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CSM4_THEON
ID   CSM4_THEON              Reviewed;         289 AA.
AC   B6YWC1;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=CRISPR system Cms protein Csm4;
DE   AltName: Full=CRISPR type III A-associated RAMP protein Csm4;
GN   Name=csm4 {ECO:0000303|PubMed:25773141}; OrderedLocusNames=TON_0896;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
RN   [2]
RP   INTERACTION WITH CAS10 (CSM1), AND SUBUNIT.
RC   STRAIN=NA1;
RX   PubMed=25773141; DOI=10.1016/j.str.2015.01.021;
RA   Jung T.Y., An Y., Park K.H., Lee M.H., Oh B.H., Woo E.;
RT   "Crystal structure of the Csm1 subunit of the Csm complex and its single-
RT   stranded DNA-specific nuclease activity.";
RL   Structure 23:782-790(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.
CC       {ECO:0000250|UniProtKB:A0A0A7HGA1}.
CC   -!- SUBUNIT: Probably part of the Csm effector complex, that includes
CC       Cas10, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity).
CC       Interacts with Cas10 (csm1) (PubMed:25773141).
CC       {ECO:0000250|UniProtKB:A0A0A7HGA1, ECO:0000269|PubMed:25773141}.
CC   -!- INTERACTION:
CC       B6YWC1; B6YWB8: csm1; NbExp=2; IntAct=EBI-16149979, EBI-16149952;
CC   -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus.
CC       {ECO:0000305|PubMed:25773141}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated Csm4 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000855; ACJ16384.1; -; Genomic_DNA.
DR   RefSeq; WP_012571856.1; NC_011529.1.
DR   PDB; 6IQW; EM; 3.35 A; E=1-289.
DR   PDB; 6MUA; X-ray; 2.91 A; B=1-289.
DR   PDB; 6MUR; EM; 3.10 A; E=1-289.
DR   PDB; 6MUS; EM; 3.60 A; E=1-289.
DR   PDB; 6MUT; EM; 3.10 A; E=1-289.
DR   PDB; 6MUU; EM; 3.00 A; E=1-289.
DR   PDB; 6O73; X-ray; 3.00 A; B=1-289.
DR   PDB; 6O74; X-ray; 2.71 A; B=1-289.
DR   PDB; 6O75; X-ray; 2.60 A; B=1-289.
DR   PDB; 6O78; X-ray; 2.80 A; B=1-289.
DR   PDB; 6O79; X-ray; 3.00 A; B=1-289.
DR   PDB; 6O7B; X-ray; 2.40 A; B=1-289.
DR   PDB; 6O7D; X-ray; 2.81 A; B=1-289.
DR   PDB; 6O7E; EM; 3.20 A; E=1-289.
DR   PDB; 6O7H; EM; 2.90 A; E=1-289.
DR   PDB; 6O7I; EM; 3.20 A; E=1-289.
DR   PDBsum; 6IQW; -.
DR   PDBsum; 6MUA; -.
DR   PDBsum; 6MUR; -.
DR   PDBsum; 6MUS; -.
DR   PDBsum; 6MUT; -.
DR   PDBsum; 6MUU; -.
DR   PDBsum; 6O73; -.
DR   PDBsum; 6O74; -.
DR   PDBsum; 6O75; -.
DR   PDBsum; 6O78; -.
DR   PDBsum; 6O79; -.
DR   PDBsum; 6O7B; -.
DR   PDBsum; 6O7D; -.
DR   PDBsum; 6O7E; -.
DR   PDBsum; 6O7H; -.
DR   PDBsum; 6O7I; -.
DR   AlphaFoldDB; B6YWC1; -.
DR   SMR; B6YWC1; -.
DR   DIP; DIP-61405N; -.
DR   IntAct; B6YWC1; 1.
DR   STRING; 523850.TON_0896; -.
DR   EnsemblBacteria; ACJ16384; ACJ16384; TON_0896.
DR   GeneID; 7017199; -.
DR   KEGG; ton:TON_0896; -.
DR   PATRIC; fig|523850.10.peg.904; -.
DR   eggNOG; arCOG03222; Archaea.
DR   HOGENOM; CLU_062371_0_1_2; -.
DR   OMA; SAYFIVE; -.
DR   OrthoDB; 69746at2157; -.
DR   Proteomes; UP000002727; 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   TIGRFAMs; TIGR01903; cas5_csm4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; RNA-binding.
FT   CHAIN           1..289
FT                   /note="CRISPR system Cms protein Csm4"
FT                   /id="PRO_0000446122"
FT   STRAND          3..13
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:6O78"
FT   HELIX           21..36
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:6O78"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:6O7H"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:6O7H"
FT   HELIX           89..96
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   HELIX           104..111
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          123..133
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:6O7H"
FT   STRAND          142..151
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   HELIX           165..170
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   HELIX           172..180
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:6O7H"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:6O7H"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:6MUU"
FT   STRAND          195..203
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          212..216
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:6O75"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:6IQW"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          271..273
FT                   /evidence="ECO:0007829|PDB:6O7B"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:6O7B"
SQ   SEQUENCE   289 AA;  32306 MW;  A7E85053E77725F1 CRC64;
     MPKFIAVKLI PKGPFRDIPR ADTLFGAIGN AISAIHGQSA VEELVDAFVG GARISSAFPY
     SGDTYYLPKP LSVEPALEGI LTGLDEEERY TTAKRLRKAK YLDLKNFELA LRLRPFTIPE
     EIPYARVDVP RVVLDRVTQD SSIYFWEEIR FREKSGVYFL YSGPREVFDG YIAPAMRFLG
     DTGIGGKSTW GAGLFEVEFH EMKIDAPGSE YSVTLSNALP TKTPVLWRLL RKGGWSFGRR
     KPRMTFIAEG SIVKNDPGGM ERLELGLSHE VYVYGLTFPL GVELPEGLE
 
 
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