CMR5_PYRFU
ID CMR5_PYRFU Reviewed; 169 AA.
AC Q8U1T0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=CRISPR system Cmr subunit Cmr5;
DE AltName: Full=CRISPR type III-B/RAMP module-associated protein Cmr5;
GN Name=cmr5 {ECO:0000303|PubMed:19945378}; OrderedLocusNames=PF1125;
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 FUNCTION, INTERACTION WITH CMR2; CMR4 AND CMR6, 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), INTERACTION WITH CMR4, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=23370277; DOI=10.1016/j.febslet.2013.01.029;
RA Park J.H., Sun J., Park S.Y., Hwang H.J., Park M.Y., Shin M., Kim J.S.;
RT "Crystal structure of Cmr5 from Pyrococcus furiosus and its functional
RT implications.";
RL FEBS Lett. 587:562-568(2013).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH
RP TARGET RNA, AND SUBUNIT.
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).
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 NRA), 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: Monomer in isolation (PubMed:23370277). Part of the type III-B
CC Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and
CC Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the
CC mature crRNA (39 or 45 nt in length), while the complex is capped by
CC Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while
CC Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA.
CC The target RNA lies antiparallel to the crRNA, with its 5' end near
CC Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage
CC occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor
CC cleavage occurring at 6 nt intervals which coincide with the proposed
CC spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Interacts
CC with Cmr4 (PubMed:23370277). Interacts with Cmr2, Cmr4 and Cmr6
CC (PubMed:25280103). {ECO:0000269|PubMed:19945378,
CC ECO:0000269|PubMed:23370277, ECO:0000269|PubMed:24119404,
CC ECO:0000269|PubMed:25280103}.
CC -!- INTERACTION:
CC Q8U1T0; Q8U1S9: cmr4; NbExp=2; IntAct=EBI-2504964, EBI-2504950;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19945378}.
CC -!- SIMILARITY: Belongs to the CRISPR system Cmr5 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81249.1; -; Genomic_DNA.
DR RefSeq; WP_011012265.1; NZ_CP023154.1.
DR PDB; 4GKF; X-ray; 2.10 A; A/B=1-169.
DR PDBsum; 4GKF; -.
DR AlphaFoldDB; Q8U1T0; -.
DR SMR; Q8U1T0; -.
DR DIP; DIP-54369N; -.
DR IntAct; Q8U1T0; 4.
DR MINT; Q8U1T0; -.
DR STRING; 186497.PF1125; -.
DR EnsemblBacteria; AAL81249; AAL81249; PF1125.
DR GeneID; 41712934; -.
DR KEGG; pfu:PF1125; -.
DR PATRIC; fig|186497.12.peg.1186; -.
DR eggNOG; arCOG02654; Archaea.
DR HOGENOM; CLU_120836_0_0_2; -.
DR OMA; YVKKMPS; -.
DR OrthoDB; 113767at2157; -.
DR PhylomeDB; Q8U1T0; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.520.30; -; 1.
DR InterPro; IPR023101; AF1862-like_dom_sf.
DR InterPro; IPR010160; CRISPR-assoc_prot_Cmr5.
DR Pfam; PF09701; Cas_Cmr5; 1.
DR SUPFAM; SSF158568; SSF158568; 1.
DR TIGRFAMs; TIGR01881; cas_Cmr5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Reference proteome.
FT CHAIN 1..169
FT /note="CRISPR system Cmr subunit Cmr5"
FT /id="PRO_0000418079"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 39..59
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:4GKF"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4GKF"
FT HELIX 133..157
FT /evidence="ECO:0007829|PDB:4GKF"
SQ SEQUENCE 169 AA; 19687 MW; 22AF2EA37ABA2249 CRC64;
MEVHMLSKDN KKSIRKTLEQ RRGEYAYYVI KEVADLNDKQ LEEKYASLVK KAPVMILSNG
LLQTLAFLLA KAETSPEKAN QILSRVNEYP PRFIEKLGND KDEHLLLYLH IVYWLRENVD
RNIDVKTLLS QDYSKVLWAT KEAIALLNWM RRFAVAMLKE EGKENEGSS
