RPOB_CYAM1
ID RPOB_CYAM1 Reviewed; 1036 AA.
AC Q85FR7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(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 -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AB002583; BAC76278.1; -; Genomic_DNA.
DR RefSeq; NP_849116.1; NC_004799.1.
DR AlphaFoldDB; Q85FR7; -.
DR SMR; Q85FR7; -.
DR STRING; 45157.CMV216CT; -.
DR PRIDE; Q85FR7; -.
DR EnsemblPlants; CMV216CT; CMV216CT; CMV216C.
DR GeneID; 844995; -.
DR Gramene; CMV216CT; CMV216CT; CMV216C.
DR KEGG; cme:CymeCp184; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_4_1_1; -.
DR Proteomes; UP000007014; Chloroplast.
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; 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; 1.
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;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1036
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048020"
SQ SEQUENCE 1036 AA; 116726 MW; 1F80C13896356E0D CRC64;
MRDLIAVQRN SYYTFLTKSL KEEFDKISPI VDYTGQLELH LITSKMELKP PKITPVQAKR
QDITYSVGMY MPVQLWNHQT GDVRQQMIYF GEIPLMTEDA TFIINGAERV VVNQIVRSPG
VYFQALWDKQ HVRTFEATFM ANRGAWIKYE LDKQKLLWVR LDKNRKMPLV IFLQALGLNL
QEIKPHLTNR EVFERSWENH AVNNTEAALV EFYKKMRPGE PATVHSAKQL LYARFFDPKK
YDLSEVGRYK LNQKLHLDIP LSVHILTTSD LLAGLDYLIQ LCLDRARVDD IDHLANRRLK
CVGELLQNQV RIGLSRLEKL LREKMTIGEK LQPSSLLNPK PLTSAIREFF ASSQLSQFMD
QINPLAELTH KRRISALGAG GLTRERAGFA VRDIHPSHYG RICPIETPEG PNAGLIGSLA
IFARVNRYGF IETPYYPVKK GQVQKSIVYL TADVEDNYRL APADVKYDRE GQICSPIVAV
RYRQEWTTCD ASHVDYMAIS PIQFISAATC LIPFLEHDDA NRALMGSNMQ RQAVPLIRAS
KPYVSTGQEK WMVQGVFSKA DGIVRSVQAT SIRIQHARGP VDYALLKYQK SNQDTCIDYR
PLVWVGEHVV KGQLIAQSAA MDSGELALGQ NVLIAYMPWE GYNFEDAFVI SERLVYEDVY
TSIHIEKYET DARQTKLGAE QITRQIPNVG EHALRQLDEH GIISVGSWVE AGSILVGKIT
PKGESDQPPE GKLLRAIFGE KNQHVKDSSL RMPNGSRGRV IHVRILSRDQ GDELPAGVNI
SVRVSVAVKR VIQVGDKMAG RHGNKGIVAR ILPRCDMPYL PDGTPVDVIL NPLGVPSRMN
VGQLFEALLG LAAHRLRKRI KIVPFDEMYH KEASRIFVHQ QLKRAALSAQ TILYDGRSGE
KFDNAVTVGM AYMLKLVHLV DEKIHARSTG PYSLVTQQPL GGRAQHGGQR LGEMEVWALE
AYGAAYTLQE LLTLKSDDME GRTATLNAIV KAQPIPRGGT PESFKVLMRE LQALGLDVTV
LQLESQALCV MQSKLD
