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Entry: RPOC_MYCA1
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ID   RPOC_MYCA1              Reviewed;        1316 AA.
AC   A0QL48;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   14-MAY-2014, entry version 50.
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=MAV_4502;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000479; ABK69395.1; -; Genomic_DNA.
DR   RefSeq; YP_883636.1; NC_008595.1.
DR   ProteinModelPortal; A0QL48; -.
DR   SMR; A0QL48; 9-136.
DR   STRING; 243243.MAV_4502; -.
DR   PRIDE; A0QL48; -.
DR   EnsemblBacteria; ABK69395; ABK69395; MAV_4502.
DR   GeneID; 4529592; -.
DR   KEGG; mav:MAV_4502; -.
DR   PATRIC; 17990697; VBIMycAvi38287_4422.
DR   eggNOG; COG0086; -.
DR   HOGENOM; HOG000218386; -.
DR   KO; K03046; -.
DR   OMA; IWNTFTK; -.
DR   OrthoDB; EOG6M9DS6; -.
DR   BioCyc; MAVI243243:GH3Y-4502-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   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   1316       DNA-directed RNA polymerase subunit
FT                                beta'.
FT                                /FTId=PRO_0000308853.
SQ   SEQUENCE   1316 AA;  147028 MW;  88C8A6CB695B4254 CRC64;
     MLDVNFFDEL RIGLATAEDI RQWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPTRDWEC
     YCGKYKRVRF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
     APKDLEKIIY FAAYVITSVD EEMRHNELST LEAEMMVERK AVEDQRDADL EARAQKLEAD
     LAELEAEGAK ADARRKVRDS GEREMRQIRD RAQRELDRLE DIWNTFTKLA PKQLIVDENL
     YRELVDRYGE YFTGAMGAES IQKLIENFDI DAEAEQLRDV IRNGKGQKKL RALKRLKVVA
     AFQQSGNSPM GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLIDL
     GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
     RVDYSGRSVI VVGPQLKLHQ CGLPKLMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERQR
     PQVWDVLEEV IAEHPVLLNR APTLHRLGIQ AFEPMLVEGK AIQLHPLVCE AFNADFDGDQ
     MAVHLPLSAE AQAEARILML SSNNILSPAS GRPLAMPRLD MVTGLYYLTT EVEGDKGEYR
     PAAKDTPEVG VYSSPAEAIM AADRGVLSVR AKIKVRLTQL RPPAEIEAEL FGANGWQPGD
     AWMAETTLGR VLFNELLPVG YPFVNKQMHK KVQASIINDL AERYPMIVVA QTVDKLKDAG
     FYWATRSGVT VSMADVLVPP RKKEILDQYE ERAEKVEKQF QRGALNHDER NEALVEIWKE
     ATDEVGQALR EHYPADNPII TIVDSGATGN FTQTRTLAGM KGLVTNPKGE FIPRPVKSSF
     REGLTVLEYF INTHGARKGL ADTALRTADS GYLTRRLVDV SQDVIVREHD CETERGIVVE
     LAERQPDGTL IRDPYIETSA YARTLGTDAV DEAGNVIVAR GEDLGDPEID ALLAAGITSV
     KVRSVLTCTT GTGVCATCYG RSMATGKLVD IGEAVGIVAA QSIGEPGTQL TMRTFHQGGV
     GEDITGGLPR VQELFEARIP RGKAPIADVT GRVRLEDGER FYKITIVPDD GSEEVVYDKL
     SKRQRLRVFK HEDGSERVLS DGDHVEVGQQ LMEGSADPHE VLRVQGPREV QIHLVREVQE
     VYRAQGVSIH DKHIEVIVRQ MLRRVTIIDS GSTEFLPGSL IDRAEFEAEN RRVVAEGGEP
     AAGRPVLMGI TKASLATDSW LSAASFQETT RVLTDAAINC RSDKLNGLKE NVIIGKLIPA
     GTGINRYRNI QVQPTEEARA AAYTIPSYED QYYSPDFGQA TGAAVPLDDY GYSDYR
//
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