RPOB_SOYBN
ID RPOB_SOYBN Reviewed; 1070 AA.
AC Q8HVY5; Q2PMT5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Glycine max (Soybean) (Glycine hispida).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Min-Gu L., Hoon-Seok Y., Jeong-Kook K.;
RT "Sequence of rpoBC gene cluster.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 437654;
RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0;
RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G.,
RA Jansen R.K.;
RT "Complete chloroplast genome sequence of Glycine max and comparative
RT analyses with other legume genomes.";
RL Plant Mol. Biol. 59:309-322(2005).
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; AF289093; AAL07334.1; -; Genomic_DNA.
DR EMBL; DQ317523; ABC25123.1; -; Genomic_DNA.
DR RefSeq; YP_538763.1; NC_007942.1.
DR AlphaFoldDB; Q8HVY5; -.
DR SMR; Q8HVY5; -.
DR STRING; 3847.GLYMA12G29365.1; -.
DR PRIDE; Q8HVY5; -.
DR GeneID; 3989291; -.
DR KEGG; gmx:3989291; -.
DR eggNOG; KOG0214; Eukaryota.
DR InParanoid; Q8HVY5; -.
DR OrthoDB; 944344at2759; -.
DR Proteomes; UP000008827; 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; 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 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1070
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048049"
FT CONFLICT 3
FT /note="G -> R (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="L -> I (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="L -> F (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="C -> W (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="R -> Q (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..36
FT /note="PEGLF -> TEELS (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="I -> M (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="L -> A (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="N -> K (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> S (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..94
FT /note="SSRDI -> TRREM (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..101
FT /note="FV -> LI (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..400
FT /note="PGG -> LED (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="R -> A (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="A -> T (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="D -> V (in Ref. 1; AAL07334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1070 AA; 120783 MW; E32A3B91E1B80D13 CRC64;
MLGDGNEGMS TLPGLNQIQF EGFCRFIDRG LPEGLFKFPK IEDTDQEIEF QLFVETYQLL
EPLINEKDAV YESLTYSAEL YVSAGLIWKS SRDIQEQTIF VGNIPLMNSL GTSIVNGIYR
IVINQILQSP GIYYRSELDP SGISVYTGTI ISDWGGRLEL EIDRKARIWA RVSRKQKISI
LVLSSAMGSN LSEILENVCY PEIFVSFLND KDKKKIGSKE NAILEFYRQF ACVGGDPVFS
ESLCKELQKK FFQQRCELGR IGRRNMNQKL NLDIPQNNTF LLPRDILTAA DHLIGMKFGM
GILDDINHLK NKRIRSVADL LQDQFGLALV RLENMVRGTI CGAIRHKLIP TPQNLVTSTP
LTTTYESFFG LHPLSQVLDQ TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR
ICPIDTSEGI NVGLIGSLAI HARIGSWGSI ESPFYEISER SKRIRMLYLS PSRDEYYMVA
TGNSLALNRD IQEEQTVPAR YRQEFLTIAW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN
RALMSSNMQR QAVPLSQSEK CIVGTGLERQ VALDSGVSAI AEHEGNIIYT NTDRIFLFGN
GDTLSIPLTI YQRSNKNTCM HQKPQVRRGK CIKKGQILAD GAATVDGELA LGKNVLVAYM
PWEGYNSEDA VLINERLVYE DIYTSFHIRK YEIQTHMTSY GSERITNKIP HLEAHLLRNL
DKNGIVILGS WVETGDILVG KLTPQMAKES SYSPEDRLLR AILGIQVSTS KETCLKLPTG
GRGRVIDVRW IQKKGGSSYN PETIRIYILQ KREIKVGDKV AGRHGNKGIV SKILSRQDMP
YLQDGRPVDM VFNPLGVPSR MNVGQIFECS LGLAGGMLER HYRITPFDER YEQEASRKLV
FSELYEASKQ TSNPWIFEPE YPGKSKIFDG RTGNSFKQPA IMGKPYILKL IHQVDDKIHG
RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIKTRQEVL
GTTIIGGTIP KPTDAPESFR LLVRELRSLA MELNHFLVSE KNFRIHRKEA
