ID   ETF1_MCV1               Reviewed;         635 AA.
AC   Q98262;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=MC095R;
OS   Molluscum contagiosum virus subtype 1 (MOCV) (MCVI).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Molluscipoxvirus.
OX   NCBI_TaxID=10280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8670425; DOI=10.1126/science.273.5276.813;
RA   Senkevich T.G., Bugert J.J., Sisler J.R., Koonin E.V., Darai G., Moss B.;
RT   "Genome sequence of a human tumorigenic poxvirus: prediction of specific
RT   host response-evasion genes.";
RL   Science 273:813-816(1996).
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; U60315; AAC55223.1; -; Genomic_DNA.
DR   PIR; T30697; T30697.
DR   RefSeq; NP_044046.1; NC_001731.1.
DR   SMR; Q98262; -.
DR   PRIDE; Q98262; -.
DR   GeneID; 1487114; -.
DR   KEGG; vg:1487114; -.
DR   Proteomes; UP000000869; 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   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 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_0000099074"
FT   DOMAIN          32..185
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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;  72878 MW;  FEB2C08224A20376 CRC64;
     MNLGIVSLFR EHVDSIPNIL PHQLATLDFL LRSILDENNS VLLFHIMGSG KTIIALLFAL
     IVSKFKKVYI LVPNINILKI FTYNMGIAVN LINSDYVLEN IHIYSTTSFY SLNYNDNVIN
     YNGLAKYNNA IFIIDEAHNI FGNNTGELMT VIKNKNKVPF LLLSGSPITN TPITLSNIIS
     IMSDEGINFS DIIIQGKKVF QILLNENGVS VLKRILRDKI SYYELQDTEL PSIVFHGRRF
     LDTRIVYCHM SKLQERDYIN VRKLCNNEMF EKNMNNVSLA VLGPLNLINN LDILFQDQDK
     ELYPNLKISN GVLYGDELVS LNISSKFKYF IARIQSLTGK HFIYFSNSTY GGLIIKYIML
     SNGYSEHNGS QGTNPKTIGG RLKTFAIVTS KMKSSLEELL AVYNSPANND GSRIMFLFSS
     NIMSESYTLK EVMHIWFMTI PDTFSQYNQI LGRSIRKFSY TNIAEPVNVY LLAAIYADFD
     DDITSLDNYS IDEINVLPFD IKKLLYLKFK TKETKRIYSI LKDISVNYTL PPHPQIVDVV
     LGELTRQFFY HHSRVRADDP ELFAAIDRVL CSPDSTRRYL DEITRGHFFV CNRVFEKALL
     YRHGEDIIVV PFKLSHDQFL WAINFRKEYN VGAPL