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RPOC_ACIET
ID   RPOC_ACIET              Reviewed;        1409 AA.
AC   B9MH46;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Dtpsy_3245;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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; CP001392; ACM34674.1; -; Genomic_DNA.
DR   RefSeq; WP_015914491.1; NC_011992.1.
DR   AlphaFoldDB; B9MH46; -.
DR   SMR; B9MH46; -.
DR   STRING; 535289.Dtpsy_3245; -.
DR   EnsemblBacteria; ACM34674; ACM34674; Dtpsy_3245.
DR   KEGG; dia:Dtpsy_3245; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_4; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000000450; 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; -; 1.
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; 2.
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..1409
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_1000165841"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         813
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         894
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1409 AA;  154551 MW;  23667255DC921748 CRC64;
     MKSLLDLFKQ FTPDEHFDAI KIGMASPEKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
     IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIDLAAP CAHIWFLKSL
     PSRLGLVLDM TLRDIERVLY FEAYVVTDPG MTPLKKFGIM SEDDYDAKRK EYGDEFVAKM
     GAEGIKELLE GIDIEIEIEK LRGDLTGSEV KVKKNAKRLK VLEAFKKSGI KPEWMILEVL
     PVLPPDLRPL VPLDGGRFAT SDLNDLYRRV INRNSRLRRL LELKAPEIIA RNEKRMLQEA
     VDSLLDNGRR GKAMTGANKR ALKSLADMIK GKSGRFRQNL LGKRVDYSGR SVITVGPTLK
     LHQCGLPKLM ALELFKPFIF SRLEAMGIAT TIKAAKKEVE AGTPVVWDIL EEVIKEHPVM
     LNRAPTLHRL GIQAFEPILI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL SVEAQLEART
     LMLASNNVLF PASGEPSIVP SQDVVLGLYH ATREKINGKG EGLVFADTGE VQRALDAGEA
     ELHAKISVRL TEWTKDKATG EFVPETKLVD TTVGRALLSE ILPKGLPFSN LNKALKKKEI
     SKLINASFRK CGLKDTVVFA DKLLQNGFRL ATHAGFSVAI DDMLVPPQKA EILARAEAEV
     KEIEQQYVSG LVTAGERYNK VVDIWGKAGD DVSKVMMDQL KVQKTIDRNG KEVNEESFNA
     IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ YFISTHGARK
     GLADTALKTA NSGYLTRRLV DVTQDLVVTE DDCGTSNGSL MRAIVEGGEV IESLRDRILG
     RTAAEEVLHP ETRAVLAQPG RMLDEDLIEE LEAAGVDEVK VRTALTCETR YGLCAKCYGR
     DLGRGGLINL GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRAAVASSVE AKSNGIIGFN
     ATMRYVTNTK GELVVIARSG EIIIQDEHGR ERERHKVPYG ATLTVKADQT IKAGTILANW
     DPLTRPIITE YAGTVKFENV EEGLTVAKQV DEVTGLSTLV VIDPKRRGSA KVVRPQVKLV
     DADGKEVKIP GTDHSVTIGF QVGALIQVRD GQEVGPGEVL ARIPMEGQKT RDITGGLPRV
     AELFEARSPK DKGMLAEMTG TISFGKETKG KVRLQITDPD GKVWDELVPK EKNVLVHEGQ
     VVNKGELIVD GPADPQDILR LLGIEELSRY IVDEVQDVYR LQGVKINDKH IEVIVRQMLR
     RVVVENPGES TYIAGEQVER SEILNTNEAL QAEGKLPATY SNVLLGITKA SLSTDSFISA
     ASFQETTRVL TEAAIMGKRD ELRGLKENVI VGRLIPAGTG LAYHQARKAK DAMDEAERRA
     IADAEAAELA SAGTDDAAAE IDGSADTAD
 
 
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