ID   DDI1_ASHGO              Reviewed;         472 AA.
AC   Q754R2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; OrderedLocusNames=AFR010C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53381.1; -; Genomic_DNA.
DR   RefSeq; NP_985557.1; NM_210911.1.
DR   AlphaFoldDB; Q754R2; -.
DR   SMR; Q754R2; -.
DR   STRING; 33169.AAS53381; -.
DR   MEROPS; A28.001; -.
DR   EnsemblFungi; AAS53381; AAS53381; AGOS_AFR010C.
DR   GeneID; 4621796; -.
DR   KEGG; ago:AGOS_AFR010C; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; Q754R2; -.
DR   OMA; PCRFTVI; -.
DR   Proteomes; UP000000591; Chromosome VI.
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   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   PROSITE; PS50030; UBA; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..472
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285304"
FT   DOMAIN          1..72
FT                   /note="Ubiquitin-like"
FT   DOMAIN          434..472
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          388..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  50975 MW;  ACE7B11D35AC00E3 CRC64;
     MNVTVSNEVT DELLGPFELS DDITLMDFMA LIDFDENEQA LWHNMRQLKS VDREKTLMQL
     GIVGESLVVV KAIKKKATEG STTRASKASA KAAKAAAKAA AVARDTPAEQ ATTVSPVAQV
     PVAVSPAVTA AVPTQPTSPS GGPAAANDII TPEDEYIETF RKSLLNSPSL ASNIPIPGVN
     QLIQDSQLFK QLIGPVLLHR RAQQQAANQM GTAQSEYVKL MSNPDDPSNQ ARISELINQQ
     EIDEQLHKAM EYTPEVFASV NMLYINMEIN GHPVKAFVDS GAQSTIMSTA LAERTGLGRL
     VDKRFRGIAR GVGKGEIIGR VHAAQVKIET QFIPCSFIVL DTNVDLLLGL DMLRRYQACV
     DLKENVLKIA GIVTPFLPEA EIPKHFDMDP SAEATNLPST SPLGNQKAAP EARDAGVGSA
     LLNRSTPATA ERTHAEEDVR RLMDLGFSRA EVLKALDHSQ GNAEYAAAFL FQ