RPOB_GUITH
ID RPOB_GUITH Reviewed; 1096 AA.
AC O78485;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9929392; DOI=10.1007/pl00006462;
RA Douglas S.E., Penny S.L.;
RT "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT sequence and conserved synteny groups confirm its common ancestry with red
RT algae.";
RL J. Mol. Evol. 48:236-244(1999).
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; AF041468; AAC35676.1; -; Genomic_DNA.
DR RefSeq; NP_050742.1; NC_000926.1.
DR AlphaFoldDB; O78485; -.
DR SMR; O78485; -.
DR GeneID; 857047; -.
DR HOGENOM; CLU_000524_4_1_1; -.
DR OMA; FMTWEGY; -.
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 Transcription; Transferase.
FT CHAIN 1..1096
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048024"
SQ SEQUENCE 1096 AA; 123295 MW; 61A73D43C6413FA2 CRC64;
MFNTTFANRT LPDLVEIQRA SFCWFLNEGL AEEIQSFSPI VNYTGNLELH LFGDQYTLRY
PKHNINECKR RDTTYSVQIY VPAQLINRET GVIKEQEVFI GDLPLMTDRG TFIINGAERV
IVNQIVRSPG IYYKSELDKQ GRRTYSSSLI SNRGAWVKFE TDRNDLVWVR IDKTRKIPAH
VFLKAMGLSD TDIYNGLRHP EYLKKTFRFE GNYTTETALI QMYNKLRPGE PATVTGGQQL
LYSRFFDPKR YDLGKVGRYK LNKKLNLSVP ENVRVLTPQD TLAAIDYLIN LKFEIGETDD
IDHLGNRRVR SVGELLQNQV RIGLNRLERI IRERMTICDI TSLTPNTLVN PKPIIASIRE
FFGSSQLSQF MDQTNPLAEL THKRRISALG PGGLNRDRAG FGVRDIHPSH YGRICPIETP
EGPNAGLIGV LATHARINTY GFIEAPFFKV QDGQVYNHSQ PIYLTADQED KYRIAPGDIT
LDETNRIATK IVPIKYRQEF TTTKPNQVDF IAVSPIQVIS IATSLIPFLE HDDANRALMG
SNMQRQAVPL LYPESPLVGT GLEAQAARDS GMVVVSIEDG QVTFVSGDKI CVTNKKGDEI
AYYLQKYQRS NQDTCINQRP TVWLGEDVIE GQVIADGAAT EGGELALGQN ILVAYLPWEG
YNYEDAFLIN ERLVYNDVYT SVHIEKYEIE ARQTKLGSEE ITRELPNVGE AALRKLDENG
IIVIGSWVEA GDILIGKVTP KGESDQPPEG KLLRAIFGEK ARDVRDTSLR VPNGGRGRIL
DVRIFTREKG DELPTGANIV IRVYIAQSRK IQVGDKMAGR HGNKGIISRI LPRQDMPYLP
DGTPVDLVLN PLGVPSRMNV GQIFECLLGL AAENLNKRFK ITPFDEMHGA EASRVLVNEK
LNEAKIKTGE NWLFDLRHPG KITLYDGRTG EAFDNPVTIG VSYMLKLVHL VDDKIHARST
GPYSLVTQQP LGGRAQHGGQ RLGEMEVWAL EAFGASYTLQ ELLTVKSDDM QGRNETLNAI
VKGKPIPRPG TPESFKVLMR ELQSLGLDIG AYKIENLPDG QTRGIEVDLM MNYQQSRLFK
PLYESMQTKN NENLFL
