ID A0A665SZ95_ECHNA Unreviewed; 555 AA.
AC A0A665SZ95;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 02-SEP-2026, entry version 25.
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:ENSENLP00000002850.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000002850.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000002850.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSENLP00000002850.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-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 AlphaFoldDB; A0A665SZ95; -.
DR Ensembl; ENSENLT00000003032.1; ENSENLP00000002850.1; ENSENLG00000001406.1.
DR Proteomes; UP000472264; Chromosome 7.
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; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
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 SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55159; eIF1-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 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:UP000472264}.
FT DOMAIN 462..535
FT /note="SUI1"
FT /evidence="ECO:0000259|PROSITE:PS50296"
FT REGION 183..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 61744 MW; 63A145DFFF7400C0 CRC64;
MFSKSFRVKS NTVIKGSDRR KLKADVSAAF ASLSADELSE LIPNKEEINV VKIYAHKGEA
VTLYVLHKNP LFFELEKRLY PTVYVLWRYP ALLPTFKTWP PVLQKLIGGA DLMLPGVVVP
STGLPQVKRG DCCAVTLVNN GASVAVGTAA LSSEEMQSSG MKGRGVCVLH TYMDNLWAFG
DKSGPPTLLD AESKGQRVNE DESEEEEEEE KEGEEKEKKE IEKNVEEEHG SAYGTATDHV
CPDFEELGLA EKNEEEDEKC KEGVEENHDN SRTPQEIMDA LLVQCFLHAL KSKPKWKLSK
FLQAMQQQHN LVQVKELTKG VESIVEVDWK NPQLRSFIVP EETGGEAVPA QGGGEGEAPY
HPPEISTLYC VSARVEPLFL EANKRTVLPS ECVSVLFSPL HSYVSINTTL CDCLLEKSEY
QEVEFLKWDD LFSRTLGKMQ ECYQIVFPGQ TAIIKKGHIE PIDISVASRG SNKKVTLIKN
LEVYCLDPAV VATALQHRVQ ASSVLQPIPG AKDKVLVQIQ GNQIHQVGSL LLDHYRIPRK
YIQGLEKAVK GGKKK
//
