ID   ETFS_ASFM2              Reviewed;        1098 AA.
AC   Q89425;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Early transcription factor large subunit homolog {ECO:0000250|UniProtKB:Q89525};
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent helicase VETFS homolog {ECO:0000250|UniProtKB:Q89525};
GN   OrderedLocusNames=Mal-114; ORFNames=g10L;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA   Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA   Hammond J.M., Smith G.L.;
RT   "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT   a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL   J. Gen. Virol. 75:1655-1684(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8376971; DOI=10.1099/0022-1317-74-9-1969;
RA   Baylis S.A., Twigg S.R.F., Vydelingum S., Dixon L.K., Smith G.L.;
RT   "Three African swine fever virus genes encoding proteins with homology to
RT   putative helicases of vaccinia virus.";
RL   J. Gen. Virol. 74:1969-1974(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative initation factor. {ECO:0000250|UniProtKB:P04308}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:P04308};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q89525}. Note=Found
CC       in association with viral nucleoid. {ECO:0000250|UniProtKB:Q89525}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X71982; CAA50813.1; -; Genomic_DNA.
DR   EMBL; X72951; CAA51456.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JQ2209; JQ2209.
DR   Proteomes; UP000000860; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00490; HELICc; 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; Helicase; Hydrolase; Late protein; Nucleotide-binding;
KW   Transcription; Transcription regulation; Virion.
FT   CHAIN           1..1098
FT                   /note="Early transcription factor large subunit homolog"
FT                   /id="PRO_0000373108"
FT   DOMAIN          17..317
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          489..689
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           246..249
FT                   /note="DEAH box"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1098 AA;  125189 MW;  ABFB5F93DC2EF293 CRC64;
     MICGLILSRL VGPGCEKGGR AFFPCDPYAS PFPSIKGLQL HNAQLFVQNF QNPNTPYSRL
     LLNWQTGTGK SIAAIAIARQ FMNHYMNFIE NAPWIFVVGF TRTIIQTEML RRPELGFVSY
     KEVAELHRLL HIAKQSGSTT SVESRHLNGF ISTLKRRLTD RNRGGFFQFY GYKEFASKLF
     NITSKGEEKN FDVLSLFHRS DEAEDTLNEN DISQFVQKIS EAETNGLIRV NQKIMEQLRG
     GLLIADEIHN VYNIQERNNY GIALQYVLDA FPPHQAPRAV FMSATPVTGS VMEYVDLLNL
     LVPRHELPNG QPLQRQQLFD NSGHSVKWKK DALALVERLS IGRVSFLLDT NTNFYPERIF
     AGKMLSYRDE KLPYLHFIEC PMSNYQLETL KQLGPDPKIS SNAYSIYDMV FPNPKFSKQT
     EPKAYGLFNS TETPAALSMA STDWLLENGV QIIEPSRRTP FNVSGSFLSL QPPTHISGLA
     FYSGKYTQMM KDILSIIREG RGKILIYHNR VRMSGVLILQ EILQSNGILN EVSSPVGTTR
     CSICAAIRDD HTHSDHQFIP VRFTILHSEI EPAVRERSLA LFNASSNLEG HQLRILIGSK
     VIVEGLNFQA VRYEMIMSLP LDIPRLIQVF GRVVRKNSHM ELPPNERNVT IYLYVSTTPD
     GGPELAKYAQ KLKEYILIQE GDKALRKHAI DGFTNQIKID KPMLESLPLS PSITPANVGA
     TVLNTFEAYG YGEQEVKTIS NIIISLFMAR PVWTYSELWK AVSTPKLIQG ITIDNKLFSE
     DNFALALISL CYSKNQCKEL LIQNRLCTIM HVPAKPEHLY IAAVLNHKKE PVLDIETYIR
     DFQPPTMHSV RITKYLEHSQ TKEPFQVLYE KFQKDFQDEP IEQVLIHYPA SFHYTMLEAL
     IIDNLAGMGA LVEVYKKFFI AFSKKDIQPF PDIFKIISHV PGDDNTLVGY ATEDSVRLIT
     SRKDKTWHEI PLYMLNINVK RKENDIVIGY MESKGKALKF KIRPPIQVLK KNEITDIRML
     NRGAVCETRG REEQQKIANQ LGISLNLTKI SAIKLCLLIR NNLLQKEMEA RNQPNGMQDG
     IRWFYLFNDK MPSLVHTS