ID   IF4A_CRYPV              Reviewed;         405 AA.
AC   O02494;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Eukaryotic initiation factor 4A;
DE            Short=eIF-4A;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A;
GN   Name=EIF4-A;
OS   Cryptosporidium parvum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=5807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Moredun;
RA   Spano F., Putignani L., Crisanti A.;
RT   "Cloning of the eIF4-A translation initiation factor gene of
RT   Cryptosporidium parvum.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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; AF001378; AAB58799.1; -; mRNA.
DR   EMBL; AF001211; AAB58726.1; -; mRNA.
DR   AlphaFoldDB; O02494; -.
DR   SMR; O02494; -.
DR   PRIDE; O02494; -.
DR   VEuPathDB; CryptoDB:cgd1_880; -.
DR   OMA; EHKDGQR; -.
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; 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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding.
FT   CHAIN           1..405
FT                   /note="Eukaryotic initiation factor 4A"
FT                   /id="PRO_0000054946"
FT   DOMAIN          62..232
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          243..404
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           31..59
FT                   /note="Q motif"
FT   MOTIF           180..183
FT                   /note="DEAD box"
FT   BINDING         75..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   405 AA;  45934 MW;  BD1E558048C6B79A CRC64;
     MTNSEQNPPS EENVQVASTG EIESNYDEIV ECFEALNLEG DLLRGIFAYG FEKPSAIQQR
     GIKPILDGYD TIGQAQSGTG KTATFVIAAL QKIDYSLNAC QVLLLAPTRE LAQQIQKVAL
     ALGDYCELRC HACVGGTSVR DDMNKLKSGV HMVVGTPGRV FDMLDKGYLR VDNLKLFILD
     EADEMLSRGF KVQIHDIFKK LPQDVQVALF SATMPNEILH LTTQFMRDPK RILVKQEELT
     LEGIRQFYVG VEKDEWKMDT LIDLYETLTI VQAIIYCNTR RRVDQLTKQM RERDFTCSSM
     HGDMDQKDRE VIMRQFRSGS SRVLITTDLL ARGIDVQQVS LVINYDLPVS PETYIHRIGR
     SGRFGKKGVS INFVTDDDIV CLRDIERHYN TQIEEMPMGI TDILQ