ID   A18_VACCW               Reviewed;         493 AA.
AC   P16712; Q76ZQ0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
DE   AltName: Full=56 kDa abortive late protein;
GN   OrderedLocusNames=VACWR138; ORFNames=A18R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2370683; DOI=10.1128/jvi.64.8.3853-3863.1990;
RA   Pacha R.F., Meis R.J., Condit R.C.;
RT   "Structure and expression of the vaccinia virus gene which prevents virus-
RT   induced breakdown of RNA.";
RL   J. Virol. 64:3853-3863(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SIMILARITY TO HELICASES.
RX   PubMed=1321883; DOI=10.1099/0022-1317-73-4-989;
RA   Koonin E.V., Senkevich T.G.;
RT   "Vaccinia virus encodes four putative DNA and/or RNA helicases distantly
RT   related to each other.";
RL   J. Gen. Virol. 73:989-993(1992).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8189502; DOI=10.1128/jvi.68.6.3642-3649.1994;
RA   Simpson D.A., Condit R.C.;
RT   "The vaccinia virus A18R protein plays a role in viral transcription during
RT   both the early and the late phases of infection.";
RL   J. Virol. 68:3642-3649(1994).
RN   [5]
RP   FUNCTION, DNA-BINDING, AND RNA-BINDING.
RX   PubMed=7545242; DOI=10.1128/jvi.69.10.6131-6139.1995;
RA   Simpson D.A., Condit R.C.;
RT   "Vaccinia virus gene A18R encodes an essential DNA helicase.";
RL   J. Virol. 69:6131-6139(1995).
RN   [6]
RP   FUNCTION.
RX   PubMed=9696793; DOI=10.1128/jvi.72.9.7012-7023.1998;
RA   Xiang Y., Simpson D.A., Spiegel J., Zhou A., Silverman R.H., Condit R.C.;
RT   "The vaccinia virus A18R DNA helicase is a postreplicative negative
RT   transcription elongation factor.";
RL   J. Virol. 72:7012-7023(1998).
RN   [7]
RP   INTERACTION WITH G2, AND POSSIBLE IDENTIFICATION IN A COMPLEX WITH G2 AND
RP   H5.
RX   PubMed=9636370; DOI=10.1006/viro.1998.9166;
RA   Black E.P., Moussatche N., Condit R.C.;
RT   "Characterization of the interactions among vaccinia virus transcription
RT   factors G2R, A18R, and H5R.";
RL   Virology 245:313-322(1998).
RN   [8]
RP   FUNCTION.
RX   PubMed=10625702; DOI=10.1074/jbc.275.2.1485;
RA   Lackner C.A., Condit R.C.;
RT   "Vaccinia virus gene A18R DNA helicase is a transcript release factor.";
RL   J. Biol. Chem. 275:1485-1494(2000).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16474121; DOI=10.1128/jvi.80.5.2127-2140.2006;
RA   Chung C.S., Chen C.H., Ho M.Y., Huang C.Y., Liao C.L., Chang W.;
RT   "Vaccinia virus proteome: identification of proteins in vaccinia virus
RT   intracellular mature virion particles.";
RL   J. Virol. 80:2127-2140(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:0000269|PubMed:10625702,
CC       ECO:0000269|PubMed:7545242, ECO:0000269|PubMed:9696793}.
CC   -!- SUBUNIT: Interacts with G2. Might be part of a transcription complex
CC       composed at least of G2, A18, and H5. {ECO:0000269|PubMed:9636370}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16474121,
CC       ECO:0000269|PubMed:8189502}. Note=Localizes to the virion core.
CC   -!- SIMILARITY: Belongs to the helicase family. Poxviruses subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M32064; AAA48350.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89417.1; -; Genomic_DNA.
DR   PIR; C36415; C36415.
DR   RefSeq; YP_233020.1; NC_006998.1.
DR   IntAct; P16712; 2.
DR   MINT; P16712; -.
DR   DNASU; 3707668; -.
DR   GeneID; 3707668; -.
DR   KEGG; vg:3707668; -.
DR   Proteomes; UP000000344; 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   GO; GO:0006353; P:DNA-templated transcription, termination; 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   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Late protein;
KW   Nucleotide-binding; Reference proteome; Transcription;
KW   Transcription regulation; Transcription termination; Virion.
FT   CHAIN           1..493
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102178"
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;  56716 MW;  DCFB6514B3DE081A 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
     ANRIYCNSII NIAKLSDLKK TIYAVDSFFE PYSTDNIRHM VKRLDGPSNK YHIYTEKLLS
     VDEPRNQLIL NTLVEEFKSG TINRILVITK LREHMVLFYK RLLDLFGPEV VFIGDAQNRR
     TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
     LDRTVYVFPN TSIKEIKYMI GNFMQRIISL SVDKLGFKQE SYRKHQESDP TSVCTTSSRE
     ERVLNRIFNS QNR