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Database: UniProt
Entry: A0A1E5R758_HANUV
LinkDB: A0A1E5R758_HANUV
Original site: A0A1E5R758_HANUV 
ID   A0A1E5R758_HANUV        Unreviewed;       325 AA.
AC   A0A1E5R758;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=DNA damage-inducible protein 1 {ECO:0000313|EMBL:OEJ82734.1};
GN   ORFNames=AWRI3580_g3717 {ECO:0000313|EMBL:OEJ82734.1};
OS   Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=29833 {ECO:0000313|EMBL:OEJ82734.1, ECO:0000313|Proteomes:UP000095358};
RN   [1] {ECO:0000313|Proteomes:UP000095358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3580 {ECO:0000313|Proteomes:UP000095358};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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:OEJ82734.1}.
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DR   EMBL; LPNN01000009; OEJ82734.1; -; Genomic_DNA.
DR   STRING; 29833.A0A1E5R758; -.
DR   VEuPathDB; FungiDB:AWRI3580_g3717; -.
DR   OrthoDB; 1332686at2759; -.
DR   Proteomes; UP000095358; 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:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR   PANTHER; PTHR12917:SF1; AT13091P; 1.
DR   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS50030; UBA; 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:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095358}.
FT   DOMAIN          108..187
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          285..325
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
SQ   SEQUENCE   325 AA;  37260 MW;  19C6FE4D6CA73EE2 CRC64;
     MAGDPIEKLR IRLINDPQTH AVLKEDFLFS LTQFKALIEF AKVQTNTENS PYFNXSLADV
     LKXYEDMAEI AYQYKIHEQY QHSYTYDPES FTTSCMLYIP IRINNVPILA FVDSGAEKSI
     LSSNFLEXLK LDKMLDKRFV GQARGVGTSN ITGRLHHVMF TFDNEFLPHS LTVLDSLGSA
     ILIGLDFMRK YKCIIDFNTN SFKITGLDVE LKFLNEGQXE KYSNRVLSEE EFKEILSSDD
     FKNXRKIQED KPVSELKEDL ELKKIRTDXS PELNKGKDEP VASFVANEQY IKQLIELGFD
     KIKIVEALTL TNNDLDKAAE LLLSL
//
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