ID E0VLX3_PEDHC Unreviewed; 528 AA.
AC E0VLX3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 Name=8229751 {ECO:0000313|EnsemblMetazoa:PHUM296570-PA};
GN ORFNames=Phum_PHUM296570 {ECO:0000313|EMBL:EEB14379.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB14379.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14379.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB14379.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14379.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM296570-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM296570-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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; AAZO01003437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235283; EEB14379.1; -; Genomic_DNA.
DR RefSeq; XP_002427117.1; XM_002427072.1.
DR AlphaFoldDB; E0VLX3; -.
DR STRING; 121224.E0VLX3; -.
DR EnsemblMetazoa; PHUM296570-RA; PHUM296570-PA; PHUM296570.
DR GeneID; 8229751; -.
DR KEGG; phu:Phum_PHUM296570; -.
DR CTD; 8229751; -.
DR VEuPathDB; VectorBase:PHUM296570; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_1_0_1; -.
DR InParanoid; E0VLX3; -.
DR OMA; PLCELMP; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000009046; 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 CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
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:SF25; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EEB14379.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEB14379.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT DOMAIN 40..171
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 201..513
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 528 AA; 58117 MW; EEA7ACA93A4180E6 CRC64;
MLSHLLRRIP SRLNSISKLR FFSSADDTLC PKSETGLILG IYSMNDGRHE TSKYTLTGQK
FNKKSCFLME SLIRKAGPCP KLGEYRILYD IDPVFPIVCV VGLGLECAGY DEDEQLDKGK
ENIRVAAGVA AKVMVQFELS KIYIEGLGHP ESTAEGAALA IWVYQDFKNP KYKRLPLAIE
LFDDNDWTGW QIGMQKAAAQ NLARSLMEAP ANKMTPIVFA QNSVEVLCKA GINVEVKVQN
WCECLGMGAF LAVGKGSCES PLFMEISYYG AGNFKERPVV LIGKGVTYDS GGLMLNKMED
LINAKGDMSG AACVVAACRA VAALQLPINI RGLIPLCENM PGCNAMKPGD IVQAMNGRSI
YIQDTRCEGR LILADALCYA QSFCPRFIVD IGSMTKGIRE GFSTAAVGVF TNSTRLWKQI
RISGIHTGDR VWRMPLFSHY ASKIKKSSSV DFKNYGRMPR SADPCRAAAF LHEFVPCGEW
LHIDNFGVSV SDGITDPPYL SRGMTGRPTR TLVEFLSQLC CRQDEGSD
//
