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Database: UniProt
Entry: A6ZQJ1
LinkDB: A6ZQJ1
Original site: A6ZQJ1 
ID   IF4A_YEAS7              Reviewed;         395 AA.
AC   A6ZQJ1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   31-JUL-2019, entry version 48.
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=Stimulator factor I 37 kDa component;
DE   AltName: Full=Translation initiation factor 1/2;
DE   AltName: Full=p37;
GN   Name=TIF1; Synonyms=TIF41A; ORFNames=SCY_3152;
GN   and
GN   Name=TIF2; Synonyms=TIF41B; ORFNames=SCY_3429;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R.,
RA   Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA   Li Y., Davis R.W., Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces
RT   cerevisiae strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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; AAFW02000152; EDN59962.1; -; Genomic_DNA.
DR   EMBL; AAFW02000044; EDN63243.1; -; Genomic_DNA.
DR   SMR; A6ZQJ1; -.
DR   IntAct; A6ZQJ1; 2.
DR   MINT; A6ZQJ1; -.
DR   PRIDE; A6ZQJ1; -.
DR   TopDownProteomics; A6ZQJ1; -.
DR   EnsemblFungi; EDN59962; EDN59962; SCY_3429.
DR   EnsemblFungi; EDN63243; EDN63243; SCY_3152.
DR   Proteomes; UP000007060; 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; 2.
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   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; RNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P10081}.
FT   CHAIN         2    395       ATP-dependent RNA helicase eIF4A.
FT                                /FTId=PRO_0000310174.
FT   DOMAIN       53    222       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      233    394       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      66     73       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        22     50       Q motif.
FT   MOTIF       170    173       DEAD box.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P10081}.
FT   MOD_RES      73     73       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P10081}.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P10081}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P10081}.
FT   MOD_RES     146    146       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P10081}.
SQ   SEQUENCE   395 AA;  44697 MW;  19D8C133C815DD48 CRC64;
     MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ RAIMPIIEGH
     DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR ELALQIQKVV MALAFHMDIK
     VHACIGGTSF VEDAEGLRDA QIVVGTPGRV FDNIQRRRFR TDKIKMFILD EADEMLSSGF
     KEQIYQIFTL LPPTTQVVLL SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN
     VEEEEYKYEC LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD
     TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR GGRFGRKGVA
     INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN
//
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