RPOC2_GRATL
ID RPOC2_GRATL Reviewed; 1228 AA.
AC Q6B8R6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Grc000138;
OS Gracilaria tenuistipitata var. liui (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX NCBI_TaxID=285951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT "Comparative analysis of the complete plastid genome sequence of the red
RT alga Gracilaria tenuistipitata var. liui provides insights into the
RT evolution of rhodoplasts and their relationship to other plastids.";
RL J. Mol. Evol. 59:464-477(2004).
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; AY673996; AAT79719.1; -; Genomic_DNA.
DR RefSeq; YP_063644.1; NC_006137.1.
DR AlphaFoldDB; Q6B8R6; -.
DR SMR; Q6B8R6; -.
DR PRIDE; Q6B8R6; -.
DR GeneID; 2944055; -.
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; 4.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1228
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067925"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 296
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"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1228 AA; 138415 MW; 183AAAB39FC7A761 CRC64;
MTQDKSIEPF FLNKVVDKSQ LRQLIIWAFR NYGIARASNM ADTLKDLGFL YATKAGISLS
LEDLRIPPAK NNLLKTTIDL INDTDTKYRK GEITAVERFQ KVIDTWNSAS DTLKKQVIKY
FTEKDPLNSI YMMAFSGARA NISQVRQLVG MRGLMADPQG QIIDLPISSN FREGLTITDY
FISSYGARKG LVDTALRTAD SGYLTRRLVD VAQDVIIREA DCNTSKGIVL ESMIDNRKTL
VSLHQALIGR VLAEDLFNPA GSKLVAKLNT EISPDLANEI ISLGISSVLV RSPITCESIK
SVCQSCYGWN LAHGRIVDLG EAVGIIAAQS IGEPGTQLTM RTFHTGGVFT GELAQTVISS
SDCQVEYPSN IILSDTRTRH GDHAFLVEKD IKLKLLDFNK KQTSLSLVKG SLLFVKHLEY
ITSGQVIAEY PISNRLITEK AQKAVLADFS GSIYLMDLSV SNIQSEQQTF KNVIKGGVIW
ILAGHVFSIP YNTQLIISEN DFIDENHLIG KTEFVSRYEG RVRILKKKQD FIQDIVIITS
SKTYINIDVL TKFYNGYTNH FLITNQQDKF ILKTLPNQTI VDQQLIAELI TNIYRTNTGG
IIKYLDLSVS DKKVDLNSKK DYYDIVDGGY VLWIGEETHE INKDISLLLV SHGQLIDEGT
EIVKNIFTNS SGIVDIIQKE GIVREIIIKP GILYPHSKFY DHKSKSRGFL KPGEIISNDL
KTDKLVYWEY FYVKNQSYTL IRPVIVYSIP SKTIQFKYSA DSFNSHICSL KLVKRIYFRD
GERVKSVSGI DIVKTYLIAE LNKDSLNLKC TLQLNLDSNN RSISRMRIVT MDKLSLKDEN
NIASTKDLYT RTRLLVTNNQ YIKSGTVVAQ TELFSSLEGQ VVSIQKNKSS NPRILLITSL
DTKVFSINNN QNIKVNINDL IYAGDEIATN IISYISGQVI SIRDNQITVR LGQPYLISEG
SFLHVNNQAL IQRGENIATL IFERVKTGDI VQGLPRIEEI LEARKKSDSF FNPHVVLDSK
FRQYVNQGLN LYDATRLSLL ILQLYLVKEL QLVYQSQGVE IADKHIEVIV RQMTSKVKIE
NGGDTDHLPG EIIELQKIEM LNKALRLASK EEALYYPILL GITKASLNTE SFISAASFQE
TTKVLTDAAI SCKLDWLRGL KENVIIGRLI PAGTGFNIYN NMQLNYQDEK YSYTKNLLSL
PQNTKNLNFE DIIVDDRNAH MYSRNNNL
