ID   EIF2D_PONAB             Reviewed;         584 AA.
AC   Q5RA63;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Eukaryotic translation initiation factor 2D;
DE            Short=eIF2d;
DE   AltName: Full=Ligatin;
GN   Name=EIF2D; Synonyms=LGTN;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
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DR   EMBL; CR859158; CAH91347.1; -; mRNA.
DR   RefSeq; NP_001125796.1; NM_001132324.1.
DR   AlphaFoldDB; Q5RA63; -.
DR   SMR; Q5RA63; -.
DR   STRING; 9601.ENSPPYP00000000303; -.
DR   GeneID; 100172724; -.
DR   KEGG; pon:100172724; -.
DR   CTD; 1939; -.
DR   eggNOG; KOG2522; Eukaryota.
DR   InParanoid; Q5RA63; -.
DR   OrthoDB; 401807at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IEA:InterPro.
DR   CDD; cd11608; eIF2D_C; 1.
DR   InterPro; IPR039757; EIF2D.
DR   InterPro; IPR039759; eIF2D_SUI1.
DR   InterPro; IPR041366; Pre-PUA.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR12217; PTHR12217; 1.
DR   Pfam; PF17832; Pre-PUA; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF47592; SSF47592; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS50296; SUI1; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..584
FT                   /note="Eukaryotic translation initiation factor 2D"
FT                   /id="PRO_0000130613"
FT   DOMAIN          93..173
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT   DOMAIN          383..467
FT                   /note="SWIB/MDM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT   DOMAIN          491..564
FT                   /note="SUI1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT   REGION          223..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61211"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41214"
SQ   SEQUENCE   584 AA;  64676 MW;  C602B22CD8231AE3 CRC64;
     MFAKAFRVKS NTAIKGSDRR KLRADVTTAF PTLGTDQVSE LVPGKEELNI VKLYAHKGDA
     VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVMP
     PAGLPQVQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
     NKSSPPSIAP LALDSADLSE EKGSVQMDST LQGDMRHMTL EGEEENGEVH QAREDKSLSE
     APEDTSTRGL NQDSTDSKTL QEQMDELLQQ CFLHALKCRV KKADLPLLAS TFLGSHMFSC
     CPEGRQLDIK KSSYKKLSKF LQQMQQEQII QVKELSKGVE SIVAVDWKHP RITSFVIPEP
     SPTSQTIQEG SREQPYHPPD IKPLYCVPAS MTLLFQESGH KKGSFLEGSE VRTIVINYAK
     KNDLVDADNK NLVRLDPILC DCILEKNEQH TVMKLPWDSL LTRCLEKLQP AYQVTLPGQE
     PIVKKGRICP IDITLAQRAS NKKVTVVRNL EAYGLDPYSV AAILQQRCQA STTVNPAPGA
     KDSLQVQIQG NQVHHLGWLL LEEYQLPRKH IQGLEKALKP GKKK