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Database: UniProt
Entry: A0A1Z5T3N0_HORWE
LinkDB: A0A1Z5T3N0_HORWE
Original site: A0A1Z5T3N0_HORWE 
ID   A0A1Z5T3N0_HORWE        Unreviewed;       311 AA.
AC   A0A1Z5T3N0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000313|EMBL:OTA30461.1};
GN   ORFNames=BTJ68_10114 {ECO:0000313|EMBL:OTA30461.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA30461.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA30461.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA30461.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OTA30461.1}.
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DR   EMBL; MUNK01000139; OTA30461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5T3N0; -.
DR   STRING; 1157616.A0A1Z5T3N0; -.
DR   VEuPathDB; FungiDB:BTJ68_10114; -.
DR   InParanoid; A0A1Z5T3N0; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000194280; 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:OTA30461.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   DOMAIN          17..88
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          284..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   311 AA;  35531 MW;  B220EC761600EC1D CRC64;
     MSLTNCRFYE EKYPEIDSFV MVNVKQIAEM GAYVKLLEYD NIDGMILLSE LSRRRIRSIQ
     KLIRVGRNEV VVVLRVDKEK GYIDLSKRRV SPEDIVKCEE RYNKSKMVHS IMRHVAEKTN
     TPIEELYQEI GWPLNKKYGH AIDAFKLSIT NPEVWNEVTF KTDMIRDELQ SYIGKRLTPT
     PTKVRADVEV TCFGYDGIDA VKEALRTAES KNTEETQVKV KLVSPPLYVL TSQTLDKNVG
     MTILEEAIQE IDKKIRSSGG NLTVKMAPKA VTENDDAELQ ALMDKREREN QEISGDEDDS
     ESDEGQANVG N
//
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