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Database: UniProt
Entry: EIF2D_PONAB
LinkDB: EIF2D_PONAB
Original site: EIF2D_PONAB 
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   28-FEB-2018, entry version 61.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC       manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC       finds its position in the P-site of 40S ribosomes, the situation
CC       that takes place during initiation complex formation on some
CC       specific RNAs. Its activity in tRNA binding with 40S subunits does
CC       not require the presence of the aminoacyl moiety. Possesses the
CC       unique ability to deliver non-Met (elongator) tRNAs into the P-
CC       site of the 40S subunit. In addition to its role in initiation,
CC       can promote release of deacylated tRNA and mRNA from recycled 40S
CC       subunits following ABCE1-mediated dissociation of post-termination
CC       ribosomal complexes into subunits (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
DR   EMBL; CR859158; CAH91347.1; -; mRNA.
DR   RefSeq; NP_001125796.1; NM_001132324.1.
DR   UniGene; Pab.6349; -.
DR   ProteinModelPortal; Q5RA63; -.
DR   SMR; Q5RA63; -.
DR   STRING; 9601.ENSPPYP00000000303; -.
DR   PRIDE; Q5RA63; -.
DR   GeneID; 100172724; -.
DR   KEGG; pon:100172724; -.
DR   CTD; 1939; -.
DR   eggNOG; KOG2522; Eukaryota.
DR   eggNOG; ENOG410XSAV; LUCA.
DR   HOVERGEN; HBG006268; -.
DR   InParanoid; Q5RA63; -.
DR   KO; K15027; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   Gene3D; 2.30.130.10; -; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
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.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Initiation factor;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    584       Eukaryotic translation initiation factor
FT                                2D.
FT                                /FTId=PRO_0000130613.
FT   DOMAIN       93    173       PUA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00161}.
FT   DOMAIN      491    564       SUI1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00200}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P41214}.
FT   MOD_RES     237    237       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P41214}.
FT   MOD_RES     254    254       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61211}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {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
//
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