CMR7A_SACS2
ID CMR7A_SACS2 Reviewed; 197 AA.
AC Q97WX5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=CRISPR system CMR subunit Cmr7 1;
GN Name=cmr7A; OrderedLocusNames=SSO1986;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=20419351; DOI=10.1007/s10969-010-9090-y;
RA Oke M., Carter L.G., Johnson K.A., Liu H., McMahon S.A., Yan X., Kerou M.,
RA Weikart N.D., Kadi N., Sheikh M.A., Schmelz S., Dorward M., Zawadzki M.,
RA Cozens C., Falconer H., Powers H., Overton I.M., van Niekerk C.A., Peng X.,
RA Patel P., Garrett R.A., Prangishvili D., Botting C.H., Coote P.J.,
RA Dryden D.T., Barton G.J., Schwarz-Linek U., Challis G.L., Taylor G.L.,
RA White M.F., Naismith J.H.;
RT "The Scottish Structural Proteomics Facility: targets, methods and
RT outputs.";
RL J. Struct. Funct. Genomics 11:167-180(2010).
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 -!- SUBUNIT: Possible homodimer. Part of the CMR ribonucleoprotein complex,
CC consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and
CC possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can
CC also be isolated. It does not cleave target RNA.
CC {ECO:0000269|PubMed:22227115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22227115}.
CC -!- SIMILARITY: Belongs to the CRISPR system Cmr7 family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42176.1; -; Genomic_DNA.
DR PIR; A90365; A90365.
DR RefSeq; WP_009993002.1; NC_002754.1.
DR PDB; 2X5Q; X-ray; 2.05 A; A/B=1-197.
DR PDBsum; 2X5Q; -.
DR AlphaFoldDB; Q97WX5; -.
DR SMR; Q97WX5; -.
DR STRING; 273057.SSO1986; -.
DR EnsemblBacteria; AAK42176; AAK42176; SSO1986.
DR GeneID; 27428312; -.
DR KEGG; sso:SSO1986; -.
DR PATRIC; fig|273057.12.peg.2062; -.
DR eggNOG; arCOG08552; Archaea.
DR HOGENOM; CLU_1472150_0_0_2; -.
DR EvolutionaryTrace; Q97WX5; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0099048; P:CRISPR-cas system; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR043959; Cmr7A.
DR Pfam; PF19021; Cmr7A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Reference proteome.
FT CHAIN 1..197
FT /note="CRISPR system CMR subunit Cmr7 1"
FT /id="PRO_0000418083"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2X5Q"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2X5Q"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 79..92
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2X5Q"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:2X5Q"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:2X5Q"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:2X5Q"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2X5Q"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:2X5Q"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:2X5Q"
SQ SEQUENCE 197 AA; 22151 MW; C8AC8DACA9BA65D6 CRC64;
MTSGAGWEEQ VFLPITNSIS SEDNNQIKIG SSVSIEYNQN GQHVSQIDDK GLHNILVLTG
YAIDESTGEL VPTFDPCDYV KGILISGKIL KGNHFKIIGI PSNKLYIIRK KDVHGNITFS
LPIKNFNTGT YQVDLRDKVT SFVSLDRDVA KTIVDNVLAK IYAKIYNSLN KEQKDKLYRD
VEEIFNYYSI KSLKSNP
