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RPOT3_NICSY
ID   RPOT3_NICSY             Reviewed;         977 AA.
AC   P69242; Q8L4F8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=DNA-directed RNA polymerase 3, chloroplastic;
DE            EC=2.7.7.6;
DE   AltName: Full=NsRpoT-C;
DE   AltName: Full=T7 bacteriophage-type single subunit RNA polymerase 3;
DE   Flags: Precursor;
GN   Name=RPOT3; Synonyms=RPOT-C;
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Leaf;
RX   PubMed=12435389; DOI=10.1016/s0006-291x(02)02579-2;
RA   Kobayashi Y., Dokiya Y., Kumazawa Y., Sugita M.;
RT   "Non-AUG translation initiation of mRNA encoding plastid-targeted phage-
RT   type RNA polymerase in Nicotiana sylvestris.";
RL   Biochem. Biophys. Res. Commun. 299:57-61(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=12061895; DOI=10.1046/j.1365-313x.2002.01318.x;
RA   Hedtke B., Legen J., Weihe A., Herrmann R.G., Boerner T.;
RT   "Six active phage-type RNA polymerase genes in Nicotiana tabacum.";
RL   Plant J. 30:625-637(2002).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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|PROSITE-ProRule:PRU10031,
CC         ECO:0000255|PROSITE-ProRule:PRU10032};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12061895, ECO:0000269|PubMed:12435389}.
CC   -!- TISSUE SPECIFICITY: The highest levels of expression are detected in
CC       the mature leaves. {ECO:0000269|PubMed:12435389}.
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AB084950; BAC22693.1; -; Genomic_DNA.
DR   EMBL; AB084951; BAC22694.1; -; mRNA.
DR   EMBL; AJ302020; CAC82576.3; -; mRNA.
DR   RefSeq; NP_001289533.1; NM_001302604.2.
DR   AlphaFoldDB; P69242; -.
DR   SMR; P69242; -.
DR   STRING; 4096.XP_009764593.1; -.
DR   GeneID; 104216269; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   Proteomes; UP000189701; Unplaced.
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:0009536; C:plastid; IDA:UniProtKB.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1320.10; -; 1.
DR   Gene3D; 1.10.287.260; -; 1.
DR   InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   PANTHER; PTHR10102; PTHR10102; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Reference proteome; Transcription; Transferase; Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           73..977
FT                   /note="DNA-directed RNA polymerase 3, chloroplastic"
FT                   /id="PRO_0000031074"
FT   ACT_SITE        678
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        753
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        910
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   977 AA;  111424 MW;  8480D08AC2A9A761 CRC64;
     MASTASYSPS PTSQWRTQKL PKRFNFYVIH NQEFGKLSQS SSLPTSSFPK TLKLPVIQMP
     INNNIQSQTT VCVSTDENLE ELVNLQKIAN GVLTKESNKR VFIQDPPWVS SLFMNSLFVR
     AKQVQGVRRE FREIERRRRY AMLRRRQIKA ETEAWEQMVE EYRELEREMC EKKLAPNLPY
     VKKLLLGWFE PLRQAIEKEQ NAETTVKHRA AFAPHIDSLP ADKMAVIVMH KLMGLLMMGG
     KEERCVQVVQ AAVQIGMAVE NEVRIHNFLE KTKKLQKHMT GAQSQEDMSR ETMILRKRVK
     SLIKRNRVVE VRKLMKSEEP ESWGRDTQAK LGCRLLELLT ETAYVQPPVD QSADTPPDIR
     PAFRHVFRIA TRDPGKSIVK KYGVIECDPL VVAGVDRTVK QMMIPYVPML VPPKKWRGYD
     KGGYLFLPSY LMRTHGSRRQ QDAVRSVPTK QMQQVYEALD TLGSTKWRVN KRILSVVESI
     WAGGGNIAGL VDRKDVPIPE LHSDDIMEVK KWKWRVRKSK KINQELHSQR CDTELKLSVA
     RKLKDEEGFY YPHNLDFRGR AYPMHPHLNH LSSDLCRGIL EFAEGRPLGK SGLRWLKIHL
     ASLYAGGIEK LCYDARLAFV ENHIDDILDS ANNPLNGNRW WLNAEDPFQC LAACINLSEA
     LKSSSPHTVF SHLPIHQDGS CNGLQHYAAL GRDSMEAAAV NLVAGDKPAD VYTEIALRVD
     HIIRGDSIKD PATDPNALLA KLLIDQVDRK LVKQTVMTSV YGVTYVGARE QIKRRLEEKG
     LIDDDRLLFT ASCYAAKVTL AALGELFQAA RGTMTWLGDC AKVIASENQP VRWTTPLGLP
     VVQPYFKTQR HVIRTSLQVL ALQREGDTVE VRKQRTAFPP NFVHSLDGSH MMMTAVACRD
     AGLQFAGVHD SFWTHACDVD QMNRILREKF VELYSMPILE DLLESFQNSY PALTFPPLPK
     RGDFDLVEVL ESPYFFN
 
 
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