RPOB_TOXGO
ID RPOB_TOXGO Reviewed; 1051 AA.
AC Q9MTD3; O97123;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA-directed RNA polymerase subunit beta;
DE EC=2.7.7.6;
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta;
DE Short=RNA polymerase subunit beta;
GN Name=rpoB;
OS Toxoplasma gondii.
OG Plastid; Apicoplast.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RH;
RA Aiello D.P., Lang-Unnasch N.;
RT "Analysis of the rpoB gene product of Toxoplasma gondii.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RH;
RA Kissinger J.C., Donald R.G., Moulton A.L., Gutell R., Aiello D.P.,
RA Lang-Unnasch N., Roos D.S.;
RT "Mapping, cloning, and complete sequence annotation of the 35-kb plastid
RT genome of Toxoplasma gondii.";
RL Submitted (JUN-1999) 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:0000250}.
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;
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 (Potential).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; AF095904; AAD17842.1; -; Genomic_DNA.
DR EMBL; U87145; AAD41152.1; -; Genomic_DNA.
DR RefSeq; NP_044569.1; NC_001799.1.
DR AlphaFoldDB; Q9MTD3; -.
DR SMR; Q9MTD3; -.
DR PRIDE; Q9MTD3; -.
DR GeneID; 1466615; -.
DR VEuPathDB; ToxoDB:TGARI_300660; -.
DR VEuPathDB; ToxoDB:TGCAST_258210; -.
DR VEuPathDB; ToxoDB:TGCAST_272740; -.
DR VEuPathDB; ToxoDB:TGCOUG_258210; -.
DR VEuPathDB; ToxoDB:TGCOUG_397150; -.
DR VEuPathDB; ToxoDB:TGDOM2_272740; -.
DR VEuPathDB; ToxoDB:TGDOM2_402140; -.
DR VEuPathDB; ToxoDB:TGDOM2_402230; -.
DR VEuPathDB; ToxoDB:TGDOM2_402260; -.
DR VEuPathDB; ToxoDB:TGFOU_300660; -.
DR VEuPathDB; ToxoDB:TGGT1_258210; -.
DR VEuPathDB; ToxoDB:TGGT1_272740; -.
DR VEuPathDB; ToxoDB:TGMAS_300660; -.
DR VEuPathDB; ToxoDB:TGME49_300660; -.
DR VEuPathDB; ToxoDB:TGP89_300660; -.
DR VEuPathDB; ToxoDB:TGPRC2_300660; -.
DR VEuPathDB; ToxoDB:TGRH88_086510; -.
DR VEuPathDB; ToxoDB:TGRUB_300660; -.
DR VEuPathDB; ToxoDB:TGVAND_258210; -.
DR VEuPathDB; ToxoDB:TGVEG_258210; -.
DR VEuPathDB; ToxoDB:TGVEG_272740; -.
DR GO; GO:0020011; C:apicoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 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; 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; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
PE 3: Inferred from homology;
KW Apicoplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..1051
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300456"
FT CONFLICT 627
FT /note="F -> I (in Ref. 1; AAD17842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1051 AA; 124290 MW; 343CD20709F39EA9 CRC64;
MNFKIKTFFS IKSNKIFYTD FYFFLKKKLI ILIKNIFPEY FNFNNKYKNW NLICLYDLLY
FKVNNINFLD NVQYINSLIK IFLPLKFQNL KTNKVFFKNL LIFELPKYNS YNYCYLNGLK
KIFISKYFTS NGIFFNKYLK RKYNIYYAKL LLTNSNFFNI ILDLKLKQIY LSIKNLKFNF
ILFLYYLGIK NTDILKYSRY KNSKILKLLI FSALQTDLVN NKKIILKNLN YLKSIFKLTI
LNKNYKNFII SKDKLNYNYG DFSKNNLLII DFIFILDLLL DLQSKKLCFK TIDHLDNKHI
NTIGNYFQHN FKFYLKKFIS IIPNLIKLQK FSLLKVYNFK ELLILNPLIQ YLEQINSFSE
LMHKYKLNNY NSFSKGILNL REICLNQLGK LCLIDTTEGI NCGLVVSFAK HIRIYKKGII
QVYFSSIFKN KTKEFLNFKT SLDQELYLIQ FNNINLRKIK YLMNVRLVYN KNNFRIKFFS
NKKSILLEFT DLFSFTENLI PFIKYNDPAR CLMGAKMQSQ SVPLLNKKKS FVITGYEKEI
ITKSDTTIKA LQEGIVLNAS SLKIHIKDLF NREIVYYLSK YKKSNQNTII HQKPLVWNGE
RVFTNQLLTQ HQDIIDSEFA IGNNLLFYYG NFCGYDFEDA VIVSKRVLYQ QLFSSLHMDI
YEFNFCYNNE NDIEFSTLEI PKQSYYIKKN LDSLGIIKEG EKILTGSILL TKIKVAKPTY
TYKSIFKLIY SIFGKTIRNI KDNSLYIQTG KSGRVSKIEL FLVNISSRHK YKTYNNSYLK
CRIFICKQRF LTVGDKLCGR YGNKGILSYI AENADLPFLQ NSFYPDIIVG ALGIPSRMNL
GQLFEALVGK ISFSYNIRIL PSFTTSSNLY FNYLKILIYN FLMFNNFKKG FNWLYNFNLP
GKFIIRDGRT GVKLKSSVLC GVSRYSKLIH LIKDKLHFRT TGPYTEILQQ PLKGKKNLGG
QRFGEMEIWA LEAFGASYNL KEILNYKSDD CFARNNLKEY LLFRNTELQN STITESFRVI
LKEFNGLILN LELFLITDDL EENYLNLTIN Y
