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RPO1C_PYRFU
ID   RPO1C_PYRFU             Reviewed;         397 AA.
AC   Q8U0M5;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE   AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000303|PubMed:21386817};
GN   Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411}; OrderedLocusNames=PF1562;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 334-371 IN COMPLEX WITH SPT4 AND
RP   SPT5.
RX   PubMed=21386817; DOI=10.1038/emboj.2011.64;
RA   Martinez-Rucobo F.W., Sainsbury S., Cheung A.C., Cramer P.;
RT   "Architecture of the RNA polymerase-Spt4/5 complex and basis of universal
RT   transcription processivity.";
RL   EMBO J. 30:1302-1310(2011).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Forms part of the jaw domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000269|PubMed:21386817}.
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_00411};
CC   -!- SUBUNIT: Part of the RNA polymerase complex (PubMed:21386817). An
CC       artificial construct of the RNAP clamp domain (including part of this
CC       protein) contacts transcription elongation factors Spt4 and Spt5
CC       (PubMed:21386817). {ECO:0000269|PubMed:21386817}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR   EMBL; AE009950; AAL81686.1; -; Genomic_DNA.
DR   RefSeq; WP_011012708.1; NZ_CP023154.1.
DR   PDB; 3QQC; X-ray; 3.30 A; A=334-371.
DR   PDBsum; 3QQC; -.
DR   AlphaFoldDB; Q8U0M5; -.
DR   SMR; Q8U0M5; -.
DR   IntAct; Q8U0M5; 1.
DR   MINT; Q8U0M5; -.
DR   STRING; 186497.PF1562; -.
DR   EnsemblBacteria; AAL81686; AAL81686; PF1562.
DR   GeneID; 41713383; -.
DR   KEGG; pfu:PF1562; -.
DR   PATRIC; fig|186497.12.peg.1628; -.
DR   eggNOG; arCOG04256; Archaea.
DR   HOGENOM; CLU_037097_1_0_2; -.
DR   OMA; TPMMTVY; -.
DR   OrthoDB; 66811at2157; -.
DR   PhylomeDB; Q8U0M5; -.
DR   EvolutionaryTrace; Q8U0M5; -.
DR   Proteomes; UP000001013; 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:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd06528; RNAP_A; 1.
DR   HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR012757; RPO1C.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT   CHAIN           1..397
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
FT                   /id="PRO_0000074022"
FT   HELIX           345..354
FT                   /evidence="ECO:0007829|PDB:3QQC"
FT   STRAND          357..359
FT                   /evidence="ECO:0007829|PDB:3QQC"
SQ   SEQUENCE   397 AA;  44404 MW;  19D46E356CA0E49F CRC64;
     MVSLSTIKSL IEKKGANLPE NVKSELYEKL KKYNEKYKLT KAEIEAIIDD VVKEYERALV
     EPGEPVGTVA AQSIGEPSTQ MTLNTFHYAG VAEINVTLGL PRIIEIVDAR KNPSTPMMTV
     YLDEEHRYDR AKAEEVARRI EGTTLENLAR STTLDLINFE FIVEIDPERL ERSGLTMEKV
     VKKLESSFKS AEFEVDGYTL IVRPKKADKI SDLRRFAEKI KKHRLKGLSG VGKTIVRKEG
     DEYVIYTEGS NFKQVLKVPG VDPTRTRTNN IHEIAEVLGI EAARNAIIDE IVSTMQEQGL
     EVDIRHIMLV ADMMTLDGIV RPIGRHGVVG EKSSVLARAA FEITVQHLFE AAEKGEVDNL
     NGVIENVLIG QPVPVGTGMV KLTMKLPLRP QKEKEEV
 
 
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