RPOC2_ARATH
ID RPOC2_ARATH Reviewed; 1376 AA.
AC P56764;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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}; OrderedLocusNames=AtCg00170;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
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; AP000423; BAA84375.1; -; Genomic_DNA.
DR RefSeq; NP_051049.1; NC_000932.1.
DR AlphaFoldDB; P56764; -.
DR BioGRID; 29979; 2.
DR IntAct; P56764; 1.
DR MINT; P56764; -.
DR STRING; 3702.ATCG00170.1; -.
DR PaxDb; P56764; -.
DR PRIDE; P56764; -.
DR ProteomicsDB; 226813; -.
DR EnsemblPlants; ATCG00170.1; ATCG00170.1; ATCG00170.
DR GeneID; 844785; -.
DR Gramene; ATCG00170.1; ATCG00170.1; ATCG00170.
DR KEGG; ath:ArthCp012; -.
DR Araport; ATCG00170; -.
DR TAIR; locus:504954641; ATCG00170.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_000524_1_0_1; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 731145at2759; -.
DR PRO; PR:P56764; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56764; baseline and differential.
DR Genevisible; P56764; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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..1376
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067914"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1376 AA; 156366 MW; 7CBB5820163E2B9D CRC64;
MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSW ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPFNPVHM MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP RNKNRMMSER
IFIQTLIGRV LADDIYIGSR CVAFRNQDLG IGLVNRLITF GTQSISIRTP FTCRSTSWIC
RLCYGRSPTH GDLVELGEAV GIIAGQSIGE PGTQLTLRTF HTGGVFTGGT AEHVRAPYNG
KIKFNEDLVH PTRTRHGHPA FLCYIDLSVI IESEDIIHSV TIPPKSFLLV QNDQYVESEQ
VIAEIREGTY TFHFKERVRK YIYSDSEGEM HWSTDVSHAP EFTYSNVHLL PKTSHLWILS
GGSCGSSLIR FSIHKDQDQM NIPFLSAERK SISSLSVNND QVSQKFFSSD FADPKKLGIY
DYSELNGNLG TSHYNLIYSA IFHENSDLLA KRRRNRFLIP FQSIQEQEKE FIPQSGISVE
IPINGIFRRN SIFAFFDDPR YRRKSSGILK YGTLKADSII QKEDMIEYRG VQKIKTKYEM
KVDRFFFIPE EVHILPESSA IMVQNYSIIG VDTRLTLNIR SQVGGLIRVE KKKKRIELKI
FSGDIHFPDK TDKISRHSGI LIPPGRGKKN SKESKKFKNW IYVQRITPTK KKFFVLVRPV
ATYEIADSIN LATLFPQDLF REKDNIQLRV FNYILYGNGK PTRGISDTSI QLVRTCLVLN
WDKNSSLEEV RAFFVEVSTK GLIQDFIRIG LVKSHISYIR KRNNSPDSGL ISADHMNPFY
SISPKSGILQ QSLRQNHGTI RMFLNRNKES QSLLILSSSN CFRMGPFNHV KHHNVINQSI
KKNTLITIKN SSGPLGTATP ISNFYSFLPL LTYNQISLIK YFQLDNLKYI FQKINSYLID
ENGIILNLDP YSNVVLNPFK LNWYFLHQNY HHNYCEETST IISLGQFFCE NVCIAKKEPH
LKSGQVLIVQ RDSAVIRSAK PYLATPGAKV HGHYSEILYE GDTLVTFIYE KSRSGDITQG
LPKVEQVLEV RSIDSISLNL EKRIKGWNKC ITRILGIPWG FLIGAELTIV QSRISLVNKI
QKVYRSQGVQ IHNRHIEIIV RQITSKVLVS EEGMSNVFLP GELIGLLRAE RTGRALEEAI
CYRAVLLGIT RASLNTQSFI SEASFQETAR VLAKAALRGR IDWLKGLKEN VVLGGVIPAG
TGFNKGLVHC SRQHTNIILE KKTKNLALFE GDMRDILFYH REFCDSSISK SDFSRI