ID   A18_CWPXB               Reviewed;         492 AA.
AC   Q8QMT5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=CPXV151;
OS   Cowpox virus (strain Brighton Red) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265872;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dietrich F.S., Ray C.A., Sharma A.D., Allen A., Pickup D.J.;
RL   Submitted (MAY-2003) 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; AF482758; AAM13592.1; -; Genomic_DNA.
DR   RefSeq; NP_619934.1; NC_003663.2.
DR   GeneID; 1486029; -.
DR   KEGG; vg:1486029; -.
DR   Proteomes; UP000152733; 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..492
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102184"
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   492 AA;  56565 MW;  3274596A0D30EA4B CRC64;
     MSLLKMEYNL YAELKKMTCG QPISLFNEDG DFVEVEPGSS FKFLIPKGFY ASTSVKTSLV
     FETLTTTDNK ITSINPTNAP KLYPLQRKVV SEVVSNMRKM IELKRPLYIT LHLACGFGKT
     ITTCYLMATH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
     IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPLMM CYFLTATPRP
     ANRIYCNSII NIAKLSDLKK TIYAVDSFFE PYSTDNIRHM VKRLDSPSNK YHIYTEKLLS
     VDEPRNQLIL DTLVEEFKSG TINRILVITK LREHMVLFYK RLLDIFGPEV VFIGDAQNRR
     TPDMVKSIKD LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
     LDRTVYVFPS TSIKEIKYVI GNFVQRIISL SVDKLGFKQE SYRKHQESEP ASVPTSSREE
     RVLNRIFNSQ NR