ID   DDI1_ASPCL              Reviewed;         404 AA.
AC   A1CDT9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=ddi1; ORFNames=ACLA_007750;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027051; EAW12016.1; -; Genomic_DNA.
DR   RefSeq; XP_001273442.1; XM_001273441.1.
DR   AlphaFoldDB; A1CDT9; -.
DR   SMR; A1CDT9; -.
DR   STRING; 5057.CADACLAP00000416; -.
DR   PRIDE; A1CDT9; -.
DR   EnsemblFungi; EAW12016; EAW12016; ACLA_007750.
DR   GeneID; 4705413; -.
DR   KEGG; act:ACLA_007750; -.
DR   VEuPathDB; FungiDB:ACLA_007750; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   OMA; IHMVQIQ; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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..404
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285305"
FT   DOMAIN          1..57
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          366..404
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          57..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   404 AA;  43915 MW;  F736A3BAD6A9927A CRC64;
     MSVELLKAIV ESETSIPANT QRLVYNNQLL GNDSQTLEQI GIGEGDMLGV HVTLRSPQAP
     ARSVGPPSTA AQQNLQRRQA AAPDPETIRL HILGDPRVRE AVRRQNPELA QAADDAHRFR
     EVLMAQQRRE AQLEAEKEAR IAMLNSDPFN PENQREIEEI IRQNAVTENL HTAMEHHPES
     FGRVTMLYIP VEVNGHKVNA FVDSGAQVTI MSPECATACN IMRLVDQRYG GIAKGVGTAT
     ILGRVHSAQI KIGSMFLPCS FTVMEGKHID LLLGLDMLRR HQACIDLKNG ALVIQDQAVP
     FLGEADIPRQ LQDEFEDEPI IKGADGAEVG ARTGAITHQA SGSSTSAAAP SSSTPRMNIR
     PAASSRWPQD SIAKITELGF TREEAIRALD AANGDLDGAI GFLI