CAS10_METJA
ID CAS10_METJA Reviewed; 800 AA.
AC Q59066;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A);
DE Short=ssDNase Cas10;
DE EC=3.1.-.-;
DE AltName: Full=Cyclic oligoadenylate synthase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:A0A0A7HFE1};
GN Name=cas10; Synonyms=csm1 {ECO:0000303|PubMed:25451598};
GN OrderedLocusNames=MJ1672;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=25451598; DOI=10.1016/j.jmb.2014.09.029;
RA Numata T., Inanaga H., Sato C., Osawa T.;
RT "Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas
RT interference complex.";
RL J. Mol. Biol. 427:259-273(2015).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat) is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). The
CC type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC cognate to the crRNA is required for all activities.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- FUNCTION: This subunit is a single-strand-specific deoxyribonuclease
CC (ssDNase) which digests both linear and circular ssDNA; it has both
CC exo- and endonuclease activity. {ECO:0000250|UniProtKB:B6YWB8}.
CC -!- FUNCTION: ssDNase activity is stimulated in the ternary Csm effector
CC complex; binding of cognate target RNA activates the ssDNase, as the
CC target RNA is degraded ssDNA activity decreases.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- FUNCTION: When associated with the ternary Csm effector complex (the
CC crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic
CC oligoadenylates (cOA) from ATP. cOAs are second messengers that
CC stimulate the ssRNase activity of Csx1, inducing an antiviral state
CC important for defense against invading nucleic acids.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:A0A0A7HFE1};
CC -!- SUBUNIT: Part of the Csm effector complex, that includes Cas10/Csm1,
CC Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Stable
CC Cas10/Csm1-Csm4 and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated;
CC Cas10 and Csm3 probably do not directly interact (PubMed:25451598).
CC {ECO:0000250|UniProtKB:A0A0A7HFE1, ECO:0000269|PubMed:25451598}.
CC -!- DOMAIN: The N-terminal HD domain has ssDNase activity. The C-terminal
CC GGDEF domain has the cOA synthesis activity.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Cas10/Csm1 family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99690.1; -; Genomic_DNA.
DR PIR; F64508; F64508.
DR RefSeq; WP_010871196.1; NC_000909.1.
DR AlphaFoldDB; Q59066; -.
DR SMR; Q59066; -.
DR STRING; 243232.MJ_1672; -.
DR EnsemblBacteria; AAB99690; AAB99690; MJ_1672.
DR GeneID; 1452581; -.
DR KEGG; mja:MJ_1672; -.
DR eggNOG; arCOG02666; Archaea.
DR HOGENOM; CLU_017487_0_0_2; -.
DR InParanoid; Q59066; -.
DR OMA; PSAFYYS; -.
DR PhylomeDB; Q59066; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd09680; Cas10_III; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR013408; Cas10/Csm1.
DR InterPro; IPR041062; Csm1_B.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF18211; Csm1_B; 1.
DR Pfam; PF01966; HD; 1.
DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Endonuclease; Exonuclease; Hydrolase;
KW Nuclease; Nucleotide-binding; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..800
FT /note="CRISPR system single-strand-specific
FT deoxyribonuclease Cas10/Csm1 (subtype III-A)"
FT /id="PRO_0000107470"
FT DOMAIN 1..92
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 578..722
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
SQ SEQUENCE 800 AA; 93633 MW; E4CD16D129C0FB0C CRC64;
MGNCNEYTAL KIGALLHDIG KFIQRASDKP KSKGHDKFGY EFLKEKFKNG FLNHLDEKTK
DKILEIVKEH HNQKIKDDLI GIVRLADWLS SGERREPKGD PENVEVLNTE EQKLLSIFET
VCIGELTENL YKNGFKYSLK PLNVSDAIFT DKPYPNENYK ELFSKFEDEI KDFKGDVSFE
ELYQLMQKYT WCIPSVTMWK KAGSLKGGLP DVSLFDHSKT TCAIACCLYQ MYVKENKKKN
KYAKEYIDDK TLEKLFNNDN GWNKEIFSLI HGDLSGIQDF VFTITTKYAT KSLKGRSFYL
DFLTEYFAKY ICKELNLPIT NILFYGGGHF YILSYKVDEN LINKLEKEIN EVLFNMFRTK
IYITIAEVGV TPNDFKKSED KESKEKTWGF AKKWKEVSEK TVEKKLRRFE YKLEGLFEPY
NRGSENRCVI CRNEFDKNEK GYAIRENESK SERICDYCAS FVALTDILKN FQMEKTIKFN
KAYPIIHLTK NKDNLSLQRE EFSFLTVKAI EKLESKFRVL SDENYFLKEY KLPHDSGELI
IPYKIWAIAF PIIENETEKR ILDFDGLAEK AFERTGTRKI GILKMDVDNL GEIFTTGLGN
DATISRMSTL SSMLTLFFTG YIPHLIKNEE FEVNGKKYKF KDNIYLVYAG GDDTLIVGAW
DAVWELAKRI RGDFKKFVCY NPYITLSAGI VFVNPKFEFK KAVNMAEEEL ENGKNYIIYE
DEETEKKVDK NALTVFNCPM NWDLEVEYNE YCWTKLKSYL EGINKEMVEL ESLVKKFNED
DLEKNLKKQL KRQIRKESYI
