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GTA_NPVOP
ID   GTA_NPVOP               Reviewed;         498 AA.
AC   O10302;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable global transactivator;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase GTA;
GN   Name=GTA; ORFNames=ORF47;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; U75930; AAC59046.1; -; Genomic_DNA.
DR   RefSeq; NP_046203.1; NC_001875.2.
DR   SMR; O10302; -.
DR   GeneID; 912031; -.
DR   KEGG; vg:912031; -.
DR   Proteomes; UP000009248; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..498
FT                   /note="Probable global transactivator"
FT                   /id="PRO_0000074316"
FT   DOMAIN          43..206
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          337..493
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           157..160
FT                   /note="DEAH box"
FT   BINDING         55..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   498 AA;  56990 MW;  FAE1023D0BB8B993 CRC64;
     MDTFKVQLQE FFSAGDGADD APCLDAPNLL EHQKRGIEWM RRRERRGRPH GGVLADDMGL
     GKTLSVMRLI ANDGDDAHKT LIVCPLSLLN HWTAEAKKHN LPLNLRQFHG GDLDESFDDA
     KAVAITYDTL RAHHKHYKTA GRASGLLARH WHRVVLDEAH VIKNHQTGVH AAACALSADN
     RWCITGTPIH NRHWDMYAII HFLRCRPFDN VGVWRMLNRN NDTNRIKSVV NKIVLKRNKA
     EIALDIPQHD VQDVHVRFDE AEARVYNELK SASQRAYDDA VASADKAGGM QDVLWLLCRL
     RQVCCHPALT KCAAMFPEHA HIFEPAYESS KCRRALELVQ RVLDTPDDKV VLVSQWVEFL
     QLVAGLLRRR GVPILLYTGQ LRVEERTAVE NQFNAADSPY RVLLMSIKCG GVGLNLTGGN
     HIIMLEPHWN PQIELQAQDR IHRMGQKKRT YVYKMIVDEE NSIERYMKAR QDKKLTFVNK
     VFDRTALNYE DIKKFFSL
 
 
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