CMR2_SACS2
ID CMR2_SACS2 Reviewed; 1045 AA.
AC Q97WX0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=CRISPR system CMR subunit Cmr2;
DE AltName: Full=CRISPR-associated protein Cas10/Cmr2, subtype III-B;
GN Name=cmr2; OrderedLocusNames=SSO1991;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN CMR COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=22227115; DOI=10.1016/j.molcel.2011.12.013;
RA Zhang J., Rouillon C., Kerou M., Reeks J., Brugger K., Graham S.,
RA Reimann J., Cannone G., Liu H., Albers S.V., Naismith J.H., Spagnolo L.,
RA White M.F.;
RT "Structure and mechanism of the CMR complex for CRISPR-mediated antiviral
RT immunity.";
RL Mol. Cell 45:303-313(2012).
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) (By
CC similarity). The CMR complex degrades RNA complementary to the crRNA
CC (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate
CC ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an
CC unpaired 3' flag on the target RNA, and is stimulated by ATP. Some
CC cleavage of the guide crRNA can also be observed. {ECO:0000250,
CC ECO:0000269|PubMed:22227115}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 Ca(2+) per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Part of the CMR ribonucleoprotein complex, consisting of crRNA
CC plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A
CC Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does
CC not cleave target RNA. {ECO:0000269|PubMed:22227115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22227115}.
CC -!- SIMILARITY: Belongs to the CRISPR system Cmr2 family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42181.1; -; Genomic_DNA.
DR PIR; F90365; F90365.
DR RefSeq; WP_009992992.1; NC_002754.1.
DR AlphaFoldDB; Q97WX0; -.
DR SMR; Q97WX0; -.
DR STRING; 273057.SSO1991; -.
DR PRIDE; Q97WX0; -.
DR EnsemblBacteria; AAK42181; AAK42181; SSO1991.
DR GeneID; 27428317; -.
DR KEGG; sso:SSO1991; -.
DR PATRIC; fig|273057.12.peg.2067; -.
DR eggNOG; arCOG02666; Archaea.
DR HOGENOM; CLU_012640_0_0_2; -.
DR InParanoid; Q97WX0; -.
DR OMA; FLVKDWI; -.
DR PhylomeDB; Q97WX0; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.2220; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR038242; Cmr2_N.
DR InterPro; IPR024615; CRISPR-assoc_Cmr2_N.
DR InterPro; IPR013407; CRISPR-assoc_prot_Cmr2.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF12469; DUF3692; 1.
DR TIGRFAMs; TIGR02577; cas_TM1794_Cmr2; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..1045
FT /note="CRISPR system CMR subunit Cmr2"
FT /id="PRO_0000418074"
FT BINDING 229
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 652
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 810
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 811
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 811
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1045 AA; 121641 MW; 2F8DCACF254DF968 CRC64;
MSTDDNSREE FLNYKIMALL HDPPNKAWVI TSRAHNLTVQ LRSVRARKSH ERVAKYIINQ
LFGDINSKTV DNADKLASSI DRYLGSIVYK EYSLFRNRSI FLKNILLSNI QRDVGNLFPK
DKSKLDNLIS EYKKLLNVTN TTNLNILKYQ LFYLIYELIW IDSRYENTPA ETRNPTHTIF
DHLYATAAMM NWIFSLEKEA KGYLLGIDTI GVADFISKGK KTRDLWISSY LVSALLWYVI
TWFIEEYGPD VILFPSLRFN QFYAFYLLEK LRKEKISEDV IDEIKELITK YIFNGDDLFE
KLEIPPYPII PGRITLILPG LIREGEEYTQ VPDDNYFISK VKERYNEGWR KLIEGLKCYS
ELKREDGFWN LVCRVLKLTE DLLQTTPLNI RVKQVSVTKD EIFNNSKLRS DSWKIYDNKY
RQLVSEFKKS KLVKVTPESR LKLFELTKFD KLPQIGEKSK RGYEFCTSCG VLPAVIIMPK
EDEFEKKLIE LGIARDEKDV RSIKNMISPG ERLCPWCLVK RALGAEPRLM RILLLGDLCS
VEKIVNEIVS KDVKIEIPST SDIASIKTFE EMIEKKNEIC EDLKEEEVCE KPNESMLSMW
QRFNKNYYTG INLTIDPEEY WFSEKRRRYY FSLFRRHRIT FPSPYYALVR ADSDYLGDLL
EGKLTPYLAG IIDSGDYANI SEKKEEVNKL LEEYLVNAGS GPIVDYVKTV LECIRGNLNK
CSCAVKIYSN EVAEVMFRAN RLLRKKLEKI DVEREVENSL KYFRTILKEG RIIVTPAWHV
SISSALNRGL LVELELINKH KGFVIYAGGD DLLAMLPVDE VLDFVKESRR AFAGVSTGRL
GNMCLENGFA RINNAYYPSL PIVGRSYSVI IAHYADPLFF VINDSYNLLE EGKEMIRYRV
MYNGEYKDAK KDVAIFRYQG LTSVIPLSLK RPIVNSVSDF NEIASIIDLI LELKKRIDEG
HISVSLLYDY EEYKHLIVAS DEKYLTEFLV KDWIKRNSLR KHVEFTIDEK LYGVRLTIEN
YPIKIPNDLI SNIVYTLRII YGGEK
