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IF4A_CRYNB
ID   IF4A_CRYNB              Reviewed;         401 AA.
AC   P0CQ71; Q55YU1; Q5KN60;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
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; OrderedLocusNames=CNBA7450;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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 (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 with
CC       external and internal environmental conditions. It is composed of at
CC       least eIF4A, eIF4E and eIF4G (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAEY01000005; EAL22977.1; -; Genomic_DNA.
DR   RefSeq; XP_777624.1; XM_772531.1.
DR   AlphaFoldDB; P0CQ71; -.
DR   SMR; P0CQ71; -.
DR   EnsemblFungi; AAW41293; AAW41293; CNA07620.
DR   EnsemblFungi; EAL22977; EAL22977; CNBA7450.
DR   GeneID; 4934011; -.
DR   KEGG; cnb:CNBA7450; -.
DR   VEuPathDB; FungiDB:CNBA7450; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA 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   CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR   Gene3D; 3.40.50.300; -; 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; 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; 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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT   CHAIN           1..401
FT                   /note="ATP-dependent RNA helicase eIF4A"
FT                   /id="PRO_0000410246"
FT   DOMAIN          59..229
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          240..401
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           28..56
FT                   /note="Q motif"
FT   MOTIF           177..180
FT                   /note="DEAD box"
FT   BINDING         72..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   401 AA;  45144 MW;  32D6418B1BBD7C68 CRC64;
     MSDTKGAAEQ GLQIDGDLIN SNWNEVVDNF DDMKLKGELL RGIYAYGFER PSAIQQRAIM
     PIVTGRDCIA QAQSGTGKTA TFSVSILQRI DTTVKKTQAL VLAPTRELAQ QIQKVVIALG
     DYLNVDCHAC VGGTAVREDI ARLNEGPHIV VGTPGRVFDM INRGALKTEA VMMFCLDEAD
     EMLSTGFKES IYEIFQLLPG ETQVVLLSAT MAPEVLDVTK KFMRDPIRIL VKKDELTLEG
     IRQFYINVEK EEWKLETLCD LYETVTITQA VIFCSTRRKV DWLTQQLHDR QFTVSAMHGD
     MKQEEREVIM KEFRSGSSRV LITTDLLARG IDVQQVSLVI NYDLPSSKEN YIHRIGRGGR
     FGRKGVAINF VSNEDKNMLE EIETYYNTQV EEMPLNVADL I
 
 
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