RPOB_ANTAG
ID RPOB_ANTAG Reviewed; 1071 AA.
AC Q85BW1; Q85UU6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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=46 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 80 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 150 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 152 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 259 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 294 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 326 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 392 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 397 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 414 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 418 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 421 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 423 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 522 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 531 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 534 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 542 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 551 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 574 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 650 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 652 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 668 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 719 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 721 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 731 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 738 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 739 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 759 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 832 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 842 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 860 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 879 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 897 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 902 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 962 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 969 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 973 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 984 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1007 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1023 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1048 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1052 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 46,
CC 421, 973, 984 and 1048 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AB086179; BAC55326.1; -; Genomic_DNA.
DR EMBL; AB087418; BAC55416.1; -; mRNA.
DR EMBL; AB087419; BAC55417.1; -; mRNA.
DR RefSeq; NP_777390.1; NC_004543.1.
DR AlphaFoldDB; Q85BW1; -.
DR SMR; Q85BW1; -.
DR GeneID; 2553423; -.
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..1071
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048010"
SQ SEQUENCE 1071 AA; 121491 MW; 532135ABBF2E78FC CRC64;
MILRKKIELF VLPEFTEIQF EGFHRFIKYG LVKELNDFPK IEDTDQEFEF QLFSRQYQLA
EPPIEERDAI YQSITYSSDL YVPAQLTERK KGRVKKQIVF LGSIPLMNSQ GTFVVNGVAR
VIINQILRSP GIYYNSELDR NGIPIYTGTI ISDWGRRLKL EIDGKTRIWA RISKKRKVSI
LVLLLAMGLD IEEILGNVCY PKLLLGCMKR KTKKEHLQST EDAIVELYKQ IYCIGGDLNF
SESISKELQK KFFQQRCELG KIGRLNLNKK LNLDVPENEN FLLPQDLLAA VDYLIKIRFG
IGVPDDIDHL KNRRVRSVTD LLQDQLKLAL NRLENSIRQA IRGANRREHL PTPKSLVTST
PLITTFKEFF GSHPLSQFLD QTNPLTEVVH KRRLSSLGPG GLTRRTASFQ VRDIHPSHYG
RICPIETSEG MNAGLVASLA IHAKVDNWGS LESPFYKISG VSEEEDMTFL SAGEDENYHI
ATGNCLALNQ TNQEEQVTPA RYRQEFVATA WNQINLRSIF PLQYFSIGTS LIPFLEHNDA
NRALMGFNMQ RQAVPLSKPE KCIVGTGLES QTALDSGSVI VATEGGRISY TDGRRITLLT
KEKEVETKLV IYQRSNNSTC IHEKPRIQLR EYVKKGQILA DGRATAGGEL ALGKNILVAY
MPWEGYNFED AILISERLIH EDIYTSIHIE RYEIEARVTS QGPERITREI PHLDNYLLRH
LDESGLVLPG SWVETGDVLV GKLTPQETEE SLRAPEGKLL QAIFGIQVVT AKETCLKVPL
GGRGRVIDIK WIYQEKTSTT YAEIVHVYIL QKREIQVGDK VAGRHGNKGI ISKILPRQDM
PYLQDGTPVD MVLSPLGVPS RMNVGQIFEC LLGLAGDFLQ KHYRVTPFDE RYEREASRKL
VFSELHEASR QTANPWLFES DNPGKSGLLD GRTGDIFEEP VTIGKAYMLK LIHQVDDKIH
ARSSGPYALV TQQPLRGKSR RGGQRVGEME VWALEGFGAA YTLEEMLTIK SDHIQARFEV
LRAIVTGELI PKPETAPESF RLLVRELRSL ALNLDHIIVS EKELRIKFKD I
