ID A0A074YNV9_AURSE Unreviewed; 310 AA.
AC A0A074YNV9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN ORFNames=AUEXF2481DRAFT_62987 {ECO:0000313|EMBL:KEQ97814.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ97814.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ97814.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ97814.1,
RC ECO:0000313|Proteomes:UP000030641};
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; KL584753; KEQ97814.1; -; Genomic_DNA.
DR RefSeq; XP_013346402.1; XM_013490948.1.
DR AlphaFoldDB; A0A074YNV9; -.
DR STRING; 1043005.A0A074YNV9; -.
DR GeneID; 25369695; -.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; A0A074YNV9; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 4371132at2759; -.
DR Proteomes; UP000030641; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000030641}.
FT DOMAIN 17..88
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 283..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; 35128 MW; 844B79A2C2617F31 CRC64;
MSLTNCRFYE EKYPDVDSLV MVNVRQVAEM GAYVKLLEYD NIDGMILLSE LSRRRIRSIQ
KLIRVGRNEV VVVLRVDKEK GYIDLSKRRV SPEDVLKCED RYNKAKMVHS IMRHVAEKTS
TPMEDLYKNI GWPLDKKYGS SLDAFRISIS NKQVWDEVEF ANNVIKEELI SYIGKRLTPQ
PTKVRADIEV TCFGYEGIDA VKNALRQAEA RNTEDTQVKV KLVSPPLYVL TSQTLDKTIG
ITVLEEAIQE VAKAITAAGG TCSIKMAPKA VTENDEAELQ ALMDKREREN QEVSGDEDES
EEDGIVAVDE
//
