ID A0A3Q2X8D3_HAPBU Unreviewed; 590 AA.
AC A0A3Q2X8D3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819, ECO:0000256|PIRNR:PIRNR017222};
DE Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000031470.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000031470.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003993,
CC ECO:0000256|PIRNR:PIRNR017222}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC {ECO:0000256|ARBA:ARBA00009573, ECO:0000256|PIRNR:PIRNR017222}.
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DR AlphaFoldDB; A0A3Q2X8D3; -.
DR STRING; 8153.ENSHBUP00000031470; -.
DR Ensembl; ENSHBUT00000023497.1; ENSHBUP00000031470.1; ENSHBUG00000017252.1.
DR GeneTree; ENSGT00730000111053; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW ECO:0000256|PIRNR:PIRNR017222}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 215..410
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 430..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 64866 MW; F5B630A04FBED665 CRC64;
MAPPVPLLAV RGSDGTSLLR GPPHCEPHAA FQRDCRPSRC VTFSTDGTLF GWCNGQNVSI
VNPSDGAVVS TFDLPKTALL EFSPLNNILV TWQLYTKTQD SPQGEANLQL WELRSGRLIK
ALYQKKVESW CPSWSEDEKI CVRIVNNELH FYEDNDFDSI ANKLHMQKVS DFALSPGGQP
SKVAVYVPGS KGAPSFVRLY QYPAFGGPTA ALANKSFFKA DRVMMQWNKK ASAVLVTAST
EVDKTGASYY GEQTLHYLGV NGETALVQLS KNGPIYDVAW SPSSTEFCVV YGFMPAKATV
FNLKCDPVYD FGTGPRNAAY YSPQGHILIL AGFGNLRGQM EVWDVKNYKQ VSKPQAPDAT
HFSWCPDGEH IVTATCSPRL RVSNGYKIWH YTGSVLQKWD VTAGSELWEV RWQSLPDGSF
PKRPIKYQAA PSQLGSTQAP PTQAYRPPAL RHLPATPSSK LHEDEPPQDL RPGASGEKSL
SKSALKNQRK REAKKAAKQV RLESPGGGVS GVWCCDWSLS DVCTFQKLKA IEELKEQQAS
GKVLQKNQVM FVDNLTLMSH KLIWAHEGQT PGAAVIGGPW VVPGGTVITL
//
