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Database: UniProt
Entry: A0A0K0D444_ANGCA
LinkDB: A0A0K0D444_ANGCA
Original site: A0A0K0D444_ANGCA 
ID   A0A0K0D444_ANGCA        Unreviewed;       208 AA.
AC   A0A0K0D444;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Peptidase_M1 domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000483901-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_0000483901-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_0000483901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A0K0D444; -.
DR   STRING; 6313.A0A0K0D444; -.
DR   WBParaSite; ACAC_0000483901-mRNA-1; ACAC_0000483901-mRNA-1; ACAC_0000483901.
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   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF276; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
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   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          59..197
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   208 AA;  23762 MW;  80C638A1B9CAF074 CRC64;
     MPFAFFVRAR PAGQLRYATI TIEACWFQLE YERRARCLTG QQAIQLIKRI QEKKKLKKLI
     SESALLYDEN LYDPLNKERV AVVIAHELAH QWFGNLVTMQ WWDDLWLNEG FATMVEYSGA
     DEISNGQMRM KDYFLLDGFT NGLAADSVAS SHPLSFKIDR ATEVLEAFDQ ISYGKGGSLL
     VMLSALIGEE IFKKSVTVSQ KKSKRKHG
//
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