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IF4A3_NICPL
ID   IF4A3_NICPL             Reviewed;         391 AA.
AC   P41380;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Eukaryotic initiation factor 4A-3;
DE            Short=eIF-4A-3;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-3;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=1719476; DOI=10.1093/nar/19.20.5491;
RA   Owttrim G.W., Hofmann S., Kuhlemeier C.;
RT   "Divergent genes for translation initiation factor eIF-4A are coordinately
RT   expressed in tobacco.";
RL   Nucleic Acids Res. 19:5491-5496(1991).
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; X61206; CAA43514.1; -; mRNA.
DR   PIR; S22579; S22579.
DR   AlphaFoldDB; P41380; -.
DR   SMR; P41380; -.
DR   PRIDE; P41380; -.
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; 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; 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..391
FT                   /note="Eukaryotic initiation factor 4A-3"
FT                   /id="PRO_0000054952"
FT   DOMAIN          49..219
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          230..391
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           18..46
FT                   /note="Q motif"
FT   MOTIF           167..170
FT                   /note="DEAD box"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   391 AA;  44194 MW;  92CD2721916BCB1E CRC64;
     MEEDRLVFET SKGVEPIASF AEMGIKDDLL RGVYQYGFEK PSAIQQRAVL PIISGRDVIA
     QAQSGTGKTS MIALTVCQIV DTKSSEVQAL ILSPTRELAA QTEKVILAIG DYINVQAHAC
     IGGKSVGEDI RKLEHGVQVV SGTPGRVCDM IKRRTLRTRG IKLLILDESD EMLSRGFKDQ
     IYDVYRYLPP ELQVVLISAT LPNEILEITS KFMTDPVRIL VKRDELTLEG IKQFFVAVEK
     EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTSKMREN NFTVSSMHGD MPQKERDAIM
     AEFRGGTTRV LITTDVWARG LDVQQVSLVI NYDLPNNREL YIHRIGRSGR FGRKGVAINF
     VKSDDIKILR DIEQYYSTQI DEMPMNVADL I
 
 
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