ID   DDI1_CRYNJ              Reviewed;         434 AA.
AC   P0CS14; Q55V04; Q5KL78;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; OrderedLocusNames=CNC00460;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017343; AAW42029.1; -; Genomic_DNA.
DR   RefSeq; XP_569336.1; XM_569336.1.
DR   AlphaFoldDB; P0CS14; -.
DR   SMR; P0CS14; -.
DR   STRING; 5207.AAW42029; -.
DR   PaxDb; P0CS14; -.
DR   EnsemblFungi; AAW42029; AAW42029; CNC00460.
DR   GeneID; 3256457; -.
DR   KEGG; cne:CNC00460; -.
DR   VEuPathDB; FungiDB:CNC00460; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; P0CS14; -.
DR   OMA; PCRFTVI; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
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   Gene3D; 2.40.70.10; -; 1.
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; 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.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..434
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285312"
FT   DOMAIN          1..77
FT                   /note="Ubiquitin-like"
FT   DOMAIN          395..434
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          315..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        212
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   434 AA;  46131 MW;  9D6B552F97DD86BC CRC64;
     MRLTIIAPDS VHEHEVSPSL LIQDIINIVE ATADLPPAVI VLTSDAGTPL TDPTRTLESY
     GLNGETATIF LTPTGPPVAS SSSIPFPDAD ADIERMRLQA LGNPSLMNDL RERDPETFAA
     IQGGTQSFKK ALQLAQSRQR DAEFEKQRQI EALNADPYDI EAQKKIEEAI RMEAVLENMQ
     HAMEYSPESF GNVTMLYINV EVNGHPVKAF VDSGAQTTII SPECAEQCGI MRLLDTRFAG
     MAEGVGTARI LGRIHSAQIK LGSLYLPCAF SVLEGRSVDL LFGLDMLKRH QCCIDLSTNT
     LRINNTEVPF LSEHELPDKA RRRGEAQVAG EMGDAAGQGV KAGVASPKIG KKTFPGEGHA
     LGAGSSTGPG TATGSASATG ARTGGTASVP SPSNRWKEDD IQTLVNLGAP RAQAIQLLEA
     SGGNVDVAAS MLFG