ID   DDI1_PHANO              Reviewed;         442 AA.
AC   Q0U3Y6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; ORFNames=SNOG_13528;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT78975.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445351; EAT78975.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001803736.1; XM_001803684.1.
DR   AlphaFoldDB; Q0U3Y6; -.
DR   SMR; Q0U3Y6; -.
DR   STRING; 13684.SNOT_13528; -.
DR   MEROPS; A28.A06; -.
DR   PRIDE; Q0U3Y6; -.
DR   GeneID; 5980656; -.
DR   KEGG; pno:SNOG_13528; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   InParanoid; Q0U3Y6; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000001055; 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; 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..442
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285318"
FT   DOMAIN          4..84
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          402..442
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          82..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  47556 MW;  A63C8C8E1C89A43E CRC64;
     MPRVTISITA PGTPSDGELL TLELPPGSTV KDLKGFIEAE TNLPAASQGI YLNGQPVSQE
     TQTLENVGIR DGEMLAVIVR QNRQQPQQPA ASRPAPVGQS DPEAVRQQVL RNPQVQAELR
     QRDPELLAIM NDADRWREAF ASRQNSAQNA ERERQNQIAL LNEDPFNVEA QRKIEDIIRQ
     ERVVENLEKA YNENPEVFVR VHMLYINTEV NGVPVKAFVD SGAQATIMSP DCAERCGIMR
     LMDTRYAGMA RGVGTARILG RVHHAEIKIG GAVMPCAFTV MEGKDVDLLF GLDMLKRYKA
     KIDLEKNALC FESIEVPFLH ESEIPRNLDE AEMNEPTVAG PNGTEIGARS GAVRPAGGSA
     AVEPSTQAGP SAAGPSSAST PAPAPAQTAP APSAPGPSTA SSFPEEHINQ LMSMFGVARQ
     EAIQALEIAS GNVDEAASVF LG