RPOC2_SOYBN
ID RPOC2_SOYBN Reviewed; 1386 AA.
AC Q8HVY3; Q2PMT3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL07336.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF289093; AAL07336.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ317523; ABC25125.1; -; Genomic_DNA.
DR RefSeq; YP_538765.1; NC_007942.1.
DR AlphaFoldDB; Q8HVY3; -.
DR STRING; 3847.GLYMA13G19555.1; -.
DR PRIDE; Q8HVY3; -.
DR GeneID; 3989293; -.
DR KEGG; gmx:3989293; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR OrthoDB; 731145at2759; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1386
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067950"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT CONFLICT 80
FT /note="L -> F (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="R -> S (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 887..904
FT /note="NPPGSRFILDNESDRTTI -> DPSSEKKEGSDHTNM (in Ref. 1;
FT AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 908..941
FT /note="FSIDSREKIQQSLSKNHGTIRMLLNRNEKCRSLI -> YSIYIYPKTKLQKS
FT FNQNQGTVRTLLGINKECQFFL (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 1347..1349
FT /note="SET -> R (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 1369..1373
FT /note="FFFFV -> LILLI (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
FT CONFLICT 1381..1386
FT /note="SQQSSI -> LQI (in Ref. 1; AAL07336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1386 AA; 159057 MW; A979080C57EF04BC CRC64;
MAERANLVFH NKVIGGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFRQA TDTSISLGID
DLLTIPSKGW LVQDAEQQSL ILEQHHHYGN VHAVEKLRQS IEIWYATSEY FRQEMNPNFR
MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIQGISVNT QNGMMPERIW
IQTLIGRVLA DDIYRGSRCI AVRNQDIGIG LINRFKTLQT QPISIRTPFT CRNTSWICRL
CYGQSPTHGH LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE QVRAPYNGKI
QFNEDLVHPT RTRHGHPAFL CYIDLYVTIE SGDIIHNVTI PPKSFLLVQN NQYVKSEQVI
AEIRAGTYTF NLKEKVRKHV YSDLEGEMHW STDVYHASEF RYSNVHILPK TSHLWILSGK
SYRSGSVSFS IRKDQDQMNI HYLSTGERDF CNLLASKKKV RHKLFRFNPS DKKERRISDY
SIFNQIISID HCHFTHPTIF HDTTDLLAKR RRNRLIIPFQ FQSIQERDKE LMLASSISIE
IPINGIFRRN SILAYFDDPQ YRTQSSGITK YRTIGINSIF KKEDFLIEYQ GVKEFKTKYQ
IKVDQFFFIP EEVHILPESS SIMVRNNSIV EVDTLITLNI RSRVRGLVRL EKKKKKIELK
IFSGDIYFPG EMDKISRHSA VLIPPRTVKK NSKEKKMKNW IYVQWITITK KKYFVLVRPV
ILYEIADRIN LVKLFPQDMF QERDNLELKV INYILSGNGK SIRGISDTSI QLVRTCLVLN
WDQDKKFSSI ENAHASFVEI SIKGLVRYFL RIDLVKSHIS YIRKRNNPPG SRFILDNESD
RTTINPFFSI DSREKIQQSL SKNHGTIRML LNRNEKCRSL IILSSSNCFQ IRSFNHGKYY
NGIKEGINQI QRDAMIPIKN SLGPLGIAPQ VAHFDFYRLI THNQISIIKN GQLDKLKETF
QVFQYYFLDE NERIYKPDLC SNIILNPFYL NWHFLHHNYC EKTFTIMSLG QFICENVCIV
QTKNAPHLKS GQILTVQMDS VGIRSANPYL ATPGATVHGH YGEILSEGDI LVTFIYEKSR
SGDITQGLPK VEQVLEVRSI DSISMNLEKR VDTWNGRITK ILGIPWGFLI GAELTIAQSR
ISLVNKIQKV YRSQGVHIHN RHIEIIVRQI TSKVLVSEDG MSNVFLPGEL IGLLRAERAG
RSLEEAICYR VLLLGITKTS LNTQSFISEA SFQETARVLS KAALRGRIDW LKGLKENVVL
GGMIPVGTGF KRIMNRSKQR QYNKMTSETK KKNLFEGEMR DILFHHREFF FFVSKNLCDT
SQQSSI
