CSM4_METJA
ID CSM4_METJA Reviewed; 376 AA.
AC Q59062;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=CRISPR system Cms protein Csm4;
DE AltName: Full=CRISPR type III-A associated RAMP protein Csm4;
GN Name=csm4; OrderedLocusNames=MJ1668;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2] {ECO:0007744|PDB:4QTS}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), SUBUNIT, MUTAGENESIS OF
RP 229-GLU-ASP-230, AND RNA-BINDING.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=25451598; DOI=10.1016/j.jmb.2014.09.029;
RA Numata T., Inanaga H., Sato C., Osawa T.;
RT "Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas
RT interference complex.";
RL J. Mol. Biol. 427:259-273(2015).
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). The
CC type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC cognate to the crRNA is required for all activities.
CC {ECO:0000250|UniProtKB:A0A0A7HGA1}.
CC -!- FUNCTION: The subunit probably binds to the 5' handle of the crRNA,
CC helping in discrimination between self- and non-self (Probable). The
CC Csm3-Csm4 complex binds both crRNA and a non-specific RNA; Csm4 alone
CC also binds RNA (PubMed:25451598). {ECO:0000269|PubMed:25451598,
CC ECO:0000305|PubMed:25451598}.
CC -!- SUBUNIT: Part of the Csm effector complex that includes Cas10, Csm2,
CC Csm3, Csm4 and Csm5 (By similarity). Stable Cas10/Csm1-Csm4, Csm3-Csm4
CC (which crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4
CC subcomplexes can be isolated (PubMed:25451598).
CC {ECO:0000250|UniProtKB:A0A0A7HGA1, ECO:0000269|PubMed:25451598}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm4 family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99688.1; -; Genomic_DNA.
DR PIR; B64508; B64508.
DR RefSeq; WP_010871192.1; NC_000909.1.
DR PDB; 4QTS; X-ray; 3.10 A; A/B=1-376.
DR PDBsum; 4QTS; -.
DR AlphaFoldDB; Q59062; -.
DR SMR; Q59062; -.
DR STRING; 243232.MJ_1668; -.
DR PRIDE; Q59062; -.
DR EnsemblBacteria; AAB99688; AAB99688; MJ_1668.
DR GeneID; 1452577; -.
DR KEGG; mja:MJ_1668; -.
DR eggNOG; arCOG03222; Archaea.
DR HOGENOM; CLU_062371_0_0_2; -.
DR InParanoid; Q59062; -.
DR OMA; NSKYHFG; -.
DR OrthoDB; 68179at2157; -.
DR PhylomeDB; Q59062; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR005510; Csm4.
DR InterPro; IPR040932; Csm4_C.
DR InterPro; IPR005537; RAMP_III_fam.
DR Pfam; PF17953; Csm4_C; 1.
DR Pfam; PF03787; RAMPs; 1.
DR TIGRFAMs; TIGR01903; cas5_csm4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Reference proteome; RNA-binding.
FT CHAIN 1..376
FT /note="CRISPR system Cms protein Csm4"
FT /id="PRO_0000107465"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 229..230
FT /note="ED->AA: No longer interacts with Csm3."
FT /evidence="ECO:0000269|PubMed:25451598"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4QTS"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:4QTS"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4QTS"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4QTS"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:4QTS"
SQ SEQUENCE 376 AA; 43851 MW; F5DC850CA5FF7DF2 CRC64;
MKMVVLKPKI NSKFHFGEGS LERNSKIFHS NSLFSAIVNN YIKLYGREDL EKNIEKIKNI
RLSSLLYKIK NIYLIPKPEH PEFYKLKGNP GIKPKDIKKI QFFSIKAYKE LLDNELDWKN
KIKHIVDYQT INKSIVISEK EIEEIKRIFG IKAEKLKHAK ISLISKHLEQ KVAIDRLKDI
TLEKDDKGQL YNIEFIKLNE NVEFYFLIDY NNEDKEFIKK LEASIKLIED EGLGGKRSIG
AGFFEKVEIV DLPEDFNEIL DENSKYNNLE YKMLLGVGIP NKDDIKNIEY YKLIEIGGYI
YSLECLTKPK RNILALTEGS IVKNDFIGDV KDISPQNDDD EQNKNNENNN KLNHKVYTHG
KPILLPFNPK RDNYGS
