位置:首页 > 蛋白库 > RPOC_METRJ
RPOC_METRJ
ID   RPOC_METRJ              Reviewed;        1403 AA.
AC   B1LY42;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
GN   OrderedLocusNames=Mrad2831_3838;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001001; ACB25813.1; -; Genomic_DNA.
DR   RefSeq; WP_012320771.1; NC_010505.1.
DR   AlphaFoldDB; B1LY42; -.
DR   SMR; B1LY42; -.
DR   STRING; 426355.Mrad2831_3838; -.
DR   EnsemblBacteria; ACB25813; ACB25813; Mrad2831_3838.
DR   KEGG; mrd:Mrad2831_3838; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000006589; Chromosome.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1403
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_1000141782"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         820
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         893
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1403 AA;  154555 MW;  B0D691DC928C2B5E CRC64;
     MNQEVMNLFN QQAQPVSFDQ IKISISSPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
     RIFGPIKDYE CLCGKYKRMK YKGVICEKCG VEVTLARVRR DRMGHIELAA PVAHIWFLKS
     LPSRIGLLLD MALKDLERIL YFESYCVIEP GLTPLKERQL LSEEEYLRAQ EEYGEDSFTA
     MIGAEAIRRI LQELDLDKIA NDLREEIAVT TSELKPKKLL KRLKIIEAFQ MSGNKPEWMI
     LTVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP DIIIRNEKRM
     LQEAVDALFD NGRRGRVITG ANKRPLKSLA DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
     PELKLHQCGL PKKMALELFK PFIYARLDAK GFSATVKQAK KLVEKEKPEV WDILDEVIRE
     HPVMLNRAPT LHRLGIQAFE PKLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQL
     EARVLMMSTN NILHPANGQP IIVPSQDIVL GLYYLSIVAE GAPGEYKPDN AKNPMQGVYG
     DMGELEHALA AKAVSLHSKI KWRWTGIGPD GEPLTKTYET TPGRVILSGA LPKHAKVPFD
     VVNKLMTKKE ISAMIDTVYR HCGQKESVIF CDRIMALGFN HAFKAGISFG KDDMVVPENK
     WSIVDTTRAL VKDYEQQYND GLITQGEKYN KVVDAWAKCS DKLAAEMMGR ISSVQKDEKG
     ADKQVNSIYM MSHSGARGSP AQMKQLAAMR GLMAKPSGEI IETPIISNFK EGLDVLEYFN
     STHGARKGLA DTALKTANSG YLTRRLVDVA QDAVIREVDC GTTSGIKMRA IVDAGQVVAT
     LATRILGRAT AEDLVAADGT VIVKTGETIE ERHLPAINAA GIQEVKIRSV LVCATKSGVC
     ATCYGRDLAR GTPVNMGEAV GVIAAQSIGE PGTQLTMRTF HIGGAAQIAD SSFIESSFEG
     TIKIRNRAVA KNTDGDLIAT GRNVAVVIVG SDGVERAVHR LQYGAKLRVD EGDKIKRGQR
     IAEWDPYTRP ILTEVDGIVA YEDLVDGQSM TETTDESTGI AKRVVVDWRG SARTSDLKPA
     MVVVDRDGKA LKLPRGSDAR YFLPVDAIIG FDPGATVKAG DILARVSTDS AKTRDITGGL
     PRVAELFEAR RPKDAAIIAE KSGTIAFGRD YKNKRRLTLT PHDGSEAVEY LIPKGKHIHL
     QDGDVVELGD YIVDGNPAPH DILAIKGVEE LAAYLVNEIQ EVYRLQGVSI NDKHIEVIVR
     QMLQKVEVTD GGDSDILSGD QIDRTELTDY NEKLLAEGKK PIQGVPVLLG ITKASLQTKS
     FISAASFQET TRVLTEAAVN GKVDTLEGLK ENVIVGSLIP AGTGSMVADI RSIARRRDAM
     ILQQKQAESG AMPVEELPPA AAE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024