RPOB_MORIN
ID RPOB_MORIN Reviewed; 1070 AA.
AC Q09X25;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=MoinCp013;
OS Morus indica (Mulberry).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Morus.
OX NCBI_TaxID=248361;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. K2;
RA Ravi V., Khurana J.P., Tyagi A.K., Khurana P.;
RT "The chloroplast genome of mulberry: structural features and comparative
RT analysis.";
RL Submitted (SEP-2005) 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_01321}.
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_01321};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; DQ226511; ABB20950.1; -; Genomic_DNA.
DR RefSeq; YP_762253.1; NC_008359.1.
DR AlphaFoldDB; Q09X25; -.
DR SMR; Q09X25; -.
DR PRIDE; Q09X25; -.
DR GeneID; 4290596; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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: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; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
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; 3.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..1070
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000276592"
SQ SEQUENCE 1070 AA; 121066 MW; 253AE4A3D4DF5383 CRC64;
MLEGGNEEIS TIPGFNQIQF EGFCRFIDQG LTEELYKFPK IEDTDQEIEF QLFVETYQLV
EPLIKERDAV YESLTYSSEL YVSAGLIWKT SRDMQEQTIF IGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRLEL EIDRKARIWA RVSRKQKISI
LVLLSAMGLN LREILENVCY PEIFLSFLKD KEKKKIKSKE NAILEFYQQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNRRL NLDIPQNTTF LLPRDILAAA DHLIGMKFGM
GILDDMNHLK NKRIRSVADL LQDQFGLALV RLENMVRGTM CGAIRHKLIP TPQNLVTSTT
LTTTYESFFG LHPLSQVLDR TNPLTQIVHG RKASYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGHWGSL ESPFYEISER SKKVRMLYLS PSIDEYYMVA
AGNSLALNRG SQEEQVVPAR YRQEFLTIEW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSRSEK CIVGTGLECQ VALDSGVPTI AEHQGKIIYT DTEKIILSGN
RDTLSIPLVI YQRSNKNTCM HQKPQVSRGK CIKKGQILAD GAATVGGELA LGKNVLVAYM
PWEGYNSEDA VLINERLVYE DIYTSFHIRK YEIHTHVTSH GPERITNEIP HLEAHLLRNL
DKNGIVMLGS WVETGDILVG KLTPQMAKES SYAPEDRLLR AILGIQISIS KETCLKLPIG
GRGRVIDVRW IQKKGGSSYN PETIRVYISQ KREIKVGDKV AGRHGNKGIV SKILPRQDMP
YLQDGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGGLLDR HYRIAPFDER YEQEASRKLV
FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGDPFEQPV IIGKPYILKL IHQVDDKIHG
RCSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
GTTMVGGPIP KPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINRKDV