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Database: UniProt
Entry: A0A1J8R164_9AGAM
LinkDB: A0A1J8R164_9AGAM
Original site: A0A1J8R164_9AGAM 
ID   A0A1J8R164_9AGAM        Unreviewed;       131 AA.
AC   A0A1J8R164;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
DE   Flags: Fragment;
GN   ORFNames=AZE42_02223 {ECO:0000313|EMBL:OJA15466.1};
OS   Rhizopogon vesiculosus.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA15466.1, ECO:0000313|Proteomes:UP000183567};
RN   [1] {ECO:0000313|EMBL:OJA15466.1, ECO:0000313|Proteomes:UP000183567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA15466.1,
RC   ECO:0000313|Proteomes:UP000183567};
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (MAR-2016) 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:OJA15466.1}.
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DR   EMBL; LVVM01003113; OJA15466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J8R164; -.
DR   STRING; 180088.A0A1J8R164; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000183567; 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; 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; 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; PF00575; S1; 1.
DR   SMART; SM00316; S1; 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:UP000183567}.
FT   DOMAIN          12..62
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   NON_TER         131
FT                   /evidence="ECO:0000313|EMBL:OJA15466.1"
SQ   SEQUENCE   131 AA;  15164 MW;  FD6FF39AD3EABC34 CRC64;
     MRYYEQRFPE VDELVMVQVR QIAEMGAYVK LLEYDNIEGM ILLSELSRRR IRSIQKLIRV
     GRNEVVVSPN TGYIDLSKRR VSPEDIIKCE ERYMKSKAVA SIMRHVASKL PSMDADAAIS
     PEEEAVEKET K
//
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