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RPOC2_DRIGR
ID   RPOC2_DRIGR             Reviewed;        1381 AA.
AC   Q06H07;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
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   Drimys granadensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX   NCBI_TaxID=224735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA   Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA   dePamphilis C.W., Boore J.L., Jansen R.K.;
RT   "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT   implications for the phylogenetic relationships of magnoliids.";
RL   BMC Evol. Biol. 6:77-77(2006).
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; DQ887676; ABH88287.1; -; Genomic_DNA.
DR   RefSeq; YP_784376.1; NC_008456.1.
DR   AlphaFoldDB; Q06H07; -.
DR   PRIDE; Q06H07; -.
DR   GeneID; 4363642; -.
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..1381
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000277189"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
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"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1381 AA;  156784 MW;  78E52FCC2641B119 CRC64;
     MEVLMAERAD LVFHNKVIDG TAMKRLISRL IDHFGMAYTS HILDQVKTMG FQQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMH
     PNFRMTDPSN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYLISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI SVSPRNGIGM
     TEKMLIQTLI GRVLADDIYM GLRCIAARNQ DIGVGLVNRF IAFRAQSIYI RTPFICRSTS
     WICRLCYGRS PTHGDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTAEHVRAP
     FNGKIKFNED LVHPTRTRHG HPAFLCYIDL YVTIESQDIL HNVNIPPKSF LLVQNDQYVE
     SEQVIAEIRA RTSTFNFKER VRKHIYSDSE GEMHWSTDVY HAPEYTYGNV HLLPKTSHLW
     ILSGGPRRSS LVPFSLHKDQ DQMNIHSLSV EQRESSDLSV TNDRARHKLF SSDPSGKKEG
     KILDYSGPAR IISNGHWNFI YPAILHENSY LLAKRRRNRF IIPFQYDQER EKELMPRSGI
     SIEIPINGIL RRNSILAYFD DPRYRRSSSG ITKYGTVEVD SIVKKEDLIE YRGAKEFSPK
     YQMKVDRFFF IPEEVHILPG SSSIMVRNNS IIGVDTRITL NTRSRIGGLV RVERKKKRIE
     LKIFSGDIHF PGEADKISRH SGILIPPGTG KKNSKESKKL QNWIYVQRIT PTKKKYFVSV
     RPVVTYEIAD GINLATLFPQ DLLQERDNVK FRVVNSILYR NGKPIRGIYY TSIQLVRTCL
     VLNWDQDRNG SIEKVKASIV EVRANDLIRD FIRIDLVKSP ISYTGKRNDM AGSGLIPDNG
     SDHTNINPFY SKVRRIQSLT QHQGTIRTLL NRNKECQSFL ILSSSNCSRI GPFNGSKSHN
     VTKESIQIKE DPMIPIRNSL GPLGTVPKIA NFDSPYYLIT HNQILLNKYL LLDNLKQTFQ
     VLKYYLMDEN GRIYNPYPCR NIIFHPFDLT WCFLHHDYCE KTSTIIVLGQ FICENENVCI
     SKYGPQIKSG QVLIVHVDSL VIRSAKPHLA TPGATVHGHY GEILYEGDTL VTFIYEKSRS
     GDITQGLPKV EQVLEVRSVD SISMNLEKRV EGWNEHIKRI LGIPWGFLIG AELTIAQSRI
     SLVNKIQKVY RSQGVQIHNR HIEIIVRQIT SKVLVSEDGM SNVFSPGELI GLLRAERTGR
     SLEEAICYRA ILWGITRASL NTQSFISEAS FQETARVLAK AALRGRIDWL KGLKENVVLG
     GMIPVGTGFK GLVHRSRQDN NIPLEIKKKN LFEGEIRDIL FHHRELFGSC IPNNFHNTPE
     Q
 
 
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