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
CP025831	Akkermansia muciniphila strain AMDK-16 chromosome, complete genome	3 crisprs	DinG,csa3,DEDDh,cas3,cas2,cas1,cas9	0	11	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: CP025831_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP025831_1

2107127-2107222

Orphan

Consensus_repeat	Method
GTCGCACCCTCACGGGCGCGTGAATTGAAGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP025831_1

>merge|CP025831|1|2107127-2107222|CRISPRCasFinder
GTCGCACCCTCACGGGCGCGTGAATTGAAGTGTTGATGAGTAACTGCCAAGCTTGGTTCATCAGGGTCGCACCCTCACGGGCGCGTGAATTGAAGT

>CP025831|1|1|2107127-2107222|CRISPRCasFinder
GTCGCACCCTCACGGGCGCGTGAATTGAAGT	GTTGATGAGTAACTGCCAAGCTTGGTTCATCAGG
GTCGCACCCTCACGGGCGCGTGAATTGAAGT

Protein	Signature genes	Signature genes Name	Protein_function
CP025831.1\|QAA55687.1\|2104026_2104635_+\|beta-phosphoglucomutase-family-hydrolase	unknown	unknown	gnl\|CDD\|223710
CP025831.1\|QAA56299.1\|2104784_2106638_+\|acetolactate-synthase,-large-subunit,-biosynthetic-type	unknown	unknown	gnl\|CDD\|215261
CP025831.1\|QAA56300.1\|2113047_2114712_+\|sulfatase	unknown	unknown	gnl\|CDD\|293763
CP025831.1\|QAA55680.1\|2097907_2098690_+\|enoyl-ACP-reductase	unknown	unknown	gnl\|CDD\|223696
CP025831.1\|QAA55681.1\|2098831_2099689_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224513
CP025831.1\|QAA55694.1\|2120649_2122788_+\|glycoside-hydrolase-family-2	unknown	unknown	gnl\|CDD\|236657
CP025831.1\|QAA55693.1\|2119229_2120330_-\|site-specific-integrase	unknown	unknown	gnl\|CDD\|271175
CP025831.1\|QAA55690.1\|2109606_2110260_-\|ribulose-phosphate-3-epimerase	unknown	unknown	gnl\|CDD\|238244
CP025831.1\|QAA55685.1\|2103300_2103522_-\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA55683.1\|2100837_2101968_-\|dihydrouridine-synthase	unknown	unknown	gnl\|CDD\|239200
CP025831.1\|QAA55689.1\|2108570_2109467_+\|phosphatidylserine-decarboxylase	unknown	unknown	gnl\|CDD\|179097
CP025831.1\|QAA55688.1\|2107416_2108250_+\|secretion-protein	unknown	unknown	gnl\|CDD\|367948
CP025831.1\|QAA55692.1\|2115995_2117198_+\|carboxynorspermidine-decarboxylase	unknown	unknown	gnl\|CDD\|143502
CP025831.1\|QAA55695.1\|2122877_2123252_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366285
CP025831.1\|QAA55686.1\|2103602_2103866_-\|30S-ribosomal-protein-S20	unknown	unknown	gnl\|CDD\|376586
CP025831.1\|QAA56301.1\|2117221_2119159_+\|biosynthetic-arginine-decarboxylase	unknown	unknown	gnl\|CDD\|235427
CP025831.1\|QAA55679.1\|2096964_2097840_+\|bifunctional-5,10-methylene-tetrahydrofolate-dehydrogenase/5,10-methylene-tetrahydrofolate-cyclohydrolase	unknown	unknown	gnl\|CDD\|223268
CP025831.1\|QAA55682.1\|2099685_2100825_-\|transglutaminase-domain-containing-protein	unknown	unknown	gnl\|CDD\|376628
CP025831.1\|QAA55684.1\|2101966_2103166_+\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	unknown	unknown	gnl\|CDD\|237367
CP025831.1\|QAA55691.1\|2115027_2115915_-\|DNA-polymerase-III-subunit-gamma-and-tau	unknown	unknown	gnl\|CDD\|237030

Protein	Function_ID	Function_description	E-value
CP025831.1\|QAA55687.1\|2104026_2104635_+\|beta-phosphoglucomutase-family-hydrolase	gnl\|CDD\|223710	COG0637, COG0637, Predicted phosphatase/phosphohexomutase [General function prediction only].	2.72666e-53
CP025831.1\|QAA56299.1\|2104784_2106638_+\|acetolactate-synthase,-large-subunit,-biosynthetic-type	gnl\|CDD\|215261	PLN02470, PLN02470, acetolactate synthase.	0
CP025831.1\|QAA56300.1\|2113047_2114712_+\|sulfatase	gnl\|CDD\|293763	cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	2.81236e-172
CP025831.1\|QAA55680.1\|2097907_2098690_+\|enoyl-ACP-reductase	gnl\|CDD\|223696	COG0623, FabI, Enoyl-[acyl-carrier-protein].	2.77822e-127
CP025831.1\|QAA55681.1\|2098831_2099689_-\|hypothetical-protein	gnl\|CDD\|224513	COG1597, LCB5, Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase [Lipid metabolism / General function prediction only].	1.77322e-43
CP025831.1\|QAA55694.1\|2120649_2122788_+\|glycoside-hydrolase-family-2	gnl\|CDD\|236657	PRK10150, PRK10150, beta-D-glucuronidase; Provisional.	6.66008e-54
CP025831.1\|QAA55693.1\|2119229_2120330_-\|site-specific-integrase	gnl\|CDD\|271175	cd00397, DNA_BRE_C, DNA breaking-rejoining enzymes, C-terminal catalytic domain. The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.	1.00372e-12
CP025831.1\|QAA55690.1\|2109606_2110260_-\|ribulose-phosphate-3-epimerase	gnl\|CDD\|238244	cd00429, RPE, Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.	2.30931e-105
CP025831.1\|QAA55683.1\|2100837_2101968_-\|dihydrouridine-synthase	gnl\|CDD\|239200	cd02801, DUS_like_FMN, Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.	1.6243e-54
CP025831.1\|QAA55689.1\|2108570_2109467_+\|phosphatidylserine-decarboxylase	gnl\|CDD\|179097	PRK00723, PRK00723, phosphatidylserine decarboxylase; Provisional.	2.32887e-125
CP025831.1\|QAA55688.1\|2107416_2108250_+\|secretion-protein	gnl\|CDD\|367948	pfam04450, BSP, Peptidase of plants and bacteria. These basic secretory proteins (BSPs) are believed to be part of the plants defense mechanism against pathogens.	1.11966e-62
CP025831.1\|QAA55692.1\|2115995_2117198_+\|carboxynorspermidine-decarboxylase	gnl\|CDD\|143502	cd06829, PLPDE_III_CANSDC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase. Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.	0
CP025831.1\|QAA55695.1\|2122877_2123252_+\|hypothetical-protein	gnl\|CDD\|366285	pfam00754, F5_F8_type_C, F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.	1.19625e-20
CP025831.1\|QAA55686.1\|2103602_2103866_-\|30S-ribosomal-protein-S20	gnl\|CDD\|376586	pfam01649, Ribosomal_S20p, Ribosomal protein S20. Bacterial ribosomal protein S20 interacts with 16S rRNA.	1.24995e-16
CP025831.1\|QAA56301.1\|2117221_2119159_+\|biosynthetic-arginine-decarboxylase	gnl\|CDD\|235427	PRK05354, PRK05354, biosynthetic arginine decarboxylase.	0
CP025831.1\|QAA55679.1\|2096964_2097840_+\|bifunctional-5,10-methylene-tetrahydrofolate-dehydrogenase/5,10-methylene-tetrahydrofolate-cyclohydrolase	gnl\|CDD\|223268	COG0190, FolD, 5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme metabolism].	2.62007e-142
CP025831.1\|QAA55682.1\|2099685_2100825_-\|transglutaminase-domain-containing-protein	gnl\|CDD\|376628	pfam01841, Transglut_core, Transglutaminase-like superfamily. This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.	2.73258e-12
CP025831.1\|QAA55684.1\|2101966_2103166_+\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	gnl\|CDD\|237367	PRK13371, PRK13371, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional.	0
CP025831.1\|QAA55691.1\|2115027_2115915_-\|DNA-polymerase-III-subunit-gamma-and-tau	gnl\|CDD\|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	0.00530894

>CP025831.1|QAA56299.1|2104784_2106638_+|acetolactate-synthase,-large-subunit,-biosynthetic-type
MSTNDKTSSAPTKTRMTGAEVLVECLVREGVDVVFAYPGGASMPIHQALSHQPKIRTILPRHEQGGAFGAEGYGRVTGKVGVCISTSGPGATNMITSIADAYLDSTPLVAITAQVMRSLIGRGAFQETDVFGMTAPIVKHSYLVTEPEELPRIIKEAFYIASTGRPGPVLIDMPKDVQEAVFTPDFDMEMDIPGYNPVLPVPADKLEELIPLIENARRPVIYAGGGIISAEASGDLLEFAERSQIPVATTLMGIGAMPETHPLSLRWLGMHGAVFANNAVNEADLVIALGARFDDRVTGAVNMFCPESTIVHIDIDASEINKNKKVAYPIRANVKDALRVLNSALAAKGWERKSSGYTRTPEWFGVIDGWKKQYPFSYEDRKGYIAPQAVIEELYRQAADKDPIICTGVGQHQMFAAQFFKFDKPRRLATSGGLGTMGYGLPASMGACLAYPDRLVVNIDGDGSMLMNIQELATIHVERLPVKCIILNNQHLGMVVQWEDLKYDSNRAQTFLADPHDNYDPTHKTEDVIYPNYPLICAGFGVKCERVLRIEELPAAITRMIESPEAYVLDVMVPHDVHVLPMILGGMSYKDVILERIAGDGSAKKASELGKEIPTAL
>CP025831.1|QAA55687.1|2104026_2104635_+|beta-phosphoglucomutase-family-hydrolase
MKKRVDLPEKKYEGYIFDLDGTLVDSMPLHYRAWREALARAGAPDHVFRTDEFYSCGGKSANDVVRFLNERYGMHMDAESTAADKRRIYLEMLEKEGMQPIQEVVEFVHSLGDAPKAIATGSAMPGASRTLAAAGLSGLFDVILTPDEVEHGKPAPDMFLKAAELLGASPDRCVVFEDAEPGMKAAAAAGMDCIQVRRPSLA
>CP025831.1|QAA55686.1|2103602_2103866_-|30S-ribosomal-protein-S20
MANTKSALKRIRQTATRTARNRAVTSKLKTLRKKVAAAVETSDKEAAAAAYNTFSSAVDKAAKVGTIPANRAANYKSKAAKAIAKIA
>CP025831.1|QAA55685.1|2103300_2103522_-|hypothetical-protein
MQQSRLDKAKLIIDRPGDFKVCEACGSIVSLTTAVCPNCNAYRFDSNTEYVVEQAVLLASREQRSVTPEDLEI
>CP025831.1|QAA55684.1|2101966_2103166_+|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase
MNQDSTRKARVNVRRAEVMEQVEKEIQQHYQSELISHIRSAGNVYNLGHTEFFLAREFGFCNGVRRAIDIAYAARRVFPDRRIFLIGDIIHNPEVNRQLEEMGIRKLPWKQLDSSYDRVAPDDVVIIPAFGVPTPFMDALEEKGVQIVDTTCGDVMKVWKRVKNYAAMGITSIIHGKATHEETSATASRALGERGRGKYLVVYDLEDARILCDYIMGRGDREAFLKRFEGCCSPGFDPDRDLEEVGIANQTTMLKTETQTLQKMVKDAIVQRDGDDDNFYVFDTICGATQDRQDALYELLKNPLDVMFVVGGYNSSNTTHLVDIAREHVPTYFIESAECIKSIQYVDAFDTKTREVRRMTTEPVVQNLGKSLKVGITAGASCPANLIEATILRIADLRK
>CP025831.1|QAA55683.1|2100837_2101968_-|dihydrouridine-synthase
MLPASTLSFFRQDNHSLPTGAFHGMHRPMLLALAPMKDVTDLAFLNTLKDLNSLPDYFITEYFRTVAHHKKMSPYILRSIDENPTGRPIYGQLVGHEPEYLARDAQVLMEHACAGVDLNMGCPAPIVCRRNAGGGMLRSLKAMDAALGALRDVLPPGAFTVKCRLGYETPDEFERILPVIASHSPDRVCIHARTVREGYRSPVHPEWVKWAAGMLKCPVVANGNIVDAATAEAWVRLARPAGLMIGRAALRNPWIFSQLHSRFQGHPAADLTFRNVLHYIRRLYERTREMQEHYVEEKHIHRMKKYLVYTARGLPDTFDHYMKRAKTARDFMRICEDILDNDAPFAPTPPEDTHLFAHFHTLLAQEEACLPPGIQV
>CP025831.1|QAA55682.1|2099685_2100825_-|transglutaminase-domain-containing-protein
MNLLPFALLPGLTAAICAAHDAIQDGVEFLRAHMPAQDRGTVTQERLVREVRLALAARSQFPWAAQVPWELYENNVLPYAVVNEPRDEWREQFHHLFAPLVSPCKTGREAALAIASLIQKTLNVRYSTERRVPHQGVKESLQSGKVSCTGQSILLICALRSVGIPARMAGVLTWNHVRGNHNWVEAWCDGEWKMLEYNEKDFNTPWVMSAISMLDPRKPENAIYATSWKKEPSGAFFPMIWEARYDEKRHALAFPPESRTVPAVNITDRYMKLANEWVVAQPEYVPGSRLMLDIREERKNGARRLPLHVVLKSEEGKVLAEGITPGPSDDMRKFLEVLLPDNISRGMLEFKLPDGTVRHEPVAHTEAPVQILNFFVSAP
>CP025831.1|QAA55681.1|2098831_2099689_-|hypothetical-protein
MKIPLFFNNTARSARAGRFRRWLDRHRDFFDVIEPESREDMLNHLVSQANSGAPAVAVAGGDGTLGIAARALCNTETVLAPFPAGTMNVFSREIGIRPDFDHALHILNTGRSKNVDLFAFNGQVFLQMAGIGADARAVELTTWEMKKKWKALAYVIAGARVCTEKQPHLTLTTDEGRVLEGRSIIFGNGRKYGGPLNFFAEADNSDGLLDAVVFRHSITSIIGEFLMAAVQGGFHSRRSGSFEYIRMTGGTVTSAEQASCELDGDYAGNAPVRITRPGSLKVFVP
>CP025831.1|QAA55680.1|2097907_2098690_+|enoyl-ACP-reductase
MSSKLLEGKVGVVVGVANKRSIAFAIAKAWHEAGAKLIFNYQGERLKDGVLKLIHENFGEDVPVYDLDVSSDESVNAFFERVRQHTDKVDCLLHSVAFAPKEALGGSFLETGREAFKISLDISAYSLVALSRAVEPMMSDNGSILAMSYLGSEKVVPNYNLMGVSKAALEACTRYLAYDLGRSRGIRVNCISAGPMQTLAARGVSGFNTMFKVYEEHAPLGRSCTGEELGATGVFLASDGAAAITGQVIYVDGGYQIMGM
>CP025831.1|QAA55679.1|2096964_2097840_+|bifunctional-5,10-methylene-tetrahydrofolate-dehydrogenase/5,10-methylene-tetrahydrofolate-cyclohydrolase
MQIIDGKQVASQVLEEVERDIARLREQGITPGLAVVLVGEDPASQVYVNSKVKKCAELGMNSRKIVLPSDASQEELLRIVRELNVDPAVHGILVQSPPPPHIDEAAVVLEIDPAKDVDGFHPENVAKLVLEDETGFVPCTPLGCMRLLKAAGIETAGANAVVIGRSMIVGKPMAHLLMSKQANATVTVAHSRTKNLPELCRSADIIVAAIGRPAFVTADFVKDGAVVVDVGINRVEDASAKRGYRIVGDVAYDEVAPKCRAITPVPGGVGPMTIAMLMANTVKACRQQTGA
>CP025831.1|QAA55688.1|2107416_2108250_+|secretion-protein
MKRYCLVSGLCLCLFMGIFSCIPEAPEHKTEKDASAIVLDEDSDIIWRNFSLGRVSFDDKAPHSKGSRIFHRLIPDTEVYIRQLSRIVLHTLYESPEECIVPVHHLRFMLEDTDGVACKWGGNGEVAISCSTRHIEGLFKDDDDAAKVYFEIRGVLLHELTHVYQQEPQGIGSYGTNREFRAFIEGIADAVRIANGGFHRGAYRPTGGSYMDGYLHAGYFFVWLRDYKDPEFLRKLNRSALEVVPWSFDGAVKYALGSEYHIDELWREYQRVMEEEK
>CP025831.1|QAA55689.1|2108570_2109467_+|phosphatidylserine-decarboxylase
MEGIRYYNRYTGREEREQVPGEKYMQWIYGTASGKAALHVLIKRGVFSRLLGWLKNRPSSARSIPSFVEEYGINMEDSLKGVGEFRHFNDFFYRRLKPGARPLAGGEDTAVFPADARHMGWERADRIKNVFVKGQRFDLPSLLGSDTLAERYAAGAVVLSRLCPTDYHRFHFPVSGVPGPWTKLGGPLASVSPYCLRGRLAWLWTNKRNLTLIRSELWGEVAMLEVGATGVGLIEETYVPGVFSARGAEKGYFAFGGSTVMCFFEPGRVSLASDLLEKTEEGLELFARQGDMMGTAAT
>CP025831.1|QAA55690.1|2109606_2110260_-|ribulose-phosphate-3-epimerase
MTIISPSLLAADFSRIGEEARRAFDSGADWLHLDIMDGHFVDNISFGPEICAAVRKAVGPDRFLDAHLMIERPDHYFDRFVRAGVNLICFHVELGDSYYIRNTLGRIREAGVKNGLALNPATSFEAVEPYLAEIDLLLVMSVVPGFGGQSFMPSVLDKVEKAVEWRTENRASFLIQMDGGIGQNNAAQCALAGADVLVAGSSTFKAPDMARAIAEMK
>CP025831.1|QAA56300.1|2113047_2114712_+|sulfatase
MSAVCGALFLFAGASALGNGSNPVSGKKPNIIVFLVDDMGWQDTSHPFWSDSQGNPKKTFLNRRYRTPNMEKLASQGMTFTDAYAHPLCTPSRVSLMSGMNPARHRVTCWVREQNGTTDANSRSLLPPDWALNGLQPIGTPARGTTKRPISGEDMRYHMTRPFATAATLPEMLKKCGYVTVHCGKAHFGTQGTPGSNPLNMGFDYNIAGTEIGHPADYRGSRHYGKGFNHVRGLDENNYYQDDVFLTEALTREAIKRLEAIRTNPREAGKPFYLYMAHYALHSPLDERAYDKRFADAYKNPEDGHKWSRTEKHYSGLIEGMDKSLGDIMKYLREHHLEKNTVLVFMSDNGGLAISGRLGNEEANYPLSFGKGSCMEGGIREPMIVSWPGVTKGGSRCAVPVVIDDFFPTLLDIAGCRNVEVPQKLDGLSLVPLLKGGRFPEDRPLLFHQPNNWGEGSRQAPQYTSSTALRQGDWKLIYRHLAQSFELYHLRKDIGEKENLASREPRKTREMAVVMGRLLRERKAQMPTYKKDNELGAPAGSSVPWPDQVKGNGF
>CP025831.1|QAA55691.1|2115027_2115915_-|DNA-polymerase-III-subunit-gamma-and-tau
MRTPSPLPPAPRIKRKRQKTAQNGTSCILFLEMGCIFLFYNVTIAIAMTNIHPFTTAAACILTAGAALFTSSCQPASPESYARQFATAQHVSVHGYNGRETLTSRVYADWGSMPANARRAMEEYIKGAEWKTMDYIRPQYFIQVDRSFWAICIDNDGNMTGIIPFRNGKDARKMSVNNHFKMLVNTTDRAPALGYAILKNLAYADGLRVSTRKADGLETPVPAPPAMKVVVPPKGAAPSAAPAAKSAATSVSEPGATEETPADDTAGTEEEPSADSAAESEDTTTTDDAAVTDDF
>CP025831.1|QAA55692.1|2115995_2117198_+|carboxynorspermidine-decarboxylase
MSAFIVSLPALERNALILRDVADAAGCRIALALKGFSCWPCFEALSPWLDGCCASGLWEARLARRRFGKHVLTYSPGHAPEEIAELAEISSHLDFNSLTQWSRFREEVMRHPRFVSGELKCGLRVNPQCSTGHTPIYDPCAPGSRLGVTPDMMQGADLSGISGLHFHTLCEQGADDLAVTMDAVERHFGHLLSRPEISWLNMGGGHWITKPDYDRKLLAALIRRIRERYGVEVWLEPGEAAAIHTGVLRCRVLDLFSAEGVNHAILDVSASAHMPDTLEMPYRPDVFQIAGDASLRSAQQPAVRLEGESYALAGKAGEKAYTYRLGAPTCLAGDRLGDYSFAEPLAVGDELVFDDMAHYTMVKTTFFNGVRHPDIAVQRKDGSVETVRRFSYEDFEARLG
>CP025831.1|QAA56301.1|2117221_2119159_+|biosynthetic-arginine-decarboxylase
MATAKEGIKQKVHGWSHHDSADLYGIDDWGNGYFRISKKGEVTVRLNDEDGGKKDVSLCDLLEGLKERGTTVPVLFRFRDLLRSRIAELNDSFRKAIKEAGYQGKYQGVYPIKVNQQRQVVEEIAEFGTKYDYGLEAGSKPELIAAMAHMHNPNAYLICNGYKDDEFIDLALTAQKMGLNIFIVLEMPSELDVIMERARRMDIRPNLGVRVKLAAKGSGLWQESAGDKSVFGLNAAQVVDVVDKLKQVDALDCLKLLHYHQGSQIPNISVVREGLTEAVRIYVDLVKEGAPLGTLDMGGGLAVDYDGSKTNFHSSCNYSIAEFARDVVEVVGDMCSKYGVPHPTLVTESGRAVVAYYSVLVFNVLDVTSAPGEEPPPELPDDAPELLKAFADTDRTLARKNMQECYNDACYYRDQLRAQFFYGNATLRQRGLGEAYYWHILSRISRMLAEMETIPEDLRELSCSMVDFYYGNFSLFQSLPDSWAIRQLFPVMPLHRLNERPTNKAVLADITCDCDGKIDHFIDREDVATALPLHAIKPGEDDYYIGVFLVGAYQETLGDLHNLLGDTNVVGVHLEGGRPVYTHEVEGDTVSDVLSYVEYDPKELINKFRTFAEQAVAEGKISPSERRRALEVFRSGLNGYTYYEL
>CP025831.1|QAA55693.1|2119229_2120330_-|site-specific-integrase
MNMKKAPNTNKLKYVGAALLEGESVTLIQAARLVLEIKEALGDEICTITRCREVVSLGLNAIKNKHQTVSFGTAAVECLRSKSHRRPRTLTDIRSIIHKLKKSNPELEHTSLRNLSVEECQNILMNTFTTSRQRHKARLILSGIFSFSVKRGWCDENPILRVDTPFLQEQEIPALTLKEITQLLKAAMEEFDGSCAAGAALMIFAGIRPQEVERLLWENIALRDGCIILNSKHTKTGGARHVTILPVLAKWLKFCRDRTKPGPGTPICPKGWTIKWRKIRKKAGWGGRKKSWVPDCLRHTYASYHAKHFKDYNLLQMEMGHRSSSLLRTRYLNMKGISPQTATRFWALTPAKVIEETKPPEEPLVS
>CP025831.1|QAA55694.1|2120649_2122788_+|glycoside-hydrolase-family-2
MNIRIHSFNVSCVGLCCVLGSFFAADAREVYPLNGSWDFSFNGKPAEKVTVPHTWNAEDAANGAQGKREDAKSVNSDAYRRGPAVYSRTLPVEPRPGKRYFIRGGGASIVSEVSVNGKPAGSHEGAFTAFCYEITPLLKKGSNTISVLVDNTQRNHIAPQRGDFSMFGGLYRPIELIETDGVCIDPLFYASPGVFITTKSLSKSKAEVEVKTLLNSDGKAGDVDVAVEILDMKGRKVAGKTVKAAAGEKNRLEVPVTLAIANPILWNGVKNPYLYQVKTSIRTADGQTDELVQPLGLRTVSVNPKEGFVLNGKTMQIKGVSRHQDMKGKGWALSPEDEARDIRLIADMGADGVRTGHYPASTNIYDLCDKAGLIVWSEVPNVNLVWDTPEFRENNRLQAREMIFQHWNHPSICMWGIFNEIGHQPEAATRGVDMEAELTELNKFVKETDPSRMTVGASNQAGRRKLNNIPDHIAFNTYPGWYGGGPETMKGNLNGYIRDYGGKMGIAVSEYGHGASVDMHENPAQRPSPTGFWHPEEWQSHAHEVNYRCIRERPEVWGAFVWNMFDFGSSSRFEGESPGINDKGLVTYDRKTPKDAYFFYRANWSPRPTVYITSRRFAERTEKTVPVKVYSNGSVVKLSVNGKPVGSVKPDDLKRAVWPEVTLKPGVNTITATASIGGKTYTDSCKWTLNPAGGDGKKDSERYQDPSLKKYK
>CP025831.1|QAA55695.1|2122877_2123252_+|hypothetical-protein
MFRIGNPDTYWHTSYTNGLPGFPHSIAVDMGTRMKFTGFIYTPRMDKDKGLISQYTFSVSDDGRNWREVKKGQFSYHYIRKDPAVQRIDFGRPVEARYFKLDARSPVRGGEQSATVAELNIITQ

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Crispr_ID: CP025831_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP025831_2

2536821-2538240

TypeII

Consensus_repeat	Method
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CRISPRCasFinder
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CRT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	PILER-CR

21 spacers

cas2,cas1,cas9

The CRISPR arrays of CP025831_2

>merge|CP025831|2|2536821-2538240|CRISPRCasFinder,CRT,PILER-CR
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATTACAAAATCTCCGTAGGGTCTGCGTCATCCGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATTTGACCGCCGAGGTAAAGTACTGTATGTCAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATACAGGGACTGGCCGCATGTCGATTGCACCGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCATACCGGATTGTTTCTGCATAAAACACCAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCTGACGATATTTTTAGGGGTACGGGTGACGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATAGCATAGCATCGAGGAAAACAATGCCGATAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATAAAAATAAAATTCTCAAAAGGTGTGATCTTGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATGAAATAAAACAATGAGCATTTACGACGACCGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCAATCGATTATACCCCCGCAACGCACCTCAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATATGACGCACAGGCCCCAGAATCATGGGATTGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCAAGGGGGTTATACCCGGCTTACTAGTCTGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATTTGTATACCTGTAGGGGTGCAATTGACATGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATAAGCCATCGCGCTCGTCACTTCTTTCACAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCTTGGGACGTTAAACCGTCCCTTGCGGATTGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCAACTGCCTTCTCTGCCATCGTGGGGAGCTGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCCTAAGCGTCTGTCATGCACAATTGCGAGGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATTTCTGCTTGGGCACTATCGCCTCCCCCTGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCAACTACCCCTAGGTGCTTGGTGTGCTGCCGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATGGTATTGAGCCAGCATTCACGTTCATCTTCGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCACCTCAACCCATGATTGAAATTTAGATAGGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAATCTACCGTTGAACCATACACCATTGAGCCGAGTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT

>CP025831|2|2|2536821-2538240|CRISPRCasFinder
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TACAAAATCTCCGTAGGGTCTGCGTCATCC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTGACCGCCGAGGTAAAGTACTGTATGTCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	ACAGGGACTGGCCGCATGTCGATTGCACCG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CATACCGGATTGTTTCTGCATAAAACACCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTGACGATATTTTTAGGGGTACGGGTGACG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AGCATAGCATCGAGGAAAACAATGCCGATA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AAAAATAAAATTCTCAAAAGGTGTGATCTT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GAAATAAAACAATGAGCATTTACGACGACC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAATCGATTATACCCCCGCAACGCACCTCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	ATGACGCACAGGCCCCAGAATCATGGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAAGGGGGTTATACCCGGCTTACTAGTCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTGTATACCTGTAGGGGTGCAATTGACATG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AAGCCATCGCGCTCGTCACTTCTTTCACA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTTGGGACGTTAAACCGTCCCTTGCGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTGCCTTCTCTGCCATCGTGGGGAGCT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CCTAAGCGTCTGTCATGCACAATTGCGAGG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTCTGCTTGGGCACTATCGCCTCCCCCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTACCCCTAGGTGCTTGGTGTGCTGCC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GGTATTGAGCCAGCATTCACGTTCATCTTC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CACCTCAACCCATGATTGAAATTTAGATAG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTACCGTTGAACCATACACCATTGAGCCGA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT

>CP025831|2|1|2536821-2538240|CRT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TACAAAATCTCCGTAGGGTCTGCGTCATCC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTGACCGCCGAGGTAAAGTACTGTATGTCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	ACAGGGACTGGCCGCATGTCGATTGCACCG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CATACCGGATTGTTTCTGCATAAAACACCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTGACGATATTTTTAGGGGTACGGGTGACG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AGCATAGCATCGAGGAAAACAATGCCGATA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AAAAATAAAATTCTCAAAAGGTGTGATCTT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GAAATAAAACAATGAGCATTTACGACGACC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAATCGATTATACCCCCGCAACGCACCTCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	ATGACGCACAGGCCCCAGAATCATGGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAAGGGGGTTATACCCGGCTTACTAGTCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTGTATACCTGTAGGGGTGCAATTGACATG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AAGCCATCGCGCTCGTCACTTCTTTCACA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTTGGGACGTTAAACCGTCCCTTGCGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTGCCTTCTCTGCCATCGTGGGGAGCT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CCTAAGCGTCTGTCATGCACAATTGCGAGG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTCTGCTTGGGCACTATCGCCTCCCCCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTACCCCTAGGTGCTTGGTGTGCTGCC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GGTATTGAGCCAGCATTCACGTTCATCTTC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CACCTCAACCCATGATTGAAATTTAGATAG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTACCGTTGAACCATACACCATTGAGCCGA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT

>CP025831|2|1|2537283-2538240|PILER-CR
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GAAATAAAACAATGAGCATTTACGACGACC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAATCGATTATACCCCCGCAACGCACCTCA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	ATGACGCACAGGCCCCAGAATCATGGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAAGGGGGTTATACCCGGCTTACTAGTCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTGTATACCTGTAGGGGTGCAATTGACATG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	AAGCCATCGCGCTCGTCACTTCTTTCACA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTTGGGACGTTAAACCGTCCCTTGCGGATT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTGCCTTCTCTGCCATCGTGGGGAGCT
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CCTAAGCGTCTGTCATGCACAATTGCGAGG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	TTCTGCTTGGGCACTATCGCCTCCCCCTG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CAACTACCCCTAGGTGCTTGGTGTGCTGCC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	GGTATTGAGCCAGCATTCACGTTCATCTTC
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CACCTCAACCCATGATTGAAATTTAGATAG
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT	CTACCGTTGAACCATACACCATTGAGCCGA
GTTTTGCCTTGAATCCAAAATAAGGCACAGTACAAT

Protein	Signature genes	Signature genes Name	Protein_function
CP025831.1\|QAA55999.1\|2539545_2542863_-\|hypothetical-protein	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|379160
CP025831.1\|QAA56000.1\|2545002_2546289_+\|O-acetylhomoserine-aminocarboxypropyltransferase/cysteine-synthase	unknown	unknown	gnl\|CDD\|225428
CP025831.1\|QAA55991.1\|2526870_2528910_-\|PRTRC-system-protein-C	unknown	unknown	gnl\|CDD\|379166
CP025831.1\|QAA56337.1\|2544427_2544868_+\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|273242
CP025831.1\|QAA55998.1\|2538599_2539535_-\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
CP025831.1\|QAA55994.1\|2531758_2532355_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377540
CP025831.1\|QAA55988.1\|2521754_2524274_-\|phenylalanine--tRNA-ligase-subunit-beta	unknown	unknown	gnl\|CDD\|234804
CP025831.1\|QAA56003.1\|2548719_2549019_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224608
CP025831.1\|QAA56001.1\|2546325_2547255_+\|cysteine-synthase-A	unknown	unknown	gnl\|CDD\|273463
CP025831.1\|QAA55996.1\|2535678_2536749_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|271177
CP025831.1\|QAA56335.1\|2532402_2534070_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223861
CP025831.1\|QAA56336.1\|2543228_2544335_+\|alanine-racemase	unknown	unknown	gnl\|CDD\|143481
CP025831.1\|QAA56002.1\|2547273_2547888_+\|thiamine-phosphate-synthase	unknown	unknown	gnl\|CDD\|234590
CP025831.1\|QAA55989.1\|2524294_2525320_-\|phenylalanine--tRNA-ligase-subunit-alpha	unknown	unknown	gnl\|CDD\|234780
CP025831.1\|QAA56338.1\|2547935_2548751_+\|hydroxyethylthiazole-kinase	unknown	unknown	gnl\|CDD\|236477
CP025831.1\|QAA55995.1\|2534915_2535485_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|200464
CP025831.1\|QAA55993.1\|2530843_2531671_+\|Ion-channel	unknown	unknown	gnl\|CDD\|369572
CP025831.1\|QAA55992.1\|2528918_2530760_+\|molecular-chaperone-HtpG	unknown	unknown	gnl\|CDD\|235366
CP025831.1\|QAA55997.1\|2538300_2538612_-\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
CP025831.1\|QAA55990.1\|2525486_2526671_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225365

Protein	Function_ID	Function_description	E-value
CP025831.1\|QAA55999.1\|2539545_2542863_-\|hypothetical-protein	gnl\|CDD\|379160	pfam13395, HNH_4, HNH endonuclease. This HNH nuclease domain is found in CRISPR-related proteins.	1.01248e-14
CP025831.1\|QAA56000.1\|2545002_2546289_+\|O-acetylhomoserine-aminocarboxypropyltransferase/cysteine-synthase	gnl\|CDD\|225428	COG2873, MET17, O-acetylhomoserine sulfhydrylase [Amino acid transport and metabolism].	0
CP025831.1\|QAA55991.1\|2526870_2528910_-\|PRTRC-system-protein-C	gnl\|CDD\|379166	pfam13402, Peptidase_M60, Peptidase M60, enhancin and enhancin-like. This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonisation of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.	5.95155e-91
CP025831.1\|QAA56337.1\|2544427_2544868_+\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|273242	TIGR00738, Putative_HTH-type_transcriptional_regulator, Rrf2 family protein. This model represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency. [Unknown function, General].	2.99251e-42
CP025831.1\|QAA55998.1\|2538599_2539535_-\|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.	4.43949e-46
CP025831.1\|QAA55994.1\|2531758_2532355_-\|hypothetical-protein	gnl\|CDD\|377540	pfam05656, DUF805, Protein of unknown function (DUF805). This family consists of several bacterial proteins of unknown function.	8.03024e-20
CP025831.1\|QAA55988.1\|2521754_2524274_-\|phenylalanine--tRNA-ligase-subunit-beta	gnl\|CDD\|234804	PRK00629, pheT, phenylalanyl-tRNA synthetase subunit beta; Reviewed.	0
CP025831.1\|QAA56003.1\|2548719_2549019_+\|hypothetical-protein	gnl\|CDD\|224608	COG1694, MazG, Predicted pyrophosphatase [General function prediction only].	0.00270034
CP025831.1\|QAA56001.1\|2546325_2547255_+\|cysteine-synthase-A	gnl\|CDD\|273463	TIGR01136, Cysteine_synthase, cysteine synthase. This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family].	1.10008e-168
CP025831.1\|QAA55996.1\|2535678_2536749_+\|hypothetical-protein	gnl\|CDD\|271177	cd00796, INT_Rci_Hp1_C, Shufflon-specific DNA recombinase Rci and Bacteriophage Hp1_like integrase, C-terminal catalytic domain. Rci protein is a tyrosine recombinase specifically involved in Shufflon type of DNA rearrangement in bacteria. The shufflon of plasmid R64 consists of four invertible DNA segments which are separated and flanked by seven 19-bp repeat sequences. RCI recombinase facilitates the site-specific recombination between any inverted repeats results in an inversion of the DNA segment(s) either independently or in groups. HP1 integrase promotes site-specific recombination of the HP1 genome into that of Haemophilus influenza. Bacteriophage Hp1_like integrases are tyrosine based site specific recombinases. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	1.3378e-17
CP025831.1\|QAA56335.1\|2532402_2534070_-\|hypothetical-protein	gnl\|CDD\|223861	COG0790, COG0790, FOG: TPR repeat, SEL1 subfamily [General function prediction only].	2.21326e-45
CP025831.1\|QAA56336.1\|2543228_2544335_+\|alanine-racemase	gnl\|CDD\|143481	cd00430, PLPDE_III_AR, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase. This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.	4.38151e-157
CP025831.1\|QAA56002.1\|2547273_2547888_+\|thiamine-phosphate-synthase	gnl\|CDD\|234590	PRK00043, thiE, thiamine phosphate synthase.	3.31757e-79
CP025831.1\|QAA55989.1\|2524294_2525320_-\|phenylalanine--tRNA-ligase-subunit-alpha	gnl\|CDD\|234780	PRK00488, pheS, phenylalanyl-tRNA synthetase subunit alpha; Validated.	0
CP025831.1\|QAA56338.1\|2547935_2548751_+\|hydroxyethylthiazole-kinase	gnl\|CDD\|236477	PRK09355, PRK09355, hydroxyethylthiazole kinase; Validated.	2.31939e-101
CP025831.1\|QAA55995.1\|2534915_2535485_-\|hypothetical-protein	gnl\|CDD\|200464	cd11325, AmyAc_GTHase, Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase.	0.00765364
CP025831.1\|QAA55993.1\|2530843_2531671_+\|Ion-channel	gnl\|CDD\|369572	pfam07885, Ion_trans_2, Ion channel. This family includes the two membrane helix type ion channels found in bacteria.	6.71223e-13
CP025831.1\|QAA55992.1\|2528918_2530760_+\|molecular-chaperone-HtpG	gnl\|CDD\|235366	PRK05218, PRK05218, heat shock protein 90; Provisional.	0
CP025831.1\|QAA55997.1\|2538300_2538612_-\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	9.33042e-28
CP025831.1\|QAA55990.1\|2525486_2526671_-\|hypothetical-protein	gnl\|CDD\|225365	COG2807, CynX, Cyanate permease [Inorganic ion transport and metabolism].	1.72535e-69

>CP025831.1|QAA55996.1|2535678_2536749_+|hypothetical-protein
MNIPTSSFPTDTDQTGILLIRSLGIPPMDAFLLLKDLLDTSRGRGDRITRAKRCIRLGGEALADRETSVPFSQAVRASLEARKHRRPRTLQEIRYMAARMMKKCPELARKQVRSITPEDCGRYLRKSFSTPRQRHKGRLILSGILNFSLKRGWCRRNAAFLVPPPILREKRIRALSLYEAKRLLHTAEQLFHGACLPACALMLYAGIRPHEVKRLTWKNINLKSGLVSLAPSHTKTGGSRHVSILPVLGAILSRTSSAGSPSRPVCPPNWEKKWMEVRRRSGILKKSGWVQDVLRHTYASYHLAHFCNQNLLQKEMGHSSPSLLLARYLNMDGITSATGAMFWTHSFVSPVPLKKD
>CP025831.1|QAA55995.1|2534915_2535485_-|hypothetical-protein
MNVSISLLIIFGTVFLVGEHVLARTLETGRAGGYYTHSGKGDRSARARFERFKSRKTPTTRTSITPISVSDQYGNRYRGDLITSTYDPSAKARAGAAAWDKRQSAKAKTIINQAEHEAQSKIAREEEAQVFRASLSRLQEAVKQGKVDKVLADKMVKVLSLRVKQGIMNRREAAGAIDYLILNNKINIK
>CP025831.1|QAA56335.1|2532402_2534070_-|hypothetical-protein
MLGDCYFWGEGIREDKREAVKWYLLAAGQGDAEAQRILGDCYSWGEGIREDKSEAVKWYRLAAEQGDAEAQRILVECYKRQGDCYFLGEGIREDKREAVKWYRLAAEQGDAEAQRILGDCYFWGEGIREDKQEAVKWYLLAAEQGDAEAQRILGACYYFGTGIREDKQEAVKWYRLAAEQKNSEARWRLGDCYFWGEGIREDKREAVKWYRLAAEQKNSEARWRLGSCYYFGTGIREDKQEAVKWYRLAAEQKNAEAQYSLGRCYYFGTGIREDKQEAVKWYRLAAEQGNAEAQWRLGDCYFWGEGIREDKQEAVKWYRLAAEQGNAKALKELGDCYFWGEGIREDKQEAVKWYRLAAEQKNAEAQYSLGRCYYFGTGIREDKQEAVKWYRLAAGQGNAEAQWRLGACYYFGTGIREDKQEAVKWYRLAAEQGNAKAQWILGGCYFGGEGIREDKQEAVKWFRLAAEQEDAEAQWMLGDCYFFGHGVGKNKREAVNWYFLSAKKGNAEAQRRLGACFYFGHGVAKNRQEAIRWYRLAAEQGNSVAISMLKKLGVM
>CP025831.1|QAA55994.1|2531758_2532355_-|hypothetical-protein
MKVMEQSEERLSRINAYNKLVDAAILTKTSSKSVADIVNHELGIECNAANVQEILKSSVSASDMHKIRREIEENASIKMENANGTSFLRKYVSFSGRISRSEYWALKLLILPIMVIILLNRVAMVWDKTGNDSGILVSFVIIFISYIYFNIVADVRRLHDIGESGWLVLLELVPLANIVIAAFLFLKVANQLVINIKT
>CP025831.1|QAA55993.1|2530843_2531671_+|Ion-channel
MNALRHMPRHVLFLRLAYQAGMCLLALVAVTLTAIDLTTEAAEWEVTADRTIYWIFVLDYVIRFSISRSKWLFVKEHPWDLLAIIPFDALFRLFRFASLGEILRLARYLDLFSYAMRFTTRIRRFFNTNGFKYICIAALVIILLGAVGIHLAEGMSLPNGIWWSFVTATTVGYGDTYPVTTSGKFLAVFLMLTGIGFVGTLTSTITSFFLSPHGGEALPYREEEIEAIKKKLDDLSSMTDEDIDTMAALLKTLRDASPAPSAGKEETPAIHSGKN
>CP025831.1|QAA55992.1|2528918_2530760_+|molecular-chaperone-HtpG
MNTETHQFQAEVRQLLDIVINALYSDREIFVRELVSNASDALEKLRLKQLTDSNIYQPDKPLEITVATDKENKTITIADTGIGMTEADLVENLGTIAHSGTKKFMEVLKQKQEGGADLIGQFGVGFYSSFMVADRVEVFTRSYEPEAASLRWSSDGREGYSIETLAEPLDRGTRIVIRLKDEYEEFSQEYRVKELLRRYSNFVGFPLNFNGEHINTVQAIWSKSKSDVKPEEYDEFYQFISHTDEKPLSYMHFSADAPIALNALLFIPRRNPEMFGFGRVDANVSLYCKRVLIDAKPEGLLPEWLRFLNGVVDSEDLPLNISREMLQDNSLVRKISDIITRRFIKHLEKLAKDDQETYREFYAQFSRYLKEGVVTSWPNKESLGKLLRFESTSTEPGETTSFEEYLTRMKEGQTAIYALTGPSRSHLENSPYLEAFKARGYEVAFFTDHGDEFVLDSLSSVDGKPVTMIDRADVELPALEEEQKDALPQEEAAALEEWLKGLYPDKFSKVTLGKRLVSGAAVALQSGNDMGPEMRAYMKAMGQEVPESHPQLELNPSNPLVKKLSALRTENPELAQMVADQIANTALLRAGMLDDPAVLAQSSQALMEQLLLK
>CP025831.1|QAA55991.1|2526870_2528910_-|PRTRC-system-protein-C
MFCERHYTAPVKGDGQFFSLGLSVPCHTKGLFPGHGRGRAFFLETIPETEQYYLTNMIFSPLLKKGVLLLALCGVLGGGVLSAQEAGGAPITEEGLKALDSNVFANEYMLALKPNVTRDRIARIKDPFVRGLATRMAEKKFDRKARALTAEPYEPVKDLAERLRTSQYSKFENPTGIFFEEGEDVLLVMGDPKGEKLNLVIHNFGRDGGHSSYPLKEGVNIIRAKNKGLGYIEYFTPNYKKAPKVHLSILSGKVNGVFVGGVSKNSDWKKMLENSPTEVVDIVGSRVHLVYPVEELKQFCPDKGEELIALYDRIIGMEQQIMGLYKYRMLPKNRMFGRVIWNGFMHADGTGAAFHNGTMKEVGNPDRIPGSAWGIAHEFGHVNQVRPAMKWVSTGEVTNNIYSAYVNYMLNPSSMRLEHERINGGDGNMIGGRFNAYLNNGILKGENWLVQSGPDKRSGGDNRPMVHDHFVKLAPLWQLELYFKVAGKGNPDFYPDIFYKAIKMDTRGKKDGELQLAFMKNACDAARQDLTDFFRKTGMLKPIDQELDDYTCARMTITEADCKNLIAYARKYKKPESPVIYYISVNSAEAYKNRLPVRGVYNQGVTEQGNRRIISHDVWKNAVVFETYKDREMVRITMAGTDSRDNSSTTVPYPEGSTRIEAVSWDGRRTLVYGKRPDK
>CP025831.1|QAA55990.1|2525486_2526671_-|hypothetical-protein
MDKAGTSGGIRGKMLLFAAFLIVCFNLRTGFDSPDPLLGTIERDMGLSLENSGLFALLPVFVLGVAAPISPRVARRMTPWKIIFWFQLLAVAGIFWRSWDGVAGLYGGMVLMGLGMGIAGAAIPGLIKHQFPDRASAMMGVYSAMIGVGSAAASGLSVPLSNMLGGWRFGLGIWIIPILLGMLVWGAYFLRHPDGVFQNDPAASGRSLLRSGKAWQVTVFYLSRVGAAYFFYTWIPIFLRQRGMSYEDAGFILSVAMFAQLPATLSAHVLEKAMGGRGLLIVMAMALAALSCWGILYLPLDWAVWMAILFGLATGTVFSRGMALMVERARTPSESIRLSGMSQGIGFTMGALLSLLFTSFLHQGGSFLPFCLVYTLFCVLGMVSGRMSARPGYV
>CP025831.1|QAA55989.1|2524294_2525320_-|phenylalanine--tRNA-ligase-subunit-alpha
MKEEIVRIQRDALARIAQASDRRGVEDARVAILGKKGELTLAQTGMKDVPREEKPAVGQLLNEARKAITEALDAKLEEVQAQADKAAVAGVDLTLPARSLPSGGLHPLTIVRDEAVRILRHMGFALADGPEIEDEFHCFDALNTPEDHPARNEKDTFYFDSGKLLRTHTSSVQIRSMEKQLPPVRVIAPGSAYRRDEIDATHLSAFNQLEGLYVDTDVSVGDLKGTLEYFLRALFGSGTEVRFRPHFFPFTEPSFEIDVKLKVDGQAPRWVEIAGCGMVDPNVFEAVDRELGLDPRSQARYTGLTGFAFGIGLDRLAMIRWGIRDIRALIENDVRFLAQFQ
>CP025831.1|QAA55988.1|2521754_2524274_-|phenylalanine--tRNA-ligase-subunit-beta
MKISLNWLSQYIDLSGLSVDEMSDMLTFAGIEVEDIRQQGVDSPYVVVARVAAAEQHPQADRLKVCQVDVGDGTLHQIVCGAQNYKVGDKVPCALPGAVLPGNFEIKVGKLRGVESRGMLCSASELGLPDKEHGLWILPQELEPGTPISQVVKADTLVEVEVTPNRPDLLSHNGMAYELAAISGREYRPVPIDDAGVELEPAGDFVRLDQPELNPYYTAVKISGVNVQESPEWLKERLVAVGLRPINNIVDITNFVLHELGTPLHAFDAAKVQGGIVTRTAYEGETFKALDGQEYTLNCTDLVVADQSGKALAIGGVMGGEESGVTDATTDIILESAWFKPSSVRATSRRLALSSDSSYRFERGTSAWNVLRGSVRAVELILQLAGGTASPTYVAGSPVPNPAHASMPSCGGADSPVSVPASLKQGKGSTVTNELGFVKLPWKSLDQISGGSISHEEGARILTALGLKQVPESPECWLIPPHRLDLTRPCDLLEEIVRVFGLDGIPSRFSGPFVAESPVDAAYNFQMELRRKLAALGFYETQTIKLIASESADGAIAQVKDALPLRPLQDGDLIRVSLPLSEDHSVLRPAHTPGLIAAAVRNSNQGVSGLRFFELGRVFRNTGGGKGRDIETDTLGILVSGDRTARSWADPRPEQASFEDLLAVMAVLAPGHRFTLTPARPREQAALGADVQLDGKACGYFARLSLARCRELGLGQPVYVAELDLRKMQEILTAPVKAAELPQFPGSSRDAAMELPLSTPNADIVKAVESAREKLLVSYSCFDVFTDPSGEKLPADRKSIAYTFLYRDPAKTLTAAEVDAAHQRVLKALTDKVKGLSFR
>CP025831.1|QAA55997.1|2538300_2538612_-|CRISPR-associated-endonuclease-Cas2
MGWLVVFFDLPTTTPEDKKNYQYFRKALLEDGYTMIQYSVYARACVTQERMATHSRRIQKMIPPDGSVRCLFVTNIQWDKMFVFHGRSCPRQEVSLPQQMLLW
>CP025831.1|QAA55998.1|2538599_2539535_-|type-II-CRISPR-associated-endonuclease-Cas1
MSYHILSIDAYTCHLSCDKGQLRCADGENSPRTIPLEDVGAVVLSSFKATLTSNLLIELARKRIGFVLCESYRPAVLLLPADRSTDTGLLRHLADMPARLRNRLWQKTLDAKCGNQTALAQAWNPHHPAIAELKRMAVTEKTAREAECARLFWSVFADTWANSDFRRGRHEEGFNNLFNYAYAILLSCILQYLFALGLDPCFGIFHQSREHAAPLAYDLMEPFRPAFDANVARWIHLCLREGKTEERAGEITREFRQHITATLQASVMYRDKQLPLKAAVEAVCRSFRKAVLAGQSGPYEPWLMTTIKWAG
>CP025831.1|QAA55999.1|2539545_2542863_-|hypothetical-protein
MSRSLTFSFDIGYASIGWAVIASVSHDDADPSVCGCGTVLFPKDDCQAFKRREYRRLRRNIRSRRVRIERIGRLLVQAQIITPEMKETSGHPAPFYLASEALKGHRTLAPIELWHVLRWYAHNRGYDNNASWSNSLSEDGGNGEDTERVKHAQDLMDKHGTATMAETICRELKLEEGKADAPMEVSTPAYKNLNTAFPRLIVEKEVRRILELSAPLIPGLTAEIIELIAQHHPLTTEQRGVLLQYGIKLARRYRGSLLFGQLIPRFDNRIISCCPVTWAQVYEAELKKGNSEQSARERAEKLSKVPTANCPEFYEYRMARILCNIRADGEPLSAEIRRELMNQARQEGKLTKASLEKAISSRLGKETETNVSNYFTLHPDSEEALYLNPAVEVLQRSGIGQILSPSVYRIAANRLRRGKSVTPNYLLNLLKSRGESGEALEKKIEKESKKKAKKKEADYADTPLKPKYATGRAPYARTVLKKVVEEILDGEDPTRPARGEAHPDGELKAHDGCLYCLLDTDSSVNQYQKERRLDTMTNNHLVRHRMLILDRLLKDLIQDFADGQKDRISRICVEVGKELTTFSAMDSKKIQRELTLRQKSHTDAVNRLKRDLPGKALSANLIRKCRIAMDMNWACPFTGATYGTHELENLELEHIVPHSFRQSNALSSLVLTWPGVNRMKGQRTGYDFVEQEQENPVPDKPNLHICSLNNYRELVEKLDDKKGHEDDRRRKKKRKALLMVRGLSHKHQSQNHEAMKEIGMTEGMMTQSSHLMKLACKSIKTSLPDAHIDMIPGAVTAEVRKAWDVFGVFKELCPEAADPDSGKILKENLRSLTHLHHALDACVLGLIPDIIPAHHNGLLRRVLAMRRIPEKLIPQVRPVANQRHYVLNDDGRMMLRDLSASLKENIREQLMEQRVIQHVPADMGGALLKETMQRVLSVDGSGEDAMVSLSKKKDGKKEKNQVKASKLVGVFPEGPSKLKALKAAIEIDGNYGVALDPKPVVIRHIKVFKRIMALKEQNGGKPVRILKKGMLIHLTSSKDPKHAGVWRIESIQDSKGGVKLDLQRAHCAVPKNKTHECNWREVDLISLLKKYQMKRYPTSYTGTPR
>CP025831.1|QAA56336.1|2543228_2544335_+|alanine-racemase
MPATSPPRAWAEIDLGAIRHNLNVVKQAAKGEYYMPVVKAGAYGHGLEQVCRTLDSEGIAFFGVANVGEARRISQAGCRTRPYILGPAFPEEREEIVLNGWRSFISTMEEAEHYNSLARLYGKTLPIHLSVDTGMGRGGFLPDQLEELLSRLGELDSLHPEGLGAHLPCADEDREITLRQIALFERMAARIREKLPLKYCHLANSAASLDYEIPSNNMCRPGLVLYGFSPIDSPWASQLRPAMALFSRLTVVRTLPEGHGISYGGTYVTDHPTRVATVGIGYADGYLRSLAHKGARVMVDGVSCPLLGRVTMDQIIVDVSRAPHAEPGMTAEIMGPHIPVTELAEKAGTISWEIFTGIGPRVPRHYNY
>CP025831.1|QAA56337.1|2544427_2544868_+|Rrf2-family-transcriptional-regulator
MKVSTRGRYALRLMIDLAHHRNEGYVSLKEISARQDITVRYLEQIIAILLKAGFVQSFRGKAGGYRLSRHPREYTTEEILKLTEGSLLPISCTAPHENPCPRAAGCATLPFWRGLQQVIENYLRRVTLEDLAEQQKEIGCDYGAGI
>CP025831.1|QAA56000.1|2545002_2546289_+|O-acetylhomoserine-aminocarboxypropyltransferase/cysteine-synthase
MSKNHRFETRQIHVGQESPDPATDARAVPIYATTSYVFKDSEQAAARFALAEPGNIYNRLMNPTADVFEQRIASLEGGAAALAVSTGAAAVTYAIQNIARAGDHIVSSSTVYGGTYNLFANTLADAGIETTFVDARDVQNFSRAIRNNTKALYVESLGNPNCDIVDMEALAEVAHAHGIPLIVDSTFATPFLFRPLEHGADIVVHSATKFIGGHGTVMGGVIVDGGKFDWTQNDKFPGISKPNPNYHGAVFAEVCGNLAYIVKIRATLLRDTGATISPFNSFLLLQGLETLSLRVERHVQNALRVADYLSSHPQVEKVNHPSLPDHPDHDLYKRYYPNGGGSIFTFEIKGGAEKARKFCESLELFSLLANVADVKSLVIHPASTTHSQMTEEELKAGGITPSTVRLSIGTEHIDDILEDLEQGFRAIL
>CP025831.1|QAA56001.1|2546325_2547255_+|cysteine-synthase-A
MKIYKNITELIGGTPLLELTNYERRNGLNATILAKLEYLNPAGSVKDRIAQAMIDAAEAAGKLKPDSVIIEPTSGNTGIGLAAVAASRGYRIILTMPETMSVERRNLLKAYGAELVLTDGALGMKGAIAKAEELAAGLPNSFIPGQFANPANPEAHFRTTGPEIWNDTEGKADIFVAGVGTGGTITGVGKYLKSRNPGIRVVAVEPFSSPVLTQGMAGPHKIQGIGAGFVPETLDTSVYDEVITVTNEDAFSTGKELARTDGVLTGISSGAALWAATQVARRPENEGKTIVVLLPDTGDRYLSTPLFTD
>CP025831.1|QAA56002.1|2547273_2547888_+|thiamine-phosphate-synthase
MKKFNLHLYLVTDEASKCRYSLLETVRKAADGGVTMVQYRSTNPDAGTCYREALPIRDFLASRGIPFIVNNRIDLALALEADGVHIGQRDLPVPSVRAMIGPDKILGLSVSNKEQLRAVDASLVDYLGMGPVFPTISKLNAPPVLSVEGFAALASQSPLPVVAIGGLDAERARQVRATGTASGIAVVSAICGAENPEAAARALA
>CP025831.1|QAA56338.1|2547935_2548751_+|hydroxyethylthiazole-kinase
MLSPTDLVQAVAADLEKIRETAPLVLSLTNSVVQPLTANLLLAIGAVPAMLNDAEEAADMLRSGTGALLVNLGTVTREQGAAMQTAVREANRLNIPWVLDPVAVGALSLRTRLAGQLKEQSPRIIRGNASEIMALAGYSSVTKGPESTSSSADALHAARELALHTGAAVLVTGRTDYSTDGRQVTATENGHAMMSRVTGVGCSMGALSAACAAVSPTPLQAAVSTAVLMGIAGEMAFEQSPAPGSFAVSLLDSLYSLSPEDVVRRARFLSL
>CP025831.1|QAA56003.1|2548719_2549019_+|hypothetical-protein
MSVERAFFPFNRLPPPWKVTPHSYGLILPAPEEAGASAEAIREKAPLENLRHAFRRYAHGAGNSIPGTCRIPPQPFAYPDRRALGLQADLVLRNTCGSL

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Crispr_ID: CP025831_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP025831_3

2613315-2613879

Orphan

Consensus_repeat	Method
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	CRISPRCasFinder
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	CRT
GTTTCAATCCACGCACTCCT	PILER-CR

8 spacers

The CRISPR arrays of CP025831_3

>merge|CP025831|3|2613315-2613879|CRISPRCasFinder,CRT,PILER-CR
TTCAATCCACGCGCACTCCTTGCGGAGTGCGACGCCAACGTGGGGAAAATTCCCCGCGCGTCCTGGTTTCAATCCACGCACTCCTTGCGGAGTGCGACTACCTACCACCTTAACCAGCGCGGCTATGATCCGGTTTCAATCCACGCACTCCTTGCGGAGTGCGACCGGGAACCTGATTCATGCCTTGAAAATCCAAAGTGTTTCAATCCACGCACTCCTTGCGGAGTGCGACTAGGTGGTATCTCCTTCGGCACCCCGGACAACCGGTTTCAATCCACGCACTCCTTGCGGAGTGCGACATCGGCATTGTCCCTTCCGTATTCTCCGTAGGAAGTTTCAATCCACGCACTCCTTGCGGAGTGCGACTTTTTCTGTGTCATGACATGTCGACCTTTACATGTTTCAATCCACGCACTCCTTGCGGAGTGCGACTGTAAAAAAACAGCAAGGGCGCGTCAATTTTCAAAGTTTCAATCCACGCACTCGTGAGAGTGCGACCGTACAAGGGCTTTACCTACATCGTGGACAACATGTTTCAATCCACGCACTCGTGAGAGTGCGACTC

>CP025831|3|3|2613315-2613746|CRISPRCasFinder
TTCAATCCACGCGCACTCCTTGCGGAGTGCGAC	GCCAACGTGGGGAAAATTCCCCGCGCGTCCTG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TACCTACCACCTTAACCAGCGCGGCTATGATCCG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	CGGGAACCTGATTCATGCCTTGAAAATCCAAAGT
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TAGGTGGTATCTCCTTCGGCACCCCGGACAACCG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	ATCGGCATTGTCCCTTCCGTATTCTCCGTAGGAA
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TTTTTCTGTGTCATGACATGTCGACCTTTACAT
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC

>CP025831|3|2|2613315-2613879|CRT
TTCAATCCACGCGCACTCCTTGCGGAGTGCGAC	GCCAACGTGGGGAAAATTCCCCGCGCGTCCTG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TACCTACCACCTTAACCAGCGCGGCTATGATCCG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	CGGGAACCTGATTCATGCCTTGAAAATCCAAAGT
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TAGGTGGTATCTCCTTCGGCACCCCGGACAACCG
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	ATCGGCATTGTCCCTTCCGTATTCTCCGTAGGAA
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TTTTTCTGTGTCATGACATGTCGACCTTTACAT
GTTTCAATCCACGCACTCCTTGCGGAGTGCGAC	TGTAAAAAAACAGCAAGGGCGCGTCAATTTTCAAA
GTTTCAATCCACGCACTCGTGAGAGTGCGACCG	TACAAGGGCTTTACCTACATCGTGGACAACAT
GTTTCAATCCACGCACTCGTGAGAGTGCGACTC

>CP025831|3|2|2613380-2613866|PILER-CR
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACTACCTACCACCTTAACCAGCGCGGCTATGATCCG
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACCGGGAACCTGATTCATGCCTTGAAAATCCAAAGT
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACTAGGTGGTATCTCCTTCGGCACCCCGGACAACCG
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACATCGGCATTGTCCCTTCCGTATTCTCCGTAGGAA
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACTTTTTCTGTGTCATGACATGTCGACCTTTACAT
GTTTCAATCCACGCACTCCT	TGCGGAGTGCGACTGTAAAAAAACAGCAAGGGCGCGTCAATTTTCAAA
GTTTCAATCCACGCACTCGT	GAGAGTGCGACCGTACAAGGGCTTTACCTACATCGTGGACAACAT
GTTTCAATCCACGCACTCGT

Protein	Signature genes	Signature genes Name	Protein_function
CP025831.1\|QAA56061.1\|2620630_2621080_-\|KH-domain-containing-protein	unknown	unknown	gnl\|CDD\|224760
CP025831.1\|QAA56051.1\|2607308_2607812_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379034
CP025831.1\|QAA56066.1\|2627098_2627674_-\|rubrerythrin-family-protein	unknown	unknown	gnl\|CDD\|153100
CP025831.1\|QAA56342.1\|2614275_2615430_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376607
CP025831.1\|QAA56059.1\|2615895_2619477_-\|proline-dehydrogenase	unknown	unknown	gnl\|CDD\|143443
CP025831.1\|QAA56057.1\|2612470_2612770_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367747
CP025831.1\|QAA56063.1\|2621604_2623860_+\|catalase-HPII	unknown	unknown	gnl\|CDD\|236886
CP025831.1\|QAA56054.1\|2609632_2611267_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378829
CP025831.1\|QAA56055.1\|2611275_2611491_-\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56056.1\|2611805_2612426_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|222807
CP025831.1\|QAA56067.1\|2627976_2628573_+\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
CP025831.1\|QAA56065.1\|2624356_2627056_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274447
CP025831.1\|QAA56052.1\|2608480_2609362_-\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56053.1\|2609354_2609636_-\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56058.1\|2612766_2613030_+\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56062.1\|2621200_2621470_+\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56060.1\|2619635_2620631_-\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56064.1\|2624160_2624364_+\|hypothetical-protein	unknown	unknown	unknown
CP025831.1\|QAA56049.1\|2606157_2606502_-\|rubrerythrin	unknown	unknown	gnl\|CDD\|275328
CP025831.1\|QAA56050.1\|2606783_2607128_-\|rubrerythrin	unknown	unknown	gnl\|CDD\|275328

Protein	Function_ID	Function_description	E-value
CP025831.1\|QAA56051.1\|2607308_2607812_-\|hypothetical-protein	gnl\|CDD\|379034	pfam13098, Thioredoxin_2, Thioredoxin-like domain.	1.41074e-13
CP025831.1\|QAA56066.1\|2627098_2627674_-\|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.	9.03876e-56
CP025831.1\|QAA56342.1\|2614275_2615430_-\|hypothetical-protein	gnl\|CDD\|376607	pfam01757, Acyl_transf_3, Acyltransferase family. This family includes a range of acyltransferase enzymes. This domain is found in many as yet uncharacterized C. elegans proteins and it is approximately 300 amino acids long.	5.74895e-18
CP025831.1\|QAA56056.1\|2611805_2612426_+\|hypothetical-protein	gnl\|CDD\|222807	PHA00662, PHA00662, hypothetical protein.	9.5243e-22
CP025831.1\|QAA56049.1\|2606157_2606502_-\|rubrerythrin	gnl\|CDD\|275328	TIGR04535, conserved_hypothetical_protein, ferritin-like protein. Two families of proteins are known to be encoded, with some regularity, next to the gene for encapsulin (pfam04454), with surrounds the target protein to form a prokaryotic proteinaceous organelle. One is the family of enzymes that includes Dyp-type peroxidases. The other is this family, with a resemblance to bacterioferritins. Encapsulin-associated forms of the proteins in these two families have a necessary C-terminal motif that resembles DGSL[SGN]IGSL[KR]. Members of this family that include the last columns of the model in the hit region (and are encoded next to the encapsulin gene) should be designated encapsulin-associated ferritin-like protein.	2.35972e-18
CP025831.1\|QAA56063.1\|2621604_2623860_+\|catalase-HPII	gnl\|CDD\|236886	PRK11249, katE, hydroperoxidase II; Provisional.	0
CP025831.1\|QAA56054.1\|2609632_2611267_-\|hypothetical-protein	gnl\|CDD\|378829	pfam12236, Head-tail_con, Bacteriophage head to tail connecting protein. This family of head-tail connector proteins is found in bacteria and viruses. Proteins in this family are typically between 516 and 555 amino acids in length. This protein is found in Phage T7 and T3 among others.	1.25267e-153
CP025831.1\|QAA56067.1\|2627976_2628573_+\|N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	9.66787e-29
CP025831.1\|QAA56061.1\|2620630_2621080_-\|KH-domain-containing-protein	gnl\|CDD\|224760	COG1847, Jag, Predicted RNA-binding protein [General function prediction only].	4.91528e-30
CP025831.1\|QAA56065.1\|2624356_2627056_-\|hypothetical-protein	gnl\|CDD\|274447	TIGR03144, cytochrome_c_biogenesis_protein_chloroplast, cytochrome c-type biogenesis protein CcsB. Members of this protein family represent one of two essential proteins of system II for c-type cytochrome biogenesis. Additional proteins tend to be part of the system but can be replaced by chemical reductants such as dithiothreitol. This protein is designated CcsB in Bordetella pertussis and some other bacteria, resC in Bacillus (where there is additional N-terminal sequence), and CcsA in chloroplast. We use the CcsB designation here. Member sequences show regions of strong sequence conservation and variable-length, poorly conserved regions in between; sparsely filled columns were removed from the seed alignment prior to model construction. [Energy metabolism, Electron transport, Protein fate, Protein modification and repair].	1.09816e-35
CP025831.1\|QAA56057.1\|2612470_2612770_+\|hypothetical-protein	gnl\|CDD\|367747	pfam03965, Penicillinase_R, Penicillinase repressor. The penicillinase repressor negatively regulates expression of the penicillinase gene. The N-terminal region of this protein is involved in operator recognition, while the C-terminal is responsible for dimerization of the protein.	3.60688e-05
CP025831.1\|QAA56059.1\|2615895_2619477_-\|proline-dehydrogenase	gnl\|CDD\|143443	cd07125, ALDH_PutA-P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA. The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.	0
CP025831.1\|QAA56050.1\|2606783_2607128_-\|rubrerythrin	gnl\|CDD\|275328	TIGR04535, conserved_hypothetical_protein, ferritin-like protein. Two families of proteins are known to be encoded, with some regularity, next to the gene for encapsulin (pfam04454), with surrounds the target protein to form a prokaryotic proteinaceous organelle. One is the family of enzymes that includes Dyp-type peroxidases. The other is this family, with a resemblance to bacterioferritins. Encapsulin-associated forms of the proteins in these two families have a necessary C-terminal motif that resembles DGSL[SGN]IGSL[KR]. Members of this family that include the last columns of the model in the hit region (and are encoded next to the encapsulin gene) should be designated encapsulin-associated ferritin-like protein.	5.35331e-17

>CP025831.1|QAA56058.1|2612766_2613030_+|hypothetical-protein
MNNPLLSTEEKRRWLARVFRDEDGEYSQADKFKALVEDTKLAALQQEEEEFKRQREIGAAPQDPILALLQAIPPAELNLHQHPLSEK
>CP025831.1|QAA56057.1|2612470_2612770_+|hypothetical-protein
MLMKALDFIQIFASNVRRLDFRLSSAQVILAVIAGYRRHSTITEATRLHPNTVTNILQDLIAQGYVNRIGDSRPYVYRPTADGEQLAGNLLDKNTFPGT
>CP025831.1|QAA56056.1|2611805_2612426_+|hypothetical-protein
MINESLLQPDTPSALDICNAALSKIGEAPLDALIANESTASRLCVLHYHPARRETLCMARWTFAATQTTLDSVSAQAPNSLTPYQFTLPADCLRVLDVECSEWKMQGRRIHASCAPLPLSYIADIENADQFDPLFMDALATRLAEKLAMPLTGNQSLRQNLNQEFHKIILPQAATVNAVQCFSNDSHPLLDLLRKIKSPSCPEECE
>CP025831.1|QAA56055.1|2611275_2611491_-|hypothetical-protein
MGFMKPSTPSASAPEQTIPVKAESVEQEVGEDYQARERQRQGMISTILARRHSSAGQGEVNPRTLLRKTLG
>CP025831.1|QAA56054.1|2609632_2611267_-|hypothetical-protein
MEERVAELNSVYKSLAAQRAPWETWWDRLRDYVLPRRLNREGEVSLPNRDAMDRMTDTTAVEACQKLASGHMSYITPSHDVWFKWSAPDDRGGDEAEAWYNQCSEIALKELSVSNFYTEIHECFLDRVALGTGSLFTGTSSDGRLLFTNIPCGQFACAENAEGRVDTYVREFAYTAHQARSMFGVKALGPKAREVLERGGNPYATTLRFLHVVRPRTRRSRRREQASHMPFESVYLSLDDQVIVEEGGYMEFPYLVTRFLKWGSGPYGLAPGRLVFPAIQQVQFLNRILDTLGEVAAFPRILELANQIGEVDLRAGGRTVITPEAASLHLPREWATQGRYDVGMDRLAQKQDAIRRAYYLPMLELWSGHRGNMTATEVMARENERVLMFSPSFTLFVSDLYSTMTRIFSLLFRMGKFPRPPRAALREGRDGSVAVGEPRVVYQSKIALVLRRLQSEGMDRSLQRLNMMIQAAPDLADHVDWDHCFRLSARVDGAPESMLRPWADVRAMRKERADLRQGASLAPAEEDPYASLNPLLDQLTAIQK
>CP025831.1|QAA56053.1|2609354_2609636_-|hypothetical-protein
MNQDTTLQQEASVREARFKRRQLLRVFDTPDGREALTFLEARFQTDLPVFQGSPGNYDPLDAMRRDAYREIFLYIRRQLQLAIKETTEEEKND
>CP025831.1|QAA56052.1|2608480_2609362_-|hypothetical-protein
MIDSIDNSMAAPIRDAEGSGAVSPETDALSETAVQTEPFPPLLGEDGGFAPDWYARFDELKGMEKSLSKFKTPEALAKSYAELERLRRYPGVENEEQMARFRRLAGLPESEEEYRLERPESTPESEWNAGLAERMARTAYRYGVPPEAMNALQETMAQAYNEAREHMEDARMEMEMQAEQSLQQEWGANYERNMGRAVAVLRRLTSETGVDADALLDNPGLGSNPDAIRLLYQASRLLDEAPLHHTGNAAPSPAEEAMRMESDPSHPLYEAYMNVNHPNHKYANELYDRLTTR
>CP025831.1|QAA56051.1|2607308_2607812_-|hypothetical-protein
MMNRHFIFALCTVLGFSVSGISMAQSVPTDKEAAAKAAKAAKVKFRWGKSLKSAQKQAAETGLPIVLLFTGTSWCGFCVKLEKEILSKKDFKQGMDGVAIGVKFEFGSSDFSKSKEAKTYNITGVPAMVVVDADGKELGRTGYVPGRTPAQYVEFFKKYAPKTAEGK
>CP025831.1|QAA56050.1|2606783_2607128_-|rubrerythrin
MPEFTNAFSGLKEDRKLTHDELVRAIRFMIAAEYESIQLYTQLAASIDDKLAQEVLWDISNEEKEHAGEFFRLLQVLAPDEQGFYDEGMGETNEKIDKLKASCPDGACSSSAAH
>CP025831.1|QAA56049.1|2606157_2606502_-|rubrerythrin
MPEFTNAFSGLKENRKLTHDELVRAIRFMIAAEYEAIQLYTQLAESIDHKLAQEVLLDISNEEKEHAGEFLRLLQVLAPDEQGFYDEGMGETNEKIDKLKASCPDGACSSSAAH
>CP025831.1|QAA56342.1|2614275_2615430_-|hypothetical-protein
MNTNQSLNSRGSHIAWVDFLRILACFLVVLAHCCDPFVGSFDGSFNFKSAVFWGSLVRPCVPLFAMISGVLLFPVTLEMGAFYSRRLKRVVVPLIVWSLALPLLYFGYFAAGVQTASPNIVMDTYTWSATVGKLYTFFFNFNYDTTPLWYVYMLVGLYLFMPIMSAWLTQARRKDVKIFLGIWIFSMTLPYIQMLAPALGYEGNYGNMGILGVCDWNPYGMFYNFSGFLGYMVLAHYLTKYPLAWSWKKTLSITIPLFLIGFAVTFFGFLETQKHFPGQYSKLEVLWYFSGINVFLMTFAIFTIVSRLRIKAGPVLSKVAALTFGVYLCHFFFVQCSYDFVNFIGLGGLPSAVKIPLMACLASVVSAALVWLLSLNRWTRKSIM
>CP025831.1|QAA56059.1|2615895_2619477_-|proline-dehydrogenase
MTDSSIPDMMAEARRGQWTDQQLAAKAVELAESILKQSNAGMRGKEKRQAQQMERMMNDPAGKAFTLALADRVFRPSSPARGAELFRYLLDGYGVPRYLSAADRFAMKMGGRFSAQFPGVVMPVITSQLRKESSNVILPAEDGKLRPHLRRRRKGGIRMNINQLGEAILGESEAHHRLQQVVDRLTDKDCDYISVKISAIFSQIHLVAFEETVKLIQERLRILYRAAITNAVTLPDGSRKPKFVNLDMEEYRDLHLTAEAFKRTLMEDEFMHLEAGIVLQAYLPDSWEEQMKLCAWAKERVEQGGARIKIRLVKGANLAMEKVEASMHGWAQAPYGTKAQADANYKRMLHYGCMPDNARYVQFGVASHNLFDLCYAMLLREREGVRDQVEFEMLEGMANHQARVIRQAADGLLLYAPVVLKEDFHSAIAYLVRRLDENTSEENFLHDLFGMTPGSRSWEVQKKRFLKACQEKDEVKYGPNRTQNRAADPIQPSHYRDAFANERDTDWSLRQNAEWINGMIAAEKEKSGEEIPLVIDGEEITTNLWGVGRDPSRHNEVSYKFAYADFDQVEHALVTADRARSSWASKSIGERAEILHRAAQELSRIRGEAIAAMVRDAGKAPTEADVEVSEAIDFCRYYAEGLDRDGMNDGVEMSPLGTICVMSPWNFPFAIPTGGVAAALMAGNTVVFKPSELAVYTAWQIVQAFWRAGVPKNVLQFVPMPRNEISRKFLMDPRLNGVIMTGSFRTGKMLRELRPDLHVLAETSGKDAMIITATADPDQAVKDLVKSAFGHSGQKCSAASVAIVEASVYDNPAFLRQLKDAAASLKVGGSWEVNSVVTPLIREPEGNLLRALTQLEPGEEWLLKPEPSEDNPCLWSPGIRLGVKPGSWFHQTECFGPVLGIIRAENLEEAIDIQNDSEFGLTGGLQSLDEREIALWKTKVQVGNAYINRVITGAIVRRQPFGGWNHSSMGPGAKAGGPNYLTMLGSWEEKALPQKLRTPGERISGLVEKLCSELPDCAKRIRSAAGSQAKWWMEEFGVEHDPSRVYGENNTFRYIPVKGILARVENMSDDDVAILLLGAKLCGVLLHLSIGTSRPWIQKMHGYYASLTVETEAELIVRMPEALQGVRFLRGTDISEALANAARARDVEVLDRPVLANGRLELLGYFREQAVSETVHRYGNLIPPPGSFKTDSV
>CP025831.1|QAA56060.1|2619635_2620631_-|hypothetical-protein
MDGSLFMRALAVIAFLALAFPGRAEMDALSVSCSAAPSLPSPVLVVYGSEEPGSAEARWLKALQPGTEERRALDEYVRDVQFVTVPRHPSVKDWEEDGSLSRAAMHGVRMLPSVVFLDSKGRVFDLVEGGSSAASLREKVSLLAEKAQRVRPVTRVNDIPKGGDPAAEASAICRELEQVPPEAWFRDYPGTMKRLEKLNCTVPAFLNAREAALRLEKNRKTAELLGESFRASKASSIRTCLEAWRACADDPSLSVEERQLILLSMVHPLWVRLEEVLYREAHTPESEDAFNQAVAVLEEVRDMNRSSVCGRRAHQLREELRRARLAAARYD
>CP025831.1|QAA56061.1|2620630_2621080_-|KH-domain-containing-protein
MTVQEIAEQSLKSLLASLGFSADIEVTETDGIVCLNISSPDSQYIIGGDGDRLDDLQYLVNRMIQRKMEDAPRVKVDCDHYRERNEARLLEKARSLAERVQESGKPMKMPPLNAYHRRLVHNALQSMEGIVTESEEGDSRYKRITIRKG
>CP025831.1|QAA56062.1|2621200_2621470_+|hypothetical-protein
MKICGSSVPYHVRNTVPALPSGNTVPFLLRNQMQETPLRKEATVFCQPAAVPRLSPLLPAANETWNTDIHSHANQKGISAQPVLYYIKS
>CP025831.1|QAA56063.1|2621604_2623860_+|catalase-HPII
MKKKKPPMEDSAAPFPNGKEAAPHYTDTIDPELIKPTPKPTPPNAEPSAPGSMKMPDNATEKIRELDAMRSNGMGQALTSNLGVKISDDQNTLKAGSRGPSLLEDFHFLEKMAHFDQERIPERVVHARGSGAHGYFQVYKSLSKYTKAAFLQDPGEKTPVFVRFSTVQGFRGSPDTVRDIRGWATKFYTKEGNYDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEMPQGQTAHDSFWDYVSLQPETLHNVMWAMSDRGIPRSFRTMEGFGIHTYKLVNEEGKSTFVRFHWKPLYGKKSLVWDEAQVLTGRDPDFHRKDLWQSIEAGDYPEYELGLQLIPEEDADQFDFDILDATKLIPEALVPVEIVGKMVLNRNPDNFFAETEQVAFCPANIVPGIDFSDDPLLQGRIFSYSDTQRHRLGGANFTEIPINRPICPFHNNQRDGFHRMQIDASPANYDPNSIGNNWPRETPPEKGGFTTSPQTVSGVKERLRSPSFAEYYSHPRLFWMSQTPVEQEHIINAFSFELGKVTRPYIRERVVDLLTRIDPDLASGVARNLGIQLTREQLSRELPRPVCGLEQDPSLSLYAHTDGNLKGLCVSLLAADGVSLKSVKEICEALHEEGIHPQIIAPHMGSVTTEEGEDLPVDGTLSGTPSVLFDSVIVPEGEQSIATLLKDGDAKYHLRQAYRHLKAIGLPGNAKAMLEAASLPQDMDDAGLLMPKDTKSLMLPFITAMKQHRVWSREPKTLDFGA
>CP025831.1|QAA56064.1|2624160_2624364_+|hypothetical-protein
MRWKEYIPGKQARQGENEKKCVLISLFSMTVKSGHHKFQKMERRQTRISCPFPGICFRIISGTCSPT
>CP025831.1|QAA56065.1|2624356_2627056_-|hypothetical-protein
MIVQSALFLDYGRLTLMDRERTDAVWKKYGRSLWNFAGSYGLGIALMLILLVLTFAGTLHQVRLSSAMGSEAAIESFFGAAYVLIPLGGENSLISLPLPGMGITCVLLFANLLIGGVFRIRWTWRHAGVLVAHGGILLLLAGIMLGNKMTVAVEQVELPQGDRVHEYSLPFDLRLNRFVPEFYPGTSKPKSYESQITVFPESGGQYDAVIRMNEPLRLSGWTLYQMSWGQDSLHPGRLISILRASHNPLEQMPKWSSYIIAVGLLWHFACVFGRYLRRKPGLASAGTAATDELQAVSAPGGKKRLRLAGICLLVAAIFGVGMLAARPDVHPVLVEHYVPWSPFLVERAGAMAVQDGGRLKPVSTYAGFHLLRTLGKRSFVVDTPEGKRKLSPVEWMLDCMFRPELAEQYPVFLVNREEVVRRLHLPDQKDKRKKYSYAQLAERWEEMTRAVREIRLLGETNLTEAQKEILSLSRNFDVMRGWMLVSRIMLENPAAMERMEFPRWFPSAGRDGERLWTAAPDKAAGAFLAMASLLERKAIGMEGAEASALRMKAEGLLLEKLAQPNEAASAGERHSLEREIFYYRLDPLYISLAVFVAAFVCLLLCALFRPAANAPLWRRFLRPGGFSLAWLTGAGGTVVLAAALVIRMLITMRSPVGNTYETIAFIACMGVLCALVVELFSKKGIVLAAGLLLGAFSCQMGILYEASQAVDHMDPLVAILRSNFLLSTHVITIVLGYAAGLLAAVLSHIYLLASPLRLIGGKTEQSLDRMAYGILCFSLVFTLVGTVFGGIWGNESWGRFWGWDPKENGALMIVLWQLTVLHARKAGWLSSWLLHFSNVVGGVIIAFAWWGVNMLGVGLHSYGFTSGRDALDMFYWSEAVLCVLFIILHYRALRRVDVR
>CP025831.1|QAA56066.1|2627098_2627674_-|rubrerythrin-family-protein
MKSIKGTETEKNLLKAFAGESEARNRYTYFAGVAKKAGYEQIAAIFLETADNEKEHAKVFFKLLKDACIEVTHAVCTAPLESTEDCLLAAAAGEHDEWSDMYPAFAEVADREGFPAIAETFRKIASVEQHHEARYLKLAENVREGRVFAKEKEIQWKCRNCGYVHTGSTAPKVCPACAHPQAFFEELADNF
>CP025831.1|QAA56067.1|2627976_2628573_+|N-acetyltransferase
MNSANTPLLETERLILRKFTENDLEALFNIYSNEEVNTYLPWFPLTSLEEAASLFKEKYREVYKRPYGYHYAICPKNSNLPAGYIHAGTDDSHDLGYGLLQEFWHRGFATEAARAVVARLKKDGMPYITATHDIRNPRSGGVMKQLGMRYQYSYEELWQPKNIPVTFRLYQLNLDGQEDRVYQEYWNRSSVRFKETDI

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
CP025831_3	3.6\|2613681\|33\|CP025831\|CRISPRCasFinder,CRT	2613681-2613713	33	NZ_AP021899	Akkermansia muciniphila strain JCM 30893 plasmid pJ30893, complete sequence	5370-5402	2	0.939
CP025831_2	2.6\|2537187\|30\|CP025831\|CRISPRCasFinder,CRT	2537187-2537216	30	NC_007491	Rhodococcus erythropolis PR4 plasmid pREL1, complete sequence	495-524	5	0.833
CP025831_2	2.6\|2537187\|30\|CP025831\|CRISPRCasFinder,CRT	2537187-2537216	30	MN850656	Flavobacterium phage fF4, complete genome	12505-12534	6	0.8
CP025831_2	2.6\|2537187\|30\|CP025831\|CRISPRCasFinder,CRT	2537187-2537216	30	NZ_CP030933	Enterococcus gilvus strain CR1 plasmid pCR1A, complete sequence	48712-48741	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP040888	Leclercia adecarboxylata strain Z96-1 plasmid pZ96-1_1, complete sequence	301065-301094	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP010351	Acinetobacter johnsonii XBB1 plasmid pXBB1-9, complete sequence	227148-227177	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP032285	Acinetobacter sp. WCHA55 plasmid pOXA58_010055, complete sequence	241227-241256	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	CP052287	Klebsiella pneumoniae strain E16KP0218 plasmid pE16KP0218-1, complete sequence	23468-23497	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP043309	Acinetobacter johnsonii strain Acsw19 plasmid pAcsw19-2, complete sequence	295068-295097	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP041047	Citrobacter sp. CF971 plasmid pBM527-1, complete sequence	3948-3977	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP035634	Enterobacter cloacae strain EN3600 plasmid unnamed2, complete sequence	105074-105103	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP022359	Shewanella bicestrii strain JAB-1 plasmid pSHE-CTX-M, complete sequence	99762-99791	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP033130	Acinetobacter wuhouensis strain WCHAW010062 plasmid pOXA23_010062, complete sequence	298554-298583	7	0.767
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NC_008573	Shewanella sp. ANA-3 plasmid unnamed1, complete sequence	225094-225123	7	0.767
CP025831_2	2.15\|2537780\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537780-2537809	30	NC_007950	Polaromonas sp. JS666 plasmid 2, complete sequence	56294-56323	7	0.767
CP025831_2	2.17\|2537912\|29\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537912-2537940	29	NZ_CP028348	Novosphingobium sp. THN1 plasmid pTHN, complete sequence	17301-17329	7	0.759
CP025831_2	2.17\|2537912\|29\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537912-2537940	29	MG962366	Rhodococcus phage Finch, complete genome	8867-8895	7	0.759
CP025831_2	2.20\|2538109\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2538109-2538138	30	NZ_CP038867	Vagococcus sp. CF-49 plasmid punnamed2, complete sequence	42051-42080	7	0.767
CP025831_2	2.20\|2538109\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2538109-2538138	30	KY389063	Staphylococcus phage phi575, complete genome	11159-11188	7	0.767
CP025831_2	2.4\|2537055\|30\|CP025831\|CRISPRCasFinder,CRT	2537055-2537084	30	NZ_KX710093	Leclercia adecarboxylata strain pP10164 plasmid pP10164-2, complete sequence	130946-130975	8	0.733
CP025831_2	2.6\|2537187\|30\|CP025831\|CRISPRCasFinder,CRT	2537187-2537216	30	NZ_CP017077	Novosphingobium resinovorum strain SA1 plasmid pSA2, complete sequence	450285-450314	8	0.733
CP025831_2	2.15\|2537780\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537780-2537809	30	NZ_CP049244	Rhizobium pseudoryzae strain DSM 19479 plasmid unnamed3, complete sequence	292959-292988	8	0.733
CP025831_2	2.17\|2537912\|29\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537912-2537940	29	NZ_CP032695	Rhizobium jaguaris strain CCGE525 plasmid pRCCGE525c, complete sequence	561236-561264	8	0.724
CP025831_2	2.17\|2537912\|29\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537912-2537940	29	NZ_CP045296	Paenibacillus cellulositrophicus strain KACC 16577 plasmid unnamed1, complete sequence	562702-562730	8	0.724
CP025831_2	2.21\|2538175\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2538175-2538204	30	MK804891	Aeromonas phage 2_D05, complete genome	8268-8297	8	0.733
CP025831_2	2.21\|2538175\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2538175-2538204	30	MK813942	Aeromonas phage 4_4512, complete genome	36541-36570	8	0.733
CP025831_2	2.21\|2538175\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2538175-2538204	30	MK804892	Aeromonas phage 4_D05, complete genome	8753-8782	8	0.733
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP020951	Rhizobium sp. CIAT894 plasmid pRheCIAT894d, complete sequence	374126-374155	9	0.7
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NC_028926	Bacillus phage Palmer, complete genome	15076-15105	9	0.7
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_CP016542	Planococcus versutus strain L10.15 plasmid pPS15-2, complete sequence	7899-7928	9	0.7
CP025831_2	2.8\|2537319\|30\|CP025831\|CRISPRCasFinder,CRT,PILER-CR	2537319-2537348	30	MT119360	Enterococcus phage nattely, complete genome	57392-57421	9	0.7
CP025831_3	3.13\|2613668\|46\|CP025831\|PILER-CR	2613668-2613713	46	NZ_AP021899	Akkermansia muciniphila strain JCM 30893 plasmid pJ30893, complete sequence	5357-5402	9	0.804
CP025831_2	2.7\|2537253\|30\|CP025831\|CRISPRCasFinder,CRT	2537253-2537282	30	NZ_MH569712	Serratia marcescens strain S120 plasmid pPM120-2, complete sequence	45142-45171	10	0.667
CP025831_3	3.4\|2613547\|34\|CP025831\|CRISPRCasFinder,CRT	2613547-2613580	34	NC_008269	Rhodococcus jostii RHA1 plasmid pRHL1, complete sequence	146066-146099	11	0.676

1. spacer 3.6|2613681|33|CP025831|CRISPRCasFinder,CRT matches to NZ_AP021899 (Akkermansia muciniphila strain JCM 30893 plasmid pJ30893, complete sequence) position: , mismatch: 2, identity: 0.939

tttttctgtgtcatgacatgtcgacctttacat	CRISPR spacer
tttttctgtgtcatgacatgtctccctttacat	Protospacer
**********************  *********

2. spacer 2.6|2537187|30|CP025831|CRISPRCasFinder,CRT matches to NC_007491 (Rhodococcus erythropolis PR4 plasmid pREL1, complete sequence) position: , mismatch: 5, identity: 0.833

-agcatagcatcgaggaaaacaatgccgata	CRISPR spacer
tcgcaca-catcgacgaaaacaatgccgatg	Protospacer
  ***.* ****** ***************.

3. spacer 2.6|2537187|30|CP025831|CRISPRCasFinder,CRT matches to MN850656 (Flavobacterium phage fF4, complete genome) position: , mismatch: 6, identity: 0.8

agcatagcatcgaggaaaacaatgccgata	CRISPR spacer
aagaaaacatcgagtaaaacaataccgata	Protospacer
*. * *.******* ********.******

4. spacer 2.6|2537187|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP030933 (Enterococcus gilvus strain CR1 plasmid pCR1A, complete sequence) position: , mismatch: 7, identity: 0.767

agcatagcatcgaggaaaacaatgccgata	CRISPR spacer
aacatagaatcgaggaaaactatgcgaaag	Protospacer
*.***** ************ **** .* .

5. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP040888 (Leclercia adecarboxylata strain Z96-1 plasmid pZ96-1_1, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

6. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP010351 (Acinetobacter johnsonii XBB1 plasmid pXBB1-9, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

7. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP032285 (Acinetobacter sp. WCHA55 plasmid pOXA58_010055, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

8. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to CP052287 (Klebsiella pneumoniae strain E16KP0218 plasmid pE16KP0218-1, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

9. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP043309 (Acinetobacter johnsonii strain Acsw19 plasmid pAcsw19-2, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

10. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP041047 (Citrobacter sp. CF971 plasmid pBM527-1, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

11. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP035634 (Enterobacter cloacae strain EN3600 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

12. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP022359 (Shewanella bicestrii strain JAB-1 plasmid pSHE-CTX-M, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

13. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP033130 (Acinetobacter wuhouensis strain WCHAW010062 plasmid pOXA23_010062, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

14. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NC_008573 (Shewanella sp. ANA-3 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
gaaaagaaaattctgaaaaggtgtaaaaat	Protospacer
.**** ******** *********.*   *

15. spacer 2.15|2537780|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NC_007950 (Polaromonas sp. JS666 plasmid 2, complete sequence) position: , mismatch: 7, identity: 0.767

caactgccttctctgccatcgtg-----gggagct	CRISPR spacer
caactgcgttctctgccatggtgttcccgg-----	Protospacer
******* *********** ***     **

16. spacer 2.17|2537912|29|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP028348 (Novosphingobium sp. THN1 plasmid pTHN, complete sequence) position: , mismatch: 7, identity: 0.759

ttctgcttgggcactatcgcctccccctg	CRISPR spacer
ttccgctcgggcactatcgcctcgtggtc	Protospacer
***.***.*************** .  *

17. spacer 2.17|2537912|29|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to MG962366 (Rhodococcus phage Finch, complete genome) position: , mismatch: 7, identity: 0.759

ttctgcttgggcactatcgcctccccctg	CRISPR spacer
tgacccttgggcaccatcgcctcgccctt	Protospacer
*  . *********.******** ****

18. spacer 2.20|2538109|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP038867 (Vagococcus sp. CF-49 plasmid punnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

cacctcaacccatgattgaaatttagatag	CRISPR spacer
cacctcaatccatgattgatattattaatg	Protospacer
********.********** ***   *  *

19. spacer 2.20|2538109|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to KY389063 (Staphylococcus phage phi575, complete genome) position: , mismatch: 7, identity: 0.767

cacctcaacccatgattgaaatttagatag	CRISPR spacer
taaatcaacccatgcttcaaatttagaaaa	Protospacer
.*  ********** ** ********* *.

20. spacer 2.4|2537055|30|CP025831|CRISPRCasFinder,CRT matches to NZ_KX710093 (Leclercia adecarboxylata strain pP10164 plasmid pP10164-2, complete sequence) position: , mismatch: 8, identity: 0.733

cataccggattgtttctgcataaaacacca	CRISPR spacer
cataccggattttttctgcacaagtagctc	Protospacer
*********** ********.**.  .*.

21. spacer 2.6|2537187|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP017077 (Novosphingobium resinovorum strain SA1 plasmid pSA2, complete sequence) position: , mismatch: 8, identity: 0.733

agcatagcatcgaggaaaacaatgccgata	CRISPR spacer
ctgccggcatcggcgaaaacaatgccgata	Protospacer
    ..******. ****************

22. spacer 2.15|2537780|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP049244 (Rhizobium pseudoryzae strain DSM 19479 plasmid unnamed3, complete sequence) position: , mismatch: 8, identity: 0.733

caactgccttctctgccatcgtggggagct	CRISPR spacer
cctttgccttctctgtcgtcgtggggatgg	Protospacer
*  .***********.*.*********

23. spacer 2.17|2537912|29|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP032695 (Rhizobium jaguaris strain CCGE525 plasmid pRCCGE525c, complete sequence) position: , mismatch: 8, identity: 0.724

ttctgcttgggcactatcgcctccccctg	CRISPR spacer
atctgcttaggcactatcgcctggaagcg	Protospacer
 *******.*************     .*

24. spacer 2.17|2537912|29|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP045296 (Paenibacillus cellulositrophicus strain KACC 16577 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.724

ttctgcttgggcactatcgcctccccctg	CRISPR spacer
aacttcttcggcactatcgcctcccaaat	Protospacer
  ** *** ****************

25. spacer 2.21|2538175|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to MK804891 (Aeromonas phage 2_D05, complete genome) position: , mismatch: 8, identity: 0.733

ctaccgttgaaccatacaccattgagccga	CRISPR spacer
gcggctgtgaaccatccaccatggagccga	Protospacer
 .. *  ******** ****** *******

26. spacer 2.21|2538175|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to MK813942 (Aeromonas phage 4_4512, complete genome) position: , mismatch: 8, identity: 0.733

ctaccgttgaaccatacaccattgagccga	CRISPR spacer
gcggctgtgaaccatccaccatggagccga	Protospacer
 .. *  ******** ****** *******

27. spacer 2.21|2538175|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to MK804892 (Aeromonas phage 4_D05, complete genome) position: , mismatch: 8, identity: 0.733

ctaccgttgaaccatacaccattgagccga	CRISPR spacer
gcggctgtgaaccatccaccatggagccga	Protospacer
 .. *  ******** ****** *******

28. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP020951 (Rhizobium sp. CIAT894 plasmid pRheCIAT894d, complete sequence) position: , mismatch: 9, identity: 0.7

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
agcgggaaaattcacaaaaggtgtgatgca	Protospacer
*. .. ******* ************* .

29. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NC_028926 (Bacillus phage Palmer, complete genome) position: , mismatch: 9, identity: 0.7

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
taaattaaaatcctcaaaaggtgtaccacc	Protospacer
 *** ******.************. . ..

30. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_CP016542 (Planococcus versutus strain L10.15 plasmid pPS15-2, complete sequence) position: , mismatch: 9, identity: 0.7

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
aaaaataaagttctcaaaaggctcaaaaga	Protospacer
*********.***********. ..*

31. spacer 2.8|2537319|30|CP025831|CRISPRCasFinder,CRT,PILER-CR matches to MT119360 (Enterococcus phage nattely, complete genome) position: , mismatch: 9, identity: 0.7

gaaataaaacaatgagcatttacgacgacc	CRISPR spacer
ataataaaaaaatgagcatttactgtttac	Protospacer
. ******* ************* ..   *

32. spacer 3.13|2613668|46|CP025831|PILER-CR matches to NZ_AP021899 (Akkermansia muciniphila strain JCM 30893 plasmid pJ30893, complete sequence) position: , mismatch: 9, identity: 0.804

tgcggagtgcgactttttctgtgtcatgacatgtcgacctttacat	CRISPR spacer
tgcgagggttcattttttctgtgtcatgacatgtctccctttacat	Protospacer
****..*  . *.**********************  *********

33. spacer 2.7|2537253|30|CP025831|CRISPRCasFinder,CRT matches to NZ_MH569712 (Serratia marcescens strain S120 plasmid pPM120-2, complete sequence) position: , mismatch: 10, identity: 0.667

aaaaataaaattctcaaaaggtgtgatctt	CRISPR spacer
tcggtaaaaattcgcaaaaggtgtgatgaa	Protospacer
  ..  ******* *************

34. spacer 3.4|2613547|34|CP025831|CRISPRCasFinder,CRT matches to NC_008269 (Rhodococcus jostii RHA1 plasmid pRHL1, complete sequence) position: , mismatch: 11, identity: 0.676

taggtggtatctccttcggcaccccggacaaccg	CRISPR spacer
tgatcctgatcttcttcggcaccctggacaacgt	Protospacer
*.. .   ****.***********.*******

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1051443 : 1059914

Streptococcus_phage(83.33%)

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
QAA54851.1\|1051443_1052544_+	DNA polymerase III subunit beta	B4UTW9	Rhizobium_phage	2.5e-42	34.3
QAA54852.1\|1052847_1053288_-	hypothetical protein	NA	NA	NA	NA
QAA54853.1\|1053390_1054443_-	hypothetical protein	NA	NA	NA	NA
QAA54854.1\|1054914_1056801_+	DNA recombinase	A0A1X9I6J1	Streptococcus_phage	1.2e-20	27.2
QAA54855.1\|1056797_1057142_+	TnpV protein	A0A1B0RXG6	Streptococcus_phage	4.0e-15	36.9
QAA54856.1\|1057516_1058206_+	hypothetical protein	NA	NA	NA	NA
QAA54857.1\|1058746_1059484_+	23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(B)	E4ZFQ0	Streptococcus_phage	3.7e-135	100.0
QAA54858.1\|1059488_1059620_+	hypothetical protein	E4ZFP9	Streptococcus_phage	7.9e-17	100.0
QAA54859.1\|1059629_1059914_+	topoisomerase	A0A1X9I6W8	Streptococcus_phage	4.1e-42	97.7

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. CP025831

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection