ID   IF4A_YEAST              Reviewed;         395 AA.
AC   P10081; D6VW46;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 247.
DE   RecName: Full=ATP-dependent RNA helicase eIF4A;
DE            EC=3.6.4.13 {ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180};
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 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
DE   AltName: Full=p37;
GN   Name=TIF1 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
GN   Synonyms=TIF41A; OrderedLocusNames=YKR059W;
GN   and
GN   Name=TIF2 {ECO:0000303|PubMed:2648398, ECO:0000303|PubMed:3057442};
GN   Synonyms=TIF41B; OrderedLocusNames=YJL138C; ORFNames=J0660;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2).
RC   STRAIN=CD11/B1830/50;
RX   PubMed=3057442; DOI=10.1093/nar/16.21.10359;
RA   Linder P., Slonimski P.P.;
RT   "Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding
RT   for a translation initiation factor.";
RL   Nucleic Acids Res. 16:10359-10359(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2).
RC   STRAIN=CD11/B1830/50;
RX   PubMed=2648398; DOI=10.1073/pnas.86.7.2286;
RA   Linder P., Slonimski P.P.;
RT   "An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and
RT   homologous to the mammalian translation initiation factor eIF-4A, can
RT   suppress a mitochondrial missense mutation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:2286-2290(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF1).
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF2).
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF2).
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [6]
RP   GENOME REANNOTATION (TIF1 AND TIF2).
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93 (TIF2).
RX   PubMed=8524228; DOI=10.1128/mcb.15.12.6632;
RA   Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J.;
RT   "Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p
RT   for glycogen accumulation in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 15:6632-6640(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-395 (TIF2).
RX   PubMed=2041753; DOI=10.1093/nar/19.10.2781;
RA   Foreman P.K., Davis R.W., Sachs A.B.;
RT   "The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2
RT   gene.";
RL   Nucleic Acids Res. 19:2781-2781(1991).
RN   [9]
RP   PROTEIN SEQUENCE OF 332-340; 342-347 AND 378-391.
RX   PubMed=1408806; DOI=10.1093/nar/20.18.4913;
RA   Smiley J.K., Brown W.C., Campbell J.L.;
RT   "The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60.";
RL   Nucleic Acids Res. 20:4913-4918(1992).
RN   [10]
RP   FUNCTION.
RX   PubMed=2668952; DOI=10.1073/pnas.86.16.6043;
RA   Blum S., Mueller M., Schmid S.R., Linder P., Trachsel H.;
RT   "Translation in Saccharomyces cerevisiae: initiation factor 4A-dependent
RT   cell-free system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6043-6046(1989).
RN   [11]
RP   FUNCTION.
RX   PubMed=2169890; DOI=10.1016/0167-4781(90)90158-x;
RA   Altmann M., Blum S., Pelletier J., Sonenberg N., Wilson T.M., Trachsel H.;
RT   "Translation initiation factor-dependent extracts from Saccharomyces
RT   cerevisiae.";
RL   Biochim. Biophys. Acta 1050:155-159(1990).
RN   [12]
RP   CHARACTERIZATION, AND MUTAGENESIS OF ALA-66; ALA-79; GLY-126; GLY-127;
RP   GLY-145; ASP-170; ASP-173; SER-311 AND ARG-347.
RX   PubMed=2046664; DOI=10.1128/mcb.11.7.3463-3471.1991;
RA   Schmid S.R., Linder P.;
RT   "Translation initiation factor 4A from Saccharomyces cerevisiae: analysis
RT   of residues conserved in the D-E-A-D family of RNA helicases.";
RL   Mol. Cell. Biol. 11:3463-3471(1991).
RN   [13]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF ALA-66.
RX   PubMed=1502180; DOI=10.1073/pnas.89.16.7664;
RA   Blum S., Schmid S.R., Pause A., Buser P., Linder P., Sonenberg N.,
RA   Trachsel H.;
RT   "ATP hydrolysis by initiation factor 4A is required for translation
RT   initiation in Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7664-7668(1992).
RN   [14]
RP   ACETYLATION AT SER-2.
RX   PubMed=9298649; DOI=10.1002/elps.1150180810;
RA   Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA   Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA   Payne W.E.;
RT   "Proteome studies of Saccharomyces cerevisiae: identification and
RT   characterization of abundant proteins.";
RL   Electrophoresis 18:1347-1360(1997).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH TIF4631 AND TIF4632.
RX   PubMed=10409745; DOI=10.1128/mcb.19.8.5557;
RA   Neff C.L., Sachs A.B.;
RT   "Eukaryotic translation initiation factors 4G and 4A from Saccharomyces
RT   cerevisiae interact physically and functionally.";
RL   Mol. Cell. Biol. 19:5557-5564(1999).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH TIF4631.
RX   PubMed=10480875; DOI=10.1074/jbc.274.38.26720;
RA   Dominguez D., Altmann M., Benz J., Baumann U., Trachsel H.;
RT   "Interaction of translation initiation factor eIF4G with eIF4A in the yeast
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:26720-26726(1999).
RN   [17]
RP   FUNCTION, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF PHE-24; PHE-42; SER-46; GLN-49 AND LYS-72.
RX   PubMed=12535527; DOI=10.1016/s1097-2765(03)00006-6;
RA   Tanner N.K., Cordin O., Banroques J., Doere M., Linder P.;
RT   "The Q motif: a newly identified motif in DEAD box helicases may regulate
RT   ATP binding and hydrolysis.";
RL   Mol. Cell 11:127-138(2003).
RN   [18]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [19]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-146, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-77 AND THR-146, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [23]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-225.
RX   PubMed=10606264; DOI=10.1017/s1355838299991410;
RA   Johnson E.R., McKay D.B.;
RT   "Crystallographic structure of the amino terminal domain of yeast
RT   initiation factor 4A, a representative DEAD-box RNA helicase.";
RL   RNA 5:1526-1534(1999).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-233.
RX   PubMed=10404596; DOI=10.1016/s0969-2126(99)80088-4;
RA   Benz J., Trachsel H., Baumann U.;
RT   "Crystal structure of the ATPase domain of translation initiation factor 4A
RT   from Saccharomyces cerevisiae -- the prototype of the DEAD box protein
RT   family.";
RL   Structure 7:671-679(1999).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-395.
RX   PubMed=11087862; DOI=10.1073/pnas.97.24.13080;
RA   Caruthers J.M., Johnson E.R., McKay D.B.;
RT   "Crystal structure of yeast initiation factor 4A, a DEAD-box RNA
RT   helicase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13080-13085(2000).
CC   -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F
CC       complex involved in cap recognition and is required for mRNA binding to
CC       ribosome. In the current model of translation initiation, eIF4A unwinds
CC       RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC       allow efficient binding of the small ribosomal subunit, and subsequent
CC       scanning for the initiator codon. {ECO:0000269|PubMed:10409745,
CC       ECO:0000269|PubMed:10480875, ECO:0000269|PubMed:12535527,
CC       ECO:0000269|PubMed:1502180, ECO:0000269|PubMed:2169890,
CC       ECO:0000269|PubMed:2668952}.
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         Evidence={ECO:0000269|PubMed:12535527, ECO:0000269|PubMed:1502180};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=470 uM for ATP {ECO:0000269|PubMed:12535527,
CC         ECO:0000269|PubMed:1502180};
CC         Vmax=2.6 pmol/sec/ug enzyme for ATP {ECO:0000269|PubMed:12535527,
CC         ECO:0000269|PubMed:1502180};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:12535527,
CC         ECO:0000269|PubMed:1502180};
CC   -!- SUBUNIT: Component of the eIF4F complex, which composition varies with
CC       external and internal environmental conditions. It is composed of at
CC       least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632)
CC       (By similarity). Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632.
CC       {ECO:0000250, ECO:0000269|PubMed:10409745,
CC       ECO:0000269|PubMed:10480875}.
CC   -!- INTERACTION:
CC       P10081; P39935: TIF4631; NbExp=10; IntAct=EBI-9017, EBI-9002;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000269|PubMed:12535527}.
CC   -!- MISCELLANEOUS: TIF1 and TIF2 code for the same protein.
CC   -!- MISCELLANEOUS: Present with 106000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X12813; CAA31301.1; -; Genomic_DNA.
DR   EMBL; X12814; CAA31302.1; -; Genomic_DNA.
DR   EMBL; X58099; CAA41110.1; -; Genomic_DNA.
DR   EMBL; X87371; CAA60817.1; -; Genomic_DNA.
DR   EMBL; Z49413; CAA89433.1; -; Genomic_DNA.
DR   EMBL; U25436; AAA91645.1; -; Genomic_DNA.
DR   EMBL; Z28284; CAA82138.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08662.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09210.1; -; Genomic_DNA.
DR   PIR; S05835; FIBY1.
DR   RefSeq; NP_012397.1; NM_001181571.1.
DR   RefSeq; NP_012985.3; NM_001179849.3.
DR   PDB; 1FUK; X-ray; 1.75 A; A=231-395.
DR   PDB; 1FUU; X-ray; 2.50 A; A/B=2-395.
DR   PDB; 1QDE; X-ray; 2.00 A; A=9-232.
DR   PDB; 1QVA; X-ray; 2.50 A; A=2-224.
DR   PDB; 2VSO; X-ray; 2.60 A; A/B=1-395.
DR   PDB; 2VSX; X-ray; 2.80 A; A/B=1-395.
DR   PDBsum; 1FUK; -.
DR   PDBsum; 1FUU; -.
DR   PDBsum; 1QDE; -.
DR   PDBsum; 1QVA; -.
DR   PDBsum; 2VSO; -.
DR   PDBsum; 2VSX; -.
DR   AlphaFoldDB; P10081; -.
DR   SMR; P10081; -.
DR   BioGRID; 33619; 466.
DR   BioGRID; 34190; 383.
DR   ComplexPortal; CPX-430; Eukaryotic translation initiation factor 4F complex, variant TIF4631.
DR   ComplexPortal; CPX-431; Eukaryotic translation initiation factor 4F complex, variant TIF4632.
DR   DIP; DIP-4571N; -.
DR   IntAct; P10081; 87.
DR   MINT; P10081; -.
DR   STRING; 4932.YJL138C; -.
DR   CarbonylDB; P10081; -.
DR   iPTMnet; P10081; -.
DR   MaxQB; P10081; -.
DR   PaxDb; 4932-YJL138C; -.
DR   PeptideAtlas; P10081; -.
DR   EnsemblFungi; YJL138C_mRNA; YJL138C; YJL138C.
DR   EnsemblFungi; YKR059W_mRNA; YKR059W; YKR059W.
DR   GeneID; 853303; -.
DR   GeneID; 853933; -.
DR   KEGG; sce:YJL138C; -.
DR   KEGG; sce:YKR059W; -.
DR   AGR; SGD:S000001767; -.
DR   AGR; SGD:S000003674; -.
DR   SGD; S000001767; TIF1.
DR   SGD; S000003674; TIF2.
DR   VEuPathDB; FungiDB:YJL138C; -.
DR   VEuPathDB; FungiDB:YKR059W; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   GeneTree; ENSGT00940000155037; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; P10081; -.
DR   OMA; FGCQALV; -.
DR   OrthoDB; 1087080at2759; -.
DR   BioCyc; YEAST:G3O-32027-MONOMER; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-72649; Translation initiation complex formation.
DR   Reactome; R-SCE-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   SABIO-RK; P10081; -.
DR   BioGRID-ORCS; 853303; 3 hits in 10 CRISPR screens.
DR   BioGRID-ORCS; 853933; 3 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P10081; -.
DR   PRO; PR:P10081; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P10081; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IMP:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0005840; C:ribosome; NAS:ComplexPortal.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR   GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR   GO; GO:0006446; P:regulation of translational initiation; NAS:ComplexPortal.
DR   GO; GO:0006413; P:translational initiation; IDA:SGD.
DR   CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   DisProt; DP02562; -.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044728; EIF4A_DEADc.
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   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF1; EUKARYOTIC TRANSLATION INITIATION FACTOR EIF-4A; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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.
DR   SWISS-2DPAGE; P10081; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Helicase; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298649,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..395
FT                   /note="ATP-dependent RNA helicase eIF4A"
FT                   /id="PRO_0000054968"
FT   DOMAIN          53..222
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          233..394
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           22..50
FT                   /note="Q motif"
FT   MOTIF           170..173
FT                   /note="DEAD box"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:9298649,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         73
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         146
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MUTAGEN         24
FT                   /note="F->A: Lethal in vivo and reduces ATP binding and
FT                   ATPase activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         42
FT                   /note="F->A: Slow growth in vivo and reduces ATP binding
FT                   and ATPase activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         46
FT                   /note="S->A: Reduces ATP binding and ATPase activity in
FT                   vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         49
FT                   /note="Q->A: Reduces ATP binding and ATPase activity in
FT                   vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         49
FT                   /note="Q->E: Increases about 3-fold ATP binding but reduces
FT                   about 2-fold ATPase activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         66
FT                   /note="A->D: Slow growth."
FT                   /evidence="ECO:0000269|PubMed:1502180,
FT                   ECO:0000269|PubMed:2046664"
FT   MUTAGEN         66
FT                   /note="A->V: Lethal and dominant negative if overexpressed
FT                   in vivo. Impairs ATP hydrolysis, RNA-helicase and
FT                   translation activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:1502180,
FT                   ECO:0000269|PubMed:2046664"
FT   MUTAGEN         72
FT                   /note="K->A: Lethal in vivo and reduces ATP binding and
FT                   ATPase activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:12535527"
FT   MUTAGEN         79
FT                   /note="A->V: In TIF1-1; no growth at 36 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         126
FT                   /note="G->D: Lethal."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         127
FT                   /note="G->D: Slow growth."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         145
FT                   /note="G->D: Lethal."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         145
FT                   /note="G->S: Slow growth."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         170
FT                   /note="D->E: Lethal."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         173
FT                   /note="D->H: Lethal."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         311
FT                   /note="S->F: Slow growth."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   MUTAGEN         347
FT                   /note="R->E,G,I,S,T: Lethal and dominant negative if
FT                   overexpressed."
FT                   /evidence="ECO:0000269|PubMed:2046664"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:1FUU"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           31..40
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           100..113
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           130..139
FT                   /evidence="ECO:0007829|PDB:1FUU"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           147..155
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           172..177
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           181..190
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          196..203
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   HELIX           206..215
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1QDE"
FT   STRAND          235..243
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           247..257
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           270..282
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          287..290
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           296..307
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          312..317
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   TURN            321..323
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          330..336
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           341..346
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          359..365
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   TURN            366..368
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   HELIX           369..378
FT                   /evidence="ECO:0007829|PDB:1FUK"
FT   STRAND          383..385
FT                   /evidence="ECO:0007829|PDB:1FUU"
FT   TURN            391..394
FT                   /evidence="ECO:0007829|PDB:1FUK"
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
//