ID   DDI1_COCIM              Reviewed;         446 AA.
AC   Q1DNB9; J3K5R6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=DNA damage-inducible protein 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; ORFNames=CIMG_12111;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704913; EAS29448.3; -; Genomic_DNA.
DR   RefSeq; XP_001241031.2; XM_001241030.2.
DR   AlphaFoldDB; Q1DNB9; -.
DR   SMR; Q1DNB9; -.
DR   STRING; 246410.Q1DNB9; -.
DR   MEROPS; A28.A06; -.
DR   EnsemblFungi; EAS29448; EAS29448; CIMG_12111.
DR   GeneID; 24163999; -.
DR   KEGG; cim:CIMG_12111; -.
DR   VEuPathDB; FungiDB:CIMG_12111; -.
DR   InParanoid; Q1DNB9; -.
DR   OMA; IHMVQIQ; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000001261; 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   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..446
FT                   /note="DNA damage-inducible protein 1"
FT                   /id="PRO_0000285311"
FT   DOMAIN          1..83
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          408..446
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          387..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   446 AA;  48041 MW;  181C6EF0F093F577 CRC64;
     MRISVSVVAS NVVVDNDLIS LDVGGEMTLA DLKAVIQSDI NIAPAAQSLF HNNQLLTDDS
     KTLSQIGVVP GDMLGMHIRV PGRELAGSQG SANPSARTTQ ESLARRQQAL PDPETLRLHM
     LGDPRVYETV RMQNPQLAAA ARDSRLFREV LSAQQRAEAD AEAAKEAKIA MLNADPFNLD
     AQREIEDIIR QNAVSENLHN AMEFSPEVFG RVTMLYIPAE VNSHKVKAFV DSGAQVTIMS
     PECAAACNIM HLVDRRYSGV AKGVGTASIL GRVHLAHIKI DDLFLPCSFT VMEGKHIDLL
     LGLDMLKRYQ ACIDLKDNVL RIRDRNVPFL HEADLPKHQD EFANEPLIHG RGGALIGGRT
     GAVTHPAGNP GSLAQNAQTL PARANLAAPV GTPSSSTAPG RNPHSPSRWP AESISKITDI
     GFTREQAIQA LDAANGDLEG AIGYLI