ID   DDI1_DEBHA              Reviewed;         448 AA.
AC   Q6BK42;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; OrderedLocusNames=DEHA2F25058g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89844.2; -; Genomic_DNA.
DR   RefSeq; XP_461429.2; XM_461429.1.
DR   AlphaFoldDB; Q6BK42; -.
DR   SMR; Q6BK42; -.
DR   STRING; 4959.XP_461429.2; -.
DR   EnsemblFungi; CAG89844; CAG89844; DEHA2F25058g.
DR   GeneID; 2903057; -.
DR   KEGG; dha:DEHA2F25058g; -.
DR   VEuPathDB; FungiDB:DEHA2F25058g; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; Q6BK42; -.
DR   OMA; IHMVQIQ; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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   Pfam; PF00240; ubiquitin; 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..448
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285313"
FT   DOMAIN          1..78
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          409..448
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          146..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  48132 MW;  4C111B48FEA0A8A4 CRC64;
     MRLTISNESN NQILSVDISE SMTLEDFQAY IQAEFDISPQ DQSLKHNGKP LSGSDKSLED
     LGLNNDDLVL LGKTSVGSTT ASSGSSVTAN SNNSNAVDFQ IEAMRTQFLS NPQLNSQLRQ
     SNPQLHSTLN NPSEFKNSVI GSLQQFQNGA TPGSYNPQQQ EQLSRLQDNP DDPESQSRIL
     EMIRQERIDE NMQLAYEIAP ESFTSVNMLY INIKVNGVLV QAFVDSGAQS TIISPKLADK
     CGISRLIDRR FVGEARGVGS QKIEGKIHSV PIAIGDSDTH IPCSFIVIDT HVDLLFGLDM
     LRRHKCVLDL ERDVLVVGGN IETKFLHESE IQANPFLPGV AGSSASAGGT GGTFGGQGIA
     LGSNSAENNN VTSSIVPANS TPDTTKQKAP NAAANAAVKR QDTGNSSSKF SESDIKQLVS
     LGFSKQEAIF ALEQSQGNVE VAASLLFQ