ID A0A3B0J8Q4_DROGU Unreviewed; 690 AA.
AC A0A3B0J8Q4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000256|ARBA:ARBA00030997};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.13.23 {ECO:0000256|ARBA:ARBA00023625};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
GN ORFNames=DGUA_6G007248 {ECO:0000313|EMBL:SPP76683.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP76683.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000256|ARBA:ARBA00023511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000256|ARBA:ARBA00023511};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; OUUW01000002; SPP76683.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0J8Q4; -.
DR OMA; IECIEVH; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF16; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 2.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:SPP76683.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 37..166
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 208..338
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 368..679
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 690 AA; 75070 MW; 296A5FB5B6791F83 CRC64;
MAGSMALARN CLRSVNQRSM AAIACADAHK GGKGLLVGLY EKEAGKGPRL TPAGEKFDDR
LHGKLSELIC ETKISGRLGR GKVFNNIDEE FRSVCVVGVG LEGIGFNELE MIDEGMENVR
VAAGIGARSL QAIECIEIHV DNMDYPEQAA EGASLATWRF EENLSKXYPD QSSTFYFLYP
HQNHSLVAQL SSTIACADAH KGGKGLLVGL YEKEAGKGPR LTPAGEKFDD RLHGKLSELI
CETKISGRLG RGKVFNNIDE EFRSVCVVGV GLEGIGFNEL EMIDEGMENV RVAAGIGARS
LQAIECIEIH VDNMDYPEQA AEGASLATWR FEENLSKKYR SIQPKMELFG SPDSDSWTRG
LFKAEAQNIS RRIAEAPANC MTPTIFAQVA VDTLCPCGIT VEVRTMEWIE QQRLHSFLTI
AKGSCEPPIV LELAYCGTSP EDKPVLLVGQ GITFNSGGIN LRPCKGMDEF RGDLNGAASI
LATMRAAAAL SLPINITAIL PLCENLPSGM SVKPGDVVTL LNAKTMSVRN IDRTGVVVLA
DPLIYGQQTY KPRLVVDIGS MCKGVKKAVG GGATGIWSNS HYVWKQFQKA GSLTGDRLWR
FPLWDFYKRR VANHRSFDLS NDGNGHASSC LAAAVLNELV PCADWAHLDT YGTGLMTTYG
LIPYLRAGQM TGRPTRTLVQ FLYQLACPNE
//
