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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//