ID   A0A0K0EGF0_STRER        Unreviewed;       573 AA.
AC   A0A0K0EGF0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Peptidase_M1 domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000856100.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000856100.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000856100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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; A0A0K0EGF0; -.
DR   STRING; 6248.A0A0K0EGF0; -.
DR   WBParaSite; SSTP_0000856100.1; SSTP_0000856100.1; SSTP_0000856100.
DR   Proteomes; UP000035681; 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; 2.
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; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01433; Peptidase_M1; 2.
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   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000035681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          53..243
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          317..395
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          412..464
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   573 AA;  67776 MW;  A62E9DB2719AB60E CRC64;
     MLLSKQMLTI VYKTINKISS TQLIILFIFY NFQQLVESKN LYDVHYKLND HFHPSKYDIK
     LSLDSHSNEI TGQVIIDILC HKTSTYLELH SDSNYIVFKH ITIRENHKNK SIVIDDPVFN
     FNTQTVILKY PKGNKYRKHK LYKLTIWYRT KFSEYLRGFM KIEDNINGKW VNSLLEMTYA
     RQVFPSFDEP RWKCVFRLQL WLSGEFAKSS YIALSNTEGS PFMFSNNLTI WTFNPTPPIP
     TYLFAVSIGK FDNYCCDKKI QKEKDICIWK LNGSKSQNNW HDVAEDVCLE IKKYKHLTDK
     YLNVNTKAKE HFLIVPCQLN GMENFGLLQV SERLWPKKNN TRSMLSFTKT LTHEMAHQFF
     GNLVTIKWWN DIWIAESLTS FISMKRPYEF RVEIDTSEDP LIDKKWAEKI PHHVYVKGPA
     VLMMLEDVIG QHLMRKLLRK FIKKYALTSV DSQDFFNILK HVTHIHMPMA LPFLKSWLYQ
     GSYPLVFIDF DEENKLFTLS QTPKYGNPKN RWLIPIWVDC AVGTVPEKLF WITKNSNLVL
     HINDLTKTNK SAAVAFNRNR SVYYNVIYNY FTM
//