RPOC2_PHATC
ID RPOC2_PHATC Reviewed; 1415 AA.
AC A0T0D9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-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 Phaeodactylum tricornutum (strain CCAP 1055/1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA Green B.R.;
RT "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT lineage.";
RL Mol. Genet. Genomics 277:427-439(2007).
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; EF067920; ABK20637.1; -; Genomic_DNA.
DR RefSeq; YP_874414.1; NC_008588.1.
DR AlphaFoldDB; A0T0D9; -.
DR STRING; 556484.A0T0D9; -.
DR PRIDE; A0T0D9; -.
DR GeneID; 4524589; -.
DR InParanoid; A0T0D9; -.
DR Proteomes; UP000000759; Chloroplast.
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; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1415
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277197"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1415 AA; 163029 MW; 88B10660D0110DA3 CRC64;
MKNYKYQNTL IGKKQLRQLL AWSFTNYDSM QACALADELK YLGFKYASQA GISISIEDLK
IPFVKNLMLE KANQEIINAE KIYLKGKITD VERFQKIIDT WSLTSESLKE QVIYYFKNYD
PLNSVYIMAF SGARGNLSQV RQLVGMRGLM SDPSGEIMNL PIKKNFREGL TITDYLMSGY
GARKGIVDTA LKTANSGYLT RRLIDVGQDV LIREKDCLTN HSFLFSVSNE ELKSLNLIYQ
KILGRVLSKP IHDPKTNRIL VPAGTQITPK LIEKFKEYNV KKFYIRSPLT CNLYRAICQN
CYGWDLANEN LVDIGEAIGI LAGQSIGEPG TQLTMRTFHT GGIFTSEARQ QITTPINGVI
RFYKTLKTVL LRTNRGEDVL ITKNSGSVIL IPDDEDQDLV QIEILRNTIL FPKNNQYIVK
DTVIGELLNT NRQIKTEVKP ILSDTCGEIF MPVLKKKINL LNNNKLLWIL SGQLYNGPIN
SFVNFYSDYK LNCRSYIFRT KIINHYSGSV EFINTKSNLY QRLIRIKNNK YAFFNSKLEK
LRYSIQHKNY LLNLQGDKYL VKIQKKDLRL YLQATRNYQV ATLITNRFKT LVGGTVYYDH
QNVYKNYKPN STINYLSRVN FLNNYKPVVS HKTIIWLGEE VYKVNCELNI LLAEHGDFIS
EGFELIPGLF SKTSGVVVIK QKNNLIHTIS IKSGLVYEGK KFKMTSKKVY YPGEIIFSHI
PITKISFCEH ITGKNIEQLL VRPIEIYEFP YLNNISAKIQ NTHNKDSNIR LSSKIIYSYK
PNQLIKGTRN LNLISTILTL KSKETVTKNL NLELSHNQKT KLIDLKISEK FNLNHYISPN
LRYKNLQSCL LIQPNQFIDR YTNLGYLESK TSNSLEIVKI KLKIKDSKQI LLISNQDCLT
VKKEKFIGKK LNDFIINSSN VNETGKIIIE NENNLTLQKG KPYFFPNCKD DNVINKTNLQ
YKTISPTRVS PRLEKNINYK ISLNYYDMMK LSVNKDCTLS EKNEDPIKIK SEFSKLFLKK
NGKLYSSLIP QFFKKFSLHT SEFSPKYKQI IQPNGLAKRT IGKMDRTLLM QSSEITKNDY
KNLKNSNYQL ALLKFVEYPF TKSTKSIGLY SITEDYFEQD VNSVFCKNSE FIEEGETLGL
LNLEKEITGD IVQGLPRIEE ILEARKKNSN IKRIPTSQKK GLLVQKSSLD TNFEFRKLGT
NIKENEKVNP HKLLKVYFNY YGWIKPFICD QKEEIKYARL IKNYEGSYKS FKKVQSFILD
SVQAVYQSQG VIINDKHLEV IIKQMTTKVL ITYEGNTPLL RREVIDLYHI QYINQIIQSQ
GKQSACYVPL LLGITKAALN NPSFISAASF QETTRVLTKA AIEGRIDWLR GLKENIIIGH
LIPAGTGSQN YRNCFKKESL VRSKLPKSFD TILTR
