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Database: UniProt
Entry: Q08F89_DPV84
LinkDB: Q08F89_DPV84
Original site: Q08F89_DPV84 
ID   Q08F89_DPV84            Unreviewed;       635 AA.
AC   Q08F89;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Early transcription factor 70 kDa subunit {ECO:0000256|ARBA:ARBA00017865};
DE   AltName: Full=ATP-dependent helicase VETFS {ECO:0000256|ARBA:ARBA00032553};
GN   ORFNames=DpV84gp093 {ECO:0000313|EMBL:ABI99077.1};
OS   Deerpox virus (strain W-1170-84) (DPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Cervidpoxvirus;
OC   Mule deerpox virus.
OX   NCBI_TaxID=305676 {ECO:0000313|EMBL:ABI99077.1, ECO:0000313|Proteomes:UP000162522};
OH   NCBI_TaxID=9872; Odocoileus hemionus (Mule deer) (Cervus hemionus).
RN   [1] {ECO:0000313|EMBL:ABI99077.1, ECO:0000313|Proteomes:UP000162522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W-1170-84 {ECO:0000313|EMBL:ABI99077.1};
RX   PubMed=15613325; DOI=10.1128/JVI.79.2.966-977.2005;
RA   Afonso C.L., Delhon G., Tulman E.R., Lu Z., Zsak A., Becerra V.M., Zsak L.,
RA   Kutish G.F., Rock D.L.;
RT   "Genome of deerpox virus.";
RL   J. Virol. 79:966-977(2005).
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|ARBA:ARBA00004328}.
CC   -!- SIMILARITY: Belongs to the helicase family. VETF subfamily.
CC       {ECO:0000256|ARBA:ARBA00008152}.
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DR   EMBL; AY689437; ABI99077.1; -; Genomic_DNA.
DR   Proteomes; UP000162522; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..185
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   635 AA;  73292 MW;  F26A25CF41244C7E CRC64;
     MNLGIVKLFS NHVNNIPNIL PHQLATLDYL VRRIIDENRS VLLFHIMGSG KTIIALLFAL
     VASRFKKVYI LVPNINILKI FNYSMDVAIN LFNSEYILEN ISIHSTTSFY SLNYNDNVIN
     YNGLSRYNNA IFIIDEAHNI FGNNTGELMT VIKNKNKIPF LLLSGSPITN TPITLSNIIS
     LMSDEEINFG DIIIQGKKVF QILLNENGVN VLKNILKGRI SYYEMPVTDL PIIQYHGRSF
     LDTKVVYCNM TKLQERDYIN VRKLCNNEMF EKNMNNVSLA VLGQLNLINN LDILFQEQDK
     ELYPNLKISN GVLYGDELIN LNISSKFKYF INKVNNLKGK QFIYFSNSTY GGLVIKYIMI
     SNGYSEYNGS QGTNPKLIKG KPKTFAIVTS KMKSSLEDLL SVYNSPSNDD GSQIMFLFSS
     NIMSESYTLK EVRHIWFMTI PDTFSQYNQI LGRSIRKFSY SNIDEPVNVY LLATVYSDFN
     DEITSLDDYS LDEINTLPFD IKKLLYLKFK TKETNRIYSI LQNISEKYDL PPHPYIVEIV
     LGEIVRQFFY HNSRINIKNE KLINSIKSVL INTDSVKRYI DNIVNGHFFV SNKVFDKSLL
     YRYKDDIITV PFKISHEPFI WGVNFRKEYN IVSSP
//
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