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 08-NOV-2023, entry version 112.
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; Fowlpox virus.
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; Segment.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
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; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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
//
