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RPOC2_PAUCH
ID   RPOC2_PAUCH             Reviewed;        1372 AA.
AC   B1X3M8;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, 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=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNAP subunit beta' {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};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=PCC_0095;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
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, organellar chromatophore.
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; CP000815; ACB42547.1; -; Genomic_DNA.
DR   RefSeq; YP_002048757.1; NC_011087.1.
DR   AlphaFoldDB; B1X3M8; -.
DR   GeneID; 6481180; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0070111; C:organellar chromatophore; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Organellar chromatophore; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1372
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000353587"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1372 AA;  151182 MW;  539EED1ECEE78599 CRC64;
     MTPSSNSVKT SRFNKVRTDI IGDTDLPNNL IKSLSKSPPH FYNHIIDKKG LRDIIAWAYK
     SHGIAATAEL ADDIKDLGFK YATVAAVSIS IDDLKIPKEK KFLLEQAEEQ ITATEERYRL
     GEITEVERHT KVIDTWTETN ERLVLAIKKN FNENDPLNSV WMMANSGARG NISQVRQLVG
     MRGLMANPQG EIIDLPIRAN FKEGLTVTEY VISSYGARKG LVDTALRTAD SGYLTRRLVD
     VAQDVIVRED DCGTERGIVV EADEKGNYGT KLVGRLAAQS VVVDNENRVL VRRNREIDLI
     TACRIEAADI PSVIVRSPLT CEAARSVCRK CYGWALAHNA LVDLGEAVGI IAAQSIGEPG
     TQLTMRTFHT GGVSTAETGL VRSTLEGSII FGSKARVRPY RTPHGVEAQQ AETDFVLQVK
     PNNGKKSQKV DITNGSLLFV SDSQEVASDT ILAQIISGSS VKKSVEKATK DVICDLAGQV
     RYDEALQPKE VIDRQGSATH KATRLGRVWV LSGDVYNLPP NAKPVIQGNS KVEEGEVLAE
     SRLSSEHGGV VRLRESTGDS REVQIVTTSM TLKDFKLLGE STHSGEIWHL EAKDTTRYLL
     KTQPGSKIGN GEVIAELADE RFRTKTGGLV KYAPGGLSIK KARSAKNGYE VNKGGTLLWI
     PQETHEINKD ISLLMIEDGQ WIEDKTEVVK DIFSQIAGIV TVTQKNDILR EITVRPGTLY
     PCNESKVIER FKGEGLLVDE EEIISKNLKA EKRVFVQSVE TSEGPQLLIR PVEEYTIPEV
     AHLPELAIVK QNSGPYLGLK ATQRLNFKDG ELIKSVEGVE LLKTQLILET FDTTPQMTVD
     VEKVTDKRSK TLERLQLVIL ETLLVRRDTI SDASHGSTHT ELQVNDGDLV KSGDVVATTQ
     ILCKEVGIVQ LPKQIDNEPI RRIIVERDQD TMTIPLGSAP LVSVGQRLVD GDLLAENDPS
     PCCGQVETIK NNTIIIRIGR PYMISSDSTL HVKDRELVQR GDSLALLVFE RQKTGDIVQG
     LPRIEELLEA RRPRDSAVLC KQPGVLTLRH DEETDSSIAV IKSANGEETE YPILLGRNLM
     VSVGQHIKAG ELLTDGPINP HELLEYLFAD LRSRKPLMEA AREAIAKVQS RLVTEVQNVY
     KSQGVTIHNK HIEVIVRQMT SKVRIEDAGE TTLLPGELIE LRHVEKVNKA MFMTSSSPAV
     FIPELLGITK ASLNTDSFIS AASFQETTRV LTEAAIEGKT DYLRGLKENV IIGRLIPAGT
     GFSGFEEELR SEAGPHPDIL DEDPAGYRRM QNLRPDYTVD MPAAASASPA ALLDDPSDDE
     LEATRSRHGI EVTTSNTAAF TRPVIVNKIM EDQILDPDII ASLQEEGLLT RE
 
 
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