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Database: UniProt
Entry: A0A074WG83_9PEZI
LinkDB: A0A074WG83_9PEZI
Original site: A0A074WG83_9PEZI 
ID   A0A074WG83_9PEZI        Unreviewed;       310 AA.
AC   A0A074WG83;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000313|EMBL:KEQ70584.1};
GN   ORFNames=M436DRAFT_53069 {ECO:0000313|EMBL:KEQ70584.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70584.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ70584.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70584.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
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DR   EMBL; KL584716; KEQ70584.1; -; Genomic_DNA.
DR   RefSeq; XP_013424859.1; XM_013569405.1.
DR   AlphaFoldDB; A0A074WG83; -.
DR   STRING; 1043004.A0A074WG83; -.
DR   GeneID; 25411706; -.
DR   HOGENOM; CLU_033458_0_1_1; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000027730; 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:KEQ70584.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT   DOMAIN          17..88
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          284..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  35136 MW;  4B3BD830F102D87C CRC64;
     MSLTNCRFYE EKYPDVDSLV MVNVRQVAEM GAYVKLLEYD NIDGMILLSE LSRRRIRSIQ
     KLIRVGRNEV VVVLRVDKEK GYIDLSKRRV SPEDVLKCED RYNKAKMVHS IMRHVAEKTS
     TPMEDLYKSI GWPLDKKYGS SLDAFRISIS NKQVWDEVEF ANNVIKEELI SYISKRLTPQ
     PTKVRADIEV TCFGYEGIDA VKTALRQAEA RNTEDTQVKV KLVSPPLYVL TSQTLDKTIG
     ITVLEEAIQE VTKTITAAGG TCSVKMAPKA VTENDDAELQ ALMDKREREN QEVSGDEDES
     DEDGIVAVDE
//
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