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Database: UniProt
Entry: A7TK55
LinkDB: A7TK55
Original site: A7TK55 
ID   IF4A_VANPO              Reviewed;         396 AA.
AC   A7TK55;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   31-JUL-2019, entry version 57.
DE   RecName: Full=ATP-dependent RNA helicase eIF4A;
DE            EC=3.6.4.13;
DE   AltName: Full=Eukaryotic initiation factor 4A;
DE            Short=eIF-4A;
DE   AltName: Full=Translation initiation factor 1;
GN   Name=TIF1; Synonyms=TIF41; ORFNames=Kpol_1060p58;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the
CC       eIF4F complex involved in cap recognition and is required for mRNA
CC       binding to ribosome. In the current model of translation
CC       initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR
CC       of mRNAs which is necessary to allow efficient binding of the
CC       small ribosomal subunit, and subsequent scanning for the initiator
CC       codon (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Component of the eIF4F complex, which composition varies
CC       with external and internal environmental conditions. It is
CC       composed of at least eIF4A, eIF4E and eIF4G (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC       subfamily. {ECO:0000305}.
DR   EMBL; DS480405; EDO17401.1; -; Genomic_DNA.
DR   RefSeq; XP_001645259.1; XM_001645209.1.
DR   SMR; A7TK55; -.
DR   STRING; 36033.XP_001645259.1; -.
DR   PRIDE; A7TK55; -.
DR   EnsemblFungi; EDO17401; EDO17401; Kpol_1060p58.
DR   GeneID; 5545619; -.
DR   KEGG; vpo:Kpol_1060p58; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; A7TK55; -.
DR   KO; K03257; -.
DR   OMA; RNPIRIL; -.
DR   OrthoDB; 726081at2759; -.
DR   PhylomeDB; A7TK55; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    396       ATP-dependent RNA helicase eIF4A.
FT                                /FTId=PRO_0000310173.
FT   DOMAIN       54    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      234    395       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      67     74       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        23     51       Q motif.
FT   MOTIF       171    174       DEAD box.
SQ   SEQUENCE   396 AA;  44592 MW;  3AA878B6098F437D CRC64;
     MSAEGVSEIE ESQIQTNYDK VVYKFDDMNL KDELLKGVYG YGFEEPSAIQ QRAILPIVEE
     HDVLAQAQSG TGKTGTFSIA ALQRIDSSIK APQALILAPT RELALQIQKV VIALAFHMDV
     KVHACIGGTS FVEDTEGLKD AQIVVGTPGR VSDNIQRHRF KTDNIKMFIL DEADEMLSSG
     FREQIYQIFT MLPPTTQVVL LSATLPGDVL EVTTKFMRNP IRILVKKDEL TLEGIKQFYI
     NVEEEQYKFD CLSDLYDSIS VTQAVIFCNT RRKVEELTQK LTESNFTVSS IYSDLPQQER
     DVIMKEFRSG SSRILISTDL LARGIDVQQV SLVINYDLPT NKENYIHRIG RGGRFGRKGV
     AINFVTNEDV GAMREIEKFY STQIEELPAD VAEMFT
//
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