RPOC2_AETCO
ID RPOC2_AETCO Reviewed; 1385 AA.
AC A4QJA5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Aethionema cordifolium (Lebanon stonecress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Aethionemeae; Aethionema.
OX NCBI_TaxID=434059;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Aethionema coridifolium chloroplast DNA.";
RL Submitted (MAR-2007) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009366; BAF49760.1; -; Genomic_DNA.
DR RefSeq; YP_001122936.1; NC_009265.1.
DR AlphaFoldDB; A4QJA5; -.
DR SMR; A4QJA5; -.
DR GeneID; 4968659; -.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1385
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353542"
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 1385 AA; 157531 MW; 52A9A3709EC19B19 CRC64;
MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPFNPVHM MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP RNKNRMMSER
IFIQTLIGRV LADDIYIGSR CVAFRNQDLG IGLVNRFITF GTQSISIRTP FTCRSTSWIC
RFCYGRSPTH GDLVELGEAV GIIAGQSIGE PGTQLTLRTF HTGGVFTGGT AEHVRAPYNG
KIKFNEDLVH PTRTRHGHPA FLCYIDLSVI IESEDIIHSV TIPPKSFLLV QNDQYVESEQ
VIAEIREGTY TFRFKERVRK YIYSDSEGEM HWSTDVYHAP EFTYSNVHLV PKTSHLWILS
GGSCGASLIL FSIHKDQDQM NIPFLSVKRK SICSLSVNND QVSQKFFSSD FSDKKKSGIP
DYSELNGIVG TSHYNLIYSA IFHENSDLLA KRRRNRFLIP FESIQEQEQE KEFMPHSGIS
IAIPINGIFR KNTIFSFFDD PRYRRKSSGI LKYGTIEADS IIQKEDMIEY RGVHKFKKNY
KMKVDRFFFI PEEVHILPES SVIMVQNYSI IRVDTRITLN IRSQVGGLIR VERKKKRIEL
KIFSGDIHFP DKTDKISRHS GILIPPGRGK PNSRESKKVK NWIYVQRITP TKKKFFVLVR
PVATYEIADS INLATLFPQD LFREKNNIQL RVVNYILYGN GKPTRGISDT SIQLVRTCLV
LNWDQDNKNS SLEEARAFFV AVSTKGLIRD FIRIGLVKSH ISYIRKRNNP PDSGLISADH
MNPFYSISPK AGIQQSLSQN NGTIRMFLNR NKESQFLLIL SSSNCFRMGP FDHVKYHNVI
NQSIKKNPLI TIKNASGPLG TTIQISNFYS FFPLLTYNKM SVIKYLQLDN LKQILKVINS
YLIDENGRIC NRDPYSNVVL NPFKLNWYFL HQNYHHNYCE EMSTLISLGQ FFCENVCIAK
KGPHLKSGQA LIVQMDSVVI RSAKPYLATP GAKVHGHYGE ILYEGDTLVT FIYEKSRSGD
ITQGLPKVEQ VLEVRSIDSI SMNLEKRIKG WNKYITGILG IPWGFLVGAE LTIVQSRLSL
VNKIQKVYRS QGVQIHNRHI EIIVRQITSK VLVSEEGMSN VFLPGELIGL LRAERTGRAL
EEAISYRAIL LGITRASLNT QSFISEASFQ ETARVLAKAA LRGRIDWLKG LKENVVLGGG
IPAGTGFNKG LVHCSRQHTN ILLEKKTKNF CLFEEDMRDI LFYHREFFDS SISKFERSFL
GFNDS
