RPOB_SACHY
ID RPOB_SACHY Reviewed; 1075 AA.
AC Q6L3A7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 80.
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=PS106;
OS Saccharum hybrid (Sugarcane).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum;
OC unclassified Saccharum.
OX NCBI_TaxID=15819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC STRAIN=cv. SP-80-3280;
RX PubMed=15526204; DOI=10.1007/s00294-004-0542-4;
RA Calsa T. Jr., Carraro D.M., Benatti M.R., Barbosa A.C., Kitajima J.P.,
RA Carrer H.;
RT "Structural features and transcript-editing analysis of sugarcane
RT (Saccharum officinarum L.) chloroplast genome.";
RL Curr. Genet. 46:366-373(2004).
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 -!- RNA EDITING: Modified_positions=156 {ECO:0000269|PubMed:15526204}, 182
CC {ECO:0000269|PubMed:15526204}, 187 {ECO:0000269|PubMed:15526204}, 206
CC {ECO:0000269|PubMed:15526204};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AE009947; AAT44685.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q6L3A7; -.
DR SMR; Q6L3A7; -.
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; -; 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; 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 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW RNA editing; Transcription; Transferase.
FT CHAIN 1..1075
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048044"
SQ SEQUENCE 1075 AA; 121632 MW; 4D2AA884A3BD9BBD CRC64;
MLRNGNEGMS TIPGFSQIQF EGFCRFINQG LAEELEKFPT IKDPDHEIAF QLFAKGYQLL
EPSIKERNAV YESLTYSSEL YVSARLIFGF DVQKQTISIG NIPIMNSLGT FIINGIYRIV
INQILLSPGI YYRSELDHKG ISICTGTIIS DWGGRLELAI DKKERIWARV SRKQKISILV
LLSAMGLNLR EILDNVSYPE IFLSFLNAKE KKRIESKEKA ILEFYQQFAC VGGDLVFSES
LCEELQKKFF QQKCELGRVG RRNMNRRLNL DIPQNNTFLL PRDVLAATDH LIGMKFGTGI
LDDDDMNHLK NKRIRSVADL LQDQFGLALG RLQHAVQKTI RRVFIRQSKP TPQTLVTPTS
TSILLITTYE TFFGTYPLAQ VFDQTNPLTQ TVHGRKVSCL GPGGLTGRTA SFRSRDIHPS
HYGRICPIDT SEGINVGLTG SLAIHARIDH WWGSIESPFY EISEKAKEKK ERQVVYLSPN
RDEYYMIAAG NSLSLNQGIQ EEQVVPARYR QEFLTIAWEQ IHVRSIFPFQ YFSIGGSLIP
FIEHNDANRA LMSSNMQRQA VPLSRSEKCI VGTGLERQTA LDSRVSVIAE REGKIISSDS
HKILLSSSGK TISIPLVAHR RSNKNTCMHQ KPRVPRGKSI KKGQILAEGA ATVGGELALG
KNVLVAYMPW EGYNFEDAVL ISERLVYEDI YTSFHIRKYE IQTDTTSQGS AEKITKQIPH
LEEHLLRNLD RNGVVRLGSW VETGDILVGK LTPQIASESS YIAEAGLLRA IFGLEVSTSK
ETSLKLPIGG RGRVIDVKWI QRDPFDIMVR VYILQKREIK VGDKVAGRHG NKGIISKILP
RQDMPYLQDG TPVDMVFNPL GVPSRMNVGQ IFESSLGLAG DLLKKHYRIA PFDERYEQEA
SRKLVFSELY EASKQTKNPW VFEPEYPGKS RIFDGRTGDP FEQPVLIGKS YILKLIHQVD
EKIHGRSTGP YSLVTQQPVR GRAKQGGQRI GEMEVWALEG FGVAHILQEI LTYKSDHLIA
RQEILNATIW GKRVPNHEDP PESFRVLVRE LRSLALELNH FLVSEKNFRV NREDV
