(data stored in ACNUC7421 zone)

SWISSPROT: RPOC_RHILO

ID   RPOC_RHILO              Reviewed;        1398 AA.
AC   Q98N65;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=mlr0277;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
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}.
DR   EMBL; BA000012; BAB47897.1; -; Genomic_DNA.
DR   RefSeq; WP_010909267.1; NC_002678.2.
DR   SMR; Q98N65; -.
DR   STRING; 266835.14021284; -.
DR   PRIDE; Q98N65; -.
DR   EnsemblBacteria; BAB47897; BAB47897; BAB47897.
DR   KEGG; mlo:mlr0277; -.
DR   eggNOG; ENOG4105D27; Bacteria.
DR   eggNOG; COG0086; LUCA.
DR   HOGENOM; HOG000218386; -.
DR   KO; K03046; -.
DR   OMA; QGVEIND; -.
DR   OrthoDB; 4421at2; -.
DR   BioCyc; MLOT266835:G1G20-220-MONOMER; -.
DR   Proteomes; UP000000552; Chromosome.
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   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; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
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;
DR   PRODOM; Q98N65.
DR   SWISS-2DPAGE; Q98N65.
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1398
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067782"
FT   METAL           71
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           73
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           86
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           89
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           462
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           464
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           466
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           810
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           884
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           891
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           894
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1398 AA;  155101 MW;  D5DD7A297B62449A CRC64;
     MNQEVMNLFN PQAPAQVFDS IRISLASPEK ILSWSFGEIK KPETINYRTF KPERDGLFCA
     RIFGPIKDYE CLCGKYKRMK YKGVICEKCG VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
     LPSRIGTLLD MTLKDIERVL YFENYIVTEP GLTALKEHQL LSEEEYMIAV DEYGEDSFTA
     MIGAEAIHDL LAGMDLEKIA GDLRSELAST TSELKQKKYL KRLKVVENFM ESGNRPEWMI
     MKVVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP GIIVRNEKRM
     LQEAVDALFD NGRRGRVITG ANKRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVTG
     PELKLHQCGL PKKMALELFK PFIYARLDAK GYSSTVKQAK KLVEKERPEV WDILDEVIRE
     HPVLLNRAPT LHRLGIQAFE PILIEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLSLEAQL
     EARVLMMSTN NILHPASGAP IIVPSQDMVL GLYYLSIVNQ NEPGEGMVFA DMGELQHALE
     TKAVTLHAKI KGRFRTVDAE GKVVSKIHDT TPGRMIIGEL LPKNVNVPYE TANQEMTKKN
     ISKMIDTVYR HCGQKETVIF CDRIMALGFA HACRAGISFG KDDMLIPDSK IKLVSDTEAL
     AKEYEQQYND GLITQGEKYN KVVDAWAKCS EKVADEMMAR IKAVEFEDNG RQKPMNSIYM
     MSHSGARGSP TQMRQLAGMR GLMAKPSGEI IETPIISNFK EGLTVLEYFN STHGARKGLA
     DTALKTANSG YLTRRLVDVA QDCIVNSVDC GTDKGLTMQP IVDAGQVVAS VGQRVLGRTA
     LDDINHPVTG DLLVKAGTLM DERDVEQIEK AGVQSVRIRS ALTCEVRVGV CAVCYGRDLA
     RGTPVNQGEA VGVIAAQSIG EPGTQLTMRT FHMGGTAQVV DSSFLEASYE GKVEIRNRNV
     VRNSDGQQMV MGRNMAVLIL DEAGKERATH RVTYGSRIFV DDGDKVKRGQ RIAEWDPYTR
     PILTEIEGRV AFEDLVDGIS VQETADESTG ITKREVIDWR STPRGNDLKP AIVVQDAKGK
     VGKLSKGGDA RFLLSVEAIL SVEPGAQVRP GDVLARIPME SAKTKDITGG LPRVAELFEA
     RRPKDHAIIA EIDGTIRFGR DYKNKRRIII EPHDSTLEPV EYLIPKGKPF HLQDGDVIEK
     GDYILDGNPA PHDILAIKGV EALASYLVNE IQEVYRLQGV SINDKHIEVI VRQMLQKVEI
     TTQGDSTYIP GDHVDVIELE EVNERLIEDG KKPAEGQPVL LGITKASLQT PSFISAASFQ
     ETTRVLTEAA VAGKTDMLQG LKENVIVGRL IPAGTGGTMS QIRRIATSRD ELIIDERRKA
     SGVEVAEPML ADMTTAAQ
//

If you have problems or comments...

PBIL Back to PBIL home page