ID Q0NP71_9POXV Unreviewed; 493 AA.
AC Q0NP71;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=DNA helicase {ECO:0000313|EMBL:ABD97706.1};
GN ORFNames=TATV_DAH68_140 {ECO:0000313|EMBL:ABD97706.1};
OS Taterapox virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=28871 {ECO:0000313|EMBL:ABD97706.1, ECO:0000313|Proteomes:UP000139570};
RN [1] {ECO:0000313|EMBL:ABD97706.1, ECO:0000313|Proteomes:UP000139570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dahomey 1968 {ECO:0000313|EMBL:ABD97706.1};
RX PubMed=16873609; DOI=10.1126/science.1125134;
RA Esposito J.J., Sammons S.A., Frace A.M., Osborne J.D., Olsen-Rasmussen M.,
RA Zhang M., Govil D., Damon I.K., Kline R., Laker M., Li Y., Smith G.L.,
RA Meyer H., LeDuc J.W., Wohlhueter R.M.;
RT "Genome sequence diversity and clues to the evolution of variola (smallpox)
RT virus.";
RL Science 313:807-812(2006).
CC -!- FUNCTION: DNA helicase which seems to act as a postreplicative
CC transcription termination factor. Involved in ATP-dependent release of
CC nascent RNA. Forms a stable complex with single-stranded DNA, and to a
CC lesser extent RNA. {ECO:0000256|ARBA:ARBA00037581}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the helicase family. Poxviruses subfamily.
CC {ECO:0000256|ARBA:ARBA00038498}.
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DR EMBL; DQ437594; ABD97706.1; -; Genomic_DNA.
DR RefSeq; YP_717447.1; NC_008291.1.
DR GeneID; 4238775; -.
DR KEGG; vg:4238775; -.
DR Proteomes; UP000139570; Genome.
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:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18785; SF2_C; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11274:SF13; HELICASE A859L-RELATED; 1.
DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:ABD97706.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000313|EMBL:ABD97706.1};
KW Hydrolase {ECO:0000313|EMBL:ABD97706.1};
KW Late protein {ECO:0000256|ARBA:ARBA00022921};
KW Nucleotide-binding {ECO:0000313|EMBL:ABD97706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000139570};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT DOMAIN 100..256
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 493 AA; 56690 MW; D12F02F9B0325E03 CRC64;
MSLLKMEYNL YAELKKMTCG QSLSLFNEDG DFVEVEPGSS FKFLIPKGFY SSPSVKTSLV
FETLTTTDNK ITSINPTNAP KLYPLQRKVV SEVVSNMRKM IELKRPLYIT LHLACGFGKT
ITTCYLMATH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
SNRIYCNSII NIAKLSDLKK TIYTVDSFFE PYSTDNIRHM IKRLDGPSNK YHIYTEKLLS
VDEPRNQLIL NTLVEEFKSG TINRILVITK LREHMVLCYK RLLDLFGPEV VFIGDAQNRR
TPDMVKSIKD LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
LDRTVYVFPN TSIKEIKYMI GNFVQRIISL SVDKLGFKQE SYRKHQESDP TSACTTSSRE
ERVLNRIFNS QNR
//
