ID   A0A183M2Z4_9TREM        Unreviewed;       372 AA.
AC   A0A183M2Z4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00015118};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001042001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001042001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC       {ECO:0000256|ARBA:ARBA00011395}.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   AlphaFoldDB; A0A183M2Z4; -.
DR   STRING; 48269.A0A183M2Z4; -.
DR   WBParaSite; SMRZ_0001042001-mRNA-1; SMRZ_0001042001-mRNA-1; SMRZ_0001042001.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   372 AA;  41724 MW;  999173E26FF30248 CRC64;
     LDNHGFRELF EEESWSLRPL DKVYITKNES TVIAAAVGGR FESGNGFTLL GAHTDSPCLR
     LKPNSERLKE GYIQLGVETY GGGLWYTWFD RDLKLAGRVI IRNAEGRLEQ RLVHINNPIA
     CVPSLAIHLN QEIKTQGFHP NSEQHLSPIL TGRPYRLANR HPPALLRLLS EETGVSEQQI
     VELELCFADA QPACVGGLYK EFIHAPRLDN LFNSYAGLHG FIESLPTLSS ECNIRLLCLF
     DHEEVGSTSA QGADSGYTLS VIRRLNKAFE MSKSFLVSAD QAHAVHPSWG ERHECYHKPQ
     FHSGVVLKYN VSQRYATNSL TAAVVREIAH LSNVPVQVSG CTFIPEWMFI LGLSSTIFFK
     RYHVNHLATE SR
//