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RPOC1_STAPU
ID   RPOC1_STAPU             Reviewed;         834 AA.
AC   Q32RY3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS   Staurastrum punctulatum (Green alga) (Cosmoastrum punctulatum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Desmidiales; Desmidiaceae; Staurastrum.
OX   NCBI_TaxID=102822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequences of the charophycean green algae
RT   Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT   extensive changes during the evolution of the Zygnematales.";
RL   BMC Biol. 3:22-22(2005).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR   EMBL; AY958085; AAX45748.1; -; Genomic_DNA.
DR   RefSeq; YP_636393.1; NC_008116.1.
DR   AlphaFoldDB; Q32RY3; -.
DR   SMR; Q32RY3; -.
DR   PRIDE; Q32RY3; -.
DR   GeneID; 4108610; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..834
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225326"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         606
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         608
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         610
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   834 AA;  95948 MW;  8FDB8A72B6C8DF81 CRC64;
     MTYSNKPTGS SLRSSRNSTL EPQSLVHREE SKRQEGPKGQ NLRIGLASPE QIRNWAERIL
     PNGEIVGRVL KPHTIHYQTH KPEKDGLFCE RIFGPIKSGF CSCGKYKGTR DNDSPPFCEQ
     CGVELTESRV RRHRMGYIQL SSPVTHVWYL KNRPSVISHL LEMPLKDVES LVYCGSFIIG
     PGTYSKFRLL GTLRIGTHER AYKRILTRKR LRTRKHFLQT KNISLASRSV TLEKSQEKVN
     DSLKLSQRII IARKRLLRLA AKPILEPKLI CNRFYVPWRI ALELFLSKWY RDCESREIIT
     GGYGIQRMLI NLNLQNKLVS LQKNWERLVE QTEKMWFPVS GKYKNSDHSA DIQREKRLII
     RSSKIIRDLI QSKTQPEWMV LSVLPVLPPD LRPIVELREG QLITSDLNEL YRKVLFRNED
     LSIWLSYQGT LVLSGLLARL QRASLQRAVD ALLANGMGSS TFRDYNKRAY KSFSALIKGK
     KGRFRENLLG KRVDYSGRSV IVVGPLLALH ECGLPREMAL ELFQPFIIRE LITRQLAPNL
     RAAKSMIQNK EPIIWKVLQV IVQNRLVLLN RAPTLHRLGI QAFQPVLVGE RAILLHPLVC
     AGFNADFDGD QMAVHVPLSW EAQVEARILM WSPSNLLSPA TGRAVAVPSQ DMLLGLYVLT
     LEGSVGIYGS RQRSFVSSSL LFTKNHEIKE SKEEDSQSKQ DFIRSLDKKS KPIKNSKYSL
     YPKFIENKSS FHKFPIFYDY DDVIISIHQG HLNLFSFLWL RWEAKYPVIS SRKGPIEYQF
     DSSGNSINIY DNSYIKKNRK GNSFSKYILT TAGRVLFNQQ IQQSIQEHFS SLRK
 
 
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