ID   A0A1I7T005_9PELO        Unreviewed;      1035 AA.
AC   A0A1I7T005;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Aminopeptidase {ECO:0000313|WBParaSite:Csp11.Scaffold417.g1137.t2};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold417.g1137.t2};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold417.g1137.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-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; A0A1I7T005; -.
DR   STRING; 1561998.A0A1I7T005; -.
DR   WBParaSite; Csp11.Scaffold417.g1137.t2; Csp11.Scaffold417.g1137.t2; Csp11.Scaffold417.g1137.
DR   eggNOG; KOG1046; Eukaryota.
DR   Proteomes; UP000095282; Unplaced.
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; 2.60.40.1910; -; 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:SF298; AMINOPEPTIDASE-RELATED; 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   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   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        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          161..353
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          409..604
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          682..996
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        445
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         444
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         448
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         467
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            534
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1035 AA;  118759 MW;  B94A15F65FFDF737 CRC64;
     MHFVIAPFAL EECRQELSPE PGRMRPFSDA VTASASTTST TAVATTVTSE QRDSPWCSAR
     PLAIGIVAVS MSFALIYFLM IVPLTTTIIP STSPFPPTSS SSSSSESGLS SKVSQATDVP
     LINSTIFVPT TDYISTTTED PLYQYIEDKH HRLQIPLIHI PLLYEVNLKL FLPWKPSVNF
     GTDNFMVEGH VRVHFTSGGG SRVLLHSDSE QHVGECIVQD EFNREIFVKH VGRGFPQVLD
     LHLATDMIHG MNYTLDIAFR SHMQQEVAAG LFSVPYTNGN ETRYVVATHL QVSEARTVFP
     CIDVPEVKAQ FDTVITHPTG TTAIANMMDN STVVDGGWTT TTFRRTPPMS TYLFALSVSD
     FPYLEVFSSR GVRSRVYCDP SKIDSAQLLA DVISPVLEFY EDYFGIPYPL EKLGLITIRQ
     TAGLYKEGQF PIAQKHNLQE IIAHEVAHQW FGNLVTMKWW NDLWLNEGFA TLISVRAVDF
     LENTTWRYED RSAELQCVAL RTDQMDGMQP VSGSKNSNFG RYFDARPAIN AIVYKKSSII
     IRMIERLIEE DIFKQGLRRF LSSFLYKNAD HEDLFNVLLY VHDSSAGGHL SGQNFSLSDV
     MDTWIRQAHF PIVHVNRIEG SIVTLRQEKY EHNVYNPPRP NEQVWKIPIF YDDPVSSKHK
     VFWLTDKRPK VFDMGGQHVV DPHQLTYMRL RYDMDMYSDI TMALLQDYKS VPANSRSRLI
     DDTMAMAENG QMSYKVAFNI TMYMTEETSY RPFQTFSAYL DFFLPRMYIH ESWPVYKKYL
     EMILGGPYDK FSNQGLDMDI DEDSDLYHTR EIVVLRACII GYEPCVQMAK ERFAELRRNC
     SGEHQLLSDN CNKISYYLRS HVYSAAINYG SKEDFDFLFK KWNLEHYLME RDRIFTGLCY
     TNDRANSDLA WKALVKNRAR ENVLARAGIC SKKLINDSLL LELFYEEKDY LKELSETADQ
     VLHSLLMLVV RNINKKKDID KFDEMLKPHP LFTRMLAGNR YQAIERMKWR QFTAPYFAGN
     ASEAIEEMGA FQRNV
//