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Database: UniProt
Entry: A0A099YV77_TINGU
LinkDB: A0A099YV77_TINGU
Original site: A0A099YV77_TINGU 
ID   A0A099YV77_TINGU        Unreviewed;       315 AA.
AC   A0A099YV77;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit 1 {ECO:0000256|ARBA:ARBA00020950};
DE   AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000256|ARBA:ARBA00033370};
GN   ORFNames=N309_03383 {ECO:0000313|EMBL:KGL73312.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73312.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL73312.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73312.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC       {ECO:0000256|ARBA:ARBA00004210}.
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
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DR   EMBL; KL885857; KGL73312.1; -; Genomic_DNA.
DR   RefSeq; XP_010221136.1; XM_010222834.1.
DR   AlphaFoldDB; A0A099YV77; -.
DR   STRING; 94827.A0A099YV77; -.
DR   GeneID; 104575488; -.
DR   KEGG; tgt:104575488; -.
DR   CTD; 1965; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd04452; S1_IF2_alpha; 1.
DR   Gene3D; 3.30.70.1130; EIF_2_alpha; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR044126; S1_IF2_alpha.
DR   InterPro; IPR024055; TIF2_asu_C.
DR   InterPro; IPR024054; TIF2_asu_middle_sf.
DR   InterPro; IPR011488; TIF_2_asu.
DR   PANTHER; PTHR10602; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   Pfam; PF07541; EIF_2_alpha; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR   SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KGL73312.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT   DOMAIN          17..88
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          292..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..315
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  36151 MW;  3B17E21561B23861 CRC64;
     MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
     KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
     YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP AILDSLDLTE EERRVLIDNI
     NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ENMPIKINLI APPRYVMTTT
     TLERTEGLSV LNQAMAVIKE KIEEKRGVFT VQMEPKVVTD TDETELARQL ERLERENAEV
     DGDDDAEEME AKTED
//
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