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Database: UniProt
Entry: A7F620_SCLS1
LinkDB: A7F620_SCLS1
Original site: A7F620_SCLS1 
ID   A7F620_SCLS1            Unreviewed;       313 AA.
AC   A7F620;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN   ORFNames=SS1G_13048 {ECO:0000313|EMBL:EDN98191.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98191.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
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DR   EMBL; CH476643; EDN98191.1; -; Genomic_DNA.
DR   RefSeq; XP_001585956.1; XM_001585906.1.
DR   AlphaFoldDB; A7F620; -.
DR   STRING; 665079.A7F620; -.
DR   EnsemblFungi; EDN98191; EDN98191; SS1G_13048.
DR   GeneID; 5482032; -.
DR   KEGG; ssl:SS1G_13048; -.
DR   eggNOG; KOG2916; Eukaryota.
DR   HOGENOM; CLU_033458_0_1_1; -.
DR   InParanoid; A7F620; -.
DR   OMA; DVNEHQR; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0005840; C:ribosome; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:EnsemblFungi.
DR   GO; GO:1990856; F:methionyl-initiator methionine tRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IEA:EnsemblFungi.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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:UP000001312}.
FT   DOMAIN          17..91
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          286..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  35405 MW;  B856F15FD31FEB98 CRC64;
     MSLTNCRFYE EKYPEIDSFV MVNVKAASQI AEMGAYVKLL EYDNIDGMIL LSELSRRRIR
     SIQKLIRVGR NEVVVVLRVD KEKGYIDLSK RRVSPEDIVR CEERYNKGKM VHSIMRHVAE
     KTKHPIEDLY EKIVWPLNKK YGHAVDAFKL SITNADTWQD VSFPNDIVAE ELKSYIGKRL
     TPQPTKVRAD VEVTCFGYEG IDAVKTALRT AEARNTADNQ VKVKLVSPPL YVLTSTCLEK
     SVGISTLEAA IVDIRKNIEA AGGGLIVKME PKAVTENDDA ELQALMEKRE RENAEVSGDE
     SMSESDENQV EVM
//
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