ID   A18_VACCA               Reviewed;         493 AA.
AC   O57227;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
DE   AltName: Full=56 kDa abortive late protein;
GN   OrderedLocusNames=MVA129R, ACAM3000_MVA_129;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) 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; U94848; AAB96522.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10528.1; -; Genomic_DNA.
DR   PIR; T37405; T37405.
DR   SMR; O57227; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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; Transcription; Virion.
FT   CHAIN           1..493
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102175"
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;  56744 MW;  98872A11AA63D47B CRC64;
     MSLLKMEYNL YAELKKMTCG QPLSLFNEDG DFVEVEPGSS FKFLIPKGFY ASPSVKTSLV
     FETLTTTDNK ITSINPTNAP KLYPLQRKVV SEVVSNMRKM IESKRPLYIT LHLACGFGKT
     ITTCYLMATH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
     IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
     SNRIYCNSII NIAKLSDLKK TIYAVDSFFE PYSTDNIRHM IKRLDGPSNK YHIYTEKLLS
     VDEPRNQLIL NTLVEEFKSG TINRILVITK LREHMVFFYK RLLDFFGSEV VFIGDAQNRR
     TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
     LDRTVYVFPS TSIKEIKYMI GNFVQRIISL SVDKLGFKQK SYRKHQESDP TSVCTTSSRE
     ERVLNRIFNS QNR