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RPOC_METEP
ID   RPOC_METEP              Reviewed;        1405 AA.
AC   A9W8N9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; OrderedLocusNames=Mext_4018;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) 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}.
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DR   EMBL; CP000908; ABY32388.1; -; Genomic_DNA.
DR   RefSeq; WP_012255172.1; NC_010172.1.
DR   AlphaFoldDB; A9W8N9; -.
DR   SMR; A9W8N9; -.
DR   STRING; 419610.Mext_4018; -.
DR   EnsemblBacteria; ABY32388; ABY32388; Mext_4018.
DR   KEGG; mex:Mext_4018; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   BioCyc; MEXT419610:MEXT_RS20180-MON; -.
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; Transcription; Transferase; Zinc.
FT   CHAIN           1..1405
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_1000141780"
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   1405 AA;  154860 MW;  1AD790FCE45C7497 CRC64;
     MNQEVMNLFN QQAQPQSFDQ IKISISSPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
     RIFGPIKDYE CLCGKYKRMK YKGVICEKCG VEVTLARVRR DRMGHIELAA PVAHIWFLKS
     LPSRIGLLLD MALKDLERIL YFESYVVIEP GLTPLKERQL LSEEEYLRAQ EEYGEDSFTA
     MIGAEAIRRI LMELDLEGIA TSLKEEIATT TSELKPKKLM KRLKIIEAFQ LSGNKPEWMI
     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 GLYYLSIVAD GSVGEHKADD KNNPMQGVFG
     DIGQLEHALA AKSVSLHSKI KWRWRGLGPD GEPVSRIYDT TPGRVILSGV LPMHPKVPFD
     VVNKLMTKKE ISAMIDTVYR HCGQKESVIF CDRIMALGFS HAFKAGISFG KDDMVVPENK
     WSIVEDTRTL VKDYEQQYND GLITQGEKYN KVVDAWAKCS DKLAAEMMGR ISAVQKDENG
     ADKQVNSIYM MSHSGARGSP AQMKQLAAMR GLMAKPSGEI IETPIISNFK EGLDVLEYFN
     STHGARKGLA DTALKTANSG YLTRRLVDVA QDAVIREVDC GTTNGIKMRA IIDAGQVVAP
     LSIRILGRAT AEDLVAQDGT VIVKTNETIE ERHLPAINAA GIQEVKIRSV LVCQTKSGVC
     ATCYGRDLAR GTPVNMGEAV GVIAAQSIGE PGTQLTMRTF HIGGAAQIAD SSFVESSFEG
     TIKIRNRSLA KNSDGDLIAT GRSVAVVIVG PDGTERAVHR LQYGARVRVD EGDTIKRGQR
     IAEWDPYTRP IVAEVDGIVG YEDLYDGQSI TETTDESTGI AKRVVIDWRG SSRTSDLKPA
     MLVLDQDGKP VKLARGSDAR YYLPVDAIIG LDPGAKVRAG DVLARVSTDS AKTRDITGGL
     PRVAELFEAR RPKDAAIIAE KSGSIAFGRD YKNKRRLTLT PHDGSDAVEY LIPKGKHIHL
     QDGDVVELGD YIVDGNPAPH DILAIKGVEE LAAYLVNEIQ EVYRLQGVSI NDKHIEVIVR
     QMLQKVEITD GGDSDILTGD QIDRTELADF NEKLLAEGKK PIQGVPVLLG ITKASLQTKS
     FISAASFQET TRVLTEAAVN GKVDTLDGLK ENVIVGSLIP AGTGSLAADI RSIARRRDNL
     ILQQRSAENA ANAAELSELP PAAAE
 
 
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