ID A0A1I8GRE0_9PLAT Unreviewed; 641 AA.
AC A0A1I8GRE0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aminopeptidase {ECO:0000313|WBParaSite:maker-uti_cns_0002864-snap-gene-0.11-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0002864-snap-gene-0.11-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0002864-snap-gene-0.11-mRNA-1}
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; A0A1I8GRE0; -.
DR WBParaSite; maker-uti_cns_0002864-snap-gene-0.11-mRNA-1; maker-uti_cns_0002864-snap-gene-0.11-mRNA-1; maker-uti_cns_0002864-snap-gene-0.11.
DR Proteomes; UP000095280; Unplaced.
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:SF276; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 21..223
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 259..467
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 532..617
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 418
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 641 AA; 72888 MW; 3E71C4F411183330 CRC64;
MLRSAADNGS ESSYRLPTDV KPVSYALTLA PFIYSSNPGD CYFTGSVSIA VEAVNDTDMF
KLHSVRLEVP TVRLRNSTGG DVIVDKIEEN VEKQWLTIKL GEPLRAGETY TVLIDRFKGK
FVKNGKTGLY LSSSYSENST EYYLVSSQLE PIHAREVFPC FDEPAMKAEF NVSLVRGREF
TALSNMPIKS SSSVPGNTWF SNSVEPKVVI KDDFETTPTM STYTLAFLVA KFESISHSDS
KGRVFTNWLS PELVKKSNFT LSVAAKAIEA FEKLLNVSYK TNITKQAGVP LLNFEAMENW
GLIIYQQNIL MYNENTTTTL SKLTNALTVS HEIVHQWFGN LVTMKWWNEI WLNEAFSTFY
SYLGLEWGSE SDLDSHFVMF QKYLFEMNFE RKRYKVHPIQ MDVSTPTEID GIFDYIVYQK
GASVVRMMHN SIGARVFGAA VSSYIRKHSY SNAGSEDFYS SLNEQLRIHK QSLDAETVMS
SHKEKSNLTW SIPITAMTNL NHTGWSRSEV AHLVHWMRGE TLRLPLDSST GWYLINLRSS
GHYQVNYDRE NWDRLAAQLT TDHTVFTPAD RASLIYDSFT LASLGIIDYS VPVRIVMGYL
KNETEFAPWA VVLRMQRMYK KDFSALSQAN VVEGLLENVF E
//
