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Database: UniProt
Entry: A0A0L6WSJ0_9AGAR
LinkDB: A0A0L6WSJ0_9AGAR
Original site: A0A0L6WSJ0_9AGAR 
ID   A0A0L6WSJ0_9AGAR        Unreviewed;       398 AA.
AC   A0A0L6WSJ0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP-dependent RNA helicase eIF4A {ECO:0000256|ARBA:ARBA00024412};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=Eukaryotic initiation factor 4A {ECO:0000256|ARBA:ARBA00032223};
GN   ORFNames=J132_01654 {ECO:0000313|EMBL:KNZ78129.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78129.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) 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. {ECO:0000256|ARBA:ARBA00024769}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000256|ARBA:ARBA00024352}.
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DR   EMBL; KQ412487; KNZ78129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WSJ0; -.
DR   STRING; 1306850.A0A0L6WSJ0; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 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; 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   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; 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 {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KNZ78129.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT   DOMAIN          25..53
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          56..226
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          237..398
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   MOTIF           25..53
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   398 AA;  44664 MW;  A25821F536BEDBE2 CRC64;
     MKGEESALQD APVDEIESNW DQVIDSFDNM DLKPELLRGI YAYGFERPSA IQQRAIVPVV
     KGHDVIAQAQ SGTGKTATFS VSILQRLDSN YKGTQALILA PTRELALQIH KVVVALGDYM
     NVSSLACVGG TAVREDIARL QSGVQVVVGT PGRAFDMIKR GALKTDGIKI MCLDEADEML
     SQGFKDQIYE VFQLLPGDTQ VALFSATMPA EVLEVSKKFM RDPVRILVKR DELTLEGIKQ
     FYIAVEKEEW KLDTLCDLYE TITITQAVIF CNTRRKVDLL TDQMLSREFT VSAMHGDMEQ
     KQREVLMKEF RTGSTRVLIT TDLLARGIDV QQVSLVINYD LPTNRENYIH RIGRGGRFGR
     KGVAINFVTT NDVPMLRDIE QFYNTQIDEM PLNVADLI
//
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