ID A0A0V0ULB2_9BILA Unreviewed; 494 AA.
AC A0A0V0ULB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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};
GN ORFNames=T09_2707 {ECO:0000313|EMBL:KRX52222.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52222.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52222.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52222.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX52222.1}.
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DR EMBL; JYDN01000264; KRX52222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ULB2; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; 1.
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; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT DOMAIN 15..157
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 494 AA; 55486 MW; 12A9252EC7143F17 CRC64;
MENSAKLMHF DAPDVTLKIF QENRARLLRE LKKVVTSPAT FILMEGGKVV NHHTTDLVEG
DSMVFRQESY FFWTFGVKEP GFYGAISVQT GETYLFAPEV ESRRSIWLGK IPSLEETKRQ
YGVTEVFYDD RIAEKLSTLG CLSVLTLTGQ NTDSELDLVE PDVNLTRFHV NNKILYPIIT
ECRVFKTDRE LEFIRYACKV TCQAHIQTMC CCEVDMSELQ LESLFRFFAS FYGKCRHIAY
TCIAASGPNA AILHYGHAGK PNDRIMKKGD LCVMDMGAEF SSYASDVTST FPISGQFLPK
QCKIYEAVLD ANRAIISKAK PEESWIVLHM TAQKIILKHL IQAGLLQGDL ESMIDVSVGS
VFMPHGVGHF LGLDVHDVGG YLKGVRSFED KKYSILRTTR VLKPRMVITV EPGCYFIETL
INQALSDRVK SEYLVKSVID DYRELVGGVR IEDVILITED GCENLTPLPR TVEEIQACVG
SKKIIPLAGD SAET
//
