ID   ETF1_VACCW              Reviewed;         637 AA.
AC   P04308; Q76ZS1; Q85350;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 118.
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;
DE   AltName: Full=VETF D6 subunit;
DE   AltName: Full=Vaccinia virus early transcription factor small subunit;
DE            Short=VETF small subunit;
GN   Name=VETFS; OrderedLocusNames=VACWR111; ORFNames=D6R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA   Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT   "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT   fragment.";
RL   Virology 153:96-112(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
RX   PubMed=3033268; DOI=10.1128/jvi.61.5.1398-1406.1987;
RA   Roseman N.A., Hruby D.E.;
RT   "Nucleotide sequence and transcript organization of a region of the
RT   vaccinia virus genome which encodes a constitutively expressed gene
RT   required for DNA replication.";
RL   J. Virol. 61:1398-1406(1987).
RN   [4]
RP   DNA-BINDING.
RX   PubMed=1869572; DOI=10.1016/s0021-9258(18)98651-5;
RA   Broyles S.S.;
RT   "A role for ATP hydrolysis in vaccinia virus early gene transcription.
RT   Dissociation of the early transcription factor-promoter complex.";
RL   J. Biol. Chem. 266:15545-15548(1991).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=2190222; DOI=10.1073/pnas.87.11.4401;
RA   Gershon P.D., Moss B.;
RT   "Early transcription factor subunits are encoded by vaccinia virus late
RT   genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4401-4405(1990).
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH RAP94 AND THE RNA POLYMERASE.
RX   PubMed=19759131; DOI=10.1128/jvi.01653-09;
RA   Yang Z., Moss B.;
RT   "Interaction of the vaccinia virus RNA polymerase-associated 94-kilodalton
RT   protein with the early transcription factor.";
RL   J. Virol. 83:12018-12026(2009).
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   -!- 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. {ECO:0000269|PubMed:19759131}.
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; M15058; AAA48262.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89390.1; -; Genomic_DNA.
DR   EMBL; M16021; AAA69630.1; -; Genomic_DNA.
DR   PIR; F01146; QQVZ11.
DR   RefSeq; YP_232993.1; NC_006998.1.
DR   SMR; P04308; -.
DR   DNASU; 3707567; -.
DR   GeneID; 3707567; -.
DR   KEGG; vg:3707567; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Direct protein sequencing; DNA-binding; Helicase;
KW   Hydrolase; Late protein; Nucleotide-binding; Reference proteome;
KW   Transcription; Transcription regulation; Virion.
FT   CHAIN           1..637
FT                   /note="Early transcription factor 70 kDa subunit"
FT                   /id="PRO_0000099071"
FT   DOMAIN          32..185
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          327..507
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   637 AA;  73831 MW;  C6F172F9E68EDD3D CRC64;
     MNTGIIDLFD NHVDSIPTIL PHQLATLDYL VRTIIDENRS VLLFHIMGSG KTIIALLFAL
     VASRFKKVYI LVPNINILKI FNYNMGVAMN LFNDEFIAEN IFIHSTTSFY SLNYNDNVIN
     YNGLSRYNNS IFIVDEAHNI FGNNTGELMT VIKNKNKIPF LLLSGSPITN TPNTLGHIID
     LMSEETIDFG EIISRGKKVI QTLLNERGVN VLKDLLKGRI SYYEMPDKDL PTIRYHGRKF
     LDTRVVYCHM SKLQERDYMI TRRQLCYHEM FDKNMYNVSM AVLGQLNLMN NLDTLFQEQD
     KELYPNLKIN NGVLYGEELV TLNISSKFKY FINRIQTLNG KHFIYFSNST YGGLVIKYIM
     LSNGYSEYNG SQGTNPHMIN GKPKTFAIVT SKMKSSLEDL LDVYNSPEND DGSQLMFLFS
     SNIMSESYTL KEVRHIWFMT IPDTFSQYNQ ILGRSIRKFS YADISEPVNV YLLAAVYSDF
     NDEVTSLNDY TQDELINVLP FDIKKLLYLK FKTKETNRIY SILQEMSETY SLPPHPSIVK
     VLLGELVRQF FYNNSRIKYN DSKLLKMVTS VIKNKEDARN YIDDIVNGHF FVSNKVFDKS
     LLYKYENDII TVPFRLSYEP FVWGVNFRKE YNVVSSP