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RPOC2_SOLLC
ID   RPOC2_SOLLC             Reviewed;        1392 AA.
AC   Q2MIB0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. LA3023;
RX   PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA   Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA   Tomkins J., Jansen R.K.;
RT   "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT   lycopersicum and comparative analyses with other Solanaceae genomes.";
RL   Theor. Appl. Genet. 112:1503-1518(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. IPA-6;
RX   PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA   Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT   "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT   solanaceous plastid genomes.";
RL   J. Mol. Evol. 63:194-207(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; DQ347959; ABC56290.1; -; Genomic_DNA.
DR   EMBL; AM087200; CAJ32383.1; -; Genomic_DNA.
DR   RefSeq; AP_004918.1; AC_000188.1.
DR   RefSeq; YP_008563078.1; NC_007898.3.
DR   AlphaFoldDB; Q2MIB0; -.
DR   STRING; 4081.Solyc08g028910.1.1; -.
DR   PaxDb; Q2MIB0; -.
DR   PRIDE; Q2MIB0; -.
DR   GeneID; 3950457; -.
DR   KEGG; sly:3950457; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
DR   OrthoDB; 731145at2759; -.
DR   Proteomes; UP000004994; Chloroplast.
DR   ExpressionAtlas; Q2MIB0; baseline and differential.
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..1392
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000277202"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1392 AA;  157121 MW;  EB85673F6CBD7B21 CRC64;
     MEVLMAERAN LVFHNKAIDG TAMKRLISRL IEHFGMAYTS HILDQVKTLG FQQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH QYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTARGI SVSPRNGIMP
     ERIFSQTLIG RVLADDIYMG SRCIATRNQA IGIGLVNRFI TFRAQPISIR TPFTCRSTSW
     ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
     NGKIKFNEDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH NVNIPPKSLL LVQNDQYVES
     EQVIAEIRAG ISTLNFKEKV RKHIYSDSDG EMHWSTDVYH APEFTYGNVH LLPKTSHLWI
     LLGGPCRSSL VYLSIHKDQD QMNAHSLSGK RRYTSNLSVT NDQARQKLFS SDFYGQKEDR
     IPDYSDLNRI ICTGQYNLVY SPILHGNSAL LSKRRRNKFI IPLHSIQELE NELMPCSGIS
     IEIPVNGIFR RNSILAYFDD PRYRRKSSGI IKYGTIETHS VIKKEDLIEY RGVKEFRPKY
     QMKVDRFFFI PEEVHILPGS SSLMVRNNSI VGVDTQITLN LRSRVGGLVR VERKKKRIEL
     KIFSGDIHFP GETDKISRHT GVLIPPGTGK RNSKEYKKVQ NWIYVQRITP SKKRFFVLVR
     PVVTYEITDG INLGTLFPPD PLQERDNVQL RIVNYILYGN GKPIRGISDT SIQLVRTCLV
     LNWNQDKKSS SCEEARASFV EIRTNGLIRH FLKINLVKSP ISYIGKRNDP SGSGLLSDNG
     SDCTNINPFS AIYSYSKAKI QQSLNQPQGT IHTLLNRNKE CQSLIILSAA NCSRMEPFKD
     VKYHSVIKES IKKDPLIPIR NSLGPLGTCL PIENFYSSYH LITHNQILVT KYLQLDNLKQ
     TFQVIKLKYY LMDENGKIFN PDPCRNIILN PFNLNWSFLH HYYCAETSKI ISLGQFICEN
     VCIAKNGPPL KSGQVILVQV DSIVIRSAKP YLATPGATVH GHYGETLYEG DTLVTFIYEK
     SRSGDITQGL PKVEQVLEVR SIDSISMNLE KRVEGWNKCI PRILGIPWGF LIGAELTIAQ
     SRISLVNKIQ QVYRSQGVQI HNRHIEIIVR QITSKVLISE DGMSNVFSPG ELIGLLRAER
     MGRALEEAIC YRVVLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV
     VLGGVIPVGT GFKGLVHPSK QHNNIPLETK KTNLFEGEMR DILFHHRKLF DSCLSKKFHD
     IPEQSFIGFN DS
 
 
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