ID   ETF1_MSEPV              Reviewed;         674 AA.
AC   Q9YVX9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=MSV113;
OS   Melanoplus sanguinipes entomopoxvirus (MsEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Deltaentomopoxvirus.
OX   NCBI_TaxID=83191;
OH   NCBI_TaxID=65742; Melanoplus sanguinipes (Migratory grasshopper).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Tucson;
RX   PubMed=9847359; DOI=10.1128/jvi.73.1.533-552.1999;
RA   Afonso C.L., Tulman E.R., Lu Z., Oma E., Kutish G.F., Rock D.L.;
RT   "The genome of Melanoplus sanguinipes entomopoxvirus.";
RL   J. Virol. 73:533-552(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; AF063866; AAC97658.1; -; Genomic_DNA.
DR   PIR; T28274; T28274.
DR   RefSeq; NP_048184.1; NC_001993.1.
DR   SMR; Q9YVX9; -.
DR   GeneID; 1449921; -.
DR   KEGG; vg:1449921; -.
DR   Proteomes; UP000172353; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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..674
FT                   /note="Early transcription factor 70 kDa subunit"
FT                   /id="PRO_0000099075"
FT   DOMAIN          34..193
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   674 AA;  78088 MW;  8F1BC451A8CE8678 CRC64;
     MNKIILEDLK ESNVPLYIPQ ILPHQLATLD FLNERSLKEK KSVLLFHKMG SGKTIISLLF
     SIIASIETKI LIILPNTSIM DIWISKLYDS LLLLNKNDKY NLNNIEFTTR SRLNEELLGT
     NKNINDIITE NIKKYDNYII IIDEAHNFFG NASGELLIHI KQNSTARYVL LTGSPISNTI
     ESLKDIVELL TNETFEYNKY IESAGNKVFQ QRINKQGIEL LKNKLTGLIS YYDEDRKDIP
     SPIFQGNIKL LNYPVVLCPM SKLQEDNYNM ISNQTENDMF IKLMMNVSLV ALGDKENYTN
     FDLLMASNKQ IFPNFYVSNG KFIGQELIDL NISSKLKYFM NSILTSPNAG KRFIYFANST
     IGSTIIRSVM IANGISEYDK EIVNNFVCVN CLKERNCNNK ECIPMKFVII TSKESNKGNN
     SYINKILSVF NEDVNENGSV IMFLFGSRII AEAYTLKDIK EIWFLTVPET KSELEQCIAR
     AIRSFAYKDK NTRVVVRICL ATTPNALSNE ISQIIEKYKD ESLSDEEKTL LLNKFEMKLV
     NYAIDLPYDL RKQLYSEFKS EKAKVAYNIF INLSILTNNI LNDNILKCFI IEKIRRYSYE
     NSRYKLKDIL SYIKKNLKFD YKNKIEDYVN EFVNDGVVVY NKSFGTCYID WFKDDIVVKQ
     IILEFNNYLL SYNY