CMR1A_PYRFU
ID CMR1A_PYRFU Reviewed; 338 AA.
AC Q8U1S5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=CRISPR system Cmr subunit Cmr1-1;
DE AltName: Full=CRISPR type III-B/RAMP module RAMP protein Cmr1-1;
GN Name=cmr1-1 {ECO:0000303|PubMed:19945378}; OrderedLocusNames=PF1130;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN CMR COMPLEX, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=19945378; DOI=10.1016/j.cell.2009.07.040;
RA Hale C.R., Zhao P., Olson S., Duff M.O., Graveley B.R., Wells L.,
RA Terns R.M., Terns M.P.;
RT "RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.";
RL Cell 139:945-956(2009).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH
RP TARGET RNA, SUBUNIT, AND RNA-BINDING.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=24119404; DOI=10.1016/j.molcel.2013.09.008;
RA Spilman M., Cocozaki A., Hale C., Shao Y., Ramia N., Terns R., Terns M.,
RA Li H., Stagg S.;
RT "Structure of an RNA silencing complex of the CRISPR-Cas immune system.";
RL Mol. Cell 52:146-152(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=25280103; DOI=10.1016/j.molcel.2014.09.002;
RA Benda C., Ebert J., Scheltema R.A., Schiller H.B., Baumgaertner M.,
RA Bonneau F., Mann M., Conti E.;
RT "Structural model of a CRISPR RNA-silencing complex reveals the RNA-target
RT cleavage activity in Cmr4.";
RL Mol. Cell 56:43-54(2014).
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 sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA),
CC formerly called psiRNA (prokaryotic silencing) in this organism. Part
CC of the Cmr ribonucleoprotein complex which has divalent cation-
CC dependent endoribonuclease activity specific for ssRNA complementary to
CC the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-
CC 3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves
CC target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA
CC complementary to the crRNA. Cleavage of invading RNA is guided by the
CC crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3'
CC end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not
CC absolutely necessary for target cleavage (PubMed:19945378).
CC {ECO:0000269|PubMed:19945378, ECO:0000269|PubMed:25280103}.
CC -!- SUBUNIT: Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an
CC elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5
CC forming a helical core along the mature crRNA (39 or 45 nt in length),
CC while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA
CC is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or
CC Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel
CC to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near
CC Cmr2 and Cmr3; major target cleavage occurs nears the junction of
CC Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals
CC which coincide with the proposed spacing of Cmr4 subunits
CC (PubMed:24119404, PubMed:25280103). {ECO:0000269|PubMed:19945378,
CC ECO:0000269|PubMed:24119404, ECO:0000269|PubMed:25280103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19945378}.
CC -!- SIMILARITY: Belongs to the CRISPR system Cmr1 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81254.1; -; Genomic_DNA.
DR RefSeq; WP_011012270.1; NC_003413.1.
DR PDB; 4W8X; X-ray; 3.00 A; A=1-338.
DR PDB; 4W8Z; X-ray; 2.70 A; A=1-338.
DR PDBsum; 4W8X; -.
DR PDBsum; 4W8Z; -.
DR AlphaFoldDB; Q8U1S5; -.
DR SMR; Q8U1S5; -.
DR DIP; DIP-54364N; -.
DR IntAct; Q8U1S5; 6.
DR STRING; 186497.PF1130; -.
DR EnsemblBacteria; AAL81254; AAL81254; PF1130.
DR GeneID; 1468999; -.
DR KEGG; pfu:PF1130; -.
DR PATRIC; fig|186497.12.peg.1191; -.
DR eggNOG; arCOG03891; Archaea.
DR HOGENOM; CLU_050338_1_0_2; -.
DR OMA; EENGIFG; -.
DR OrthoDB; 122742at2157; -.
DR PhylomeDB; Q8U1S5; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR007522; CRISPR-assoc_prot_TM1795.
DR InterPro; IPR005537; RAMP_III_fam.
DR Pfam; PF03787; RAMPs; 1.
DR TIGRFAMs; TIGR01894; cas_TM1795_cmr1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Reference proteome;
KW RNA-binding.
FT CHAIN 1..338
FT /note="CRISPR system Cmr subunit Cmr1-1"
FT /id="PRO_0000418070"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4W8X"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4W8Z"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:4W8Z"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4W8Z"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4W8X"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 182..200
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 231..258
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:4W8Z"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:4W8Z"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:4W8Z"
SQ SEQUENCE 338 AA; 38895 MW; 65EF194EF9A9851C CRC64;
MFIEEFEIES ITSTHLLEVL TREYPEVRSP SIKGAMRWWF RALAGSYFGD DAQKLKEIEN
QVFGSTKERS RVKISVTPLS SPKRLNLKEF KDKNVGYIWF SINLLGKRGT ITHYYPPGSR
FRVVLESPSE RVIKLATLSL WALVSLGSVG FRSRRGTGSM KIVRASSEVL EDLGLTTEFN
SIDEFKDSLK RVLDVTGEIL GVKNSETNKS LPSYATLKFS DVEVFGPGKN TWEVLAQFNN
SYKEYLRRRI KKYQRIIFGL PRFKLRGVRK DLRRASPLWF GVVEIGGKPY GRIIKFFQST
FHPEVRSKHI VDWNVLSNFD WFISSRLPVT KVWGGWSG
