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Database: UniProt
Entry: A0A368FHI6_ANCCA
LinkDB: A0A368FHI6_ANCCA
Original site: A0A368FHI6_ANCCA 
ID   A0A368FHI6_ANCCA        Unreviewed;       315 AA.
AC   A0A368FHI6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Arylesterase {ECO:0000313|EMBL:RCN30449.1};
GN   ORFNames=ANCCAN_23780 {ECO:0000313|EMBL:RCN30449.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN30449.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN30449.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN30449.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC       2};
CC   -!- SIMILARITY: Belongs to the paraoxonase family.
CC       {ECO:0000256|ARBA:ARBA00008595}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCN30449.1}.
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DR   EMBL; JOJR01001554; RCN30449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368FHI6; -.
DR   STRING; 29170.A0A368FHI6; -.
DR   Proteomes; UP000252519; Unassembled WGS sequence.
DR   GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   PANTHER; PTHR11799:SF12; PARAOXONASE-RELATED; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR602640-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252519}.
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         144
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   DISULFID        17..308
FT                   /note="In form B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ   SEQUENCE   315 AA;  35138 MW;  D2125227E80B22E1 CRC64;
     MVLDVNKRVY NHRPGPCRRV EGIAHGAEDI ALLEDEGIAF ITSGLFYMFP RAKEVQGRIS
     LYDFNQDGTY HAEALTINGD HDQENFHPHG ISHFVTSSGV VRLFVINHSK SFEHSVMVFD
     WNRKSRQLDL VKVIKDDKFI RPNNLVAVSE DAFILTNDGS AQTPITNFLE AFSMIPSGSI
     VYYDGKASSW LMSTTTSPNG VAIDRAGKHL IVSHANTETI SVYRIGEGYR SLSHLVDVPL
     LTTMDNLYVD KEGAVWTVLR IKFSKGFKSW EITEPFVDDG RLLSASSVAV PFKNQLLIGS
     VCRELVHCSI TAETV
//
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