ID   DDI1_NEUCR              Reviewed;         439 AA.
AC   Q7S906;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=ddi-1; ORFNames=NCU05292;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002239; EAA32827.3; -; Genomic_DNA.
DR   RefSeq; XP_962063.3; XM_956970.3.
DR   AlphaFoldDB; Q7S906; -.
DR   SMR; Q7S906; -.
DR   STRING; 5141.EFNCRP00000005017; -.
DR   MEROPS; A28.A06; -.
DR   EnsemblFungi; EAA32827; EAA32827; NCU05292.
DR   GeneID; 3878211; -.
DR   KEGG; ncr:NCU05292; -.
DR   VEuPathDB; FungiDB:NCU05292; -.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; Q7S906; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; IPR001969; Aspartic_peptidase_AS.
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   SMART; SM00213; UBQ; 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..439
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285317"
FT   DOMAIN          1..82
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          398..438
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          82..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..388
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  47770 MW;  EF3D418345B48BB7 CRC64;
     MQITIAIQDT TGDDQDFLSL QVFPDMTLET LRNSIQAETS HHPSTQHLYH NGNLITDNSK
     TLTQLNVTDG DMLALHVRET QRATAVPESQ QGRPAAPPQQ DPEFLRLQFL ANPALRAEVE
     RTAPDLAAAI NDPQRWAQLF RERYDREQRE RAERHRIIQQ LNEDPFNPEA QARIEEIIRQ
     ERVTENLQTA MEHNPEVFGT VHMLYLDVEV NGAKVKALVD SGAQATIMSP DIAEACGIMR
     LVDKRYGGIA KGVGTAKIIG RVHTAPVKIG SLFLPCSFTV MEGKNVDMLL GLDMLKRYQA
     CIDLAKNALV IQGEEIPFLG EADIPKATEE ALQDEPTIEG PGGTTIGQRT GAVSGPGTAQ
     HRQGQAGPST AAQPGPSAPA PAPASASAPA PRAPQARSFP REHIEQLVAL GADEQKAIRA
     LEATDGNVEY AASLIFEGF