ID   ETF1_MYXVL              Reviewed;         635 AA.
AC   Q9Q8L9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Early transcription factor 70 kDa subunit;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase VETFS;
DE   AltName: Full=ETF small subunit;
GN   Name=VETFS; OrderedLocusNames=m081R;
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: Acts with RNA polymerase to initiate transcription from early
CC       gene promoters. Is recruited by the RPO-associated protein of 94 kDa
CC       (RAP94) to form the early transcription complex, which also contains
CC       the core RNA polymerase. ETF heterodimer binds to early gene promoters
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a 70 kDa and a 82 kDa subunit. Part of the
CC       early transcription complex composed of ETF, RAP94, and the DNA-
CC       directed RNA polymerase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC       other proteins required to synthesize early mRNAs are packaged within
CC       the virion core along with the DNA genome. This is necessary because
CC       viral early mRNAs are synthesized within minutes after virus entry into
CC       the cell and are extruded through pores in the core particle.
CC   -!- SIMILARITY: Belongs to the helicase family. VETF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF170726; AAF14969.1; -; Genomic_DNA.
DR   RefSeq; NP_051795.1; NC_001132.2.
DR   SMR; Q9Q8L9; -.
DR   GeneID; 932122; -.
DR   KEGG; vg:932122; -.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Transcription;
KW   Transcription regulation; Virion.
FT   CHAIN           1..635
FT                   /note="Early transcription factor 70 kDa subunit"
FT                   /id="PRO_0000099076"
FT   DOMAIN          32..185
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          326..505
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           135..138
FT                   /note="DEXH box"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   635 AA;  73219 MW;  FBD821BDD5A9A0E8 CRC64;
     MNSAVIELFR HHVNNIPNIL PHQLATLDYL VRSIIDENKS VLLFHIMGSG KTIIALLFAL
     VASRFKKVYI LVPNINILKI FNYSMDVVIN LFNADYILEN IFIYSTTSFY SINYNDNVIN
     YNGLSRYNNA IFIIDEAHNI FGNNTGELMT VIKNKNKIPF LLLSGSPITN TPITLSNIIS
     LMSDEEINFG DIIIQGKKVF QILLNEHGVN VLKNILKGRI SYYKMPDTDL PGIQYHGKSF
     LDTRVVYCNM SKLQEKDYIN VRKMCNNEMF EKNMNNVSLA VLGQLNLINN LDILFQEQDK
     ELYPNLKINN GVLYGEELVT LNISSKFKYF ITKIESLKGK HFIYFSNSTY GGLIIKYIML
     SNGYSEYNGS QGTHPKLIHG RPKTFAIVTS KMKASLEDLL VTYNSLANDD GSQIMFLFSS
     NIMSESYTLK EVRNIWFMTI PDTFSQYNQI LGRSIRKFSY KDITQPVNVY LLAAVYSDFN
     DTIESLDDYS LEEINTLPFD IKKLLYLKFK TKETNRIYSI LENISDSYTQ PPHPHIVEIV
     LGEIVRQFFY HHSRIKHNDE RLLAAVKSVL TNTEAAKKYI KEIVDGHFFV SNKVFDKSLL
     YMYNDEIITV PFKLSHEPFV WGVNFRKEYN VVSSP