ID   A18_RFVKA               Reviewed;         478 AA.
AC   Q9Q8X0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=s108R;
OS   Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS   Kasza)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=10272;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA   Willer D.O., McFadden G., Evans D.H.;
RT   "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL   Virology 264:319-343(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; AF170722; AAF17991.1; -; Genomic_DNA.
DR   RefSeq; NP_051997.1; NC_001266.1.
DR   GeneID; 1486952; -.
DR   KEGG; vg:1486952; -.
DR   Proteomes; UP000000868; 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_0000102188"
FT   DOMAIN          98..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          302..468
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
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;  55252 MW;  A4884FA99763CAF2 CRC64;
     MSVCLEVDYT LYTELKKFLN GQPLFLFNAD KNYVEVVPSS TLKFYIPIGL FSNSNVALIR
     PVHTTCTNHI ESVDVTFPNL YPLQKHVVAE VTTSMRQKLS THRPMYMTLH LSCGFGKTVT
     ACYLMVVHRR KTVICVPNKM LIHQWKVAVE LTKLSYIIST DGVSMLLKQL RTKTADVLII
     VSRHLSNDYF CKKIHDEYDT FILDESHMYN LMNNSALTKF LTFYPPRICY FLTATPRLMN
     RIYCNDVVNV LKVSALTKRL KIVEYFFEPY STDCIRQMAK HLNTENNKYH IYTEKILTED
     LPRNNLIVET VSREFRNETI ERVIVIVKLR KHMTFFYDRF VKEFGTDYVY LGDAKNKDTS
     TVVKSLLQKK KFIFVSTSHY SGTGLDIPSL DSLVICCAVL NSMQIEQLLG RVCRESESVK
     KTVFLFPNTS IREIKHSLGF FTERIVSIST DKLGFEQEGI EGTKEEPVLT KAFSSQTR