ID   A18_CAMPM               Reviewed;         493 AA.
AC   Q8V2N7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=CMLV136;
OS   Camelpox virus (strain M-96).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=203173;
OH   NCBI_TaxID=9836; Camelus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12033760; DOI=10.1006/viro.2001.1343;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Sandybaev N.T., Kerembekova U.Z.,
RA   Zaitsev V.L., Kutish G.F., Rock D.L.;
RT   "The genome of camelpox virus.";
RL   Virology 295:1-9(2002).
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; AF438165; AAL73843.1; -; Genomic_DNA.
DR   RefSeq; NP_570526.1; NC_003391.1.
DR   GeneID; 932665; -.
DR   KEGG; vg:932665; -.
DR   Proteomes; UP000152221; 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_0000102181"
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;  56717 MW;  9D57B0E4664432A6 CRC64;
     MSLLKMEYNL YTELKKMTCG QSLSLFNEDG DFVEVEPGSS FKFLIPKGFY SSPSVKTSLV
     FDTLTTTDNK ITSINPTNAP KLYPIQCKVV SEVVSNMRKM IELKRPLYIT LHLACGFGKT
     ITTCYLMAIH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSILLK ELKTQSPDVL
     IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
     SNRIYCNSII NIAKLSDLKK TIYVVDSFFE PYSTDNIRHM IKRLDGASNK YHIYTEKLLS
     VDEPRNQLIL NTLVEEFKSG TINRILVITK LREHMVLFYK RLLNLFGPEV VFIGDAQNRR
     TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETAL
     LDRRVYVFPN TSIKEIKYMI GNFVQRIISL SVDKLGFKQE SYRKHQESDP TSACTTSSRE
     ERVLNRIFNS QNR