RPOC2_CRUWA
ID RPOC2_CRUWA Reviewed; 1379 AA.
AC A4QKS1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 Crucihimalaya wallichii (Rock-cress) (Arabidopsis campestris).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Crucihimalayeae; Crucihimalaya.
OX NCBI_TaxID=78192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Crucihimalaya wallichii 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}.
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DR EMBL; AP009372; BAF50276.1; -; Genomic_DNA.
DR RefSeq; YP_001123452.1; NC_009271.1.
DR AlphaFoldDB; A4QKS1; -.
DR GeneID; 4962749; -.
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..1379
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353554"
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 1379 AA; 156736 MW; CCF32A85E3A9693E 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 IGLVNGLITS GTQSISIRTP FTCRSTSWIC
RLCYGRSPTH GDLVELGEAV GIIAGQSIGE PGTQLTLRTF HTGGVFTGGT AEHVRAPYNG
KIKFNEDLVH PTRTRHGHPA FLCYIDLSVI IESEDIIHSV TIPPKSFILV QNDQYVESEQ
VIAEIREGTY TFHFKERVRK YIYSDSEGEM HWSTDVSHAP EFTYSNVHLL PKTSHLWILS
GSSCGSSLIL FSIHKDQDQM NIPFLSVERK SISSLSVNND QVSQKFLSSD FADQKKSGIP
DYSELNGNLG TSHYNFIYSA IFHKNSDLLA KRRRNRFLIP FQSIQEQEKE FIPHSGISIE
IPINGIFRRN SIFAFFDDPR YRRKSSGILK YGTLKADSII QKEDMIEYRG VQKFKTKYEM
KVDRFFFIPE EVHILPESSD IMVQNYSIIG VNTRLTLNIR SQVGGLIRVE RKKKRIELKI
FSGDIHFPDK TDKISRHSGI LLPPGKGKTN SKESKKFKNW IYVQRITPTK KKFFVLVRPV
ATYEIADSIN LATLFPQDLF REKDNIQLRV FNYILYGNGK PTRGISHTSI QLVRTCLVLN
WDQDNKNSSL EEVRAFFVEV STKGLIRDFI RIGLVKSHIS YIRKRNNSPD SGLISADHMN
PFYSISPKAG ILQQSLRQNH GTIRMFLNRN KESQSLLILS SSNCFRMGPF NHVKYHNVIN
ESIKKNPLIT IKNSSGPLGT AAQISNFYSF LPLLTYNKIS VIKYLQLDNL KDIFQVINSY
LIDENGRIFN LDPYSNVVLN PFKLNWYFLH KNYHHNYCEE TSTIISLGQF FCENLCIAKK
EPQLKSGQVL IVQRDSVVIR AAKPYLATPG AKVHGHYREI LYEGDTLVTF IYEKSRSGDI
TQGLPKVEQV LEVRSIDSIS LNLEKRIKGW NKCITRILGI PWGFLIGAEL TIVQSRISLV
NKIQKVYRSQ GVQIHNRHIE IIVRQITSKV LVSEEGMSNV FLPGELIGLL RAERTGRALE
EAICYRAVLL GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGVI
PAGTGFNKGL VHCSRQHTNI LLEKKTKNFS LFEGDMRDIL FYHREFCDSS ISKSDFSRI
