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Database: UniProt
Entry: J4UC07_TRIAS
LinkDB: J4UC07_TRIAS
Original site: J4UC07_TRIAS 
ID   J4UC07_TRIAS            Unreviewed;       296 AA.
AC   J4UC07;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000313|EMBL:EJT48465.1};
GN   ORFNames=A1Q1_02486 {ECO:0000313|EMBL:EJT48465.1};
OS   Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS   KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT48465.1, ECO:0000313|Proteomes:UP000002748};
RN   [1] {ECO:0000313|EMBL:EJT48465.1, ECO:0000313|Proteomes:UP000002748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC   7654 {ECO:0000313|Proteomes:UP000002748};
RX   PubMed=23104369; DOI=10.1128/EC.00237-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Draft genome sequence of CBS 2479, the standard type strain of
RT   Trichosporon asahii.";
RL   Eukaryot. Cell 11:1415-1416(2012).
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJT48465.1}.
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DR   EMBL; ALBS01000203; EJT48465.1; -; Genomic_DNA.
DR   RefSeq; XP_014179223.1; XM_014323748.1.
DR   AlphaFoldDB; J4UC07; -.
DR   GeneID; 25986000; -.
DR   KEGG; tasa:A1Q1_02486; -.
DR   VEuPathDB; FungiDB:A1Q1_02486; -.
DR   HOGENOM; CLU_033458_0_1_1; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000002748; Unassembled WGS sequence.
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:EJT48465.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          10..81
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   296 AA;  33530 MW;  AC9C678F4F80E232 CRC64;
     MVRFYENKYP ELVMVQVQSI EDMGAYVKLL EYDGIEGMIL LSELSRRRIR SVQKLIRVGR
     NEVVVVMRVD PDKGYIDLSK RRVSAEEVVK CEEQYEKGRA VDSILTQVAK RRNVPTESLY
     EQIAWPLQRK YGHAYEAFKL SIQEPEVVFG PLEIEPDTLA ELKHTIARRL TPKPVKVRAD
     IEVRCFAYNG IEAIRKALKA GEALSTEAVP IKVRLVAPPL YVMSTTSTDK SAAIETMEKA
     VEAINQTITE EKGDMLVKMA PKVVSETEDA ELKALMEEFE QANMDVAGDD DSDEED
//
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