ID   Q4KXL2_LEIDO            Unreviewed;       678 AA.
AC   Q4KXL2;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   22-FEB-2023, entry version 72.
DE   SubName: Full=Dipeptidylcarboxypeptidase {ECO:0000313|EMBL:AAV80217.1};
GN   Name=DCP {ECO:0000313|EMBL:AAV80217.1};
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661 {ECO:0000313|EMBL:AAV80217.1};
RN   [1] {ECO:0000313|EMBL:AAV80217.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16257064; DOI=10.1016/j.molbiopara.2005.09.014;
RA   Goyal N., Duncan R., Selvapandiyan A., Debrabant A., Baig M.S.,
RA   Nakhasi H.L.;
RT   "Cloning and characterization of angiotensin converting enzyme related
RT   dipeptidylcarboxypeptidase from Leishmania donovani.";
RL   Mol. Biochem. Parasitol. 145:147-157(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; AY665610; AAV80217.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4KXL2; -.
DR   VEuPathDB; TriTrypDB:LdBPK_020710.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_020012600; -.
DR   VEuPathDB; TriTrypDB:LDHU3_01.0970; -.
DR   BRENDA; 3.4.15.1; 2947.
DR   BRENDA; 3.4.15.5; 2947.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 3.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:AAV80217.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          227..674
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   678 AA;  76548 MW;  FAFC83012FB60781 CRC64;
     MSANPLLQQS TLQYQYPPFD RIAVEHYAPA FEQGMAEQMA EIEVIKSNPD APTLENTVVA
     LERSGAQLKR ARLVFQNLCS AHTNPEMQSL EQAYAPKFAV HTDKIYLDGA LYHRIKAVYD
     ARASLAGEDL RLVEHYEREF RKAGAALHDS DKEKLKQVNE RLATLESDFA KKVMGTRKTA
     SLVVDDVAEL EGLSEDEIAT AQKEAESLGH PGKYALIIVN TTQQPLLASL RSRETRRRLF
     EASVQRAGRG DENDTSAIIV EIAQLRLRKA RLLGKKSFSE WQLQNQMADP ASAEALLRDM
     GDAAASKVKR EAADIKQMIR EEGGDFELAP WDWKYYAERV RKQRYDLDEN ETKPYFELNN
     VLERGVFYTA EKLYGVTMQR RTDLPVYHPD VMSFEMFDCT GESLAIFCLD PYARASKRGG
     AWMTFYVRQS SLLGQKPVVY NVLNVVKPAE GRPTLLSRSD VTTLFHEFGH GLHGMLSNLK
     YSTLSGTSVA RDFLEFPSQI NEHWAMYDAV LKNYAIHYET KEPIPQALVD RMKAAETYGA
     GFHTIEVVKA AYLDLCWHLV AEETAVLPPA QMEEAAMKSF GVGMTEVPPR YHSGYFMHTF
     SGGYASNYYV YQWARVLDCD GFEWFLENGG LTRENGDHLR ACVLSVGNSV DANVAYEKFA
     GRKANMKAFL RINGLLDE
//