RPOC2_VITVI
ID RPOC2_VITVI Reviewed; 1394 AA.
AC Q0ZJ30;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Vitis vinifera (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Maxxa;
RX PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA Daniell H.;
RT "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT genome sequences: effects of taxon sampling and phylogenetic methods on
RT resolving relationships among rosids.";
RL BMC Evol. Biol. 6:32-32(2006).
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}.
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DR EMBL; DQ424856; ABE47524.1; -; Genomic_DNA.
DR RefSeq; YP_567066.1; NC_007957.1.
DR AlphaFoldDB; Q0ZJ30; -.
DR STRING; 29760.VIT_15s0024g01960.t01; -.
DR EnsemblPlants; Vitvi09g01816_t001; Vitvi09g01816_P001; Vitvi09g01816.
DR GeneID; 4025097; -.
DR Gramene; Vitvi09g01816_t001; Vitvi09g01816_P001; Vitvi09g01816.
DR KEGG; vvi:4025097; -.
DR eggNOG; ENOG502R2HI; Eukaryota.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000009183; Chloroplast.
DR ExpressionAtlas; Q0ZJ30; baseline and differential.
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..1394
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277205"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1394 AA; 158576 MW; CA88D4BA84E33E46 CRC64;
MGVLMTERAN LVFHNKVIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
TNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI SVSPRNGMIP
ERIFIQTLIG RVLADDIYMG PRCIAIRNQD IGIGLVNRFI TFQAQTISIR TPFTCKSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNEDW VHPTRTRHGH PAFLCYIDLY VTIESEGIIH NVNIPPKSFL LVQNDQYVES
EQVIAEIRAG TYTFNFKERV RKHIYSDSEG EMHWSTDVYH APEFTYGNVH LLPKTSHLWI
LSGGSCRFSI VPFSIHKDQD QMSVRSLSVE RRYISNPSVT NDQVIHEFFS SDLSGKKEGR
IPAYSELNRI IYTGRYNLID PAILHENSDL LAKRRRNRFI IPFQSIQEGE KELMPPSGIS
IEIPINGIFR RNSILAYFDD PRYRRNSSGI TKYGTIEAHS IVKKEDLIEY RGVKEFKPKY
QMKVDRFFFI PEEVHILPGS ASIMVRNNSI IGVDTRITLN TRSRVSGLVR VERKKKRIEL
KIFSGDIQFP GETNKISRHI GILIPPGTRK KNSKESKKLK NWIYVQGITP TKKKYFVLVR
PVVTYEIADG INLATLFPQD LLQERDNMHL QVVNYILYGN GKPIRGISDT SIQLVRTCLV
LNWYQEKKSS PIEKTHASFM EVRTNGLIRD FLTINLVKSY ISYTGKRNDP SSSGLIADNG
SDHTNINPFY SIYPKERIQQ LLRQRQKKNQ GTIRTLLNRN KECQSLIILS SSNCSRMGPF
NDVKYHNVIK ESIKKDTPIP IRNSLGPLGT ALQITNFYSF YHLITHNHIL VTKYFQLDNF
KQTFQTLKYY LMDENGITYN PDPCSNIILN PFNLNWYFLH HNYCEETSTI ISLGQFICEN
VCIAKNGPHL KSGQVLIVQV DSVVIRSAKP YLATLGATVH GHYGEILYEG DTLVTFIYEK
SRSGDITQGL PKVEQVLEVR SIDSISMNLE KRVEGWNEHI TRILGIPWGF FIGAELTIAQ
SRISLVNKIQ KVYRSQGVQI HNRHIEIIVR QITSKVLVSE DGMSNVFSPG ELIGLLRAER
TGRAFEEAIC YRTILLGITR ASLNTQSFIS EASFQETARV LAKAALWGRI DWLKGLKENV
VLGGMIPVGT GFKGLVHRSR QHNNIPLEME TKKNNLFERE MRDILFHHRE LFDSCSSKNF
HDTSEQSFMG FNDS
