
NC_004917.1\|WP_034367370.1\|63575_64319_+\|Ni/Fe-hydrogenase,-b-type-cytochrome-subunit	unknown	unknown	gnl\|CDD\|273985
NC_004917.1\|WP_011114900.1\|61813_63544_+\|nickel-dependent-hydrogenase-large-subunit	unknown	unknown	gnl\|CDD\|366057
NC_004917.1\|WP_011114902.1\|64326_64866_+\|HyaD/HybD-family-hydrogenase-maturation-endopeptidase	unknown	unknown	gnl\|CDD\|99873
NC_004917.1\|WP_011114897.1\|58323_59910_-\|phosphoethanolamine-transferase	unknown	unknown	gnl\|CDD\|225105
NC_004917.1\|WP_011114886.1\|46497_47934_-\|catalase	unknown	unknown	gnl\|CDD\|163712
NC_004917.1\|WP_011114894.1\|55393_56263_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|293786
NC_004917.1\|WP_011114896.1\|56956_58327_+\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|376878
NC_004917.1\|WP_034365739.1\|51261_51792_+\|molybdopterin-adenylyltransferase	unknown	unknown	gnl\|CDD\|181837
NC_004917.1\|WP_011114888.1\|48724_49975_+\|molybdopterin-molybdotransferase-MoeA	unknown	unknown	gnl\|CDD\|238452
NC_004917.1\|WP_011114898.1\|59969_60287_-\|thioredoxin	unknown	unknown	gnl\|CDD\|200072
NC_004917.1\|WP_011114889.1\|50020_50245_+\|MoaD/ThiS-family-protein	unknown	unknown	gnl\|CDD\|334994
NC_004917.1\|WP_034365728.1\|50244_50706_+\|molybdenum-cofactor-biosynthesis-protein-MoaE	unknown	unknown	gnl\|CDD\|223391
NC_004917.1\|WP_011114891.1\|50689_51253_+\|molybdopterin-guanine-dinucleotide-biosynthesis-protein-B	unknown	unknown	gnl\|CDD\|349770
NC_004917.1\|WP_011114899.1\|60642_61803_+\|hydrogenase-small-subunit	unknown	unknown	gnl\|CDD\|273053
NC_004917.1\|WP_011114903.1\|64862_66656_+\|hypothetical-protein	unknown	unknown	unknown
NC_004917.1\|WP_011114883.1\|44514_45162_-\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|238449
NC_004917.1\|WP_011114895.1\|56476_56956_+\|cyclic-pyranopterin-monophosphate-synthase-MoaC	unknown	unknown	gnl\|CDD\|236483
NC_004917.1\|WP_011114885.1\|46020_46497_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|293786
NC_004917.1\|WP_011114884.1\|45309_45990_+\|DedA-family-protein	unknown	unknown	gnl\|CDD\|223659

Protein	Function_ID	Function_description	E-value
NC_004917.1\|WP_011114887.1\|48103_48688_+\|GTP-cyclohydrolase-II	gnl\|CDD\|234745	PRK00393, ribA, GTP cyclohydrolase II RibA.	1.42041e-106
NC_004917.1\|WP_034367370.1\|63575_64319_+\|Ni/Fe-hydrogenase,-b-type-cytochrome-subunit	gnl\|CDD\|273985	TIGR02125, CytB-hydogenase, Ni/Fe-hydrogenase, b-type cytochrome subunit. This model describes a family of cytochrome b proteins which appear to be specific for nickel-iron hydrogenase complexes. Every genome which contains a member of this family posesses a Ni/Fe hydrogenase according to Genome Properties (GenProp0177), and most are gene clustered with other hydrogenase components. Some Ni/Fe hydrogenase-containing species lack a member of this family but contain other CytB homologs (pfam01292) which may substitute for it.	3.82374e-97
NC_004917.1\|WP_011114900.1\|61813_63544_+\|nickel-dependent-hydrogenase-large-subunit	gnl\|CDD\|366057	pfam00374, NiFeSe_Hases, Nickel-dependent hydrogenase.	0
NC_004917.1\|WP_011114902.1\|64326_64866_+\|HyaD/HybD-family-hydrogenase-maturation-endopeptidase	gnl\|CDD\|99873	cd06062, H2MP_MemB-H2up, Endopeptidases belonging to membrane-bound hydrogenases group. These hydrogenases transfer electrons from H2 to a cytochrome that is bound to a membrane-located complex coupling electron transfer to transmembrane proton translocation. Endopeptidase HybD from E. coli is well studied in this group. Maturation of [NiFe] hydrogenases include proteolytic processing of large subunit, assembly with other subunits, and formation of the nickel metallocenter. Hydrogenase maturation endopeptidase (HybD) cleaves a short C-terminal peptide after a His or an Arg residue in the large subunit (pre-HybC) of hydrogenase 2 (hyb operon) in E. coli. This cleavage is nickel dependent. A variety of endopeptidases belong to this group that are similar in function and sequence homology. They include such proteins as HynC, HoxM, and HupD.	7.49572e-55
NC_004917.1\|WP_011114897.1\|58323_59910_-\|phosphoethanolamine-transferase	gnl\|CDD\|225105	COG2194, COG2194, Predicted membrane-associated, metal-dependent hydrolase [General function prediction only].	5.42744e-109
NC_004917.1\|WP_011114886.1\|46497_47934_-\|catalase	gnl\|CDD\|163712	cd08156, catalase_clade_3, Clade 3 of the heme-binding enzyme catalase. Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.	0
NC_004917.1\|WP_011114894.1\|55393_56263_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	1.21641e-13
NC_004917.1\|WP_011114896.1\|56956_58327_+\|DNA-recombination-protein-RmuC	gnl\|CDD\|376878	pfam02646, RmuC, RmuC family. This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures.	5.52235e-102
NC_004917.1\|WP_034365739.1\|51261_51792_+\|molybdopterin-adenylyltransferase	gnl\|CDD\|181837	PRK09417, mogA, molybdenum cofactor biosynthesis protein MogA; Provisional.	1.67008e-115
NC_004917.1\|WP_011114888.1\|48724_49975_+\|molybdopterin-molybdotransferase-MoeA	gnl\|CDD\|238452	cd00887, MoeA, MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.	1.58767e-135
NC_004917.1\|WP_011114898.1\|59969_60287_-\|thioredoxin	gnl\|CDD\|200072	TIGR01068, Thioredoxin-like_protein_slr0233, thioredoxin. Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport].	6.4135e-41
NC_004917.1\|WP_011114889.1\|50020_50245_+\|MoaD/ThiS-family-protein	gnl\|CDD\|334994	pfam02597, ThiS, ThiS family. ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.	7.49306e-10
NC_004917.1\|WP_034365728.1\|50244_50706_+\|molybdenum-cofactor-biosynthesis-protein-MoaE	gnl\|CDD\|223391	COG0314, MoaE, Molybdopterin converting factor, large subunit [Coenzyme metabolism].	2.09236e-36
NC_004917.1\|WP_011114891.1\|50689_51253_+\|molybdopterin-guanine-dinucleotide-biosynthesis-protein-B	gnl\|CDD\|349770	cd03116, MobB, molybdopterin-guanine dinucleotide biosynthesis protein B. Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.	5.48459e-54
NC_004917.1\|WP_011114899.1\|60642_61803_+\|hydrogenase-small-subunit	gnl\|CDD\|273053	TIGR00391, small_subunit, hydrogenase (NiFe) small subunit (hydA). Called (hupA/hydA/hupS/hoxK/vhtG) Involved in hydrogenase reactions performing different specific functions in different species eg (EC 1.12.2.1) in Desulfovibrio gigas,(EC 1.12.99.3) in Wolinella succinogenes and (EC 1.18.99.1) in E.coli and a number of other species and (EC 1.12.99.-) in the archea. [Energy metabolism, Electron transport].	0
NC_004917.1\|WP_011114883.1\|44514_45162_-\|carbonic-anhydrase	gnl\|CDD\|238449	cd00884, beta_CA_cladeB, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.	4.08581e-93
NC_004917.1\|WP_011114895.1\|56476_56956_+\|cyclic-pyranopterin-monophosphate-synthase-MoaC	gnl\|CDD\|236483	PRK09364, moaC, cyclic pyranopterin monophosphate synthase MoaC.	4.61749e-90
NC_004917.1\|WP_011114885.1\|46020_46497_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	1.40382e-21
NC_004917.1\|WP_011114884.1\|45309_45990_+\|DedA-family-protein	gnl\|CDD\|223659	COG0586, DedA, Uncharacterized membrane-associated protein [Function unknown].	2.20198e-37

>NC_004917.1|WP_034365739.1|51261_51792_+|molybdopterin-adenylyltransferase
MHTIKIGILVSSDRASQGVYEDISGKAIQEVLNEFILNPCEYHYHIISDEQELIEKNLKLLSDKKGCDLIVTTGGTGPAKRDVTPEATQNVCEKMLPGFGELMRSVSLKYVPTAILSRQSAGIRGKSLIINLPGKPKSIRECLEAVFPAVPYCIDLIEGGYIHANTANIHIFRPKT
>NC_004917.1|WP_011114891.1|50689_51253_+|molybdopterin-guanine-dinucleotide-biosynthesis-protein-B
MTHHSKLTHTPIIFAFSGKSNSGKTTLICKLCEYLKPKAKVAVIKHDPKDKAIFDTQGKDSYEFFQRSSAVALLSPTRTILQIKHNENSQNTQEIESNALFRVLKQFKSYDYIFIEGLKTLPFPRIVIAREHIESSYIPYANAFAIDESVKNTHILPSNLPIFNLNDVGQIAAFINAYPKSTSFKGA
>NC_004917.1|WP_034365728.1|50244_50706_+|molybdenum-cofactor-biosynthesis-protein-MoaE
MLNLYKGALPTCEIYTKWENLAQSKNAGALSIFTGIVRAENNISALSFDIYEPLLRKWFDKWQQKAQNHFDTYICMAHSVGDVLCGQSSYMCGIISAQRKGVLGIYEDFIEDFKANAPIWKYDVINHQRIYAKERSKPLQGSGILGSQNDTSF
>NC_004917.1|WP_011114889.1|50020_50245_+|MoaD/ThiS-family-protein
MIRVDFLGPMSDIPSRELEARTLYELKEILNQDETLRSWLDISAVAVNDEIIEDLSYPLSYGDKVALLPPVCGG
>NC_004917.1|WP_011114888.1|48724_49975_+|molybdopterin-molybdotransferase-MoeA
MAAYPTLISYEEALEILQNLPIKPLGTQQVHFKNALHRICAQDICAPQDYPAYPTAAMDGYAIIFEDLPLLLSQGLKILPPNKAGNPTRPTLEKGYAIKTFTGSLMPINADTLIIVEHITLKNNRIFLNVPKEQVCKSQWIRQVGDNYKKGEILLRKGDKIGAFEIGLLAELNCNFIQVYQKVRVGVICVGDEIVEVGAMSEHTNMVRSVNTHLLESLLLEMNQEPIIYPILKDDKALIKATYEQALKECDVLLSAGGMSMGDYDYTQEVIKELTQIQFKGVRLKPGKPVTCGIFCNANKTTFVLGLPGFPNSCAITFLLFGSFILARLQNNIYKPITLQAKLLEDVYRTDSRMEFRACELINDNGTLGVKFSTKKSLQSSMINNLTHNTALALLAENGSNLQAGESIQIMLLNQF
>NC_004917.1|WP_011114887.1|48103_48688_+|GTP-cyclohydrolase-II
MKYEISEQAKLPTRFGNFFTKSFREYGKNNTLFEHLVVFTHTLGETPLVRIHSECLTGDVFGSKKCDCGNELALAMEQIAHNTEGGMLIYLRQEGRGIGLFNKINAYALQDKGYDTVEANQQLGFAGDMRSYEIVGEIFKHFHITHINLLTNNPRKIDALAPYAKVVRHSIITPSNPHNQAYLEVKKQKLGHLL
>NC_004917.1|WP_011114886.1|46497_47934_-|catalase
MSKKFTTATGTPLGDNQNSITAGKKGPTLLQDTWLLEKLAHFDRERIPERVVHAKGSAAYGELTITNDITQYTKAELFNKVGKKTKAFLRFSVVAGERGAADAERDVRGFALKLYTNEGNWDIVGNNTPVFFIKDAIKFPDFIHTQKRDPKTNMKSPTAMWDFWSLHPESLHQVTILMSDRGIPRSYREMHGFGSHTYSFINAKNERFWVKFHFVCLQGIHNLTNKESEAVIAKDRESHQKDLFENIEKGNFPKWRFCIQVMSEKEAENYRFNPFDLTKVWSHKDYPLIEVGILELNKNPENYFAEVEQAAFNPANIVPGVGYSPDKVLQGRLFSYGDTQRYRLGINHTQLPVNAPIVPVNNTHRDGFMQQGQFGDRRNYEPSYFNDYVEDKNALEPPLFVQEGDVMYKYDHREYEDDYFVQAGDLYRLMTAEQKEALCQNIKESMEGVPDEIKKRQLEHFKKADKAYGKRVAELLGL
>NC_004917.1|WP_011114885.1|46020_46497_-|ankyrin-repeat-domain-containing-protein
MKFTPEEEHKLEELCQYAFECARNNDVDSLEIMLNAGLNVNLANHQGNTLLMLAAYHNNLEAARILLERGALVDKKNDKNQTPLAGVCFKGYDEMARLLLAFGANPNENNGMGLTPITCACLFRRKNILRLLLKYSQNKLTFMQKISLFFLGIKKFHF
>NC_004917.1|WP_011114884.1|45309_45990_+|DedA-family-protein
MGALLGNIINSIVEIVGNLGYIGIFIMMFLESSFFPFPSEVVMIPAGYLVFKGEMNAIIAVICGIAGSLAGALFNYYIALKFGRDFLIRYGKYVFFTESTMQKMEAFFIKHGPMSTFVGRLITIIRQYISLPAGLARMNLVKFCLYTSLGAGIWVIILTLIGYYAGVWFGTDMSVDSIIHAFTSTTPTTQEIELKNIVKQAGLYTLGFVILCLVGYICYWRIQKQA
>NC_004917.1|WP_011114883.1|44514_45162_-|carbonic-anhydrase
MKELFEGAIKFREEDFNEHKELYESLKKRQEPHTLLITCTDSRVVPNLITNSLPGDLFVIRNMGNIVPPYLGSDKGIRGGYLATTSGIEYALSILGIKNVIICGHSDCGACSAIYEPPEELEKAPYVKKWIELLEPVKQKVDALKPGSKAKRRWLMEQVNIEHQLENLMTYPFVEERFDRGELNIYGWYYIIETGEILNYNMIQREFKPINKIKS
>NC_004917.1|WP_011114894.1|55393_56263_-|ankyrin-repeat-domain-containing-protein
MKTLEEIKAMDRKQRNALQEELFALVLTNDIERVKAFLQEYPLQESFYEANIKDGTYKLFLFQVEYVLAEAAMAYEKYKDPAMIEFLQEWGLRIDYHHNGYGRNALTSYIEEGGEDEVVIKYLLDKGLTCEKRGDDGYGRTCMHWWARRNYYETLKIAITKAGANVDVLDRLGETPLFHSVEESSNYKATQILIELGANVNYYDGSYTPLDAAQGAKNKKLLKDAGAKSARSFRKIEKEAHLAFGVDLDEPDKEAYHAALDKLTDEQREEINKLVNQGIAEMMSKQKAK
>NC_004917.1|WP_011114895.1|56476_56956_+|cyclic-pyranopterin-monophosphate-synthase-MoaC
MQLTHLNKQNNPTMVDVSDKHITTREAYASGVISMSEQAFESAINHTGKKGPITQTAIIAAIMGSKKTSEIIPMCHPLMINKINVDITPNPAEHSITLGVLVKCEGKTGVEMEALTGVSIGLLTIYDMLKAIDKSMVISDIALQSKSGGKSGDFVREDS
>NC_004917.1|WP_011114896.1|56956_58327_+|DNA-recombination-protein-RmuC
MLLHISTLLLIICASFVLSGGSIWLWLHHRFKKKQSQLIATHNATTQSLQIQIQNLEKHIQTLSLEYAQATTTLQMIESSHTQRLNDMQKVCEARLLEEKTRSEHMIHTLKEQFYHTQEEQDKNKEELKNAFKAISADILRQNTQSFNQMQLLSLQPLREEITRFTKQLNDNHTATLTQHTALQTQIEQLSKLNVQLSNDAHNLTNALKGGNKAQGNWGEIILQRVFENSGLQEGREYELQISMRDEQSQILRPDAIVKLPKSGNEQRCVIVDSKTSLVAYEKLCNAQNEMQKLSAQKELAHSIQMHFNNLSAKNYHQYLQGQKLDFVLMFIPIEGAFLEAMQYDSTLYDRAYQKGVVLVSPTTIMAVLKIIHNLWQIEYRDKNINKIFNEIKKLFERIEKFENVLEQLGRNIDTMRKTYDDVMTKYNGKQGIAPKSKDIDKLLKGTEILQIEEGR
>NC_004917.1|WP_011114897.1|58323_59910_-|phosphoethanolamine-transferase
MLKYFKTFPRLYLNYHLLILLSSAFIVFCLNHFFNTTFNTTAHQVGFDYLVWLNGVIHILILALAFEIISLRLSVKYVIGIVLLLCSVCGFYMDSLGVAFDEDIIQSIFETHIDEAFDLMSFGLIKYVLLFGVFPIILLTFIKLKKKPFVRAFTQKIVFIIILSMLIGGSYGLWGKDIVFVFKAQKKLEKILNPIAPIRSLFLYIQHLQEKQSFVPTLIAKDATLAKEIPPQIVVFVIGESARSANFALNGYVKPTNPYTNTLNIISFKEFYSCGVITAISVPCMLTNYTQETYTNRNLSLYINNILDIAQSVGYEVWYLGNNGGKCVGGCDRNIKHTIIYPTDSLDSVMLPDIKNIIANAHKMRQNTFIVVHQYGSHGASYNKRYPPDWTRFTPVCEEKELSKCTYEEIINAYDNSLVYSDWILAQMIENLQKIDDMRSMLWYVSDHGESLGELGQYMHGGLGYNLAPKYQKHIPSIMWFSTGWENAPAKARERINHHLSHDYVFHTLLHILGIHTQDYQQALDIMP
>NC_004917.1|WP_011114898.1|59969_60287_-|thioredoxin
MAKYKELTNDNFDTEALSGVALVDFWAPWCNPCKMLSPVIDKLADEYEGKAKICKVNVDEQGELSKRFGIRNIPTILFMKDGEIKDQVTGAMPEQVIRQKLDSIL
>NC_004917.1|WP_011114899.1|60642_61803_+|hydrogenase-small-subunit
MKTQDAYQELFKKASQRLDELSKLPAHNAEKDLLQELESKGFSRRDFMKWSGMMTAALALPATFAPLTAKAAEVANRLPVVWLHMAECTGCSESLLRSDAPSIDSLIFDYISLEYHETVMAASGWQAEHNLENAIEKYAGQYILMVEGGIPKGSSEFYLTIGGHARTGAEEARHAAKGAKAIFAIGTCSSFGGVQAAHPNPTNAVPLSEITNRSVINVPGCPPSEKNIVGNVLHFILFGSLPSLDAYNRPTWAYGLRIHDLCERRGRFDAGQFVQHFGDENAQKGYCLYKVGCKGPYTFNNCSKLRFNQHTSWPIQAGHGCIGCSEPHFWDTMNPFEEPIGNRLYATSFNGMGADKTADTIGAVVLGAAAIGIAAHAIISSTQNAK
>NC_004917.1|WP_011114900.1|61813_63544_+|nickel-dependent-hydrogenase-large-subunit
MTKRIIVDPITRIEGHLRIEVIVDENNVIQDAFSTSTLWRGLETIVKNRDPRDAGFIVQRICGVCTYSHYKAGITAVENALGIKPPLNAILTRTLMNISLFLHDHAVHFYTLHGLDWCDITSALKADCAAAAKLAFKYSPNPICTGENELKAVQEKVSTFVKQGALGPFANAYWGHKTYHFTPEQNLIVLSHYLKLLEVQRVIAQMMAIFGAKNPHPQSLTVGGVTSVMDILDPSRLGEWLTKYKEVTEFINRAYWADIIMAAEAYKNEDSVLKGCGVKNFISFQEMQVGPEEWLFSSGIIKDGDLSKVYPIDESKITEEAIHSWYEDNQPLHPYDGKTNPQYTGFKDAQTIGPDGKLIDSKVIDENGKYSWIKSPRYDGEPMEVGPLASVLVGYASGNKAIVDIVNELLSVTGLPKEALFSTLGRTAARAIECKVVADHGIKAFNALVANIASGDKNTCAPYSIDKNKEYKGRFIGNVPRGMLSHWVRIKNGVIENYQAVVPSTWNAGPRDANGKKGPYEMSLIGTQVKDITQPLEIIRHIHSFDPCIACAVHVMDTKGNELSQYKVEPSFARLR
>NC_004917.1|WP_034367370.1|63575_64319_+|Ni/Fe-hydrogenase,-b-type-cytochrome-subunit
MFKKELHMHEEFSGLTRIFHWLRALCIFTLIATGFYIAYPFIMSNPDTTQATLQGSIQGQVVIEQSMGAVSTSYLQGYIRSVHLIMGFVLIAISFFRIYLFFFDKKSLPERISLNQALQPKIWIAQIKTYMFIGNHPHIDGTYNPIQFVTYLCLGILVFLISLTGVVLYYNVYNNGLGAILEFCFKWVEVLCGGLSSVRNLHHIFTWAIIIFIPVHIYFAVWNSIKYPNGGVDAIVSGIRYTDEVKV
>NC_004917.1|WP_011114902.1|64326_64866_+|HyaD/HybD-family-hydrogenase-maturation-endopeptidase
MKILVLGIGNILFGDEGIGVHLANFLKLNYRFSGENEVEFVDGGTLASMLIPLITSYDKVLILDCVDVNNANIGEVYYFDFDNVPNIITWAGSAHEVEMLQTLRLTAINGDLPPVKIIGIIPEVIGEDTAFTLSQPVKEGAKIMEKLALEFLEENGIHAQKVDNRDLQEVANGSFRGYE
>NC_004917.1|WP_011114903.1|64862_66656_+|hypothetical-protein
MIYDFRFYNKNQDESFFLFLLASKAQVLNLEAFFYTYAEHTHCLIPNIPALRESYTQICPNQPIPSLFDCPYESKAYAQLILQFANEISLELPLSLYFCFRELHTIAPPTPFYTTLCKESLRQSLPHAFPELPLHIQNSFQDSHTILTQFHTPKTYYYTALETKEILNPSSDMFALLNPPNSYAHKPLISPDKTYFIHIVNMLKEKQSVPFCTQRGLQILSLSPTPHTHTTILCDIASIKTYFRTHQAHIDTLASFEKPLTHLVPKEVFQEHFPIDECGLVLIGLPYDMPLALISALLLQDDIGYFFLSYDMQHTYPAPFDFCHSQAFNAQTLTISHNGILIDTHIAQQYTLESLINAHLHTYTQTDISTPSEDSLPQSHLIIYLSTTHPSAFLIKDQKSKILLDIAFECNPHLILQNIIQSYENGDELIKSFGAHSPQLLKRIFALPETSQLSHNLTDIFGVISFILGFSSTYDTPTDKNALFYRAYRFVRERGPRIDYKLLRKDNTISLDYNRIVRSCISFKCADMEDEILAYGVLDSLSEFLATLVRDTKTNLAIDNVLLLGDMLGNSIFLDKLLGYLPKDIHLILPQDGMLDY

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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
NC_004917_1	1.1\|54375\|40\|NC_004917\|PILER-CR	54375-54414	40	NC_004917.1	53925-53964	0	1.0
NC_004917_1	1.2\|54461\|46\|NC_004917\|PILER-CR	54461-54506	46	NC_004917.1	53983-54028	0	1.0
NC_004917_1	1.2\|54461\|46\|NC_004917\|PILER-CR	54461-54506	46	NC_004917.1	53383-53428	1	0.978
NC_004917_1	1.2\|54461\|46\|NC_004917\|PILER-CR	54461-54506	46	NC_004917.1	53533-53578	2	0.957

1. spacer 1.1|54375|40|NC_004917|PILER-CR matches to position: 53925-53964, mismatch: 0, identity: 1.0

atgttgcaaatatgagaaatatgtttggtgaaacagatgt	CRISPR spacer
atgttgcaaatatgagaaatatgtttggtgaaacagatgt	Protospacer
****************************************

2. spacer 1.2|54461|46|NC_004917|PILER-CR matches to position: 53983-54028, mismatch: 0, identity: 1.0

taaatgggatacaagcaatgttacaaatatgagtgaaatgtttgat	CRISPR spacer
taaatgggatacaagcaatgttacaaatatgagtgaaatgtttgat	Protospacer
**********************************************

3. spacer 1.2|54461|46|NC_004917|PILER-CR matches to position: 53383-53428, mismatch: 1, identity: 0.978

taaatgggatacaagcaatgttacaaatatgagtgaaatgtttgat	CRISPR spacer
taaatgggatacaagcaatgttacaaatatgagtgaaatgttttat	Protospacer
******************************************* **

4. spacer 1.2|54461|46|NC_004917|PILER-CR matches to position: 53533-53578, mismatch: 2, identity: 0.957

taaatgggatacaagcaatgttacaaatatgagtgaaatgtttgat	CRISPR spacer
taaatgggacacaagcaatgttacaaatatgagtgaaatgtttcat	Protospacer
*********.********************************* **

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

68642 : 76854

Synechococcus_phage(28.57%)

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_011114906.1\|68642_69584_+	cysteine synthase family protein	A0A1W6JHY1	Lactococcus_phage	1.0e-49	38.4
WP_011114907.1\|69561_70341_-	hypothetical protein	A0A2H4UTC9	Bodo_saltans_virus	2.6e-06	26.6
WP_011114908.1\|70334_70496_-	hypothetical protein	NA	NA	NA	NA
WP_011114909.1\|70591_71065_+	hypothetical protein	NA	NA	NA	NA
WP_041308899.1\|71261_71825_+	DUF2972 domain-containing protein	NA	NA	NA	NA
WP_011114911.1\|71862_72771_-	DUF1792 domain-containing protein	A0A1V0SAI7	Catovirus	6.2e-07	24.3
WP_011114912.1\|72767_73244_-	alpha-1,2-fucosyltransferase	A0A1D8KQA0	Synechococcus_phage	3.7e-11	34.6
WP_011114913.1\|73213_73666_-	alpha-1,2-fucosyltransferase	NA	NA	NA	NA
WP_034368123.1\|73682_74774_-	DegT/DnrJ/EryC1/StrS family aminotransferase	E5ES42	Bathycoccus_sp._RCC1105_virus	3.0e-48	33.6
WP_011114915.1\|74800_75763_-	alpha-1,2-fucosyltransferase	A0A222YW11	Synechococcus_phage	8.0e-05	33.0
WP_011114916.1\|75765_76854_-	glycosyltransferase family 2 protein	R9S8I6	Prochlorococcus_phage	3.3e-07	28.7

Anti-CRISPR protein detection

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