CAS10_THET8
ID CAS10_THET8 Reviewed; 805 AA.
AC Q53W19;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
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 {ECO:0000305|PubMed:28663439, ECO:0000305|PubMed:28722012};
DE EC=2.7.7.- {ECO:0000305|PubMed:28663439, ECO:0000305|PubMed:28722012};
GN Name=cas10 {ECO:0000305}; Synonyms=csm1 {ECO:0000305};
GN OrderedLocusNames=TTHB147;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROBABLE FUNCTION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=28663439; DOI=10.1126/science.aao0100;
RA Kazlauskiene M., Kostiuk G., Venclovas C., Tamulaitis G., Siksnys V.;
RT "A cyclic oligonucleotide signaling pathway in type III CRISPR-Cas
RT systems.";
RL Science 357:605-609(2017).
RN [3]
RP PROBABLE FUNCTION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=28722012; DOI=10.1038/nature23467;
RA Niewoehner O., Garcia-Doval C., Rostoel J.T., Berk C., Schwede F.,
RA Bigler L., Hall J., Marraffini L.A., Jinek M.;
RT "Type III CRISPR-Cas systems produce cyclic oligoadenylate second
RT messengers.";
RL Nature 548:543-548(2017).
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)
CC (Probable). The type III-A Csm effector complex binds crRNA and acts as
CC a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding
CC of target RNA cognate to the crRNA is required for all activities
CC (Probable). {ECO:0000305}.
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. The active cOA in this bacteria is
CC cyclic tetraadenylate (cA4), presumably made by this enzyme. cOAs are
CC second messengers that stimulate the ssRNase activity of Csm6, inducing
CC an antiviral state important for defense against invading nucleic
CC acids. {ECO:0000305|PubMed:28663439, ECO:0000305|PubMed:28722012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 ATP = cyclic tetraadenylate + 4 diphosphate;
CC Xref=Rhea:RHEA:58280, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:142457; Evidence={ECO:0000305|PubMed:28663439,
CC ECO:0000305|PubMed:28722012};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:A0A0A7HFE1};
CC -!- SUBUNIT: Probably part of the Csm effector complex, that includes
CC Cas10, Csm2, Csm3, Csm4, Csm5 and mature crRNA.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
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; AP008227; BAD71943.1; -; Genomic_DNA.
DR RefSeq; WP_011229152.1; NC_006462.1.
DR RefSeq; YP_145386.1; NC_006462.1.
DR AlphaFoldDB; Q53W19; -.
DR SMR; Q53W19; -.
DR EnsemblBacteria; BAD71943; BAD71943; BAD71943.
DR GeneID; 3169523; -.
DR KEGG; ttj:TTHB147; -.
DR PATRIC; fig|300852.9.peg.2095; -.
DR HOGENOM; CLU_017487_0_0_0; -.
DR OMA; PSAFYYS; -.
DR PhylomeDB; Q53W19; -.
DR Proteomes; UP000000532; Plasmid pTT27.
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.
PE 3: Inferred from homology;
KW Antiviral defense; ATP-binding; Endonuclease; Exonuclease; Hydrolase;
KW Nuclease; Nucleotide-binding; Plasmid; Reference proteome; RNA-binding;
KW Transferase.
FT CHAIN 1..805
FT /note="CRISPR system single-strand-specific
FT deoxyribonuclease Cas10/Csm1 (subtype III-A)"
FT /id="PRO_0000446113"
FT DOMAIN 542..702
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT REGION 1..99
FT /note="HD domain"
FT /evidence="ECO:0000305"
FT REGION 99..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 90302 MW; 272542612C6B4EF7 CRC64;
MLGDGLSVAL AGLLHDVGKL YSRARWGERD DQVPDRTHTA YTAHFVREHA GLFRGAGLDP
DWLARTASRH HEGWRDRPQY RPETPEEWCV ALADTYASKE REEGEGGGSP PEVPLSPPFR
RLLLGGEEGR EGGYSPVGAG GRVGLEAGGL YPEERPNVSK DVYKRLLERL EGRLEEMARF
SLGKEALVLN LALALQETLS LVPSDTQSEP DVSLYDHLRL TAAIAHALWL FHGGSPSAQN
LRQDGEKFLL VVGDMGGIQG HIYRIAGAEA GVGGIAKRLR ARSLEVSLAA EAMALGLLWR
LGLTSLNRIL GAGGKFYLLL PNTEEARAAL EGTREAWGRW ALKRGGSLVP HLAWVAFRGQ
DFRDFAALLK RLHEALAREK LRPFAFLAST GGVLGAPLRP CAACGLEPAR RDEPGSLCPD
CEREAALGAR LPRSDRVGFF LEEAPRPYLD FPGLKVGLGG PLEGAFHLFR ARLDFAPWPD
PSEAKPLLGH LPRVEHALKA KGWSLEAYRA WAEEEGLLED EEPHPEKVLT FAELAALSEG
APYLGALMLD ADRMGEAFAT GFRREGRDLA TPSRLAALSR TLEVFFTTEV LTLLEEPRRY
RERLGWDDLE AQRKEARYPL LYSVYSGGDD LFLLGPWDAL LDFALDLERL YRLFTRHPRL
TLSGGFLLVP PSLPVPELAR LLGEAEKRAK AEGRERLFLF GQAVPWETLR GLRAWAEGLR
QDLRAERVSR AQVYRWLLLW RRFSPLEDPG ERMRYKPLLA YALRRVRERD EEAWKRYLKL
LDHQDPAWAY LPVWVQWALY RERRV
