ETF1_VARV
ID ETF1_VARV Reviewed; 637 AA.
AC P0DOO0; P33056; Q9QNI6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
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;
GN Name=VETFS; ORFNames=D6R;
OS Variola virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=10255;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bangladesh-1975;
RX PubMed=8264798; DOI=10.1038/366748a0;
RA Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT "Potential virulence determinants in terminal regions of variola smallpox
RT virus genome.";
RL Nature 366:748-751(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Garcia-1966;
RX PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT "Alastrim smallpox variola minor virus genome DNA sequences.";
RL Virology 266:361-386(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22579; AAA60844.1; -; Genomic_DNA.
DR EMBL; Y16780; CAB54696.1; -; Genomic_DNA.
DR PIR; F72162; F72162.
DR PIR; T28534; T28534.
DR SMR; P0DOO0; -.
DR Proteomes; UP000111493; Genome.
DR Proteomes; UP000119805; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00271; Helicase_C; 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 3: Inferred from homology;
KW Activator; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Transcription; Transcription regulation; Virion.
FT CHAIN 1..637
FT /note="Early transcription factor 70 kDa subunit"
FT /id="PRO_0000448131"
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"
FT VARIANT 136
FT /note="K -> E (in strain: Garcia-1966)"
FT VARIANT 462
FT /note="V -> A (in strain: Garcia-1966)"
SQ SEQUENCE 637 AA; 73830 MW; FA1E882BCF0CDFD7 CRC64;
MNTGIIDLFD NHVDSIPTIL PHQLATLDYL VRTIIDENRS VLLFHIMGSG KTIIALLFAL
IASRFKKVHI LVPNINILKI FNYNMGVAMN LFNDEFIAEN IFIHSTTSFY SLNYNDNVIN
YNGLSRYNNS IFIVDKAHNI 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 YVDISEPVNV YLLAAVYSDF
NDEVTSLNDY TQDELINVLP FDIKKLLYLK FKTKETNRIY SILQEMSETY SLPPHPSIVK
VLLGELVRQF FYNNSRIKYN DAKLLKMVTS VIKNKEDARN YIDDIVNGHF FVSNKVFDKS
LLYKYENDII TVPFRLSYEP FVWGVNFRKE YNVVSSP