IF4A_LEIBR
ID IF4A_LEIBR Reviewed; 403 AA.
AC Q25225; A4H393;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=LbrM01_V2.0740, LbrM_01_0740;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2903;
RX PubMed=7699334; DOI=10.1084/jem.181.4.1527;
RA Skeiky Y.A.W., Guderian J.A., Benson D.R., Bacelar O., Carvalho E.M.,
RA Kubin M., Badaro R., Trinchieri G., Reed S.G.;
RT "A recombinant Leishmania antigen that stimulates human peripheral blood
RT mononuclear cells to express a Th1-type cytokine profile and to produce
RT interleukin 12.";
RL J. Exp. Med. 181:1527-1537(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
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; U19888; AAA80219.1; -; Genomic_DNA.
DR EMBL; FR798975; CAM36502.1; -; Genomic_DNA.
DR RefSeq; XP_001561513.1; XM_001561463.1.
DR AlphaFoldDB; Q25225; -.
DR SMR; Q25225; -.
DR STRING; 5660.Q25225; -.
DR GeneID; 5412356; -.
DR KEGG; lbz:LBRM_01_0740; -.
DR VEuPathDB; TriTrypDB:LbrM.01.0740; -.
DR VEuPathDB; TriTrypDB:LBRM2903_010013700; -.
DR InParanoid; Q25225; -.
DR OMA; EHKDGQR; -.
DR Proteomes; UP000007258; Chromosome 1.
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 Gene3D; 3.40.50.300; -; 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 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; 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_0000054948"
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"
FT CONFLICT 363
FT /note="R -> V (in Ref. 1; AAA80219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 45327 MW; 7AC069DCC7227164 CRC64;
MSQQDRVAPQ DQDSFLDDQP GVRPIPSFDD MPLHQNLLRG IYSYGFEKPS SIQQRAIAPF
TRGGDIIAQA QSGTGKTGAF SIGLLQRLDF RHNLIQGLVL SPTRELALQT AEVISRIGEF
LSNSAKFCET FVGGTRVQDD LRKLQAGVVV AVGTPGRVSD VIKRGALRTE SLRVLVLDEA
DEMLSQGFAD QIYEIFRFLP KDIQVALFSA TMPEEVLELT KKFMRDPVRI LVKRESLTLE
GIKQFFIAVE EEHKLDTLMD LYETVSIAQS VIFANTRRKV DWIAEKLNQS NHTVSSMHAE
MPKSDRERVM NTFRSGSSRV LVTTDLVARG IDVHHVNIVI NFDLPTNKEN YLHRIGRGGR
YGRKGVAINF VTEKDVELLH EIEGHYHTQI DELPVDFAAY LGE
