ID   A18_YMTV5               Reviewed;         478 AA.
AC   Q6TUQ9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 74.
DE   RecName: Full=Transcript termination protein A18;
DE            EC=3.6.4.-;
GN   OrderedLocusNames=110R;
OS   Yaba monkey tumor virus (strain VR587) (YMTV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus;
OC   Yaba monkey tumor virus.
OX   NCBI_TaxID=928314;
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9557; Papio hamadryas (Hamadryas baboon).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14645589; DOI=10.1128/jvi.77.24.13335-13347.2003;
RA   Brunetti C.R., Amano H., Ueda Y., Qin J., Miyamura T., Suzuki T., Li X.,
RA   Barrett J.W., McFadden G.;
RT   "Complete genomic sequence and comparative analysis of the tumorigenic
RT   poxvirus Yaba monkey tumor virus.";
RL   J. Virol. 77:13335-13347(2003).
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; AY386371; AAR07466.1; -; Genomic_DNA.
DR   RefSeq; NP_938365.1; NC_005179.1.
DR   GeneID; 2943580; -.
DR   KEGG; vg:2943580; -.
DR   Proteomes; UP000008596; Segment.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
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   CDD; cd18785; SF2_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR11274:SF13; HELICASE A859L-RELATED; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_0000102190"
FT   DOMAIN          98..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          307..454
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;  55285 MW;  5961D49A3A5F429E CRC64;
     MSVCTEIDYK LYTELRKIAG NSLFLFNEDG DFVEVVSNSS FKFLLPVGLF SSMDIPLKKP
     IECNTDNDIE HSKNVVMPNL YPFQERVASE VLSSIKKKVE LKRPMYVTLH LACGFGKTIT
     TCYLLSVHKK KAVICLPNKM LINQWKRAIE SININHLVSV DGVGNLLKEL VKKPADILII
     VSRHLSNKEF CKKIHVDYDV FVLDESHMYN LMNNSTVTRF LTYYPPKICY FLTATPRRVN
     RIYCNDVINV SNSSDLKKYI KIVEFFFETY SSDTIRQMVK KLNTNYNKYH MYTEKILAED
     VPRNKLILDT IIYDFEKMIV NRLIIVTKLR KHMMFFYTNL IEKFGSDIVY LGDAKNKNIS
     DIVKKIKSIN RFIFISTTNY SGTGLDVPTL DSLVICSAVM NSMQIEQILG RICRYSISKT
     RTVIVFPNTS IKEIKHMIGF FTQKIITLAI EKLGFKKIDK KGNKQEFALC KAFNLQTR
//