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Database: UniProt
Entry: O93120
LinkDB: O93120
Original site: O93120 
ID   ETF1_VACCA              Reviewed;         637 AA.
AC   O93120; Q6J3C7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-NOV-2019, entry version 88.
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;
DE   AltName: Full=Vaccinia virus early transcription factor small subunit;
DE            Short=VETF small subunit;
GN   Name=VETFS; OrderedLocusNames=MVA103R, ACAM3000_MVA_103; ORFNames=D6R;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
RA   Osborne J., Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts with RNA polymerase to initiate transcription from
CC       early gene promoters. Is recruited by the RPO-associated protein
CC       of 94 kDa (RAP94) to form the early transcription complex, which
CC       also contains the core RNA polymerase. ETF heterodimer binds to
CC       early gene promoters (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:0000250}. Note=All the enzymes
CC       and other proteins required to synthesize early mRNAs are packaged
CC       within the virion core along with the DNA genome. This is
CC       necessary because viral early mRNAs are synthesized within minutes
CC       after virus entry into the cell and are extruded through pores in
CC       the core particle (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. VETF subfamily.
CC       {ECO:0000305}.
DR   EMBL; U94848; AAB96515.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10501.1; -; Genomic_DNA.
DR   PIR; T37379; T37379.
DR   PRIDE; O93120; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; Genome.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 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; Complete proteome; DNA-binding; Helicase;
KW   Hydrolase; Late protein; Nucleotide-binding; Transcription;
KW   Transcription regulation; Virion.
FT   CHAIN         1    637       Early transcription factor 70 kDa
FT                                subunit.
FT                                /FTId=PRO_0000099068.
FT   DOMAIN       32    185       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      327    507       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      45     52       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       135    138       DEXH box.
SQ   SEQUENCE   637 AA;  73845 MW;  66A172FF3B55DBE0 CRC64;
     MNTGIIDLFD NHVDSIPTIL PHQLATLDYL VRTIIDENRS VLLFHIMGSG KTIIALLFAL
     VASRFKKVYI LVPNINILKI FNYNMGVAMN LFNDEFIAEN IFIHSTTSFY SLNYNDNVIN
     YNGLSRYNNS IFIVDEAHNI 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 YADISEPVNV YLLAAVYSDF
     NDEVTSLNDY TQDELINVLP FDIKKLLYLK FKTKETNRIY SILQEMSETY SLPPHPSIVK
     VLLGELVRQF FYNNSRIKYN DTKLLKMVTS VIKNKEDARN YIDDIVNGHF FVSNKVFDKS
     LLYKYENDII TVPFRLSYEP FVWGVNFRKE YNVVSSP
//
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