CMR6_PYRFU
ID CMR6_PYRFU Reviewed; 340 AA.
AC Q8U1T1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=CRISPR system Cmr subunit Cmr6;
DE AltName: Full=CRISPR type III-B/RAMP module RAMP protein Cmr6;
GN Name=cmr6 {ECO:0000303|PubMed:19945378}; OrderedLocusNames=PF1124;
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 (2.15 ANGSTROMS) OF 101-340, FUNCTION, INTERACTION
RP WITH CMR4 AND CMR5, 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). Interacts with Cmr4 and Cmr5
CC (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 Cmr6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009950; AAL81248.1; -; Genomic_DNA.
DR RefSeq; WP_011012264.1; NZ_CP023154.1.
DR PDB; 4W8V; X-ray; 2.15 A; A/B=101-340.
DR PDBsum; 4W8V; -.
DR AlphaFoldDB; Q8U1T1; -.
DR SMR; Q8U1T1; -.
DR DIP; DIP-54368N; -.
DR IntAct; Q8U1T1; 3.
DR STRING; 186497.PF1124; -.
DR PRIDE; Q8U1T1; -.
DR DNASU; 1468993; -.
DR EnsemblBacteria; AAL81248; AAL81248; PF1124.
DR GeneID; 41712933; -.
DR KEGG; pfu:PF1124; -.
DR PATRIC; fig|186497.12.peg.1185; -.
DR eggNOG; arCOG02661; Archaea.
DR HOGENOM; CLU_053305_2_1_2; -.
DR OMA; VYETSIR; -.
DR OrthoDB; 98478at2157; -.
DR PhylomeDB; Q8U1T1; -.
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; IPR010172; CRISPR-assoc_prot_TM1791.
DR InterPro; IPR005537; RAMP_III_fam.
DR PANTHER; PTHR39965; PTHR39965; 1.
DR Pfam; PF03787; RAMPs; 1.
DR TIGRFAMs; TIGR01898; cas_TM1791_cmr6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Reference proteome;
KW RNA-binding.
FT CHAIN 1..340
FT /note="CRISPR system Cmr subunit Cmr6"
FT /id="PRO_0000418081"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4W8V"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:4W8V"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 255..264
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4W8V"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4W8V"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4W8V"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4W8V"
SQ SEQUENCE 340 AA; 38742 MW; 3E7578E79510FB32 CRC64;
MKEVVKLVLL GERQNSLNLS LYFNKYPPTI IYPEVLEDRN KKLASPSGSQ RKISLLVLNQ
GVLQFNKIKE TIEKSLPIET KVKLPQKAYE LYKKYYQDYT DMLNSLHAIT GKFKTQSRLV
VGLGDESVYE TSIRLLRNYG VPYIPGSAIK GVTRHLTYYV LAEFINEGND FYKRAKTVQD
AFMKGDPKEI LSNAKVPERC SRLCKEFLRI FGEKKVPEII DELIRIFGTQ KKEGEVVFFD
AIPIAEEIAD KPILELDIMN PHYGPYYQSG EKNVPPPGDW YDPIPIFFLT VPKDVPFLVA
VGGRDRELTE KAFSLVKLAL RDLGVGAKTS LGYGRLVEYV
