ID   A18_FOWPN               Reviewed;         462 AA.
AC   Q9J550;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=FPV183;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; AF198100; AAF44527.1; -; Genomic_DNA.
DR   RefSeq; NP_039146.1; NC_002188.1.
DR   GeneID; 1486755; -.
DR   KEGG; vg:1486755; -.
DR   Proteomes; UP000008597; 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; IPR001650; Helicase_C.
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.
DR   PROSITE; PS51194; HELICASE_CTER; 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..462
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102180"
FT   DOMAIN          99..255
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          308..459
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           205..208
FT                   /note="DEAH box"
FT   BINDING         112..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   462 AA;  53501 MW;  2A7786A6B27E4A93 CRC64;
     MSYITVIDDK LYSSLRKLVG YSPLYLFNDK GDFVEVMKNS EFRFLIPSGY FSNSNVPLYG
     LTFSYGRNWM KDRQKIILPE LYPIQRRVIE EIILQFSRKC KEKRPLYTTL HLACGFGKTV
     TASYLIGTHK KNAVVSVPNK LILKQWENSI SSLKVSYYVS YEGVSKLLKV LTSKSFSILV
     VVDKHFSNKE FCELVYENYD VFILDEAHIY NLMNESIMTS FLCYYPPRIC YFLTATPRQQ
     NAVYCNSIIN FIKFSPLQKI LYVIRELYNE YTNPSIRAHV SQLQTTANKY HLYTEKALAE
     DIHRNKTIVD KIIETFKTNQ GNRILVITKL RNHMIIIYND LRKVLSDKVY LGDAQKKSTT
     DMIKELRTID NFILVSTLHY AGTGLDIPNL DSLFICNTVM NSMQSEQVMG RICRDTGSSP
     TRSIYLFINT SIKEIKSLVG VFTQRFAQQA TKLGFREVSQ MA