ID   A0A0K0EFC7_STRER        Unreviewed;      1062 AA.
AC   A0A0K0EFC7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Aminopeptidase {ECO:0000313|WBParaSite:SSTP_0000819000.1};
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_0000819000.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000819000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|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; A0A0K0EFC7; -.
DR   STRING; 6248.A0A0K0EFC7; -.
DR   WBParaSite; SSTP_0000819000.1; SSTP_0000819000.1; SSTP_0000819000.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF21; PROTEIN CBG03367; 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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000035681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..360
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          395..601
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          702..1010
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        467
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            552
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1062 AA;  124877 MW;  2A149D7D6E787563 CRC64;
     MTSQDKEQTE VFFTTTNNEV ISSKEKNNFN IIRGKSFIFI VMIGGILLFI AGFLLIHFGD
     ELFHSTTPYT DDPFNNIIQY LNKGRNQTST GFLEPGLGKD NLNDFPSIYI TYTPKDSNLP
     IWRKNFISKN KTMPLYINST SYKLSSIHTR SKGITLTPYL YEIFFQIYYD LILTEKNEPQ
     YKYNNIVVNI TIYLHCHKRT NVIKLNQKNL TLWDRSFKLE KISNNNNENI DIVNVILNDP
     HETLEFVASK DLIPSNNYSL SLAYSVSLDH DDLAGLYKMS YRTNSSVDGI VLGTQLQTEF
     ARRLFPCYDQ PDMKAEFLIS VRHPTAAKVI SNSPARLTVT SGNGYETTYF YKTKKMSTYL
     LAVVVSFFRY KETNHNGIPI RIYTEPMKID GVDLALETTK KLLDYYEKYF DIKYPLPKLD
     IHTYPQMRVH AMENWGIITI KTDNLVYQKN VHTFKHRYEI IKTISHETSH MWFGCLVTTT
     NWDLLWLNEG FATFMAFKGA EGIGSEKTLS DGLYYFDLQN LCMDIDQRFS NTHPIIPKIR
     NTKYIVKNKI LYVKSALILF MIEEVIGEEM FRESLHQFIK ENEYKNVDNQ QLLETMEFVV
     DKRKGNNSIL PVNITLTKFV EDWILQEGFP LVTVIKNSDN SLSLMQEVMD SERNIDNRFA
     NKWTIPIFIQ DKIPQKYLLK WIVPGENLTI HQYTLPLDPH CRGYYRIKYT NEIYDQFYQT
     LLTNHTSIST PSRARLIDDA FSLAEFNYID YSIPLKLIQY YTKEKNYVPM AVFFKHFKNL
     KKIYSQEAFF AHFTNYTNEI LKCTYNYVNS KQFTNDKSFV GFSLISDVTS YVCDNGDIEC
     IRESLKLFNN LKAICAEYRL SNSSCNTIPM YRKQIVYQAA ARYGDEGAFE FLLKKYKEED
     YGTEKKIIRA ALLCTKNEHL FLMFLKNSLF ELDGMPLLGD LRQFIYDLYA FSSHWRIVKK
     LIMDKTYFEA LYVKYKSIPI HFSYFFKFLH AYCYNDEQYD ELKEFYQRED ENIKHLGAGV
     MIEIEKNLVE CEKRIKHRKS KNFKRIEESL FAILKSYKIK CD
//