ID R4G463_RHOPR Unreviewed; 528 AA.
AC R4G463;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA75895.1};
RN [1] {ECO:0000313|EMBL:JAA75895.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA Azambuja P., Braz G.R.C., Oliveira P.L.;
RT "An insight into the transcriptome of the digestive tract of the blood
RT sucking bug, Rhodnius prolixus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:RPRC014324-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) 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; ACPB03007327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GAHY01001615; JAA75895.1; -; mRNA.
DR AlphaFoldDB; R4G463; -.
DR STRING; 13249.R4G463; -.
DR EnsemblMetazoa; RPRC014324-RA; RPRC014324-PA; RPRC014324.
DR VEuPathDB; VectorBase:RPRC014324; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_1_0_1; -.
DR InParanoid; R4G463; -.
DR OMA; MPLWKYF; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000015103; 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:SF16; 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 2: Evidence at transcript level;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:JAA75895.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT DOMAIN 53..168
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 199..512
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 528 AA; 57469 MW; 0415AF9F622FC985 CRC64;
MRTPVLKAIS LIRTPFSRSY CECSGSGSNR TGLVLGTYQP ETSCHETGST EFKFTPTGVK
FNEETGGKLK DLVQGAGIRK GCAHVFTNVS NDFAAVAVAG LGPEGLGWNE IEVLDECKEN
IRIATAHGTR ALQDEGMSNI LVEPFTNTEA AAESAFLSVW RYQELKNKQK QLATPRLDLY
GESDKDGWER GKLKSGNQNL ARKLEDTPAN LMTPTIFAEN AVDLLCPCGV SVEVRDKDWI
EEKRMNPFLT VAKGSCEPPL FLEVGYCGGP IEGQPIVLVG KGITFDTGGM CLKKCEHMSE
YRADLAGAAV VLAVIKTAAQ MVLPMNIFGL IPLCENMLGG LAMKPGDVVI ASNGKSITIE
DTDNEGRLTL IDALNYSHFF KPCAVVCVST IADGVRRNLG TSSSATFSTS QALWRELERA
GGETGDRLWR LPFWKVYQHR ITTDYLNVDV HNVGKNGISG DVCKAAAFLL EFMSVKDFVH
IDISGTGKLS NGVGHPYLRE GTMTGRPTRT LVQFLYQIAC PHTRGDEC
//
