ID A0A0N4X6G6_HAEPC Unreviewed; 582 AA.
AC A0A0N4X6G6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Xaa-Pro dipeptidase {ECO:0000256|ARBA:ARBA00044141};
DE EC=3.4.13.9 {ECO:0000256|ARBA:ARBA00044051};
DE AltName: Full=Imidodipeptidase {ECO:0000256|ARBA:ARBA00044351};
DE AltName: Full=Peptidase D {ECO:0000256|ARBA:ARBA00044252};
DE AltName: Full=Proline dipeptidase {ECO:0000256|ARBA:ARBA00044284};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001995801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001995801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline;
CC Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9;
CC Evidence={ECO:0000256|ARBA:ARBA00043793};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000256|ARBA:ARBA00043990}.
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DR AlphaFoldDB; A0A0N4X6G6; -.
DR WBParaSite; HPLM_0001995801-mRNA-1; HPLM_0001995801-mRNA-1; HPLM_0001995801.
DR Proteomes; UP000038042; Unplaced.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 2.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR48392; -; 1.
DR PANTHER; PTHR48392:SF2; PEPTIDASE D; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 2.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 2.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 341..467
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 582 AA; 65845 MW; 3B6BEAF5399BF315 CRC64;
LERYHLLYCA VSAEVKSKIS KMKIENIIFT SDLERPCSLM FRLNMDARIL YPIMAELRLI
KTDKELEVIR YVCKIASLAH RAMMKAVRVG LHEYQLESVF RHTCYFHGGC RHQAFTCVVA
SGVNGAILHY GHAAVPNDKR IEDGDMCLCD MGPEYNCYAG DITTTYPANG KYTEKQKMVY
NAVLEANRAV FKAAKPGTRW IDMHMLAEKV ILIHLKKAGL LIGDIDEMME ARLGAVFMPH
GLGHFLGLDV HDVAGYLGAS SKLPGLKSLR TTRTLQERMV SDNNRTRLLF YRFMLDDAFN
DPKLAKFMVK AEIDKYRGEG GVRIEDDVVI WEKGNENLSD VPRTTEENVA PRSVVLLRGG
SDMNRYNTDE TGVPFRQESY FFWAFGVHES DFYGAIDVDT GKSCLFPPIL DPSYAIWDGK
ISDESFFKSK YEVDEVHFRA KNTISDHIRR LNIKKVLLLR AENSDSGNIL EPPSFPDKEL
GCNSSILHYG HANAPNDKLI KDGDMCLFDM GPEYNCYASD VTTSFPANGK FSEKQKIVYN
AVLEANRAKA GLLTGLLKSF ESNSGYHRSW LSNKHNHQLL SR
//
