ID A0A0D2DE63_9EURO Unreviewed; 313 AA.
AC A0A0D2DE63;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN ORFNames=PV06_06920 {ECO:0000313|EMBL:KIW41353.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41353.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW41353.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41353.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223}.
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DR EMBL; KN847337; KIW41353.1; -; Genomic_DNA.
DR RefSeq; XP_016261569.1; XM_016408089.1.
DR AlphaFoldDB; A0A0D2DE63; -.
DR STRING; 215243.A0A0D2DE63; -.
DR GeneID; 27358994; -.
DR VEuPathDB; FungiDB:PV06_06920; -.
DR HOGENOM; CLU_033458_0_1_1; -.
DR OrthoDB; 4371132at2759; -.
DR Proteomes; UP000053342; 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:UP000053342}.
FT DOMAIN 21..92
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 35588 MW; 8D3ACBE87C3DE965 CRC64;
MSDPESLTNC RFYEEKYPEI ESFVMVNVKQ IAEMGAYVKL LEYDNIDGMI LLSELSRRRI
RSIQKLIRIG RNEVVVVLRV DKEKGYIDLS KRRVSAEDIV RCEERYNKSK SVHSIFRHVA
EKTKTPILKL YENIGWPLNK KYVHANDAFK LSITNPEVWN DVAFPNEVVK EELISYISKK
LTPHPTKVRA DVEVTCFKYD GIDAVKDALR KAEAKNTPDT QVKVKLVSPP HYVLTSQCLD
KTMGIQLLEQ AIKDIEESIK EAGGGCVVKM APKAVTEHDD AELQALMDKR AKENEEVSGD
EDVSESDEGP EVA
//
