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Database: UniProt
Entry: A0A0D1WRI9_EXOME
LinkDB: A0A0D1WRI9_EXOME
Original site: A0A0D1WRI9_EXOME 
ID   A0A0D1WRI9_EXOME        Unreviewed;       394 AA.
AC   A0A0D1WRI9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=SMP-30/Gluconolactonase/LRE-like region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV10_06267 {ECO:0000313|EMBL:KIV91760.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV91760.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV91760.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV91760.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN847523; KIV91760.1; -; Genomic_DNA.
DR   RefSeq; XP_016223334.1; XM_016371041.1.
DR   AlphaFoldDB; A0A0D1WRI9; -.
DR   GeneID; 27324112; -.
DR   VEuPathDB; FungiDB:PV10_06267; -.
DR   HOGENOM; CLU_033924_1_0_1; -.
DR   OMA; NACEDVK; -.
DR   OrthoDB; 1936438at2759; -.
DR   Proteomes; UP000054302; 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   PRINTS; PR01785; PARAOXONASE.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
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:UP000054302};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..394
FT                   /note="SMP-30/Gluconolactonase/LRE-like region domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002236232"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT   BINDING         64
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         135
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         188
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         250
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         293
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         294
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"
SQ   SEQUENCE   394 AA;  43481 MW;  8CA2B8F4FC107E30 CRC64;
     MSSKLPTSAL LVLLSIIIYS QSPVLLQLLG QANIDKTRLI KWSNSKPLNN HDCKVMHQAD
     ACEDVKIHYA SNTAFLACGD PIGRTNWYPC AGVRHPEKRA EASFREQLFK YDIKSGLTTK
     LELEGFDGDF ITHGIDVYEF PDDSTKVHIF AVNHGRTGDS IEIFSHNLGS NTAKLIKKVT
     HPNIKTANGV SAMGPFDFYI TNDHYFARGP LRVLEETYGP FTWSTNVQYC DANNPEVICK
     QATGTFPGAN GINSWNDRLF VGDARNGTVT VFQIQEDRSL TWLRQIDLGA AADNINILPT
     TGDPIVAVFP TLEDLPAYLD NVRSLGKDFL VPAAALRLDS SRDYTPELIY FDDGSVVSFM
     TTGAVDPYNR LFIASSVLQF GGFAVCKLRP GAVV
//
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