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 27-MAR-2024, entry version 101.
DE RecName: Full=Protein DDI1 homolog;
DE EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
GN Name=ddi1; ORFNames=DDB_G0288187;
OS Dictyostelium discoideum (Social amoeba).
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.Q54JB0; -.
DR MEROPS; A28.A04; -.
DR PaxDb; 44689-DDB0266774; -.
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; QIGNDHL; -.
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 CDD; cd14310; UBA_cnDdi1_like; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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 PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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
//
