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HELI1_TNAVC
ID   HELI1_TNAVC             Reviewed;         974 AA.
AC   Q06VC2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Putative ATP-dependent RNA helicase;
DE            EC=3.6.4.13;
GN   ORFNames=ORF161;
OS   Trichoplusia ni ascovirus 2c (TnAV-2c).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=328615;
OH   NCBI_TaxID=7100; Noctuidae (owlet moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16876847; DOI=10.1016/j.virol.2006.06.029;
RA   Wang L., Xue J., Seaborn C.P., Arif B.M., Cheng X.W.;
RT   "Sequence and organization of the Trichoplusia ni ascovirus 2c
RT   (Ascoviridae) genome.";
RL   Virology 354:167-177(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DQ517337; ABF70676.1; -; Genomic_DNA.
DR   RefSeq; YP_803383.1; NC_008518.1.
DR   GeneID; 5141674; -.
DR   KEGG; vg:5141674; -.
DR   Proteomes; UP000001323; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 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; Reference proteome.
FT   CHAIN           1..974
FT                   /note="Putative ATP-dependent RNA helicase"
FT                   /id="PRO_0000329956"
FT   DOMAIN          67..237
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          413..595
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           185..188
FT                   /note="DEAH box"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   974 AA;  110725 MW;  D9D7E8EC651099E5 CRC64;
     MFKYALPLYP TMEISTESWS LTSLERINSF IEIGNQDEMI YINKDDSTKV FDEIKPMRHQ
     ILIGNMMSSR SPVDSLILMH GVGTGKTLTA ILSIINNISD TEFGMKRALI LTPNRAILSS
     FKEEVFNCCM HHYGAGFHTN VEHEVRNIIN ELFKFDTIRS FCNKIAIKSD EIIHKEWNAS
     FIVIDEAHDV APSGIDYPKL NRFMKILSTR KLLLMTATPM RNGSSDLIPL HNLMMKKQVH
     DISLEEFHGN YVEINRRRPP SEDGDSIVFS VETPKIAFMT KFAGLISYLP SDALRLDNVN
     VINVGDNTTY GGVLLSTTNI VSHNMSELME RIYSGLLNDN NNTNRRGDVA LLDQRQASRF
     IFPDGQYGTL GYMAWMNSNT GKATLRFKRE LRFGSNMETV LGAVEKFSPR YANIAKTVYE
     CARRGEKSIV YDDLVTGSGL LVLATILEAI GMKRGSGSNR NSFVCMTREV MTVSQIVAAQ
     RVFNSPENYD GSIISVILGS RVISEGLTFK DVQHEHVVAH WNDSETEQII GRGIRVGSHS
     KLLETLNTPV TVKVYRHATI YNREPDKSVD VIMYATSEMK RKNINTITEA LRSIAMTCPE
     LESRSISRTI CAFTPHEENI SNVVPLHHPT IRRTFMDRLN ETFNYEKDEY FVTRMENFCS
     AYNLNYQSDG GMRLMFILLK LIQTTPQLDI NKFINCDGYF VYTTKTVDEY NSCRTLRYPF
     DVSYKSTKRL YYDTIVSLIT EPNLIKAYET NPNYPLTKLP LHVITIILEK AISRKLLLTS
     DDEHQNAYHI QALDTFKQYY HIVYESGGGS NSNSATDIKA VCWLSASVAG ESTKYRICVS
     DQNTWKDCPD DMKEQVNNIK VTKDNTTIFQ MREKSLSHYG QKNPFSNDFC LRVIPQNSLS
     AKYDKRRIAS GKKCTTWDNA TLGRIKQNLG IESPLLHERT TMSRSDSCKL IESRLEEIDA
     VVTDVACGVQ AKRK
 
 
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