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RPO10_THEKO
ID   RPO10_THEKO             Reviewed;          65 AA.
AC   Q5JJC9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00250};
DE   AltName: Full=DNA-directed RNA polymerase subunit N {ECO:0000255|HAMAP-Rule:MF_00250};
GN   Name=rpo10 {ECO:0000255|HAMAP-Rule:MF_00250};
GN   Synonyms=rpoN {ECO:0000255|HAMAP-Rule:MF_00250}; OrderedLocusNames=TK1499;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_00250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00250};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00250};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC       polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00250}.
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DR   EMBL; AP006878; BAD85688.1; -; Genomic_DNA.
DR   RefSeq; WP_011250450.1; NC_006624.1.
DR   PDB; 4QIW; X-ray; 3.50 A; N/V=1-65.
DR   PDB; 6KF3; EM; 3.90 A; N=1-65.
DR   PDB; 6KF4; EM; 3.97 A; N=1-65.
DR   PDB; 6KF9; EM; 3.79 A; N=1-65.
DR   PDBsum; 4QIW; -.
DR   PDBsum; 6KF3; -.
DR   PDBsum; 6KF4; -.
DR   PDBsum; 6KF9; -.
DR   AlphaFoldDB; Q5JJC9; -.
DR   SMR; Q5JJC9; -.
DR   STRING; 69014.TK1499; -.
DR   PRIDE; Q5JJC9; -.
DR   EnsemblBacteria; BAD85688; BAD85688; TK1499.
DR   GeneID; 7418657; -.
DR   KEGG; tko:TK1499; -.
DR   PATRIC; fig|69014.16.peg.1459; -.
DR   eggNOG; arCOG04244; Archaea.
DR   HOGENOM; CLU_143122_1_1_2; -.
DR   InParanoid; Q5JJC9; -.
DR   OMA; YCCRRMF; -.
DR   OrthoDB; 123859at2157; -.
DR   PhylomeDB; Q5JJC9; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00250; RNApol_arch_Rpo10; 1.
DR   InterPro; IPR023580; RNA_pol_su_RPB10.
DR   InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR   InterPro; IPR000268; RPABC5/Rpb10.
DR   PANTHER; PTHR23431; PTHR23431; 1.
DR   Pfam; PF01194; RNA_pol_N; 1.
DR   PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1.
DR   SUPFAM; SSF46924; SSF46924; 1.
DR   PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..65
FT                   /note="DNA-directed RNA polymerase subunit Rpo10"
FT                   /id="PRO_0000121360"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   HELIX           31..37
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:4QIW"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:4QIW"
SQ   SEQUENCE   65 AA;  7590 MW;  72635A4FE75AA221 CRC64;
     MIVPVRCFTC GKVLADKYYE FKKRVEAGED PGKVLDDLGV ERYCCRRTLL SHVELIDQVM
     VYKVY
 
 
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