IF4A_ENCCU
ID IF4A_ENCCU Reviewed; 425 AA.
AC Q8SQM5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=ECU09_1200;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
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; AL590451; CAD27090.1; -; Genomic_DNA.
DR RefSeq; XP_955671.1; XM_950578.1.
DR AlphaFoldDB; Q8SQM5; -.
DR SMR; Q8SQM5; -.
DR STRING; 284813.Q8SQM5; -.
DR GeneID; 860456; -.
DR KEGG; ecu:ECU09_1200; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_1200; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q8SQM5; -.
DR OMA; FTHRNGR; -.
DR OrthoDB; 726081at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
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 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..425
FT /note="ATP-dependent RNA helicase eIF4A"
FT /id="PRO_0000255981"
FT DOMAIN 69..241
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 252..425
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 38..66
FT /note="Q motif"
FT MOTIF 187..190
FT /note="DEAD box"
FT BINDING 82..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 425 AA; 48490 MW; 5A1DD46E9C8FA6AC CRC64;
MKQVTEQAED FVDTRSSGTE IREFEDLRSD SSQIRMFDTW EDYGLKEDLL KGIYSIGFET
PSFIQKAAIQ PIIDGRDIRA QAQSGTGKTG AFAVAALQIC DMSQDVTQIL VLASTREIAA
QNAARFEDLG CFMGARVALL SGGSPIAADK VALEKKPHIV VGTPGRVEHM ININELSMDN
IKLFVIDEAD EMLKAGFQEQ VKSIFRRITN KDEVQIAMFS ATYDEEELRV SEEILINPVI
IDLRYNDQTL KGIRQYFIDL RKEPPFRKGR EDYLLPKLVT LYDIFRKQRL GQSIVFINSK
EDARIVYDWL IRHEWECELI SAELTQAERE RTLNRFRGGT GRCLISSGLL SRGIDIQNLS
VVFCLDVPSF ERKSTYIHRI GRSGRYGRKG IAINIVYEHE LKNLKAIERF YNTTIKELPA
DFSFQ
