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Database: UniProt
Entry: A7HCH6
LinkDB: A7HCH6
Original site: A7HCH6 
ID   RPOC_ANADF              Reviewed;        1395 AA.
AC   A7HCH6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   14-MAY-2014, entry version 47.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta';
DE            Short=RNAP subunit beta';
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase subunit beta';
DE   AltName: Full=Transcriptase subunit beta';
GN   Name=rpoC; OrderedLocusNames=Anae109_2220;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Fields M., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter sp. Fw109-5.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1
CC       beta' and 1 omega subunit. When a sigma factor is associated with
CC       the core the holoenzyme is formed, which can initiate
CC       transcription (By similarity).
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
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DR   EMBL; CP000769; ABS26422.1; -; Genomic_DNA.
DR   RefSeq; YP_001379406.1; NC_009675.1.
DR   ProteinModelPortal; A7HCH6; -.
DR   SMR; A7HCH6; 20-167.
DR   STRING; 404589.Anae109_2220; -.
DR   PRIDE; A7HCH6; -.
DR   EnsemblBacteria; ABS26422; ABS26422; Anae109_2220.
DR   GeneID; 5377390; -.
DR   KEGG; afw:Anae109_2220; -.
DR   PATRIC; 20929711; VBIAnaSp113478_2328.
DR   eggNOG; COG0086; -.
DR   HOGENOM; HOG000218386; -.
DR   KO; K03046; -.
DR   OMA; AYDSEFL; -.
DR   OrthoDB; EOG6M9DS6; -.
DR   BioCyc; ASP404589:GHMT-2236-MONOMER; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime.
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; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
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   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN         1   1395       DNA-directed RNA polymerase subunit
FT                                beta'.
FT                                /FTId=PRO_0000353287.
SQ   SEQUENCE   1395 AA;  155080 MW;  3D8761B7DEA1A1F3 CRC64;
     MKDIFNFFEK PKDPLSFSAI RISLASPDKI RQWSHGEVKK PETINYRTFK PERDGLFCAK
     IFGPVKDYEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RLGHITLATP VAHIWFLKSL
     PSRIGNLLDI TLKDLEKVLY CESYIVIDPK ETTLQRGELL SEDRYHKSME EFGEEAFLAG
     MGGEAVLELL KVVGPADKGH GEGVHGLADE LRAQMKEATS DAKRKKIAKR LKVVEAFVQS
     GNKPDWMMLE VIPVIPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLQELNAPDI
     IIRNEKRMLQ EAVDALFDNG RRGKTITGPN KRPLKSLSDM LKGKQGRFRQ NLLGKRVDYS
     GRSVIVVGPE LKLHQCGLPK IMALELFKPF IYNKLEEKGY VTTIKSAKKM VEKERPEVWD
     ILDEVIREHP VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV
     PLSIEAQMEA RVLMMSTNNI LSPAHGKPII VPSQDIVLGI YYMTRERAFA RGEGKVFASE
     EEVRAAYDQG EVDLQAKIWV RLDGKRVETT VGRVLLYDIV PKRLPFESIN KVMDKKQLQN
     LIDLTYRLCG EKETVLLADR VRSMGYGNAT RAGISIALEN MIIPRKKQEL LERAMGEVDD
     IQTQYTEGLI TIGERYNKVI DIWAQVTEEV AQEMMSQIGQ ETAIGTGKDG KREERKQPSF
     NPIYIMADSG ARGSAQQIRQ LAGMRGLMAK PSGEIIETPI TANFREGLNV LQYFISTHGA
     RKGLADTALK TANSGYLTRR LVDVAQDAII TEYDCGAMDG ITLGALVEGG EIIEPMGERI
     LGRVALDDIH DPFASSVLVK ANEEIDESKV KLIENAGIDK VKIRSVLTCQ ARRGICVECY
     GRDLARGRKV NIGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRRAEQST IENRNPGLVK
     FHNVAVAKKK DGTLIVMNRN GEIIVTDDQG RERERYGVVY GAKLLVRDGQ KIETSTLLAE
     WDPYSMPIIT EVAGHVKYGD LVDGVTISEQ VDEITGLARK AVIASKDPDA RPRISIKDDQ
     GKTRKLANSE ADARYMLPEG ANLVVNDGDE VDAGDVIAKM PRETTKTKDI TGGLPRVAEL
     FEARKPKEHA VISEIDGVVA FGKDTKGKRK VVITPEVDGK LRPDLAKEYL IGKGKHISVH
     TGDRVRAGEA LMDGAANPHD ILRVLGEKEL ARWLVDEVQE VYRLQGVKIN DKHIETIVRQ
     MLRRVRIVDV GDTNFLADEQ VEKFVFEEEN DKVITAGGRP AQGEPLLLGI TKASLSTESF
     ISASSFQETT KVLTEAAISG KVDHLRGLKE NVIMGRLIPA GTGLPHYKHL DIEVETPVDA
     VEEAEEALAV ASGEE
//
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