ID   DDI1_MACFA              Reviewed;         396 AA.
AC   Q95JI3; Q95JM3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protein DDI1 homolog 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1; ORFNames=QtsA-15268, QtsA-17104;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RA   Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA   Sugano S.;
RT   "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT   libraries.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable aspartic protease (By similarity). Seems to act as a
CC       proteasomal shuttle which links the proteasome and replication fork
CC       proteins like RTF2. Required, with DDI2, for cellular survival
CC       following replication stress. Together or redudantly with DDI2, removes
CC       RTF2 from stalled forks to allow cell cycle progression after
CC       replication stress and maintains genome integrity (By similarity).
CC       {ECO:0000250|UniProtKB:I7HUG0, ECO:0000250|UniProtKB:Q8WTU0}.
CC   -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR   EMBL; AB070158; BAB63103.1; -; mRNA.
DR   EMBL; AB070198; BAB63143.1; -; mRNA.
DR   RefSeq; NP_001271475.1; NM_001284546.1.
DR   AlphaFoldDB; Q95JI3; -.
DR   SMR; Q95JI3; -.
DR   STRING; 9541.XP_005579534.1; -.
DR   MEROPS; A28.A01; -.
DR   GeneID; 102146826; -.
DR   CTD; 414301; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0097752; P:regulation of DNA stability; ISS:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
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; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..396
FT                   /note="Protein DDI1 homolog 1"
FT                   /id="PRO_0000287087"
FT   DOMAIN          1..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          82..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="S -> P (in Ref. 2; BAB63103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43998 MW;  ACFE8D2DB029E023 CRC64;
     MLITVYCVRR DLSEATFSLQ VSPDFELRNF KVLCEAESRV PAEEIQIIHM ERLLIEDHCS
     LGSYGLKDGD VVVLLQKDNV GPRAPGRAPN QPRIDFSGIA VPGTSSSRPQ HPGQQQQRTP
     AAQRSHGLAS GETVGVPQGL GSPGLIRSML LSNPHDLSLL KERNPPLAEA LLSGSLETFS
     QVLMAQQREK ALREQERLHL YTADPLDREA QAKIEEEIRQ QNIEENMNIA IEEAPESFGQ
     VTMLYINCKV NGHPLKAFVD SGAQMTIMSQ ACAERCNIMR LVDRRWAGVA KGVGTQRIIG
     RVHLAQIQIE GDFLQCSFSI LEDQPMDMLL GLDMLRRHQC SIDLKKNVLV IGTTGTQTYF
     LPEGELPLCS RMVNGKDESS DKEITHSVMD SGRKEH