(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHQ7_GEOS0

ID   A0A0F6BHQ7_GEOS0        Unreviewed;      1190 AA.
AC   A0A0F6BHQ7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 32.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
DE            Short=RNAP subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000256|HAMAP-Rule:MF_01321};
GN   OrderedLocusNames=GY4MC1_0102 {ECO:0000313|EMBL:ADP72958.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72958.1};
RN   [1] {ECO:0000313|EMBL:ADP72958.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72958.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
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:0000256|HAMAP-Rule:MF_01321,
CC         ECO:0000256|RuleBase:RU363031};
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:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU000434}.
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DR   EMBL; CP002293; ADP72958.1; -; Genomic_DNA.
DR   RefSeq; WP_003247543.1; NC_014650.1.
DR   EnsemblBacteria; ADP72958; ADP72958; GY4MC1_0102.
DR   KEGG; gmc:GY4MC1_0102; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   BioCyc; GSP581103:G1GOQ-129-MONOMER; -.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHQ7.
DR   SWISS-2DPAGE; A0A0F6BHQ7.
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031, ECO:0000313|EMBL:ADP72958.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01321,
KW   ECO:0000256|RuleBase:RU363031}.
FT   DOMAIN          28..454
FT                   /note="RNA_pol_Rpb2_1"
FT                   /evidence="ECO:0000259|Pfam:PF04563"
FT   DOMAIN          140..290
FT                   /note="RNA_pol_Rpb2_2"
FT                   /evidence="ECO:0000259|Pfam:PF04561"
FT   DOMAIN          374..410
FT                   /note="RNA_pol_Rpb2_2"
FT                   /evidence="ECO:0000259|Pfam:PF04561"
FT   DOMAIN          469..537
FT                   /note="RNA_pol_Rpb2_3"
FT                   /evidence="ECO:0000259|Pfam:PF04565"
FT   DOMAIN          547..614
FT                   /note="RNA_pol_Rpb2_45"
FT                   /evidence="ECO:0000259|Pfam:PF10385"
FT   DOMAIN          676..1069
FT                   /note="RNA_pol_Rpb2_6"
FT                   /evidence="ECO:0000259|Pfam:PF00562"
FT   DOMAIN          1071..1146
FT                   /note="RNA_pol_Rpb2_7"
FT                   /evidence="ECO:0000259|Pfam:PF04560"
FT   REGION          1153..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1190
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1190 AA;  133521 MW;  A3D99C5B05F89B1C CRC64;
     MTGRLVQYGR HRQRRSYARI SEVLELPNLI EIQTSSYKWF LDEGLREMFR EISPIEDFSG
     NLSLEFIDYS LGEPKYTVEE AKERDVTYAA PLRVKVRLIN KETGEVKEQD VFMGDFPLMT
     ETGTFIINGA ERVIVSQLVR SPSVYYSEKV DKNGKRGFSA TVIPNRGAWL EYETDAKDVV
     YVRIDRTRKL PVTVLLRALG FGSDQEIIDL IGDNEYLRNT LEKDNTDSTE KALIEIYERL
     RPGEPPTIEN AKNLLISRFF DPKRYDLASV GRYKINKKLH IKNRLFNQRL AETLVDPETG
     EVIAEKGTIV DRRTLNRILP YLENGVGLRV HKPFGGVVEE EIALQSIKIY APNDPDGEQV
     INVISNGYIA EDVKHITPAD IIASISYFFN LLHGVGDTDD IDHLGNRRLR SVGELLQNQF
     RIGLSRMERV VRERMSIQDT NTITPQQLIN IRPVIAAIKE FFGSSQLSQF MDQTNPLAEL
     THKRRLSALG PGGLTRERAG FEVRDVHYSH YGRMCPIETP EGPNIGLINS LSTYAKVNKF
     GFIETPYRRV DPETGRVTDQ IDYLTADEED NYVVAQANVP LAEDGTFLEE NVVARFRGEN
     IVVKRDRVDY MDVSPKQVVS AATACIPFLE NDDSNRALMG ANMQRQAVPL LEPEAPIVGT
     GMEYVSARDS GAAVICKHRG IVERVEAKEI WVRRLIEVDG KEVKGDLDKY RLLKFVRSNQ
     GTCYNQRPIV KKGDIVEKGE ILADGPSMDK GELALGRNVL VAFMTWDGYN YEDAIIMSER
     LVKEDVYTSI HIEEYEAESR DTKLGPEEIT RDIPNVGEDA LKNLDERGIV RIGAEVKDGD
     LLVGKVTPKG MTELTAEERL LHAIFGEKAR EVRDTSLRVP HGGGGIVLDV KVFNREDGDE
     LPPGVNQLVR VYIVQKRKIS EGDKMAGRHG NKGVISRILP EEDMPFLPDG TPIDIMLNPL
     GVPSRMNIGQ VFELHLGMAA KKLGLHIASP VFDGATEEDV WNILEEAGMP RDAKTVLYDG
     RTGEPFDNRV SVGIMYMIKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV
     WALEAYGAAY TLQEILTVKS DDVVGRVKTY EAIVKGENIP EPGVPESFKV LIKELQSLGM
     DVTILTSDEK EINMENFDEE DDVHSADSLV PEVKSAEDEK AGKKGVATKE
//

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