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Database: UniProt
Entry: A0A098VT72_9MICR
LinkDB: A0A098VT72_9MICR
Original site: A0A098VT72_9MICR 
ID   A0A098VT72_9MICR        Unreviewed;       241 AA.
AC   A0A098VT72;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=DNA-damage inducible protein 2-related protein {ECO:0000313|EMBL:KGG52197.1};
GN   ORFNames=DI09_1p470 {ECO:0000313|EMBL:KGG52197.1};
OS   Mitosporidium daphniae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX   NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52197.1, ECO:0000313|Proteomes:UP000029725};
RN   [1] {ECO:0000313|EMBL:KGG52197.1, ECO:0000313|Proteomes:UP000029725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UGP3 {ECO:0000313|EMBL:KGG52197.1,
RC   ECO:0000313|Proteomes:UP000029725};
RC   TISSUE=Spores {ECO:0000313|EMBL:KGG52197.1};
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 DDI1 family.
CC       {ECO:0000256|ARBA:ARBA00009136}.
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:KGG52197.1}.
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DR   EMBL; JMKJ01000111; KGG52197.1; -; Genomic_DNA.
DR   RefSeq; XP_013238624.1; XM_013383170.1.
DR   AlphaFoldDB; A0A098VT72; -.
DR   GeneID; 25258937; -.
DR   VEuPathDB; MicrosporidiaDB:DI09_1p470; -.
DR   HOGENOM; CLU_1152018_0_0_1; -.
DR   OrthoDB; 1332686at2759; -.
DR   Proteomes; UP000029725; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR   PANTHER; PTHR12917:SF1; AT13091P; 1.
DR   Pfam; PF09668; Asp_protease; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029725}.
FT   DOMAIN          116..206
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
SQ   SEQUENCE   241 AA;  26747 MW;  C4E48C1E727778D6 CRC64;
     MQKTGLETFH LYLPDEKKNI ELDDNSLTVG NVFKQNITSV IGIIPPKGKT LGVAKQKKKE
     RLSSVLSNEL STFFSPKNPQ ISTQDQNLYH ALEHFPESFG RVVLLFIKVS LAGSSYTALI
     DTGAQASIIC SSIIASNHEI SKAVDKRFFG TANGVGQSKI LGKVHSIELI LWQELQKKEA
     VVLPCGFHVM DMTNSGKIEI ILGLDMLKRH QVILDLGNNC LSVHGYKIKF LSEWELPDNL
     K
//
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