ID A0A0C2D9N2_9BILA Unreviewed; 666 AA.
AC A0A0C2D9N2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE SubName: Full=Putative leukotriene A-4 hydrolase/aminopeptidase {ECO:0000313|EMBL:KIH58952.1};
GN ORFNames=ANCDUO_10830 {ECO:0000313|EMBL:KIH58952.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH58952.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH58952.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH58952.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN732514; KIH58952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2D9N2; -.
DR MEROPS; M01.A18; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; 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; cd09599; M1_LTA4H; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726:SF6; LEUK-A4-HYDRO_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
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:0000313|EMBL:KIH58952.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIH58952.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634015-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 510..655
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 430
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 153..155
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 311..316
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 611..613
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 666 AA; 76099 MW; 18BDA0B7B1253A3A CRC64;
MYNSKKIVHT ICSSMCQCHR PRRDPCSAAN NHDVVVTHTA IKWEVHFQLK MLIGQATLTC
SVLRKTDKIL LDVRDLSIRS VTVNGKVVDY RIAPNVYTFF GSKMTIYLPL EFQQEGRELN
VVVVYSTSPE ATALQWMKKE QTADKKAPYL FSQCQAIHAR SIVPCMDTPS VKSTYEAQVE
DQTSVFEVTV PTGLTCLMSA IGEGSKGDEE FTTFFFKQPV AIPSYLIAIV VGALEKRDIS
ERSVFLLYSR TSHGLPKVFC CRVAVWAEPS VVDKAHWEFS ETEDILACAE EIAGKYIWGR
YDMVCLPPSF PFGGMENPCL TFLTPTLIAG DRSLVSVIAH EIAHSWSGNL VTNSSWEHFW
LNEGFTMFIE RKICGRLVSE DYRQFMAFNG WTNALMPAVY EQFTPTHQFT KLIQDHTNVD
PDVAFSCVPY EKGSALLFYL EQKLGGPEVF EAYLRDYINT FAHKAIDSYQ WKKHLHDYFS
DKKDILSTVD FDAWFYAVGM PPEKPDYGQA MVVSCEALFR QWIDADEETA DKITADTYKS
MQPLQQIEFI SQLWQHDPPL EHWKLAALNK LYGLNDSENS EILLNWIRLC IKAKWEPVIE
KALKFVTSQG RLKFCRPVYR DLTAWPAAKS QARDAYIKTR SSMHPITAEM IAKDLHMRHS
THTVCF
//