ID   ETF1_FOWPN              Reviewed;         633 AA.
AC   P21966; Q9J5F2;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 107.
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=FPV057; ORFNames=FPD6;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-1;
RX   PubMed=2165135; DOI=10.1099/0022-1317-71-7-1517;
RA   Tartaglia J., Winslow J., Goebel S.J., Johnson G.P., Taylor J.,
RA   Paoletti E.;
RT   "Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox
RT   virus: relatedness to the central portion of the vaccinia virus HindIII D
RT   region.";
RL   J. Gen. Virol. 71:1517-1524(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; X17202; CAA35069.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44401.1; -; Genomic_DNA.
DR   PIR; F35216; F35216.
DR   RefSeq; NP_039020.1; NC_002188.1.
DR   SMR; P21966; -.
DR   GeneID; 1486605; -.
DR   KEGG; vg:1486605; -.
DR   Proteomes; UP000008597; 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.
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..633
FT                   /note="Early transcription factor 70 kDa subunit"
FT                   /id="PRO_0000099073"
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"
FT   CONFLICT        605..633
FT                   /note="NDIIVVPFNLLFTEYSWMINFRKELNVVV -> K (in Ref. 1;
FT                   CAA35069)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   633 AA;  73020 MW;  C17DE6EA97EE4D25 CRC64;
     MNLEILELFN GHIDNIPNIL PHQLATLDYL LRTILDHNES VLLFHIMGSG KTIIALLFAL
     IVSKFKKVYI LVPNINILNI FTYNLDLATN LINTEYVIEN IHIYSTINFY SLNYNDNVVN
     YNALSKYNDS IFIIDEAHNI FGNNTGELMT IIKNKNKVPF LLLSGSPITN TPITLSNIIS
     IMSDEGINFN DIIIQGKKVF QIILNEKGVS VLKNILKNKI SYYELCDTEL PSIIFHGKEF
     LDTKVVYCKM SKLQETDYIN VRKLCNNEMF EKNMTNVSLA VLGPLNLANS LELLFVEQDK
     ELYPNLKIND GVLYGDELTK LNISSKFKYF IDTIGNLTGK NFIYFSNSTY GGLVIKYIML
     NNGYSEYAGS QGTNPKMING HLKTFAIVTS KMKSSLEDLL EVYNSPGNDN GEKIMFLFSS
     NIMSESYTLK EVRNIWFMTI PDTFSQYNQI LGRSIRKFSY KDVSKPVNVY LLATVYSDFN
     DTITSLDDYS IDDINTLPFD IKKLLYLKFK TKETKRIYSI LKDLSINYRS SPHPYITDVV
     LGELVRQFFY HNSRVSINDA KLFKMVNSIF KSKEKTQKYI EKITDDHFFV TNKVFEKSLL
     YKHKNDIIVV PFNLLFTEYS WMINFRKELN VVV