ID   DDI1_CANGA              Reviewed;         426 AA.
AC   Q6FQE9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; OrderedLocusNames=CAGL0I06787g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Probable aspartic protease. May be involved in the regulation
CC       of exocytosis. Acts as a linker between the 19S proteasome and
CC       polyubiquitinated proteins via UBA domain interactions with ubiquitin
CC       for their subsequent degradation. Required for S-phase checkpoint
CC       control. {ECO:0000250|UniProtKB:I7HUG0, ECO:0000250|UniProtKB:P40087}.
CC   -!- SUBUNIT: Binds ubiquitin and polyubiquitinated proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR   EMBL; CR380955; CAG60482.1; -; Genomic_DNA.
DR   RefSeq; XP_447545.1; XM_447545.1.
DR   AlphaFoldDB; Q6FQE9; -.
DR   SMR; Q6FQE9; -.
DR   STRING; 5478.XP_447545.1; -.
DR   MEROPS; A28.001; -.
DR   EnsemblFungi; CAG60482; CAG60482; CAGL0I06787g.
DR   GeneID; 2889069; -.
DR   KEGG; cgr:CAGL0I06787g; -.
DR   CGD; CAL0130071; CAGL0I06787g.
DR   VEuPathDB; FungiDB:CAGL0I06787g; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; Q6FQE9; -.
DR   OMA; EQPMDIL; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:EnsemblFungi.
DR   GO; GO:1904855; F:proteasome regulatory particle binding; IEA:EnsemblFungi.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0009306; P:protein secretion; IEA:EnsemblFungi.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   CDD; cd05479; RP_DDI; 1.
DR   CDD; cd01796; Ubl_Ddi1_like; 1.
DR   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR033882; DDI1_N.
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   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..426
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285309"
FT   DOMAIN          1..80
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          387..426
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  47570 MW;  EBC62E577C5CAF4A CRC64;
     MQLTVTNDVN GEVYGPLELS GDMMLMDLVA LLEVDCAFES GKQQLYFNGK ELKPDVEKTL
     EELGIGNDDL IVIRGQPVSS NSIANSTSAI ELDDDAYVEQ FRLQLLSNSA LRNSLRMPFA
     DIDSLVNDPQ QFKTHMGPVI IQRRRMQSAM PTNPYGIPDE EYKKLMTNPE DPEHKKRLQE
     LQDKQLIDEQ LRNALEYTPE VFAQVSMLYI NMEINGHPVK AFVDSGAQMT IISPRLAEKT
     ELKRFIDNRF IGEARGVGTG KILGRVHQVQ VKIETQFIPC SFVVLDSNVD LLLGLDMLKR
     HQACIDLEKN VLRIAGTETK FLGEAEIPKG TSFDAVGNPQ PPVEIKESAD HSKKKMKTSF
     TITPKVKPVK ADNLLNNSSP MGNTGRTFPE KTIKQLMDLG FSRQEVIQAL VSTNGNAEFA
     ASLLFQ