ID   DDI1_BOVIN              Reviewed;         396 AA.
AC   Q2T9Z1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein DDI1 homolog 1;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=DDI1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) 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; BC111200; AAI11201.1; -; mRNA.
DR   RefSeq; NP_001071488.1; NM_001078020.2.
DR   AlphaFoldDB; Q2T9Z1; -.
DR   SMR; Q2T9Z1; -.
DR   STRING; 9913.ENSBTAP00000003750; -.
DR   MEROPS; A28.A01; -.
DR   PaxDb; Q2T9Z1; -.
DR   PRIDE; Q2T9Z1; -.
DR   GeneID; 539082; -.
DR   KEGG; bta:539082; -.
DR   CTD; 414301; -.
DR   eggNOG; KOG0012; Eukaryota.
DR   InParanoid; Q2T9Z1; -.
DR   OrthoDB; 817208at2759; -.
DR   Proteomes; UP000009136; 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   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_0000287085"
FT   DOMAIN          1..81
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          84..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43878 MW;  BF5A041D0976BDC3 CRC64;
     MLLTVYCVRR DLSEATFSLQ VRPDFELHNF LVLCELESGI PAEETQIVYM ERLLVNDHCS
     LGSYGLKDGD MVILLQKEAM RPRSPERAAG LCSMEPAGPA LPGTSGSRPH QRAQSAQHSS
     RRGSGEKAGP GQGLDSPALV RSMLLSSPHD LSLLKERNPS LAEALLSGNL ESFSQVLMEQ
     QRERALREQE RLRLFSADPF DLEAQAKIEE EIRQQNIEEN MSIAMEEAPE SFGQVAMLYI
     NCRVNGHPLK AFVDSGAQMT IMNQVCAERC NIIRLVDRRW AGVAKGVGTQ RILGRVHLAQ
     IQIEGDFLQC SFSILEEQPM DMLLGLDMLR RHQCSIDLKR NVLVIGTTGT QTSFLPEGEL
     PPCAKLVSGM GPEESSDKET ANAIKHSVMD SGRKKH