RPOC2_PHYPA
ID RPOC2_PHYPA Reviewed; 1330 AA.
AC P60290;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=12954768; DOI=10.1093/nar/gkg726;
RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT evidence for the loss and relocation of rpoA from the chloroplast to the
RT nucleus.";
RL Nucleic Acids Res. 31:5324-5331(2003).
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; AP005672; BAC85071.1; -; Genomic_DNA.
DR RefSeq; NP_904221.2; NC_005087.1.
DR AlphaFoldDB; P60290; -.
DR PRIDE; P60290; -.
DR GeneID; 2546817; -.
DR KEGG; ppp:2546817; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR InParanoid; P60290; -.
DR OrthoDB; 731145at2759; -.
DR Proteomes; UP000006727; 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; 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..1330
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067940"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1330 AA; 154004 MW; B19A602AB7D4CCD0 CRC64;
MLFYNKVMDR TAIKQLISRL ITHFGITYTT YILDQLKTVG FKQATQAAIS LGIDDLLTAP
SKSWLIQDAE QQGYISEKHY RYGNVHAVEK LRQLIETWYA TSEYLKQEMN PNFRMTDPLN
PVHMMSFSGA RGSTSQVHQL VGMRGLMSDP QGQIIDLPIQ SNFREGLSLT EYIISCYGAR
KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR KVDCGTSENI FVTPLQNNYK KNNKLIGRIL
ADNIYINGRC IAIRNQDITT NLVISLINFQ RKGIFIRSPL ICKSMLWICQ LCYGWSLTHG
NLIELGEAVG IIAGQSIGEP GTQLTLRTFH TGGVFTGDIA EHIRTPFNGI IQFDTNSVYP
TRTRHGHPAW ICNNNLSVVI KSKKKLHNLV IPTQSLLLVQ SNQYVESKQV IAEVRAKTSP
FKEKVQKYIY SNLSGEMHWS SKVQHSSEYI HSNVHLLRKT GHIWILAGNF DKDNKFSFIF
YQNQDKLDNK LPIAKQTLNY FQLKEHFLNN FWNSIYSSII LYNYRFLEKK NNKYEKKLLF
QFMLKLPKNG ILKQNDIFAI FNDPKYRIKN SGIIKYGNIK VDLINKKNDI FEDQKTKTVR
PRYKILKEGN FFLLPEEVYI LDQSSFSSIL VKNNSFIKAG TKITFNISSK ITGFVKIKKK
FNNFKIKILP GSIYYPKEKQ KNFKQNGILI PPGEKIFEQF RAKNWIYLEW IVLSKDNSFF
LIRPAIEYKI IFNDNPLTLP IPFYLDLLKE QKKIKIQTVK YILYEDSEEV EINPDTDIQL
IQTCLILNWE TKVFIKEAHI SFIKIRINKI IKNFFQINLI ENINLMNKKK NNNIILNYLF
KKKRYIINQK DCEKILLLSK TWGIIRTPSN KNQEKSFFLI LSPFNLFQTI LFDKTKQNLK
IENNVEKLFT YEPKKIIKTF NIEKRKNFVE FLGLLGYLQN ITKSFQLFSC KKFSDKSIPI
NFSIIDNLKK KIKISKWFFL NENKKVQKFF LTQNTILSLL NWSFPIFDLA KKKTQLFNLG
HFFCDGLSIA EYPTFSESGQ IIAIYDDLSL VIRLAKPYLA TGGAIIHNNY GEIVKEGDIL
ITLIYERLKS GDIIQGLPKV EQLLEARLTN PVSINLEKGF GEWNKDMTNF FGSLWGYFLS
AQISMEQSQV NLVNQIQKVY RSQGVNISDK HIEIIVRQMT SKVFTLEDGM TNGFLPGELI
EFARAKRMNR ALEEVIPYKP VLLGITKASL NTQSFISEAS FQETTRVLAK AALRGRIDWL
KGLKENVILG GIIPTGTGCE EVLWQITLEK QKNILLKKNK SKLFHNKVKD IFLYKKLSIS
FTSEKIHKNY
