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RPO10_METAC
ID   RPO10_METAC             Reviewed;          62 AA.
AC   Q8TT41;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=MA_0598;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM04042.1; -; Genomic_DNA.
DR   RefSeq; WP_011020647.1; NC_003552.1.
DR   AlphaFoldDB; Q8TT41; -.
DR   SMR; Q8TT41; -.
DR   STRING; 188937.MA_0598; -.
DR   EnsemblBacteria; AAM04042; AAM04042; MA_0598.
DR   GeneID; 1472490; -.
DR   KEGG; mac:MA_0598; -.
DR   HOGENOM; CLU_143122_2_1_2; -.
DR   InParanoid; Q8TT41; -.
DR   OMA; YCCRRMF; -.
DR   OrthoDB; 123859at2157; -.
DR   PhylomeDB; Q8TT41; -.
DR   Proteomes; UP000002487; 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   3: Inferred from homology;
KW   Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..62
FT                   /note="DNA-directed RNA polymerase subunit Rpo10"
FT                   /id="PRO_0000121348"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00250"
FT   BINDING         43
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"
SQ   SEQUENCE   62 AA;  7163 MW;  D23C62EADB6675C7 CRC64;
     MIPVRCFSCG KVISNYWDEY KRRVTDGEGS AAVLDDLGIT RYCCRRMFLS HVELVDVLSP
     YQ
 
 
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