ID   DDI1_DICDI              Reviewed;         450 AA.
AC   Q54JB0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Protein DDI1 homolog;
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN   Name=ddi1; ORFNames=DDB_G0288187;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Probable aspartic protease. {ECO:0000250|UniProtKB:I7HUG0}.
CC   -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR   EMBL; AAFI02000109; EAL63324.1; -; Genomic_DNA.
DR   RefSeq; XP_636826.1; XM_631734.1.
DR   AlphaFoldDB; Q54JB0; -.
DR   SMR; Q54JB0; -.
DR   STRING; 44689.DDB0266774; -.
DR   MEROPS; A28.A04; -.
DR   PaxDb; Q54JB0; -.
DR   EnsemblProtists; EAL63324; EAL63324; DDB_G0288187.
DR   GeneID; 8626495; -.
DR   KEGG; ddi:DDB_G0288187; -.
DR   dictyBase; DDB_G0288187; ddi1.
DR   eggNOG; KOG0012; Eukaryota.
DR   HOGENOM; CLU_020435_2_0_1; -.
DR   InParanoid; Q54JB0; -.
DR   OMA; IHMVQIQ; -.
DR   PhylomeDB; Q54JB0; -.
DR   PRO; PR:Q54JB0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:dictyBase.
DR   CDD; cd05479; RP_DDI; 1.
DR   Gene3D; 2.40.70.10; -; 1.
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; 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; Coiled coil; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Protein DDI1 homolog"
FT                   /id="PRO_0000329303"
FT   DOMAIN          2..77
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          411..450
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          78..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          321..346
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        342..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  50572 MW;  2E02472EB8D00975 CRC64;
     MAEITISIEN ENFIQVNLQP DQTVEDLKRR VEFETTILVN NQVLTLDGKV LDNEKKLSDY
     SIKGGDFLLI TKNVLRAPQQ RSQQPQQPQQ PQQPQQQRQP QRDPLNSPQD ILDHFTNNPE
     DLTQVINSNP ALANAILSKD MKFLTHFVEQ IKEQRRIQEL ALKDPYGEEY QKLAYQHIQQ
     QNIEKNMQHA MEHTPEVFAS VYMLYIECSI NGHPLKAFVD TGAQQSIMSE KCAERCEISR
     IIDTRFHGIA KGVGTSKIIG RVHSTDLKLG NSLFSVSLSI LQNQDVDFIL GLDMLKRHQV
     ILDLNRGVLQ IANEKIEFLH EKDLKEILNK EQNDLEEDTK KATANSLSPS TTSTTTTTTT
     TTSPQTPTNA TSPVNNNNNN NNNNNNTRPP INSPPVAKTP QPTPQPTTNQ YASESNIQTL
     IGLGCSRDKA IRLLTQAKGN VDVAASMFFG