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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
 
 
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