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Database: UniProt
Entry: A0A098VPS9_9MICR
LinkDB: A0A098VPS9_9MICR
Original site: A0A098VPS9_9MICR 
ID   A0A098VPS9_9MICR        Unreviewed;       344 AA.
AC   A0A098VPS9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN   ORFNames=DI09_4p430 {ECO:0000313|EMBL:KGG50960.1};
OS   Mitosporidium daphniae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX   NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG50960.1, ECO:0000313|Proteomes:UP000029725};
RN   [1] {ECO:0000313|EMBL:KGG50960.1, ECO:0000313|Proteomes:UP000029725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UGP3 {ECO:0000313|EMBL:KGG50960.1,
RC   ECO:0000313|Proteomes:UP000029725};
RC   TISSUE=Spores {ECO:0000313|EMBL:KGG50960.1};
RA   Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA   Ebert D.;
RT   "A new species of microsporidia sheds light on the evolution of extreme
RT   parasitism.";
RL   Submitted (APR-2014) 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:KGG50960.1}.
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DR   EMBL; JMKJ01000444; KGG50960.1; -; Genomic_DNA.
DR   RefSeq; XP_013237387.1; XM_013381933.1.
DR   AlphaFoldDB; A0A098VPS9; -.
DR   GeneID; 25260180; -.
DR   VEuPathDB; MicrosporidiaDB:DI09_4p430; -.
DR   HOGENOM; CLU_033458_0_1_1; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000029725; 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:UP000029725}.
FT   DOMAIN          48..119
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          320..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38821 MW;  AB138F76D8798072 CRC64;
     MPSSSSSPTP AQASTSSASI SKTSISKINV DRDKYDCRMY ENKYPEVDDL VMVNVRQIAE
     MGAYVTLLEY NNIEGMVLLS ELSRRRIRSI QKLIRVGRNE VVVVLRVDKE KGYIDLSKRR
     VSPEEVQKCE EKFLKSKAVH TIMRNISEKH SISTESLYEQ LGWPLYKQFG HAYDAFKLAI
     EEPERVFGGP ENPYGLDAKV LDDILVNINR RLLPQKAKIR ADIEVMCYTF EGIEAIKEAL
     RAGETLSTEQ IPIKIKLVAP PLYVIFTNCF DKIQGLELLA ASIAKISEKI VSFGGMLNVK
     MNPRVVSDVD DLELDAMMKR AEQENAEVSG DEDNSEEDDS ERAS
//
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