ID   A18_VAR67               Reviewed;         493 AA.
AC   P0DSZ5; P33827; Q76PY3; Q89165;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
DE   AltName: Full=56 kDa abortive late protein;
GN   ORFNames=A18R, A19R;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Blinov V.M.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
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; X69198; CAA49063.1; -; Genomic_DNA.
DR   PIR; A36850; A36850.
DR   RefSeq; NP_042166.1; NC_001611.1.
DR   GeneID; 1486493; -.
DR   KEGG; vg:1486493; -.
DR   Proteomes; UP000002060; Genome.
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.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Late protein;
KW   Nucleotide-binding; Reference proteome; Transcription; Virion.
FT   CHAIN           1..493
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102179"
FT   DOMAIN          100..256
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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;  56676 MW;  71EEBBEC13D208BF CRC64;
     MSLLKMEYNL YAELKKITCG QSLSLFNEDG DFVEVEPGSL FKFLIPKGFY SSPSVKTSLV
     FETLTTTDNK ITSINPTNAP KLYPLQHKVV SEVVSNMRKM IKLKRPLYIT LHLACGFGKT
     ITTCYLMATH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
     IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
     SNRIYCNSII NIAKLSDLKK TIYAVDSFFE PYSTDNIRHM IKRLDGPSNK YHIYTEKLLS
     VDEPRNQLIL NTLVEEFKSG TINRVLVITK LREHMVLFYK RLLDLFGPEV VFIGDAQNRR
     TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
     LDRTVYVFPN TSVKEIKYMI GNFVQRIISL SVDKLGFKQE SYRKHQESDP TSVCTASSRE
     ERVLNRIFNS QNR