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Database: UniProt
Entry: C1GY16_PARBA
LinkDB: C1GY16_PARBA
Original site: C1GY16_PARBA 
ID   C1GY16_PARBA            Unreviewed;       421 AA.
AC   C1GY16;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Serum paraoxonase/arylesterase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PAAG_03299 {ECO:0000313|EMBL:EEH41736.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH41736.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH41736.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293999; EEH41736.2; -; Genomic_DNA.
DR   RefSeq; XP_002794754.2; XM_002794708.2.
DR   AlphaFoldDB; C1GY16; -.
DR   GeneID; 9097769; -.
DR   KEGG; pbl:PAAG_03299; -.
DR   VEuPathDB; FungiDB:PAAG_03299; -.
DR   eggNOG; ENOG502S58R; Eukaryota.
DR   HOGENOM; CLU_035172_1_0_1; -.
DR   OMA; NDHYITK; -.
DR   OrthoDB; 1695422at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059}.
FT   BINDING         68
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         189
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         253
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         300
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         301
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   421 AA;  47133 MW;  2EA20436111A17B9 CRC64;
     MNLHPFSNNF YYQTTTVLAL VGVTLSGLFY KPLVSKLDTL YTLPPAWHPF EGGSVNIRFT
     DTIENTEDIL IDHDRAIAII SFDPGRTEWN TVMGIFKNPD PKGSLVIFDY ASTGKAKELE
     LIDFPEEADF HPLGVNIFRS SPDASTRLFV INHRRTGSTV EVFDVNYDLH QAKYIRTISD
     NDKTIVSPNS IAPVSYTQFY VTNDHRYIAR TSPILSKIET FFSRPWTWVT FVDFSLPDEF
     KYTIVADNIA FSNGILVTPT GKEVVVASSS SDALYIYKRD TKTNLLSKDW ERVPVNFHPD
     NINFDDSLDI SDPTVFDAEG RFLRGLVVAG HPSLIKIFKM SRNPGSANAP SWVAEIRRGT
     GVDPAPCPAG PRQGELYSRT LYQSNGEQYM SSTTGALDSK RGHLLVSGLY AKGILDISWK
     V
//
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