ID   A0A158PA30_ANGCA        Unreviewed;       666 AA.
AC   A0A158PA30;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Aminopeptidase {ECO:0000313|WBParaSite:ACAC_0000893401-mRNA-1};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000893401-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000893401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A158PA30; -.
DR   STRING; 6313.A0A158PA30; -.
DR   WBParaSite; ACAC_0000893401-mRNA-1; ACAC_0000893401-mRNA-1; ACAC_0000893401.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
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   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF106; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          86..156
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          196..401
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          425..647
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            354
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   666 AA;  76606 MW;  580834249F034E6C CRC64;
     MKKSILFSIL LNFVIFDIKK GLIECLNILF YLKHMPNILL PHLGWEVFLG AGLRCTARGF
     IPLAGSRKLS PAFPSGIFHH STYFRRSAVT QFEPTYARKM FPCFDEPNFK ATFLLSVIRE
     AHHVVRSNMH INVSKEYVNG LYLDVFHRTI KMSTYLLAVA ILDSYDYVRR TTRNTRDPIE
     VRLYAPQNVI KGQSEFSLDT AVRALEYFEN YFDISYPLKK IDLVALDDFS EGAMENWGMI
     TFRDSALLYT DGITSAQNKE HIALVICHEV AHQWFGNLVT MDWWNDLWLN EGFANYMEFR
     CVDRLFPDWN IMTRFYAENV ALSHELDGLR SSRAVSSHTF NQTNIIGLFD AISYHKASAI
     IRMLQSLTGE RNFQRSLIQY LNKYAYGNAK GAHLWEIVEK DNPFQRIHNT RIVSVSWPLM
     KSSKWVVANT DGLSYVKVLY DRKNYAELTN QLRINHTAIS AIDRTMILVD AFDFSKSSKL
     NIEVYLNLLL YATEEMDRLA WMMINKQMKY IESLIEETPF AHIFKDLQRT LILRPYERVG
     WSTNTSMTPA QKGLQAEVIG TACRLRNRDC VKQAQHQSLC SLVMFRPSPE LLGVILNEGV
     SQGGRAAWDN AYTAYQEAKS PTEKNQLISA MASTTQSTLI SRLNRCLNNH LVVFRLNIVI
     STSASA
//