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CSL4_ARCFU
ID   CSL4_ARCFU              Reviewed;         179 AA.
AC   O30033;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Exosome complex component Csl4 {ECO:0000255|HAMAP-Rule:MF_00975};
GN   Name=csl4 {ECO:0000255|HAMAP-Rule:MF_00975}; OrderedLocusNames=AF_0206;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND
RP   ZINC, FUNCTION, SUBUNIT, AND DOMAIN.
RX   PubMed=16285927; DOI=10.1016/j.molcel.2005.10.018;
RA   Buttner K., Wenig K., Hopfner K.P.;
RT   "Structural framework for the mechanism of archaeal exosomes in RNA
RT   processing.";
RL   Mol. Cell 20:461-471(2005).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND
RP   ZINC, FUNCTION, AND SUBUNIT.
RX   PubMed=20392821; DOI=10.1093/nar/gkq238;
RA   Hartung S., Niederberger T., Hartung M., Tresch A., Hopfner K.P.;
RT   "Quantitative analysis of processive RNA degradation by the archaeal RNA
RT   exosome.";
RL   Nucleic Acids Res. 38:5166-5176(2010).
CC   -!- FUNCTION: Non-catalytic component of the exosome, which is a complex
CC       involved in RNA degradation. Increases the RNA binding and the
CC       efficiency of RNA degradation. Helpful for the interaction of the
CC       exosome with A-poor RNAs (Probable). {ECO:0000305|PubMed:16285927,
CC       ECO:0000305|PubMed:20392821}.
CC   -!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer of
CC       Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-
CC       like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts with
CC       DnaG (Probable). {ECO:0000305|PubMed:16285927,
CC       ECO:0000305|PubMed:20392821}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00975}.
CC   -!- DOMAIN: Contains an N-terminal domain that mediates interactions with
CC       the hexameric ring, a central S1 domain and a C-terminal zinc-ribbon
CC       domain. {ECO:0000269|PubMed:16285927}.
CC   -!- MISCELLANEOUS: The zinc ion has probably a structural role.
CC       {ECO:0000305|PubMed:16285927}.
CC   -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00975}.
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DR   EMBL; AE000782; AAB91036.1; -; Genomic_DNA.
DR   PIR; F69275; F69275.
DR   RefSeq; WP_010877717.1; NC_000917.1.
DR   PDB; 2BA1; X-ray; 2.70 A; A/B/C=1-179.
DR   PDB; 3M7N; X-ray; 2.40 A; A/B/C=1-179.
DR   PDB; 3M85; X-ray; 3.00 A; A/B/C=1-179.
DR   PDBsum; 2BA1; -.
DR   PDBsum; 3M7N; -.
DR   PDBsum; 3M85; -.
DR   AlphaFoldDB; O30033; -.
DR   SMR; O30033; -.
DR   STRING; 224325.AF_0206; -.
DR   EnsemblBacteria; AAB91036; AAB91036; AF_0206.
DR   GeneID; 24793740; -.
DR   KEGG; afu:AF_0206; -.
DR   eggNOG; arCOG00676; Archaea.
DR   HOGENOM; CLU_067135_1_1_2; -.
DR   OMA; CGNVETR; -.
DR   OrthoDB; 111542at2157; -.
DR   PhylomeDB; O30033; -.
DR   EvolutionaryTrace; O30033; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00975; Exosome_Csl4; 1.
DR   InterPro; IPR039771; Csl4.
DR   InterPro; IPR019495; EXOSC1_C.
DR   InterPro; IPR025721; Exosome_cplx_N_dom.
DR   InterPro; IPR030850; Exosome_Csl4_arc.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022967; S1_dom.
DR   PANTHER; PTHR12686; PTHR12686; 1.
DR   Pfam; PF14382; ECR1_N; 1.
DR   Pfam; PF10447; EXOSC1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Exosome; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..179
FT                   /note="Exosome complex component Csl4"
FT                   /id="PRO_0000424720"
FT   DOMAIN          58..137
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT                   ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT                   ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT                   ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT                   ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT   STRAND          9..12
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          28..40
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          60..68
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          70..80
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   TURN            125..127
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:3M85"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:2BA1"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:3M7N"
FT   TURN            172..177
FT                   /evidence="ECO:0007829|PDB:3M7N"
SQ   SEQUENCE   179 AA;  19597 MW;  3106D5592EF6EAF7 CRC64;
     MRFVMPGDRI GSAEEYVKGE GVYEEGGELF AAVAGKLIIK DRVAKVESIS PIPEIVKGDV
     VLGRVVDLRN SIALIEVSSK KGENRGPSNR GIGILHVSNV DEGYVKEISE AVGYLDILKA
     RVIGDNLRLS TKEEEMGVLR ALCSNCKTEM VREGDILKCP ECGRVEKRKI STDYGKGEW
 
 
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