RPOC1_SOYBN
ID RPOC1_SOYBN Reviewed; 687 AA.
AC Q8HVY4; Q2PMT4;
DT 16-JAN-2004, 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_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
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_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; AF289093; AAL07335.1; -; Genomic_DNA.
DR EMBL; DQ317523; ABC25124.1; -; Genomic_DNA.
DR RefSeq; YP_538764.1; NC_007942.1.
DR AlphaFoldDB; Q8HVY4; -.
DR SMR; Q8HVY4; -.
DR STRING; 3847.GLYMA01G15382.1; -.
DR PRIDE; Q8HVY4; -.
DR GeneID; 3989292; -.
DR KEGG; gmx:3989292; -.
DR OrthoDB; 774084at2759; -.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..687
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067899"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 151..152
FT /note="VV -> IA (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> L (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="H -> Y (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="I -> T (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> T (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..217
FT /note="ILMDSSLI -> TIIDYSFA (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..231
FT /note="PDNE -> TG (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
FT CONFLICT 685..687
FT /note="Missing (in Ref. 1; AAL07335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 79667 MW; BE508BCC6DE51747 CRC64;
MIDQYKHQQL RIGSVSPQQI SAWAKKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIRDK KDDPKFCEQC GVEFIDSRIR RYQMGYIKLA CLVTHVWYLK
RLPSYIANLL DKSLKELESL VYCDFSFARP VVKKPTFLRL RGSFEYEIQS WKHSIPLFFT
TQGFDIFRNR EISSGAGAIR EQLADLDLRI LMDSSLIEWK ELGEEGSPDN ENEWEDRKVG
RRKNFLVRRI ELAKHFLRTN IEPEWMVLCL LPVLPPELRP IIQIDGGKLM SSDINELYRR
VIYRNNTLID LLTTSRSTPG ELVMCQEKLV QEAVDTLLDN GIRGQPMRDG HNKVYKSFSD
IIEGKEGRFR ETLLGKRVDY SGRSVIVVGP SLSLHRCGLP REIAIELFQT FLIRGLIRKH
FASNIGIAKS KIREKEPIVW EILQEVMQGH PVLLNRAPTL HRLGIQAFQP ILVEGRAICL
HPLVCKGFNA DFDGDQMAVH VPLSLEAQAE ARLLMFSHTN LLSPAIGDPI SVPTQDMLIG
LYILTSGNRR GIYSNRYNPR NCGNFRNLKN ERIRDNNYKY TKKKEPFFCN SYDAIGAYQQ
KRINFDSPLW LRWRLDQRII SSREVPIEVH YESLGTYHEI YEHYLVVRST KKEIRSIYIR
TNVGHISFYR EIEEAIQGFC RAYSYDI
