EIF2A_XENLA
ID EIF2A_XENLA Reviewed; 582 AA.
AC Q7ZY11;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Eukaryotic translation initiation factor 2A;
DE Short=eIF-2A;
GN Name=eif2a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000250|UniProtKB:Q9BY44}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC044026; AAH44026.1; -; mRNA.
DR AlphaFoldDB; Q7ZY11; -.
DR SMR; Q7ZY11; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; PTHR13227; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; Translation regulation; WD repeat.
FT CHAIN 1..582
FT /note="Eukaryotic translation initiation factor 2A"
FT /id="PRO_0000286080"
FT REPEAT 21..63
FT /note="WD 1"
FT REPEAT 73..124
FT /note="WD 2"
FT REPEAT 273..314
FT /note="WD 3"
FT REPEAT 358..402
FT /note="WD 4"
FT REGION 436..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..580
FT /evidence="ECO:0000255"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 64817 MW; 95B5238816763027 CRC64;
MAPPMPLLSV RGSDGIQLVL GPPKFTDSET FQRDPSKNCK VSRFTKDGKL FGWCNGEVIN
IVNCSDSKLL HTLDLPKVVS LEFSPKNTIL ATWQTYTTGK DGTAGTPNLQ LYDLKSGKIS
NVKSFIQKKM ENWSPHWSDD ENICARNVNN EVHFFENNNF DTIANKLHLQ KVSDFELSPG
EQPCKVAVYV PGSKGAPSFV RLYQYPNFSG PNSALANKSF FKADRVAMLW NSKATAVLVT
ASTDVDKTGA SYYGEQTLHY IAVNGESAVV QLPKNGPIYD VTWNKNATEF CVVYGFMPAK
ATVFNLKCDP IFDFGTGPRN AAFYSPQGHI LVLAGFGNLR GQMEVWDVKK YKLISKPTAS
DATFFSWCPN GEHIITATCS PRLRVGNGYK IWHYTGTLLH KYDVPANSEL WQVSWQPFPD
GVFPAKAIVY QAVPGDLPTQ ESKPAEAYRP PALRNKPVSS YKLHEDEPPQ SMMPQSTEKP
MSKTALKNQK KREAKKAAKQ ESKMDEPAES DSTNVQNNTP VAVNTGDPET DKKIKNLKKK
LKAIEQLKEL QSSGKTLEKN QIEKIQKEDI LLKELEDLEI GV