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Database: UniProt
Entry: IF4A_LEIMA
LinkDB: IF4A_LEIMA
Original site: IF4A_LEIMA 
ID   IF4A_LEIMA              Reviewed;         403 AA.
AC   O62591; E9AC68;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Probable eukaryotic initiation factor 4A;
DE            Short=eIF-4A;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A;
GN   ORFNames=LmjF.01.0770;
GN   and
GN   ORFNames=LmjF.01.0780;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=10077609; DOI=10.1073/pnas.96.6.2902;
RA   Myler P.J., Audleman L., deVos T., Hixson G., Kiser P., Lemley C.,
RA   Magness C., Rickel E., Sisk E., Sunkin S., Swartzell S., Westlake T.,
RA   Bastien P., Fu G., Ivens A., Stuart K.;
RT   "Leishmania major Friedlin chromosome 1 has an unusual distribution of
RT   protein-coding genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2902-2906(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B.G., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(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: eIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E and EIF4G (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FR796397; CBZ11882.1; -; Genomic_DNA.
DR   EMBL; FR796397; CBZ11883.1; -; Genomic_DNA.
DR   PIR; A81464; A81464.
DR   RefSeq; XP_003721599.1; XM_003721551.1.
DR   RefSeq; XP_003721600.1; XM_003721552.1.
DR   AlphaFoldDB; O62591; -.
DR   SMR; O62591; -.
DR   STRING; 5664.O62591; -.
DR   EnsemblProtists; CBZ11882; CBZ11882; LMJF_01_0770.
DR   EnsemblProtists; CBZ11883; CBZ11883; LMJF_01_0780.
DR   GeneID; 12983087; -.
DR   GeneID; 12983088; -.
DR   KEGG; lma:LMJF_01_0770; -.
DR   KEGG; lma:LMJF_01_0780; -.
DR   VEuPathDB; TriTrypDB:LmjF.01.0770; -.
DR   VEuPathDB; TriTrypDB:LMJFC_010013300; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_010013100; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_010013100; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   InParanoid; O62591; -.
DR   OMA; FGCQALV; -.
DR   Proteomes; UP000000542; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; ISA:GeneDB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IPI:GeneDB.
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; ISO:GeneDB.
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; IBA:GO_Central.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; ISA:GeneDB.
DR   CDD; cd17939; DEADc_EIF4A; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   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; 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; Helicase; Hydrolase; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..403
FT                   /note="Probable eukaryotic initiation factor 4A"
FT                   /id="PRO_0000291643"
FT   DOMAIN          57..230
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          241..401
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..54
FT                   /note="Q motif"
FT   MOTIF           178..181
FT                   /note="DEAD box"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   403 AA;  45327 MW;  97FB8FCE6AA92DCD CRC64;
     MAQNDKIAPQ DQDSFLDDQP GVRPIPSFDD MPLHQNLLRG IYSYGFEKPS SIQQRAIAPF
     TRGGDIIAQA QSGTGKTGAF SIGLLQRLDF RHNLIQGLVL SPTRELALQT AEVISRIGEF
     LSNSSKFCET FVGGTRVQDD LRKLQAGVIV AVGTPGRVSD VIKRGALRTE SLRVLVLDEA
     DEMLSQGFAD QIYEIFRFLP KDIQVALFSA TMPEEVLELT KKFMRDPVRI LVKRESLTLE
     GIKQFFIAVE EEHKLDTLMD LYETVSIAQS VIFANTRRKV DWIAEKLNQS NHTVSSMHAE
     MPKSDRERVM NTFRSGSSRV LVTTDLVARG IDVHHVNIVI NFDLPTNKEN YLHRIGRGGR
     YGRKGVAINF VTEKDVELLH EIEAHYHTQI DELPVDFAAY LGE
//
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