ID I2E2P4_VIGUN Unreviewed; 1371 AA.
AC I2E2P4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:AFJ91862.1};
OS Vigna unguiculata (Cowpea).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AFJ91862.1}.
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; Vigna.
OX NCBI_TaxID=3917 {ECO:0000313|EMBL:AFJ91862.1};
RN [1] {ECO:0000313|EMBL:AFJ91862.1}
RP NUCLEOTIDE SEQUENCE.
RA Aragao F.J.L., Mota A.P.Z.;
RL Submitted (MAR-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; JQ755301; AFJ91862.1; -; Genomic_DNA.
DR RefSeq; YP_006460345.1; NC_018051.1.
DR GeneID; 13080423; -.
DR KEGG; vun:13080423; -.
DR OrthoDB; 806648at2759; -.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AFJ91862.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:AFJ91862.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 93..157
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 172..350
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1199..1286
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1371 AA; 157376 MW; 669E61E752B4B537 CRC64;
MAERTNLMFH NKVIGGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFRQA TATSISLGID
DLLTIPSKGW LVRDAEHQNL ILEKQHHYGN VHAVEKLRQS IEIWYATSEY FRQEMNPNFR
MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVIRRTDC GTIRGISVNT QNETMPESSW
TQTLIGRVLA DDIYRGSRCI AIRNQDIGIG LFNRLKTFQT QPISIRTPFT CRNTSWICRL
CYGQSPTQGH LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE QVRAPYNGKI
KFNEDLVHPT RTRHGHPAFL CYIDLYVSIE NGDIIHNVTI PPKSFLLVQN NQYVKSEQVI
AEILAGTYTF NLKEKVRKHV YSDLEGEMHW STDVYHASEF KYSNVHILPK TSHLWILSGK
SDRSASVSFS TRKDQDQLNI HYLSTGERDI CNHLASNNKV RHNLFRFTPS EKKERRISDY
SKNNQILCKD HCHFTHPAIF HDTTDLLAKR RRNRFIIPFQ FQSIQERDKA LMLASSISIE
IPIHGIFRRN SIFAYFDDPQ YRTQSSGITK YRTIDINYIF KKEDFLIEYP GIQEFKTKYQ
IKVDQFFFIP EEVYILPEFS SIMVRNNSII EVDTPITVNI RSQVSGLVRL EKKKKKIQLK
IFSGNIYFPG EMDKISRHSA MLIPPRTVKK NSKGSKKKMK NWIYAQWITI MKKKYFVLVR
PVILYEIADR INLIQFFSQD MLQERDNLEL QIIHYILSGN GKSIRGISNS NTSIQLVRTC
LVLNWDQDKK LSSIEKGHAS FVELSIKGLV RYFLKMDLGK SHISYIRKRK DPLGSRFILD
NESDWTNINP FFFIDPREKV QQSLSQNHGT IHMLLNRNEK CRSLIILSSS NCFQIRSFHD
GKYYNGIKEE INPIQRDPLI PIQNSLGPLG IALQVAHFYF YLLITNNQIS INKNGQLDKL
KETFQVFKYY LIDENEIIYK SDLSSNILLN PFYLNWHFFH HNYCEKKTFP IISLGQFICE
NVCIVQTKNE PHLKSGQILT VQMDSVGIRS ANPYLATPGT TVHGHYGEIL SEGDILVTFI
YQKSRSGDIT QGLPKVEQVL EVRSIDSISI NLEKRVDTWN GRITRILGIP WGFFISAELT
IAQSRISLVN QIQKVYRSQG VHIHNRHIEI IVRQITSKVL VSEDGMSNVF LPGELIGLLR
AERAGRSLEE SICYRVLLLG ITKTSLNTQS FISEASFQET ARVLSKAALR GRIDWLKGLK
ENVVLGGMMP VGTGFKRIIY RSKQRQYNKI TPETKKRIYV IHQNNLGFKN S
//
