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_009922	Alkaliphilus oremlandii OhILAs, complete genome	2 crisprs	csa3,cas3,DEDDh,PD-DExK,RT,DinG,WYL	1	0	5	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NC_009922_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_009922_1

876320-876423

Orphan

Consensus_repeat	Method
AAAATAAAGTTTGTTCGCTCAGGCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_009922_1

>merge|NC_009922|1|876320-876423|CRISPRCasFinder
AAAATAAAGTTTGTTCGCTCAGGCTCACAAACTTTATGTCGCACTCAACTCTAGGTGAGGCTTAGAGTTTCAAGTGCTCAAAATAAGGTTTGTTCGCTCAGGCT

>NC_009922|1|1|876320-876423|CRISPRCasFinder
AAAATAAAGTTTGTTCGCTCAGGCT	CACAAACTTTATGTCGCACTCAACTCTAGGTGAGGCTTAGAGTTTCAAGTGCTC
AAAATAAGGTTTGTTCGCTCAGGCT

Protein	Signature genes	Signature genes Name	Protein_function
NC_009922.1\|WP_012158665.1\|879316_879610_+\|BMC-domain-containing-protein	unknown	unknown	gnl\|CDD\|132899
NC_009922.1\|WP_012158667.1\|880439_881075_+\|phosphate-propanoyltransferase	unknown	unknown	gnl\|CDD\|237899
NC_009922.1\|WP_012158651.1\|865745_866882_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NC_009922.1\|WP_012158670.1\|882013_883099_+\|ethanolamine-utilization-protein-EutH	unknown	unknown	gnl\|CDD\|237906
NC_009922.1\|WP_012158658.1\|872076_872421_+\|BMC-domain-containing-protein	unknown	unknown	gnl\|CDD\|132886
NC_009922.1\|WP_012158652.1\|866974_868099_+\|TlpA-family-protein-disulfide-reductase	unknown	unknown	gnl\|CDD\|239264
NC_009922.1\|WP_012158653.1\|868261_869125_+\|4Fe-4S-binding-protein	unknown	unknown	gnl\|CDD\|223425
NC_009922.1\|WP_012158662.1\|876515_877169_+\|ethanolamine-utilization-microcompartment-protein-EutL	unknown	unknown	gnl\|CDD\|185303
NC_009922.1\|WP_012158669.1\|881702_881975_+\|EutN/CcmL-family-microcompartment-protein	unknown	unknown	gnl\|CDD\|377017
NC_009922.1\|WP_012158657.1\|870912_872052_+\|iron-containing-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|341459
NC_009922.1\|WP_012158666.1\|879691_880429_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227149
NC_009922.1\|WP_012158660.1\|874021_875389_+\|ethanolamine-ammonia-lyase-subunit-EutB	unknown	unknown	gnl\|CDD\|237897
NC_009922.1\|WP_012158663.1\|877181_877775_+\|BMC-domain-containing-protein	unknown	unknown	gnl\|CDD\|132885
NC_009922.1\|WP_012158655.1\|869806_870250_+\|EutP/PduV-family-microcompartment-system-protein	unknown	unknown	gnl\|CDD\|371185
NC_009922.1\|WP_012158659.1\|872570_874001_+\|ethanolamine-ammonia-lyase-reactivating-factor-EutA	unknown	unknown	gnl\|CDD\|377642
NC_009922.1\|WP_012158668.1\|881080_881689_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274184
NC_009922.1\|WP_012158671.1\|883138_883597_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|114941
NC_009922.1\|WP_012158654.1\|869445_869790_+\|BMC-domain-containing-protein	unknown	unknown	gnl\|CDD\|132886
NC_009922.1\|WP_012158664.1\|877774_879253_+\|acetaldehyde-dehydrogenase-(acetylating)	unknown	unknown	gnl\|CDD\|131570
NC_009922.1\|WP_012158656.1\|870252_870834_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	unknown	unknown	gnl\|CDD\|376665

Protein	Function_ID	Function_description	E-value
NC_009922.1\|WP_012158665.1\|879316_879610_+\|BMC-domain-containing-protein	gnl\|CDD\|132899	cd07059, BMC_PduA, 1,2-propanediol utilization protein A (PduA), Bacterial Micro-Compartment (BMC) domain. PduA is encoded within the 1,2-propanediol utilization (pdu) operon along with other homologous carboxysome shell proteins PduB, B', J, K, T, and U. PduA is thought to be required for the formation of the outer shell of bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduA might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, like PduU does, at present no experimental evidence directly supports this view.	1.71051e-38
NC_009922.1\|WP_012158667.1\|880439_881075_+\|phosphate-propanoyltransferase	gnl\|CDD\|237899	PRK15070, PRK15070, phosphate propanoyltransferase.	9.95326e-114
NC_009922.1\|WP_012158651.1\|865745_866882_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	6.26855e-53
NC_009922.1\|WP_012158670.1\|882013_883099_+\|ethanolamine-utilization-protein-EutH	gnl\|CDD\|237906	PRK15086, PRK15086, ethanolamine utilization protein EutH; Provisional.	3.60021e-155
NC_009922.1\|WP_012158658.1\|872076_872421_+\|BMC-domain-containing-protein	gnl\|CDD\|132886	cd07046, BMC_PduU-EutS, 1,2-propanediol utilization protein U (PduU)/ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain. PduU encapsulates several related enzymes within a shell composed of a few thousand protein subunits. PduU exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu organelle. This proteinaceous noncarboxysome microcompartment is involved in coenzyme B12-dependent degradation of 1,2-propanediol. The core of PduU is related to the typical BMC domain and its natural oligomeric state is a cyclic hexamer. Unlike other typical BMC domain proteins, the 3D topology of PduU reveals a circular permuted variation on the typical BMC fold which leads to several unique features. The exact functions related to those unique features are still not clear. Another difference is the presence of a deep cavity on one side of the hexamer as well as an intermolecular six-stranded beta barrel that seems to block the central pore that is present in other BMC domain proteins. EutS proteins included in this CD are sequence homologs of PduU. They are encoded within eut operon and may be required for the formation of the outer shell of bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutS might also form hexamers and play similar functional roles in the construction of the eut organelle outer shell at present no experimental evidence directly supports this view.	5.80439e-55
NC_009922.1\|WP_012158652.1\|866974_868099_+\|TlpA-family-protein-disulfide-reductase	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	3.15003e-20
NC_009922.1\|WP_012158653.1\|868261_869125_+\|4Fe-4S-binding-protein	gnl\|CDD\|223425	COG0348, NapH, Polyferredoxin [Energy production and conversion].	1.47721e-21
NC_009922.1\|WP_012158662.1\|876515_877169_+\|ethanolamine-utilization-microcompartment-protein-EutL	gnl\|CDD\|185303	PRK15405, PRK15405, ethanolamine utilization microcompartment protein EutL.	5.00872e-132
NC_009922.1\|WP_012158669.1\|881702_881975_+\|EutN/CcmL-family-microcompartment-protein	gnl\|CDD\|377017	pfam03319, EutN_CcmL, Ethanolamine utilisation protein EutN/carboxysome. The crystal structure of EutN contains a central five-stranded beta-barrel, with an alpha-helix at the open end of this barrel (Structure 2HD3). The structure also contains three additional beta-strands, which help the formation of a tight hexamer, with a hole in the center. this suggests that EutN forms a pore, with an opening of 26 Angstrom in diameter on one face and 14 Angstrom on the other face. EutN is involved in the cobalamin-dependent degradation of ethanolamine.	5.20394e-35
NC_009922.1\|WP_012158657.1\|870912_872052_+\|iron-containing-alcohol-dehydrogenase	gnl\|CDD\|341459	cd08180, PDD, 1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism. 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.	1.02247e-177
NC_009922.1\|WP_012158666.1\|879691_880429_+\|hypothetical-protein	gnl\|CDD\|227149	COG4812, EutT, Ethanolamine utilization cobalamin adenosyltransferase [Amino acid transport and metabolism].	3.56117e-05
NC_009922.1\|WP_012158660.1\|874021_875389_+\|ethanolamine-ammonia-lyase-subunit-EutB	gnl\|CDD\|237897	PRK15067, PRK15067, ethanolamine ammonia-lyase subunit EutB.	0
NC_009922.1\|WP_012158663.1\|877181_877775_+\|BMC-domain-containing-protein	gnl\|CDD\|132885	cd07045, BMC_CcmK_like, Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment (BMC) domain. Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). Potential functional differences between the two types are not yet fully understood. In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shells at present no experimental evidence directly supports this view.	1.09571e-36
NC_009922.1\|WP_012158655.1\|869806_870250_+\|EutP/PduV-family-microcompartment-system-protein	gnl\|CDD\|371185	pfam10662, PduV-EutP, Ethanolamine utilisation - propanediol utilisation. Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.	5.74215e-78
NC_009922.1\|WP_012158659.1\|872570_874001_+\|ethanolamine-ammonia-lyase-reactivating-factor-EutA	gnl\|CDD\|377642	pfam06277, EutA, Ethanolamine utilisation protein EutA. This family consists of several bacterial EutA ethanolamine utilisation proteins. The EutA protein is thought to protect the lyase (EutBC) from inhibition by CNB12.	0
NC_009922.1\|WP_012158668.1\|881080_881689_+\|hypothetical-protein	gnl\|CDD\|274184	TIGR02536, putative_ethanolamine_utilization_protein, ethanolamine utilization protein. This family of proteins is found in operons for the polyhedral organelle-based degradation of ethanolamine. This family is not found in proteobacterial species which otherwise have the same suite of genes in the eut operon. Proteobacteria have two genes that are not found in non-proteobacteria which may complement this genes function, a phosphotransacetylase (pfam01515) and the EutJ protein (TIGR02529) of unknown function.	2.66315e-13
NC_009922.1\|WP_012158671.1\|883138_883597_+\|cupin-domain-containing-protein	gnl\|CDD\|114941	pfam06249, EutQ, Ethanolamine utilisation protein EutQ. The eut operon of Salmonella typhimurium encodes proteins involved in the cobalamin-dependent degradation of ethanolamine. The role of EutQ in this process is unclear.	1.65396e-68
NC_009922.1\|WP_012158654.1\|869445_869790_+\|BMC-domain-containing-protein	gnl\|CDD\|132886	cd07046, BMC_PduU-EutS, 1,2-propanediol utilization protein U (PduU)/ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain. PduU encapsulates several related enzymes within a shell composed of a few thousand protein subunits. PduU exists as a hexamer which might further assemble into the flat facets of the polyhedral outer shell of the pdu organelle. This proteinaceous noncarboxysome microcompartment is involved in coenzyme B12-dependent degradation of 1,2-propanediol. The core of PduU is related to the typical BMC domain and its natural oligomeric state is a cyclic hexamer. Unlike other typical BMC domain proteins, the 3D topology of PduU reveals a circular permuted variation on the typical BMC fold which leads to several unique features. The exact functions related to those unique features are still not clear. Another difference is the presence of a deep cavity on one side of the hexamer as well as an intermolecular six-stranded beta barrel that seems to block the central pore that is present in other BMC domain proteins. EutS proteins included in this CD are sequence homologs of PduU. They are encoded within eut operon and may be required for the formation of the outer shell of bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutS might also form hexamers and play similar functional roles in the construction of the eut organelle outer shell at present no experimental evidence directly supports this view.	2.15699e-60
NC_009922.1\|WP_012158664.1\|877774_879253_+\|acetaldehyde-dehydrogenase-(acetylating)	gnl\|CDD\|131570	TIGR02518, Acetaldehyde_dehydrogenase_acetylating, acetaldehyde dehydrogenase (acetylating).	0
NC_009922.1\|WP_012158656.1\|870252_870834_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	gnl\|CDD\|376665	pfam01923, Cob_adeno_trans, Cobalamin adenosyltransferase. Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.	2.58117e-75

>NC_009922.1|WP_012158660.1|874021_875389_+|ethanolamine-ammonia-lyase-subunit-EutB
MILKTKLFGKTYQFSSVMEVMGKANEEKSGDNLAGVAAESAEERVAAKVVLSQLKLSDLFNNPAVPYEKDEVTRIIIDHVNLKTYERIKNWTVAELREWILNSNTTNYDIHRISNGLTAEMVAAVAKIMSNLDLIVGAQKIVVTKTANTTIGVPGTFSTRLQPNHTTDNVDGIMATVMEGLSMGAGDAVIGLNPVDDTTESVKRILHKFNDFINKWEIPTQHVVLAHVATQMEAMEQGAPTGLVFQSIAGSEKGNAAFGISAKMLSEAKDMALKLGTAVGPNVMYFETGQGSELSSDAHNGVDQLTMEARCYGFAKHFDPFLVNTVVGFIGPEYLYDSKQVIRAGLEDHFMGKLTGISMGCDVCYTNHMKADQNDAENLTVLLATAGVNFIMGIPNGDDIMLNYQTTGFHEGASIRQLLNKRTIKEFDQWLEKMGFSENGRLTSKAGDASVFLKG
>NC_009922.1|WP_012158659.1|872570_874001_+|ethanolamine-ammonia-lyase-reactivating-factor-EutA
MAETLLSVGIDIGTSTTQLILSELSIENMASVFTIPRISITDKKVIFKSDIIFTPILENNLIDSDGIKEFVEEQYKKAGITKSAIQTGAVIITGETVRKENARSVANALSGFAGDFVVATAGPDLESIIAGKGAGTYSYSKNHHTTAVNLDIGGGTTNLVVFNDGDIEDTACFDIGGRLIKVDSSGIIRYISPKVEKIIRKEALDLRLNEKVDLKELDKLLDIFVQVLENSVRIGKRSPYFELLITNKQLTTKLQIKCISFSGGVADGITKEGVQNPFEYGDIGLLLGKKIRESSLMTALNVIPTVETIRATVVGAGSHTTDVSGSTITYKKEILPLQNIPILQLSKDDEDANNCGNLGNIIQEKVKWFMVDGEVQTVGLGIEGVHNPSFQLIQNLAREIIEGLDLLIQKKLPLVIIVKEDMAKALGHSLYAHLPENYPFVCIDSVYVRNGDYIDIGKPIAEGSVLPVVVKTLVFN
>NC_009922.1|WP_012158658.1|872076_872421_+|BMC-domain-containing-protein
MEKNERVIQEYVPGKQITVAHVIAKADSELYQKMGIVQSGNEAVGILTITPSEASIIAVDIATKAAEIEIGFVDRFSGAVVIIGDVSSVKIALENILDTMASLLDFTVVPLSST
>NC_009922.1|WP_012158657.1|870912_872052_+|iron-containing-alcohol-dehydrogenase
MQKIRFGTALYIGEDSLKRLSDFKNEKIFIVTDSFIASSALLPQIRSYMDPSTEILVFSEVIPDPPIDNIVAGLEYSKDFSATILLAIGGGSAIDAAKAMLYFGKLTGRFSGIRFITIPTTSGTGSEVTDFSIITDDEKGTKYPLITEEILPNEAILDAGLIAGLPPKQTADTGMDVLTHAIEAYVSTNANDISDALSEKAIRYVFTYLERAYKNGGDKEAREKMHMASTMAGMAFNITSLGINHGIAHAAGARWHIPHGRINSILLPHVIRHNAGMVEGNYGKNRTLAAGRYAEIAKFLELNAGNVQAGVRSLVNAILALQKKLSMPKSLSEWGITKEQFESDKNRVAEAALADRCTETNPVTLTKEDVIHILRKSFI
>NC_009922.1|WP_012158656.1|870252_870834_+|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase
MQIYTRTGDKGYTRIIGGTKLAKDSERIKAYGTIDELNSFVGYAITLIKNNDALKKELIQIQQYLFDCGNDLAMPRGKGTYRVTPDLTEWIEGCIDAHVAIPREVESFILPGGSPAASILHICRTVARRAEREIVTFQWTNDMNEEVLIFINRLSDYFFSVARVANANEGIEDVLYERSGKVFHMELKKEHLQ
>NC_009922.1|WP_012158655.1|869806_870250_+|EutP/PduV-family-microcompartment-system-protein
MKKIMLIGSVGSGKTTLCQRIQGESIKYKKTQSVEFYSQMIDTPGEFVLHRRFYSALQMMAASSDVIGFVCSVVESGQTFSPYFAQNFTKQCVGIITKIDLAPNEEAIINAEKRLELAGVSKIFRLSAMKDEGVAELIDYLSKEKEG
>NC_009922.1|WP_012158654.1|869445_869790_+|BMC-domain-containing-protein
MSLLERKIFESVPGKQVTLAHIIANPDDRIFEKLGLNNEKYHAIGILTITPPEVAIIAVDIAKKTAPIKIGFVDRFSGSVFILGDVSAVQSAMEQVVISLRELMRFTVPKITRT
>NC_009922.1|WP_012158653.1|868261_869125_+|4Fe-4S-binding-protein
MKKLWEYVKKRPLIQVVASILTNYNLRGFATGRIYKGNTKIACVPGLNCYSCPGAIGSCPIGSLQAVVGGNRYNFSYYVMGILILFGVLFGRFICGFLCPFGFIQDILYKIQIFKLKVPKKMDQLLRWLKYALLLILVILLPIFLTDEFGTAPPYFCQWICPAGTLGGGLPLILKNKSLRSMLGVLFGWKVTLLILIVLSSVFIYRPFCKYICPLGAIYSIFNYFSFYQMHIDKLKCNGCKACQRHCNMNVEVIRNINSPECIRCGKCKDVCKQGAITSGFKLICKE
>NC_009922.1|WP_012158652.1|866974_868099_+|TlpA-family-protein-disulfide-reductase
MKVENLFYKEENRVKKQIIKLGTVLLLIASTMIFILNGCSQKINGTNVNKKYAEKGMVNLIGEPYNYEKGTVDKGIGLGFVLTDKENELMEKEQLGIERNPRLGYTFSYITENGVKMLKEPSILDGKTDMPNITAAFFNYAAIYKIPNDSKDEIGEITMKYLTDTYSNKKAVATLKEHTYYFAWNEDYSSIDDLSEQDKKNIEALISNFDSFVNNFCIFPSSNVEKNMKNFNAKMLNGGNFTQEDFAKYDITMVNIWATWCRGCVEEMPELQAVYEKLPENMNMISICSNAGTEAELAKEILDKKGCKFPTLIPDEKLEESLLDYLDAYPTTVFVDSKGNIIGEEQIGAPSQNKEDVTDAYLNLMNEILERFSK
>NC_009922.1|WP_012158651.1|865745_866882_+|HAMP-domain-containing-histidine-kinase
MKEGISLRGRLTFITSILLVLLCIAFTVSGMYNLNVNVVDPLQLIIRIDMDQVARQTEQGVPEFMLDNLNEIIIEETIGPYSRFSFLFMVVAIVIGTSIMYFLSGLVLKPAQKLATDIACINKDTLSRRITNFKAGDELNSIANSFNGMLDRLQLAFDREQRFSAAAAHELKTPLTVIKTNLDVFDLDETHSKEDVEDILGVVKKQTDRMVMLVNDLMILSTNHACNRNDKVSIDKLLAEIREEMLPDMINKSIKFRMDTVPCNITANAVMIKHAISNLLNNAIKYNVDGGQISVSAYTEENRCIICIVDTGIGIEEDKTKYIFEPFYRVDKSRSRTVGGAGLGLAITKEIIMQHKGTIVHGKNEPQGSKFTVTLPLA
>NC_009922.1|WP_012158662.1|876515_877169_+|ethanolamine-utilization-microcompartment-protein-EutL
MKNERLGANVLSVKIIPNVDDGLAKELNLAPNQKSLGIITADSDDVTYVALDEATKASDVAVVYAKSMYAGAANASTKLAGEVIGILAGPSPAEIRSGLDRAVEVITNEASFYSANEDNSIVYFAHTVSRTGSYLSKGANVREGEAIAYLIAPPLEAIVAIDAALKASAVKMKVFYGPPTETNYAGALLTGSQSACRAACEAFAKAVEAVADNPTSY
>NC_009922.1|WP_012158663.1|877181_877775_+|BMC-domain-containing-protein
MAKALGLIEVRGKLGAILAADAAIKAASVRLLGSEVVSGGLTTIHIIGDIAAVKAAVEAGVVAVADKNCLISSHVIPRLDDQVERMLEKTLGRKEERPSDLKESNESTTKGKIEEEKPDKAVVPSNGSQEISKENLKSSINTIVGTSFDKEDLEKMRVTDLRSLAYQSDLSTIKKSEIKTANKTILIEALMDKGVEH
>NC_009922.1|WP_012158664.1|877774_879253_+|acetaldehyde-dehydrogenase-(acetylating)
MGLIDKDLVSIQETRDLLKKAKEAQKEIAKLSQEQIDTICKAIAKATFDNRVKLAKMAQEETGFGRWQDKVLKNAFASRDVLNAIKDMKTIGIIKNNPAAKYMEVAVPVGVIAGLIPSTNPTSTVIYKSLISIKAGNAIVFSPHPSALNCIKETVRIINEAGRSVGLPEGAISVITRVTMQATNELMKNENTDLILATGGSAMVRAAYSSGTPAIGVGPGNGPAFIERSADIPRAVELIIESKTFDNGTVCASEQSIIVEDISKEKVIAEFKKQGGYFLSKEDALKLEKYILRPNGTMNPNIVGRTAQVVAELAGISVPKDAKVLIAEETRVGNLAPYSREKLSPILAFYTVNTWQEARDLSIQILNFEGAGHTMVLHTTNDKIAEEFGLKVPVSRFLINCSATLGGIGATTNLMPALTLGCGAIGGSSTSDNVGPQNLFNLRRVVYGVRTLEEIRGEDVFAEGNAIDLEGSGFNKEQLVDLLVERVLQRLK
>NC_009922.1|WP_012158665.1|879316_879610_+|BMC-domain-containing-protein
MANTNALGMIETKGLVAAVEAADAMVKAANVTLIGKEQVGGGLVTVMVRGDVGAVKAATDAGAAAAEAVGELISVHVIPRPHMEVDVILPKYDTQNA
>NC_009922.1|WP_012158666.1|879691_880429_+|hypothetical-protein
MTILTESKIKKLLRTTKLKETRHLVLEPGTVITPSAKEYLKDIVIEYRHISEEHESRQQEATFPMTRLKENEPKGVKNIQDVLVYRNGNGQEIWKSHLRYLFKVKADGIISHILTIQKKSYHVGKMALVEALNTILVVVKTISMETLSPEILNQIQEIERLSEDKKPYMASLYPEGFFMPTYQDEECVLALFELHGCLQELEHFIAREMKEILILEDYILFVSIATILKDYCWILMVQSKEKSVE
>NC_009922.1|WP_012158667.1|880439_881075_+|phosphate-propanoyltransferase
MTKNNMDKIVDAVVARIHEVMDQTFEIEASGRHIHLNREAIDALFGVGYQLRPSKYLSQPGEFASEERVDVKGPKGTIHNVIILGPERKHCQVEVSITDARILGVNAPVHLSGNIENTPGVVIMNGSRSFALDRGVIVAKRHIHIKETDAKKFGVKDQDRVSVQVFSERPLIFDDVIVRISPKFETYMHIDYDEANACGHKKGVRGRIITR
>NC_009922.1|WP_012158668.1|881080_881689_+|hypothetical-protein
MDNIEIFVQKITDILMQRLEKEEPRKTLAFLGKEYTSIRTYYEQKGYRIVSFQEKMDEVIVTELPILNMNRLALGLPQGEDEIIIWDRLLKQKKVMVLQEGMELYISRQNISPALLQVLEHYKKQLVKYGVSILPLKNFEKSRETIHDVKNEAHKGGKKELLTIAKVREMNLQEGDIFEADPNTIITALARDYMRDLGVQIR
>NC_009922.1|WP_012158669.1|881702_881975_+|EutN/CcmL-family-microcompartment-protein
MFIGKVVGSLWATRKDEKLNGLKFLLIEKQRNEQEADPDLVVAVDRVGAGIGESVLITTGSSGRLSFDGKGIPVDMVIVGIIDTVDYPKK
>NC_009922.1|WP_012158670.1|882013_883099_+|ethanolamine-utilization-protein-EutH
MSINEIIIWIMAIIMVIGAIDRSIGNRVGLGQQFEEGILAMGSLALSMAGIIVIAPKLSDWLSPIVVPLYKMLGADPAMFAGTLLANDMGGFFLAQQMTTDPLIVLFSGGILGAMLGATLVFTIPVGLGIISSEDTKYLAQGVLCGIVTIPIGAFVAGVVMGMPAVKVFMNLIPIIVVAILISIGLFKIPEGMIKGFNVFGKIIVAVAAIGLAIGGLDLLLGIKVFENQDTLEVGFQTVGSIAITLAGAYGLVFLITRIFKKPLLRLGQLLGMNDIAAAGLIASLANNIAMFQTVKGMDRRGKVINIAFAVSASFTFGDHLGFTAGVAPELITPMIIGKLVGGISAIFVAIFLSKSVFGIE
>NC_009922.1|WP_012158671.1|883138_883597_+|cupin-domain-containing-protein
MLNIDRSEIEKLVRGIIMEEYGQKLNDASKRKVDPSGIMSIALPLFSVDEENRLDTGNPNHKVYTKDLVSLMESPRLGCGLMVMEDTTFDWTLGYDEIDYIIEGTLTIIIDGRRITANAGEVILIPRNSKIQFSVDGKARFIYVTYPADWQS

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Crispr_ID: NC_009922_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_009922_2

3051307-3051422

Orphan

Consensus_repeat	Method
GGCTTAGAACTTCAAGTGCTTAAAATAAAATTTGTTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_009922_2

>merge|NC_009922|2|3051307-3051422|CRISPRCasFinder
GGCTTAGAACTTCAAGTGCTTAAAATAAAATTTGTTCCCTTAGGCTCACAAACTTTATGGCGCACTCAGTTCTAGATGAGGCTTAGAACTTCAAGTGCTTAAAATAAAATTTGTTC

>NC_009922|2|2|3051307-3051422|CRISPRCasFinder
GGCTTAGAACTTCAAGTGCTTAAAATAAAATTTGTTC	CCTTAGGCTCACAAACTTTATGGCGCACTCAGTTCTAGATGA
GGCTTAGAACTTCAAGTGCTTAAAATAAAATTTGTTC

Protein	Signature genes	Signature genes Name	Protein_function
NC_009922.1\|WP_012160644.1\|3054424_3055015_+\|rubrerythrin-family-protein	unknown	unknown	gnl\|CDD\|153100
NC_009922.1\|WP_012160648.1\|3058266_3059052_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
NC_009922.1\|WP_156774465.1\|3045349_3045967_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NC_009922.1\|WP_156774536.1\|3057425_3058163_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|225375
NC_009922.1\|WP_041719445.1\|3043097_3044189_+\|DnaD-domain-protein	unknown	unknown	gnl\|CDD\|377797
NC_009922.1\|WP_012160638.1\|3049883_3050816_-\|YybS-family-protein	unknown	unknown	gnl\|CDD\|370773
NC_009922.1\|WP_012160635.1\|3045970_3047314_-\|replicative-DNA-helicase	unknown	unknown	gnl\|CDD\|273206
NC_009922.1\|WP_012160642.1\|3052275_3053604_-\|PhoH-family-protein	unknown	unknown	gnl\|CDD\|224787
NC_009922.1\|WP_012160631.1\|3041424_3042927_-\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341067
NC_009922.1\|WP_012160646.1\|3056577_3057405_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NC_009922.1\|WP_041719449.1\|3055105_3055327_-\|hypothetical-protein	unknown	unknown	unknown
NC_009922.1\|WP_012160645.1\|3055370_3056150_-\|DnaJ-domain-containing-protein	unknown	unknown	gnl\|CDD\|365959
NC_009922.1\|WP_041720045.1\|3047845_3049849_-\|phosphoesterase	unknown	unknown	gnl\|CDD\|226404
NC_009922.1\|WP_156774535.1\|3051839_3052127_-\|DUF2508-family-protein	unknown	unknown	gnl\|CDD\|378478
NC_009922.1\|WP_012160639.1\|3050862_3051192_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378899
NC_009922.1\|WP_156774534.1\|3039668_3041147_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|366703
NC_009922.1\|WP_041720046.1\|3053769_3054180_-\|hemerythrin-family-protein	unknown	unknown	gnl\|CDD\|274154
NC_009922.1\|WP_012160633.1\|3044201_3045182_+\|DNA-replication-protein-DnaC	unknown	unknown	gnl\|CDD\|235871
NC_009922.1\|WP_012160640.1\|3051483_3051750_-\|pro-sigmaK-processing-inhibitor-BofA	unknown	unknown	gnl\|CDD\|377835
NC_009922.1\|WP_012160636.1\|3047402_3047849_-\|50S-ribosomal-protein-L9	unknown	unknown	gnl\|CDD\|234659

Protein	Function_ID	Function_description	E-value
NC_009922.1\|WP_012160644.1\|3054424_3055015_+\|rubrerythrin-family-protein	gnl\|CDD\|153100	cd01041, Rubrerythrin, Rubrerythrin, ferritin-like diiron-binding domain. Rubrerythrin domain is a nonheme iron binding domain found in many air-sensitive bacteria and archaea and member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The homodimeric rubrerythrin protein contains a binuclear metal center located within a four helix bundle. Many, but not all, rubrerythrin proteins have a second domain with a rubredoxin-like hexacoordinated iron center. Rubrerythrin is thought to reduce hydrogen peroxide as part of an oxidative stress protection system but its function is still poorly understood.	4.41093e-55
NC_009922.1\|WP_012160648.1\|3058266_3059052_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	7.86176e-123
NC_009922.1\|WP_156774465.1\|3045349_3045967_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	1.10302e-19
NC_009922.1\|WP_156774536.1\|3057425_3058163_-\|alpha/beta-hydrolase	gnl\|CDD\|225375	COG2819, COG2819, Predicted hydrolase of the alpha/beta superfamily [General function prediction only].	4.12869e-35
NC_009922.1\|WP_041719445.1\|3043097_3044189_+\|DnaD-domain-protein	gnl\|CDD\|377797	pfam07261, DnaB_2, Replication initiation and membrane attachment. This family consists of several bacterial replication initiation and membrane attachment (DnaB) proteins, as well as DnaD which is a component of the PriA primosome. The PriA primosome functions to recruit the replication fork helicase onto the DNA. The DnaB protein is essential for both replication initiation and membrane attachment of the origin region of the chromosome and plasmid pUB110 in Bacillus subtilis. It is known that there are two different classes (DnaBI and DnaBII) in the DnaB mutants; DnaBI is essential for both chromosome and pUB110 replication, whereas DnaBII is necessary only for chromosome replication. DnaD has been merged into this family. This family also includes Ftn6, a cyanobacterial-specific divisome component possibly playing a role at the interface between DNA replication and cell division. Ftn6 possesses a conserved domain localized within the N-terminus of the proteins. This domain, named FND, exhibits sequence and structure similarities with the DnaD-like domains pfam04271 now merged into pfam07261.	1.64697e-11
NC_009922.1\|WP_012160638.1\|3049883_3050816_-\|YybS-family-protein	gnl\|CDD\|370773	pfam09991, DUF2232, Predicted membrane protein (DUF2232). This family of bacterial proteins are multi-pass membrane proteins with up to 10 (2 x 4/5) transmembrane regions. The exact function of this potential pore molecule is not known, but in many instances it is associated with ABC-transporter-like domains, implying that it is part of a secretion system that uses energy.	3.86647e-48
NC_009922.1\|WP_012160635.1\|3045970_3047314_-\|replicative-DNA-helicase	gnl\|CDD\|273206	TIGR00665, DnaB, replicative DNA helicase. This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites. [DNA metabolism, DNA replication, recombination, and repair].	0
NC_009922.1\|WP_012160642.1\|3052275_3053604_-\|PhoH-family-protein	gnl\|CDD\|224787	COG1875, COG1875, NYN ribonuclease and ATPase of PhoH family domains [General function prediction only].	0
NC_009922.1\|WP_012160631.1\|3041424_3042927_-\|M1-family-metallopeptidase	gnl\|CDD\|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	7.52897e-175
NC_009922.1\|WP_012160646.1\|3056577_3057405_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	5.9923e-25
NC_009922.1\|WP_012160645.1\|3055370_3056150_-\|DnaJ-domain-containing-protein	gnl\|CDD\|365959	pfam00226, DnaJ, DnaJ domain. DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.	1.7105e-18
NC_009922.1\|WP_041720045.1\|3047845_3049849_-\|phosphoesterase	gnl\|CDD\|226404	COG3887, COG3887, Predicted signaling protein consisting of a modified GGDEF domain and a DHH domain [Signal transduction mechanisms].	0
NC_009922.1\|WP_156774535.1\|3051839_3052127_-\|DUF2508-family-protein	gnl\|CDD\|378478	pfam10704, DUF2508, Protein of unknown function (DUF2508). This family is conserved in Firmicutes. Several members are annotated as being the protein YaaL. The function is not known.	1.23477e-07
NC_009922.1\|WP_012160639.1\|3050862_3051192_-\|hypothetical-protein	gnl\|CDD\|378899	pfam12643, MazG-like, MazG-like family. This family of short proteins are distantly related to the MazG enzyme. This suggests that these proteins are enzymes that catalyze a related reaction.	3.27877e-27
NC_009922.1\|WP_156774534.1\|3039668_3041147_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	2.0645e-49
NC_009922.1\|WP_041720046.1\|3053769_3054180_-\|hemerythrin-family-protein	gnl\|CDD\|274154	TIGR02481, hemeryth_dom, hemerythrin-like metal-binding domain. This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.	2.60408e-30
NC_009922.1\|WP_012160633.1\|3044201_3045182_+\|DNA-replication-protein-DnaC	gnl\|CDD\|235871	PRK06835, PRK06835, DNA replication protein DnaC; Validated.	3.20624e-161
NC_009922.1\|WP_012160640.1\|3051483_3051750_-\|pro-sigmaK-processing-inhibitor-BofA	gnl\|CDD\|377835	pfam07441, BofA, SigmaK-factor processing regulatory protein BofA. This family contains the sigmaK-factor processing regulatory protein BofA (Bypass-of-forespore protein A) (approximately 80 residues long). During sporulation in Bacillus subtilis, transcription is controlled in the developing sporangium by a cascade of sporulation-specific transcription factors (sigma factors). Following engulfment, processing of sigmaK is inhibited by BofA. It has been suggested that this effect is exerted by alteration of the level of the SpoIVFA protein.	0.000195327
NC_009922.1\|WP_012160636.1\|3047402_3047849_-\|50S-ribosomal-protein-L9	gnl\|CDD\|234659	PRK00137, rplI, 50S ribosomal protein L9; Reviewed.	2.27664e-63

>NC_009922.1|WP_012160639.1|3050862_3051192_-|hypothetical-protein
MFDFQKNNIDISRNIKMVEFLKCELLNSISVVFEALYKGAKDSQEMILEGLANIILVTYSLGRRLGVDYDAIDQKVQDKARVHILEEHHLEKWYGDLSSLHQHLKDNRK
>NC_009922.1|WP_012160638.1|3049883_3050816_-|YybS-family-protein
MQNNNYRKILMEALLIAVVATIFAISALQVSILPMILILIPVPFMILSYRHGHKYSIFSFIVFIVLMGVATNFNNAFYLGVIFAPMTIAMSYYLAKEKEPCVVIGAGTVATILSIAMVFKIITLVGGADIVKEISIMAEQIVNTQVDLLKSLEADIPSTESILSYLLLLIPGILMIQSLLIAMGNYYLAVNLLSRIKSLEFNRPQFSTFRLPQSFIMGSFMIVVLSYLTKYIEGIYYTSLITTVVILFMALFFIQGISVISFLIKRTNINNVVRVLLIGIIILISPLLTAVSFIGLIDSIVDIRKLERRE
>NC_009922.1|WP_041720045.1|3047845_3049849_-|phosphoesterase
MRNSKFIKMLVPDTRIYLIMLFIFILIISYYNKAIGIIGIFLLAYLIYYNLKISNIRREEWTKYIEGLSSDIDSATKYAVLNLPIPLTIVEFDGTITWYNRKFLEVLDTKDLLEKDIQDIIPNFDLRNLLQTENELSEVMNINNKYFKVVYNIVKLPKGHTSNYIIMLYWIDVTKFEELAKKYYREQMVVGLIQVDNYDEVMQSTEEMRRPLVGAEIEHRLNLWAGKINGFIRKYSKDKFMVIFQHEYLEKLEQKKFEIIDEIREINQGNTMPITLSIGIGVYGENALQTWNFANGAKDLALGRGGDQVAVKKGDKISFYGGKAKAVEKRTKVKARVVSHALRELIDQSTNVIVMGHKISDLDAFGSALGIYRAAKNRGKDAYIVLNGSNPSIEGLLDRIYEIEEYNSVIISCDEAKVKTLRTSLLVVVDTHRPNFTECPELLKISDKIVLIDHHRKGTDFIENAVLNYHETYASSTSELVTELLSYMEEKISMPPIEADALLAGIAVDTKNFTFKTGVRTFEAASILRRAGADTTSVKQLFEDEFNTIITRADVIRRAEIIYQTIAISTVEDISRASQLIAAQAADELLDARGITASFVLGRKDDTMVFISGRSMGDINVQVILEKLGGGGHMTIAGAQIEGISMEEAKEALEAAIEEYFEEGEEE
>NC_009922.1|WP_012160636.1|3047402_3047849_-|50S-ribosomal-protein-L9
MKVILLQDVKGLGKKGEVVNASDGYARNFLFPKKLAAEATQGNVKTLNEQKTSQELKKQQEVEEAKELAKKIENSPIEIIAKAGDGGRLFGSVTSKDLAETLEKQHHIKIDKRKITLPEPIRELGVRHVEIKLHVGVVGKLTVNIKEA
>NC_009922.1|WP_012160635.1|3045970_3047314_-|replicative-DNA-helicase
MEDLKLINKVPPNSIEAEQSVLGSMLLDREAIIIVLEFLRGSDFYKEAHKEIFEAMYDLFNRNEPVDLVTLTEELKKREKLDAIGGIPYLTSLASGVPITSNVRYYAEIVERKSLLRKLIKSSQDIIHLGYSSDVEVLDVIEQAQKSIYDISQDRSNEGFTHIRELLSDTFDKIEELYENKKGITGLTTGFMDLDKKLSGFHRTDLILVAARPAMGKSAFSLNLAQNAAIKAGASVAIFSLEMSKEQLMLRMLAAEAMVDLGKIQIGNLNEEEWAKIAGAMAPLSQSKIYFDDTPGISVMEMRSKCRRLKMEKGLDLVLIDYLQLMEGEGRSESRQQEIASISRNLKIMAKELDCPVIALSQLSRAPELRADHRPILSDLRESGAIEQDADLVMFLYRDEYYHPDSDKKNVGEVIIAKHRHGETGTVDLFWLGQFQKFLDYEKYRDA
>NC_009922.1|WP_156774465.1|3045349_3045967_-|GNAT-family-N-acetyltransferase
MVGDRMIVAKGQNIYIKKLERSDVDRMHDWGRHTDPLFYCYNFPQMNQMERDYWYKTKALSFTRRCFVVFNNEDELVGYIALRNVKIFRRTSDLGIVFDPSKVNQGYGTEGIKAFLTYYFEEMKMKTLNLKVSIFNKRAQRCYEKCGFESKGIVWDEFEDQSLPIFMDDYFVPYRHFFKKEKRVLKCQFINMAITKNQYQKLLNK
>NC_009922.1|WP_012160633.1|3044201_3045182_+|DNA-replication-protein-DnaC
MIEQFVQEILREYEIKRNAARASREKRIQEVYHRIPRIQEIDGELNKTGISISRALIKGVDDPEKTVASFKEYLDQLKRERAILLTENNIPMQYLDENFSCNECRDTGFTQGGQKCKCFKQQLITKAYDMSNLSNVLKKENFKTFNLSLFSDEPFDGQSLSPKQNMLDILNVSEGFVFNFEENNEENLLFYGETGLGKTFLTNCIAKALLDRGKIVIYQTSFKLLEILEDLRFNNDTKDRTKYNLLFEADLLIIDDLGTEMTNTFTNSEIFNIINSRLLSNKKTIVSTNLSPKEMMDRYDDRIFSRLFSKFTVLHFYGKDLRWETR
>NC_009922.1|WP_041719445.1|3043097_3044189_+|DnaD-domain-protein
MSFIKGNTSIDLGDTPIENIFIDVYMPMTNGTFVQVYLLGYKYAFDRDPNMEVSNLSIAKHLNIPLSDVLSAWDFWESKKIIVKHPSDDGDENNYKVEFVNLKQLYIDNNYKPTYAISSEESTASQKPSTYTCSPEDLLEANKVPEIRALFVEIRKIIARELQPNEMSKIIELIKRYNVDTPLIAEAFRYSKEQGKARHILSFASGVIRNWYDQGIFTVEELNDHLGKQSQRYEIYNKVFKSLGFASRGPSEAEKKIMDSWVDQFHFTIDVILAACQNSSKTSNPSINYIHAILKSWYESGIKEVGDIERLDKIERKSTSSKPVQAANKIKTKFHLAKSRGDKYTADELEALILNNQKNKLNR
>NC_009922.1|WP_012160631.1|3041424_3042927_-|M1-family-metallopeptidase
MYQIKLRKKLYLWGIVLVVFLIPVVLNFIWNTGQVQRVFNTVTQHKEIAEYTINAVFSKEDRIIRGQQHTSYENTSDNEVESIYFHLYPNAFKDSKTAPFQRGDMVRAYPNGFDKGWIKIHSVVEGKNKVDYRIMGKGDTNLRVTPKEPIKPGERIALTIDFEVKLPNAVGRMGYGENTVNIANWYPILSVFDKNGWNLEPYYAIGDPFYSKTAEYSVNFTIPEEYKLATTGNIIKVSDGNKSKTYKINANNVRDFAIVLSENFTVSKGLVEDIEVLSYTIGGQKKEEALKYGMDSLAIFNQLFGKYPYEQLSIVASDFFIGGMEYPNIVLISQELYEVKENFPLEYVIAHEVAHQWWYGIVGNNEITEPWLDEALTEYATLLYFEEKYGDTVKDEVYDKMIKKQYEALGKARKGKEDHILRSLKEFEDALEYSSIVYSKGAMFLEELRQQMGDESFIKAMREYYEAFQFKNATTEDFYNVVQKNSTSDLKDLFSEWLNK
>NC_009922.1|WP_156774534.1|3039668_3041147_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MKAISSKVNKIDQTSLKGQVKKAQNKSSYKKLHNKNIDFKAYINEFKNNKNFRYKAVGAALSLSLVSGIYFQVNSSVEAYTITVDNNVIAIVREEEDFIQALEQVKSEAAEDFGQDVVLNKEPIFVQSEVKKAQITELDEIIKNIKSQIDIQLKAAAIVVNGETVAIVKDSKTAEGILADVKAPFLEKGETEYDAIEFAEKVEIVEVGAELSDIITVEEALQKIAIGTDEEKIHEVMKGENPWTIAQKYGLKMSDIEKANPGLNPQKIQIGQKLSLIVPKPLVSVRTKEYVELVEAIPFETEYEKTPSLYEGDKKITVQGENGQREVKAYLVKENGVELNMEVLEEKIISQPKTRVIAQGTKERPATMATGVFTNPTRGRLTSPFGMRWGRRHTGIDIASSKGTTVTAADAGRVSFAGRQGSYGNLVIIDHENGYQTYYAHNSKIVINKGERVYKGQKIAEMGNTGNSTGVHLHFEVRKNGTPVNPQSFVRY
>NC_009922.1|WP_012160640.1|3051483_3051750_-|pro-sigmaK-processing-inhibitor-BofA
MGLELSIIMAYAFGLILLYIFGWILLIPLKWFVRLVFNSIVGGIMLFILNLIGGIWGIGLAINPLSAVVVGVLGIPGILLLFLFKYIL
>NC_009922.1|WP_156774535.1|3051839_3052127_-|DUF2508-family-protein
MVKKKEKSFTSLVSALGNMYNRMNPSSDQEKGNDEELAQCVRQAYEEWQAAENFFHSVSDPDLVDHAIYKLEATKARYVYLLKQAKSNGIRMNMH
>NC_009922.1|WP_012160642.1|3052275_3053604_-|PhoH-family-protein
MKKTFVLDTSVLLHDPRSLYAFGDNSVVIPAVVIEEIDKKKNLLDIIGRNAREVARELDDLRQQNSLSKGVRLENGGTLQIELNHKSFAHVAEWFNEINNDNRILAVALNLQLEQRKDEIKKSVVLISKDTIMRIKADSLGIESQDYLHDKIEYTYENYTGYRECVVPSHMVDRFYEEGGLEDTYFKEEGLLPNQFILLRAKEIPSKSAIGRFDKEAGVIRSLVFGENTYWGIRGRNAEQRMAMEVLLNDDIKLVTLTGKAGTGKTLLALAAGLQKTNDERIYKKLLITKPVIPVGRDIGYLPGDKNEKLRPWVQPIYDNLELLLGTKSLTKLEDTLIGMNRIEIEALTYIRGRSVPNQFIIIDEAQNLTKHEIKTIITRVGEGSKIVLMGDTEQIDHPYLDSECNGLTYIINKFKNENLAAHITFRKVERSALAQLAANLL
>NC_009922.1|WP_041720046.1|3053769_3054180_-|hemerythrin-family-protein
MFKWKERFETGIEEIDKQHKRLFEIGTQIYNLASKDDGTDHYDAIVGLIHELKDYTVYHFRYEEEQLEKANYSDIEAHKMEHQRFIDKLNETEAEDIDVNQKQVLMDMIEFIINWVSGHIVGTDFKYRELLMETLK
>NC_009922.1|WP_012160644.1|3054424_3055015_+|rubrerythrin-family-protein
MKFLKGTQTAVNLLTAFAGESQARNRYTYYAAQAKKEGYVQISNFFTETADNEKEHAKRFYKFLKEDNALNGESLEIAAAFPIALGDTAFNLKHAAAGENEEWTEAYPEFARIADEEGFPEVAVAFRKIAEVEKHHEARYLKLLSNIENGSVFKKEESTFWKCNNCGYIHEGDHAPEVCPACVHPQGHFEILAENY
>NC_009922.1|WP_041719449.1|3055105_3055327_-|hypothetical-protein
MNIGAISLVTAIMFGILQYLSHRDFDKYYKEKATEVQESKDILRYIHNMERRSIIMWFFIMINIRIIIANIAK
>NC_009922.1|WP_012160645.1|3055370_3056150_-|DnaJ-domain-containing-protein
MKMIKKILGKILMGISGLIAIVIDGLIQLTENIVVYTGKFLKGCLAVASMGGCLFFLLFANLGLRILTNSIGFSVIALMLLFLIFGGRVVSELKYRKYIITEFLRNTANYWIDEEKYTYKTFHSYKEAYRRAEEERIREEQRRYYEQQRQWEERFKQQWYQQYHQSGQGTYGSYGGQGAYGQGSMNPTLDFKNKFERSCDILGVPYDADRQQIKTAYRKKAKEYHPDLSKLPDATKRFQELNTAHEFLSDENLQRYGRM
>NC_009922.1|WP_012160646.1|3056577_3057405_-|helix-turn-helix-transcriptional-regulator
MGVITMEANKLAEIFIKASPTVVDIRKIRIEPGQADYGYITSLYAFIIPVKGEAKFIFNDIPYHLNPGKVIHAGPNIKVNKRVVGDSIWEYYLIHYSLKNTALEDDFVEIPYELTIGRNIKVLEMLKSMNKAWRISDPISSLKVQSLFYNLLYEIFKSHHDQAKEEDRWIVEEAMNYIHAYYMEPITLKDLAKRYDLDKNRFSRLFNRYAGARPMNYLISYRMKRASELLLTSNFSVREVSENVGYTNVSYFTKLFKKYNGQLPSTYRRKFYETL
>NC_009922.1|WP_156774536.1|3057425_3058163_-|alpha/beta-hydrolase
MEEFGERKIYGYMPPSYDGGLEKFPVVYLQDGGDFFLPEKNRVLSVLEGNFEKNKLKEVILIGIEPKQRLDEYSPWYATALSKRFKDFGGKGDVYIRFIVEELKPFIDASFNTDPSVEGTGIMGASLGGLISMYAACVYPEVFGRIGCISASFWYEDFLEYIVRREISNIRSKKIYMDVGSLEGHGKDSRQIFMVSNTKAIYDAFLEKGIGNENIRLEIDHGASHNYKFFADRFPKAIEWLFSKD
>NC_009922.1|WP_012160648.1|3058266_3059052_-|ABC-transporter-ATP-binding-protein
MTILKTENLETCYEKSTVFKDINFSVEEGEITTIIGPNGCGKSTLLKTIGRIIKQKNGDVLLKGTNINQLNTKKIAQDLALLPQNPTAPQEIKVEELISYGRFPHCKKISKLTAKDREIIEWAMEITKVMDYRDREIGSLSGGQRQKVWLAMALAQETDVLLLDEPTTYLDMSHQLEVLKIVDQLNREKRCTIVMVLHDINHAARFSHKIVAMKAGKIIAEGKPTEVITKDVLKKVFNIDARIMMDTENKAPVCFGYDSAL

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
NC_009922_1	1.1\|876345\|54\|NC_009922\|CRISPRCasFinder	876345-876398	54	NC_009922.1	2343874-2343927	2	0.963

1. spacer 1.1|876345|54|NC_009922|CRISPRCasFinder matches to position: 2343874-2343927, mismatch: 2, identity: 0.963

cacaaactttatgtcgcactcaactctaggtgaggcttagagtttcaagtgctc	CRISPR spacer
cacaaactttatgtcgcactcaactctaggtaaagcttagagtttcaagtgctc	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

147164 : 154982

Streptococcus_phage(50.0%)

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_012158004.1\|147164_148088_+	ATP-binding cassette domain-containing protein	A0A2H4PQG7	Staphylococcus_phage	6.9e-38	43.3
WP_012158005.1\|148080_148833_+	ABC transporter permease subunit	NA	NA	NA	NA
WP_012158006.1\|148865_149789_+	HAMP domain-containing histidine kinase	Q8QKV7	Ectocarpus_siliculosus_virus	3.7e-15	27.2
WP_012158007.1\|150209_151253_+	ATP-binding cassette domain-containing protein	G9BWD6	Planktothrix_phage	4.6e-30	34.5
WP_012158008.1\|151236_151917_+	ABC transporter permease	NA	NA	NA	NA
WP_012158009.1\|152103_153345_+	glutamate-5-semialdehyde dehydrogenase	A0A1X9I5D4	Streptococcus_phage	6.1e-106	50.9
WP_012158010.1\|153358_154150_+	glutamate 5-kinase	A0A1X9I5D0	Streptococcus_phage	4.7e-43	37.4
WP_012158011.1\|154160_154982_+	pyrroline-5-carboxylate reductase	A0A1X9I6T5	Streptococcus_phage	6.1e-46	41.4

DBSCAN-SWA_2

585738 : 593581

Synechococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012158411.1\|585738_587091_+	NCS2 family permease	A0A0R6PHV4	Moraxella_phage	3.9e-58	32.8
WP_012158412.1\|587165_588341_+	5-(carboxyamino)imidazole ribonucleotide synthase	NA	NA	NA	NA
WP_012158413.1\|588353_588860_+	5-(carboxyamino)imidazole ribonucleotide mutase	A0A2P0VNU7	Tetraselmis_virus	1.2e-23	42.3
WP_012158414.1\|588902_590309_+	amidophosphoribosyltransferase	A0A0M3SGR2	Mollivirus	1.4e-61	36.4
WP_012158415.1\|590341_591367_+	phosphoribosylformylglycinamidine cyclo-ligase	A0A0E3F760	Synechococcus_phage	1.9e-68	43.7
WP_012158416.1\|591363_591993_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	1.7e-19	33.5
WP_012158417.1\|592042_593581_+	bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase PurH	Q58MG4	Prochlorococcus_phage	3.4e-66	45.4

DBSCAN-SWA_3

1380441 : 1395329

Thermoanaerobacterium_phage(33.33%)

integrase

attL 1374704:1374719|attR 1397457:1397472

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
1374704:1374719	attL	NA	NA	NA	NA
WP_012159135.1\|1380441_1382256_+	DNA primase	A0A1S5RH03	Helicobacter_phage	2.2e-43	33.3
WP_012159136.1\|1382273_1383392_+	RNA polymerase sigma factor RpoD	A0A2I7SAT0	Vibrio_phage	2.4e-37	32.1
WP_012159137.1\|1383472_1383688_-	hypothetical protein	NA	NA	NA	NA
WP_041719065.1\|1383785_1384487_+	methyltransferase	NA	NA	NA	NA
WP_012159139.1\|1384471_1385590_+	Nif3-like dinuclear metal center hexameric protein	A0A1S5V250	Saudi_moumouvirus	8.7e-19	46.9
WP_012159140.1\|1385657_1386062_+	ribonuclease HI family protein	G3MBN7	Bacillus_virus	9.1e-11	32.2
WP_012159141.1\|1386603_1387746_-\|integrase	site-specific integrase	A0A0A8WIF9	Clostridium_phage	4.1e-56	34.9
WP_012159142.1\|1387792_1388290_-	ImmA/IrrE family metallo-endopeptidase	Q0H245	Geobacillus_phage	4.0e-08	30.7
WP_012159143.1\|1388307_1388700_-	helix-turn-helix transcriptional regulator	A0A0A7RTK4	Clostridium_phage	6.8e-19	39.5
WP_012159144.1\|1388906_1389116_+	helix-turn-helix transcriptional regulator	I3VYZ0	Thermoanaerobacterium_phage	7.7e-14	60.7
WP_012159145.1\|1389168_1389384_+	helix-turn-helix domain-containing protein	A0A2I7SCU5	Paenibacillus_phage	2.6e-12	63.5
WP_156774420.1\|1389465_1389612_+	hypothetical protein	NA	NA	NA	NA
WP_012159146.1\|1389608_1389950_+	hypothetical protein	NA	NA	NA	NA
WP_012159148.1\|1391306_1391714_+	hypothetical protein	I3VYY4	Thermoanaerobacterium_phage	1.4e-38	58.5
WP_012159149.1\|1391725_1391890_+	hypothetical protein	NA	NA	NA	NA
WP_012159150.1\|1391891_1392626_+	hypothetical protein	I3VYY1	Thermoanaerobacterium_phage	3.5e-69	56.4
WP_012159151.1\|1392653_1395329_+	DUF927 domain-containing protein	I3VYX9	Thermoanaerobacterium_phage	1.8e-259	50.9
1397457:1397472	attR	NA	NA	NA	NA

DBSCAN-SWA_4

1692948 : 1700903

uncultured_Mediterranean_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012159441.1\|1692948_1693506_-	SMC-Scp complex subunit ScpB	A0A1B1IVT7	uncultured_Mediterranean_phage	2.0e-16	34.1
WP_012159442.1\|1693498_1694269_-	chromosome segregation and condensation protein ScpA	A0A1B1IVW1	uncultured_Mediterranean_phage	3.6e-08	35.8
WP_012159443.1\|1694353_1695514_-	D-alanyl-D-alanine carboxypeptidase	NA	NA	NA	NA
WP_012159444.1\|1695722_1697048_-	pyrimidine-nucleoside phosphorylase	A0A0H3UZD4	Geobacillus_virus	2.3e-127	55.5
WP_012159445.1\|1697047_1697875_-	purine-nucleoside phosphorylase	Q5YBA4	Grouper_iridovirus	1.1e-58	41.2
WP_012159446.1\|1697887_1698709_-	purine-nucleoside phosphorylase	Q5YBA4	Grouper_iridovirus	6.1e-62	41.7
WP_012159447.1\|1698735_1699908_-	phosphopentomutase	NA	NA	NA	NA
WP_012159448.1\|1700018_1700903_-	site-specific tyrosine recombinase XerD	A0A0K2CP59	Brevibacillus_phage	6.0e-39	32.4

DBSCAN-SWA_5

2062615 : 2123365

Tupanvirus(18.18%)

protease,transposase,tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012159798.1\|2062615_2063185_+\|protease	rhomboid family intramembrane serine protease	NA	NA	NA	NA
WP_049753825.1\|2063172_2065422_-	EAL domain-containing protein	G3MA91	Bacillus_virus	3.9e-26	36.5
WP_012159800.1\|2065600_2066788_-	FprA family A-type flavoprotein	NA	NA	NA	NA
WP_012159801.1\|2066956_2068225_-	uracil-xanthine permease	Q9KX94	Enterobacteria_phage	3.5e-56	35.2
WP_012159802.1\|2068581_2068749_+	DUF3787 domain-containing protein	NA	NA	NA	NA
WP_012159803.1\|2068792_2072323_-	pyruvate:ferredoxin (flavodoxin) oxidoreductase	NA	NA	NA	NA
WP_012159804.1\|2072583_2074071_+	threonine synthase	NA	NA	NA	NA
WP_012159805.1\|2074080_2074974_+	homoserine kinase	NA	NA	NA	NA
WP_012159806.1\|2074979_2075420_+	ACT domain-containing protein	NA	NA	NA	NA
WP_012159807.1\|2075474_2076155_-	hydrolase	NA	NA	NA	NA
WP_012159808.1\|2076302_2076800_+	hypothetical protein	NA	NA	NA	NA
WP_012159809.1\|2076933_2078547_+	putative manganese-dependent inorganic diphosphatase	NA	NA	NA	NA
WP_012159810.1\|2078717_2079629_-	chemotaxis protein CheV	Q56AR1	Bacillus_thuringiensis_phage	4.0e-54	35.9
WP_012159811.1\|2079742_2080012_-	DUF3343 domain-containing protein	NA	NA	NA	NA
WP_012159812.1\|2080021_2080234_-	preprotein translocase subunit TatB	NA	NA	NA	NA
WP_012159813.1\|2080226_2081339_-	YedE-related selenium metabolism membrane protein	NA	NA	NA	NA
WP_012159814.1\|2081629_2083882_-	S-layer homology domain-containing protein	NA	NA	NA	NA
WP_012159815.1\|2083960_2084752_-	EF2563 family selenium-dependent molybdenum hydroxylase system protein	NA	NA	NA	NA
WP_012159816.1\|2085077_2086466_-	MATE family efflux transporter	NA	NA	NA	NA
WP_012159817.1\|2086698_2087190_+	YajQ family cyclic di-GMP-binding protein	NA	NA	NA	NA
WP_156774440.1\|2087257_2087947_-	phosphatidic acid phosphatase	NA	NA	NA	NA
WP_012159819.1\|2088179_2090693_-	U32 family peptidase	Q6DW11	Phage_TP	3.4e-31	31.0
WP_012159820.1\|2090827_2091382_-	cell division protein ZapA	NA	NA	NA	NA
WP_041719239.1\|2091530_2093924_-\|tRNA	phenylalanine--tRNA ligase subunit beta	NA	NA	NA	NA
WP_012159822.1\|2093940_2094960_-\|tRNA	phenylalanine--tRNA ligase subunit alpha	A0A2K9L3A8	Tupanvirus	2.9e-29	33.9
WP_156774441.1\|2095370_2095466_-	YqzL family protein	NA	NA	NA	NA
WP_012159823.1\|2095556_2096393_-	RNA methyltransferase	NA	NA	NA	NA
WP_012159824.1\|2096406_2097051_-	TrkA family potassium uptake protein	NA	NA	NA	NA
WP_012159825.1\|2097062_2098412_-	TrkH family potassium uptake protein	NA	NA	NA	NA
WP_012159826.1\|2098576_2098936_-	50S ribosomal protein L20	NA	NA	NA	NA
WP_012159827.1\|2098967_2099162_-	50S ribosomal protein L35	NA	NA	NA	NA
WP_083757157.1\|2099182_2099701_-	translation initiation factor IF-3	A0A2L0UZ54	Agrobacterium_phage	1.3e-12	32.9
WP_041719931.1\|2100091_2101678_+\|protease	ATP-dependent zinc metalloprotease FtsH	M4QNJ1	Ostreococcus_lucimarinus_virus	1.3e-100	45.6
WP_012159830.1\|2101759_2103670_-\|tRNA	threonine--tRNA ligase	A0A2K9L297	Tupanvirus	7.8e-145	40.4
WP_012159831.1\|2104071_2104674_-	DUF445 family protein	NA	NA	NA	NA
WP_012159832.1\|2104798_2105710_-	sporulation protein YtxC	NA	NA	NA	NA
WP_012159833.1\|2105965_2106223_+	ferrous iron transport protein A	NA	NA	NA	NA
WP_012159834.1\|2106245_2108183_+	ferrous iron transport protein B	NA	NA	NA	NA
WP_012159835.1\|2108289_2109555_-	group II intron reverse transcriptase/maturase	A0A0U4J920	Pseudomonas_phage	8.3e-34	29.3
WP_156774442.1\|2109742_2109889_-	hypothetical protein	NA	NA	NA	NA
WP_012159836.1\|2110601_2110883_-	hypothetical protein	NA	NA	NA	NA
WP_156774436.1\|2111239_2112103_-\|transposase	IS3 family transposase	A0A1P8CWQ3	Bacillus_phage	2.5e-42	35.6
WP_012159746.1\|2112111_2112405_-\|transposase	transposase	NA	NA	NA	NA
WP_083757159.1\|2113095_2113272_-	hypothetical protein	NA	NA	NA	NA
WP_156774443.1\|2113208_2113370_-	hypothetical protein	NA	NA	NA	NA
WP_012159837.1\|2113488_2113890_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_012159838.1\|2114256_2114745_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_012159839.1\|2115366_2115975_-	DUF1311 domain-containing protein	NA	NA	NA	NA
WP_012159840.1\|2116340_2116895_-	hypothetical protein	NA	NA	NA	NA
WP_012159841.1\|2117266_2117668_-	hypothetical protein	NA	NA	NA	NA
WP_012159842.1\|2118104_2118323_-	DUF4177 domain-containing protein	NA	NA	NA	NA
WP_156774444.1\|2118665_2119190_-	ferritin-like domain-containing protein	NA	NA	NA	NA
WP_041719249.1\|2119439_2119676_-	hypothetical protein	NA	NA	NA	NA
WP_012159844.1\|2119994_2120408_-	RidA family protein	NA	NA	NA	NA
WP_012159845.1\|2120583_2120853_-	hypothetical protein	NA	NA	NA	NA
WP_012159846.1\|2121291_2121837_-	hypothetical protein	NA	NA	NA	NA
WP_012159746.1\|2122199_2122493_+\|transposase	transposase	NA	NA	NA	NA
WP_156774445.1\|2122501_2123365_+\|transposase	IS3 family transposase	A0A1P8CWQ3	Bacillus_phage	6.6e-43	36.0

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. NC_009922

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