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
//