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Database: UniProt
Entry: A0A0C2D9N2_9BILA
LinkDB: A0A0C2D9N2_9BILA
Original site: A0A0C2D9N2_9BILA 
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}.
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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
//
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