ID A0A2H3IHF2_9EURO Unreviewed; 393 AA.
AC A0A2H3IHF2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Arylesterase {ECO:0000313|EMBL:PCG92009.1};
GN ORFNames=PENO1_090940 {ECO:0000313|EMBL:PCG92009.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG92009.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG92009.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG92009.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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 -!- PTM: Glycosylated. {ECO:0000256|PIRSR:PIRSR602640-4}.
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:PCG92009.1}.
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DR EMBL; NPFK01000385; PCG92009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IHF2; -.
DR OrthoDB; 1695422at2759; -.
DR Proteomes; UP000218381; 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:SF30; -; 1.
DR PANTHER; PTHR11799; PARAOXONASE; 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, ECO:0000256|PIRSR:PIRSR602640-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..393
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013729472"
FT BINDING 137
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 249
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"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
SQ SEQUENCE 393 AA; 43709 MW; A6A7AE2D5F03874B CRC64;
MVSVIRLSLS IVALALLYPF VAERARVVRL LVDNAPHKFT EVNTFADSSI KFADRLRNCE
DGLMIDEDHV AIFSCDAGRD VWNTVMGTFT PDLSTVPHGN LHLYRYGQKT ASDEEAKLRT
IELRDFAGIK DFHPLGIEYH RPTSTLYVCN HSFNGSRIEV FSLDFSDSSK NPVATYQRTI
ISPLIKSPNA IAVLSDHELY VTSDHYFLQR YNPVLSWLET YLGLPLGGVF YVNLLTNEIR
TVARVPFSNG ITLLNETTVA VASSSTAAVR FYEMSSDRSL KQTGAVNVDF MPDNLSTDKN
GVLLITGHPH PPTLDKMRLE RFECLMNSAV GNLNCVDGKA PFWVAEWSAD AGVKTLFTSK
DRLAGGCTSL RDTEYNVGIT LGLYGKGAFV WKQ
//
