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YR470_MIMIV
ID   YR470_MIMIV             Reviewed;         357 AA.
AC   Q5UQD9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative DNA directed RNA polymerase subunit R470;
DE            EC=2.7.7.6;
GN   OrderedLocusNames=MIMI_R470;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50736.1; -; Genomic_DNA.
DR   RefSeq; YP_003986977.1; NC_014649.1.
DR   SMR; Q5UQD9; -.
DR   GeneID; 9925095; -.
DR   KEGG; vg:9925095; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; SSF55257; 2.
DR   SUPFAM; SSF56553; SSF56553; 1.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase; Virion.
FT   CHAIN           1..357
FT                   /note="Putative DNA directed RNA polymerase subunit R470"
FT                   /id="PRO_0000253449"
SQ   SEQUENCE   357 AA;  41630 MW;  C730441AD6127A4D CRC64;
     MSKSKSSRST DIIDIYAKPD IKLKVLEPRQ DRELRVELEG RSINHAIVNA VRRSVMLYVP
     IYGFHRSNIH IELNKFKNMY NFDLMYNIFE TLPIFDVPNF MDLIDPDVYL PVELSKNLFG
     RFVQEQYTEQ SDQEDKLVDA TKKLFKIELT LNYKNNTADD KYISSHDCVI KIDGKTSDGY
     LKRRPICLFV LKPSEEISLR AEANLGIAKN FAAYEATTNA IHEEKNPNKY VITYKTLEQL
     NKYVILNKAC TIIYKKLENL QDYLLRTYTE DRDPTEQIDI ELYGEDHTLG TILENVLQQC
     EYVEKAGYCM PHLLIDKILV SYKLYDDSEI GPIKVLNDCI TYLIKLYKQL ADLVPKK
 
 
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