ID H3AJI9_LATCH Unreviewed; 596 AA.
AC H3AJI9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 04-NOV-2026, entry version 74.
DE RecName: Full=Eukaryotic translation initiation factor 2D {ECO:0000256|ARBA:ARBA00013816};
DE AltName: Full=Ligatin {ECO:0000256|ARBA:ARBA00030186};
GN Name=EIF2D {ECO:0000313|Ensembl:ENSLACP00000009810.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000009810.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Ensembl:ENSLACP00000009810.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2026) to UniProtKB.
CC -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC the P-site of 40S ribosomes, the situation that takes place during
CC initiation complex formation on some specific RNAs. Its activity in
CC tRNA binding with 40S subunits does not require the presence of the
CC aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC its role in initiation, can promote release of deacylated tRNA and mRNA
CC from recycled 40S subunits following ABCE1-mediated dissociation of
CC post-termination ribosomal complexes into subunits.
CC {ECO:0000256|ARBA:ARBA00025522}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eIF2D family.
CC {ECO:0000256|ARBA:ARBA00010359}.
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DR EMBL; AFYH01111200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01111207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006000440.1; XM_006000378.3.
DR AlphaFoldDB; H3AJI9; -.
DR FunCoup; H3AJI9; 2760.
DR STRING; 7897.ENSLACP00000009810; -.
DR Ensembl; ENSLACT00000009886.1; ENSLACP00000009810.1; ENSLACG00000008651.1.
DR GeneID; 102363323; -.
DR KEGG; lcm:102363323; -.
DR CTD; 1939; -.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR InParanoid; H3AJI9; -.
DR OMA; AACNNTE; -.
DR OrthoDB; 199771at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000008651; Expressed in chordate pharynx and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:InterPro.
DR CDD; cd11608; eIF2D_C; 1.
DR CDD; cd11610; eIF2D_N; 1.
DR CDD; cd21156; PUA_eIF2d-like; 1.
DR FunFam; 3.10.400.20:FF:000002; Eukaryotic translation initiation factor 2D; 1.
DR FunFam; 3.30.780.10:FF:000007; Putative eukaryotic translation initiation factor 2d; 1.
DR Gene3D; 3.10.400.20; -; 1.
DR Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR048247; eIF2D_N.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR048248; PUA_eIF2d-like.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR058886; SWIB_eIF2D.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR057429; WH_eIF2D.
DR PANTHER; PTHR12217; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR PANTHER; PTHR12217:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF26292; PUA_elF2D; 1.
DR Pfam; PF01253; SUI1; 1.
DR Pfam; PF26291; SWIB_eIF2D; 1.
DR Pfam; PF25304; WHD_eIF2D; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55159; eIF1-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 392..479
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 503..576
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 188..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 66207 MW; 026EB99ACF179661 CRC64;
MFVKPFRVKS NTSIKGSDRR KLKADIGASF PSLSAEQLSE LIPNKEELNV LKIYTHKGDA
VTVYVTHKNP VFFEVEKKLY PTVYTLWSCS DLLPALTTWP AVLQKLAGGA DLMLPGVVMP
PTGLPQVQRG SLCAVTLVGN GAPVGVGIAT MSSEEMLGAG MKGKGLTLTH TYLDLLWGFG
DKSNPPMVAP LVPEPAEMVD SSEEKEDSPV DAINNQDFNP PPELENLQIS GGHSDFTEGK
EPSESADTVA AENGEEATME QLEAEEKAPQ EDMDQLLLQC FLHAVKYKVK KSDLPLLTST
FLRNHMYSCR PEGKQLDIKK SSYKKLSKFL QCMQQRKIIL VKELSKGVES IVDVEWKHED
IRSFKVPEIS SSADSTEIRN TGDEDKPYLP PEILPLYSVS AKLVPLFQES RHKKGDILSS
SEVRSIITNY VKSNELVNET NKNFVTINPI LCDCVLDKSE HSEITSLKWD DLFARCLQRM
QPCHQVTFSG QEPIIRKGNI EPIDITVAQR GSNKKVTLIK NLELYGLDPN SVASTLQQRV
QASAITHPLP GSKDRVQVQI QGNQINQVGK LLFEDYRILR KYVQGMDKAP KSGKKK
//
