ID   A18_ECTVM               Reviewed;         493 AA.
AC   Q8JL96;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=EVM121;
OS   Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265874;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14675635; DOI=10.1016/s0042-6822(03)00520-8;
RA   Chen N., Danila M.I., Feng Z., Buller R.M., Wang C., Han X.,
RA   Lefkowitz E.J., Upton C.;
RT   "The genomic sequence of Ectromelia virus, the causative agent of
RT   mousepox.";
RL   Virology 317:165-186(2003).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G2. Might be part of a transcription complex
CC       composed at least of G2, A18, and H5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Localizes to the
CC       virion core. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. Poxviruses subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF012825; AAM92426.1; -; Genomic_DNA.
DR   RefSeq; NP_671640.1; NC_004105.1.
DR   GeneID; 951582; -.
DR   KEGG; vg:951582; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Late protein;
KW   Nucleotide-binding; Transcription; Virion.
FT   CHAIN           1..493
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102185"
FT   DOMAIN          100..256
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          309..456
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           206..209
FT                   /note="DESH box"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   493 AA;  56759 MW;  2203EB30A58D8DD9 CRC64;
     MSLLKMEYNL YAELKKMTCG QPISLFNEDG DFVEVEPGSS FKFLIPKGFY SSPSVKTSLV
     FETLTTTDNK ITSINPINAP KLYPLQRKVV SEVVSNMRKM IELKRPLYIT LHLACGFGKT
     ITTCYLMATH GRKTIICVPN KMLIHQWKTL VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
     IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
     ANRIYCNSII NIAKLSDLKK TIYVVDSFFD PYSTDNIRHM IKRLDGPSNK YHIYTEKLLS
     VDEPRNQLIL DTLVEEFKSG TINRILVITK LREHMVMFYK RLLDLFGPEV VFIGDAQNRR
     TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
     LDRTVYVFPS TSIKEIKYMI GNFVQRIISL SVDKLGFKQE SYRKHQESDP TSTCTTSSRE
     ERVLNRIFNS QNR