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Database: UniProt
Entry: A0A3B4BFX1_9GOBI
LinkDB: A0A3B4BFX1_9GOBI
Original site: A0A3B4BFX1_9GOBI 
ID   A0A3B4BFX1_9GOBI        Unreviewed;       692 AA.
AC   A0A3B4BFX1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000027329.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000027329.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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; A0A3B4BFX1; -.
DR   STRING; 409849.ENSPMGP00000027329; -.
DR   Ensembl; ENSPMGT00000029115.1; ENSPMGP00000027329.1; ENSPMGG00000022040.1.
DR   Proteomes; UP000261520; 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; 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:SF271; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 2.
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          36..165
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          201..418
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          490..548
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   DOMAIN          556..682
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            352
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   692 AA;  78414 MW;  F833B96F13B89BD0 CRC64;
     HSYNVTLWPH LSPNTENLYI FTGNTHNGPT WQEPAPSIKS TWLQPITQYM VIHLNGKLKA
     GHRYQLFSAF SGELADDLAG FYRSEYEEDG LKKVVATSQM HPTHARKTFP CFDEPALKAV
     FNITLIHPQG TVALSNGKEI GQSYEISKWA FTTRFESTEK MSSYLLAVIV CDFTFLSYIF
     VCFEIRIWAR RKAIQSGQGN YALNVTGPIL DFFQNYYNIS YPLSKSDQIA LPDFYFGAME
     NWGLVTYRET NLLYDPVGSS NRNKETTVTI IAHELAHMWF GNLVTLKWWN EVWLNEGFAS
     YVSYLGKDMI VLDDIHRVFA VDALTSSHPL SSYEEDILKP EQISEQFDAI SYSKGASVLR
     MLSDFLSEPV FVQGLSTYLT AFSYGNTIGS DLWQHLNMAG KNNNMSLPHH VGEIMNTWTL
     QMGFPVVTID TATGNVTQTH FLLDPESNVT VKYTWLIPVR WMKAGVLQSN VWWFSKKTEM
     NSDMRSGGAW ILANVNVTGY YRMNYDLGNW ERLLIQLNTD HQVIPLINRA QIIDDAFNLA
     RCADYMNVRL SSSLTLDIHA NVRSVVYCSA IAAGAEREWD FGWSQFKSAA VASEASKLMS
     ALACATKPEL LQRYEYLSFT LNSTMIRKQD ASAVITAVAS NRVGQSMAWD FVREYGVGAF
     SFATIISGVT ARFSTQAELQ QVCPHWRRKI PQ
//
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