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Database: UniProt
Entry: A3GFI4
LinkDB: A3GFI4
Original site: A3GFI4 
ID   IF4A_PICST              Reviewed;         397 AA.
AC   A3GFI4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   31-JUL-2019, entry version 70.
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=PICST_74636;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; AAVQ01000001; EAZ63353.1; -; Genomic_DNA.
DR   RefSeq; XP_001387376.1; XM_001387339.1.
DR   SMR; A3GFI4; -.
DR   STRING; 4924.XP_001387376.1; -.
DR   PRIDE; A3GFI4; -.
DR   EnsemblFungi; EAZ63353; EAZ63353; PICST_74636.
DR   GeneID; 4851033; -.
DR   KEGG; pic:PICST_74636; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; A3GFI4; -.
DR   KO; K03257; -.
DR   OMA; RNPIRIL; -.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
DR   Proteomes; UP000002258; 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    397       ATP-dependent RNA helicase eIF4A.
FT                                /FTId=PRO_0000285135.
FT   DOMAIN       54    224       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      235    396       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       172    175       DEAD box.
SQ   SEQUENCE   397 AA;  44720 MW;  A6C77BBE47809EED CRC64;
     MSSDGIKEID SDLIETNYDN VVYKFDDLNL KPNIVRGIFG YGYETPSAIQ QRAILPITEG
     RDVLAQAQSG TGKTATFTIS ALQRIDENEK STQALILAPT RELALQIKNV ITSIGLYLNV
     TVHASIGGTS MQDDIEAFRS GVQVVVGTPG RVFDMIERRY FKTEKVKMFI MDEADEMLSS
     GFKEQIYNIF RLLPETTQVV LLSATMPQDV LEVTTKFMNN PVRILVKKDE LTLEGIKQFY
     INVELEDYKF DCLCDLYDSI SVTQAVIFCN TRSKVEFLTT KLKAENFTVS AIHADLPQAE
     RDTIMKEFRS GSSRILIATD LLARGIDVQQ VSLVINYDLP SNKENYIHRI GRGGRFGRKG
     VAINFVTERD VGMMREIEQF YSTQIEEMPA DIGALFN
//
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