DDI1_LEIMA
ID DDI1_LEIMA Reviewed; 390 AA.
AC I7HUG0;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Protein DDI1 homolog {ECO:0000250|UniProtKB:Q8WTU0};
DE EC=3.4.23.- {ECO:0000269|PubMed:22933181, ECO:0000305|PubMed:21266539};
DE AltName: Full=DDI1-like protein {ECO:0000303|PubMed:22933181};
GN Name=DDI1 {ECO:0000303|PubMed:22933181};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000312|EMBL:CCB84598.1};
RN [1] {ECO:0000312|EMBL:CCB84598.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22933181; DOI=10.1007/s12192-012-0368-9;
RA Perteguer M.J., Gomez-Puertas P., Canavate C., Dagger F., Garate T.,
RA Valdivieso E.;
RT "Ddi1-like protein from Leishmania major is an active aspartyl
RT proteinase.";
RL Cell Stress Chaperones 18:171-181(2013).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ASP-205.
RX PubMed=21266539; DOI=10.1096/fj.10-178947;
RA White R.E., Powell D.J., Berry C.;
RT "HIV proteinase inhibitors target the Ddi1-like protein of Leishmania
RT parasites.";
RL FASEB J. 25:1729-1736(2011).
CC -!- FUNCTION: Aspartic protease (PubMed:22933181, PubMed:21266539).
CC {ECO:0000269|PubMed:22933181, ECO:0000305|PubMed:21266539}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin, diazoacetyl-DL-norleucine
CC methyl ester (DAN) and nelfinavir (PubMed:22933181). Inhibited by the
CC proteinase inhibitors lopinavir and ritonavir (PubMed:21266539).
CC {ECO:0000269|PubMed:21266539, ECO:0000269|PubMed:22933181}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 uM for RE-(EDANS)-SQNYPIVQK-(DABCYL)-R (at 37 degrees Celsius
CC and pH 4-6.5) {ECO:0000269|PubMed:22933181};
CC KM=7.6 uM for Bz-RGFFL-4MbetaNA (at 37 degrees Celsius and pH 4)
CC {ECO:0000269|PubMed:22933181};
CC KM=1.18 uM for Bz-RGFFP-4MbetaNA (at 37 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:22933181};
CC pH dependence:
CC Optimum pH is 5 with RE-(EDANS)-SQNYPIVQK-(DABCYL)-R as substrate.
CC {ECO:0000269|PubMed:22933181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40087}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR EMBL; FR872380; CCB84598.1; -; mRNA.
DR PDB; 5YQ8; X-ray; 2.25 A; A/B/C/D=184-313.
DR PDB; 5YS4; X-ray; 2.30 A; A/B/C/D/E/F=182-311.
DR PDBsum; 5YQ8; -.
DR PDBsum; 5YS4; -.
DR AlphaFoldDB; I7HUG0; -.
DR SMR; I7HUG0; -.
DR STRING; 5664.LmjF.01.0610; -.
DR VEuPathDB; TriTrypDB:LmjF.01.0610; -.
DR VEuPathDB; TriTrypDB:LMJLV39_010011400; -.
DR VEuPathDB; TriTrypDB:LMJSD75_010011400; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cytoplasm; Hydrolase; Protease.
FT CHAIN 1..390
FT /note="Protein DDI1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443528"
FT REGION 322..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /evidence="ECO:0000305"
FT MUTAGEN 205
FT /note="D->A: When expressed in a DDI1-deficient yeast
FT mutant with high levels of protein secretion, fails to
FT restore normal low protein secretion levels probably due to
FT loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21266539"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5YQ8"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:5YQ8"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5YQ8"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 257..268
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5YQ8"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:5YQ8"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5YQ8"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5YQ8"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5YQ8"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:5YQ8"
SQ SEQUENCE 390 AA; 41744 MW; 1BBA4058C3265E4E CRC64;
MVQLTIDNAR GVTLCRVSLP ANATVQQLLL QLTVAKPELR QAQAIRNDVR HVTHRLTPAS
TTTTTTTSVV SSNAQTLLQA GLVGQGATAE TLVVLMAADA PAAASSAAAA APSPTKAVAA
QILDLFGCAS ASPSAGVRSQ ASVVPSTMDE RQLELQRRIY AQIQQQQIDE NLANALEYTP
EAFAKVTMLY VPCTINQVLV KAFVDSGAQN SIMNKRTAER CGLMRLVDVR MRDVAVGVGR
QEICGRIHMT PVNLAGMYIP FAFYVIEDQA MDLIIGLDQL KRHQMMIDLK HNCLTIDNIN
VPFLPENDLP ALAALGDDEN AMHAPRHQDP ATTATTASNP AAPVLSEGER QARIEGFMTV
SGITDPTQAA ELLEAADWNP NVAAALLFDT
