ID   A18_MYXVL               Reviewed;         478 AA.
AC   Q9Q8J2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=m108R;
OS   Myxoma virus (strain Lausanne) (MYXV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=31530;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562494; DOI=10.1006/viro.1999.0001;
RA   Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X.,
RA   Macaulay C., Willer D.O., Evans D.H., McFadden G.;
RT   "The complete DNA sequence of myxoma virus.";
RL   Virology 264:298-318(1999).
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; AF170726; AAF14996.1; -; Genomic_DNA.
DR   RefSeq; NP_051822.1; NC_001132.2.
DR   GeneID; 932054; -.
DR   KEGG; vg:932054; -.
DR   Proteomes; UP000000867; 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; PF00271; Helicase_C; 1.
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..478
FT                   /note="Transcript termination protein A18"
FT                   /id="PRO_0000102186"
FT   DOMAIN          98..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          302..454
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          456..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           204..207
FT                   /note="DESH box"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   478 AA;  54952 MW;  4D8037A55D8AE0EA CRC64;
     MSVCSEIDYA LYTELKKFLN SQPLFLFNAD KNFVEVVPSS SFKFYIPIGV FSNSDVALIR
     PVHTTCTNHI ESADATFPNL YPLQKRVVAE VTTSMRQKLS THRPMYMTLH LSCGFGKTIT
     ACYLMVVHRR KTVICVPNKM LIHQWKAAVE LTKLSYIIST DGVSVLLKQL RTKTADVLII
     VSRHLSNDYF CKKIHDEYDT FILDESHMYN LMNNSALTKF LTFYPPRICY FLTATPRLAN
     RIYCNDVVNV LKVSTLMKRL KIVEYFFEPY STECIRQMAK HLNTENNKYH IYTEKILAED
     LPRNNLIVDT VSREFKHGLV ERVIVVVKLR KHMTFFYDKF VEEFGTDYVY LGDAKNKDTS
     AVVKSLLQKK KFIFVSTSHY SGTGLDIPSL DSLVICCAVL NSMQIEQLLG RVCRESESVK
     KTVFLFPNTS IREIKHSLGF FTERIVSVST DKLGFQQEGK EGTKEEPALT KAFSSQIR