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Database: UniProt
Entry: A0A1Y2HPV9_9FUNG
LinkDB: A0A1Y2HPV9_9FUNG
Original site: A0A1Y2HPV9_9FUNG 
ID   A0A1Y2HPV9_9FUNG        Unreviewed;       452 AA.
AC   A0A1Y2HPV9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORZ36648.1};
GN   ORFNames=BCR44DRAFT_1432324 {ECO:0000313|EMBL:ORZ36648.1};
OS   Catenaria anguillulae PL171.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX   NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ36648.1, ECO:0000313|Proteomes:UP000193411};
RN   [1] {ECO:0000313|EMBL:ORZ36648.1, ECO:0000313|Proteomes:UP000193411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PL171 {ECO:0000313|EMBL:ORZ36648.1,
RC   ECO:0000313|Proteomes:UP000193411};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ36648.1}.
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DR   EMBL; MCFL01000016; ORZ36648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2HPV9; -.
DR   OrthoDB; 1695422at2759; -.
DR   Proteomes; UP000193411; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          337..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
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         196
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         197
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         255
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"
FT   BINDING         302
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   452 AA;  48188 MW;  67A6370F32DC0C33 CRC64;
     MPGIDSKSGA SASPAKPAAA SSAKPSAAAA GTSAKTTILY ALAGVAAVLS IVLGYYYPTL
     STMYGRLFFN PSAWPHHASA NLGKRCRFLD KSLFGCEDIV VHGEFAYLAF VLRLSFKENK
     LTKMHLSGFK PVAPGTLGLS LHGLSVTDGT KPNKLSLAAV NHRKGGSCVE LFDHRVGTDE
     LIHKETVCDP LIYNPNDVAL VSPRSFYVTN MVTKDSTPND VKKQLLLAQP TGTLVFRDGT
     AGQVRKVRDG LHAANGVSVA PNGRQLLVSE TSSHELSIWD IQADYSVRSA EPKLPLGFAP
     DNIATIPETG NWVVSGPAAS WPFAKAEGAD FAYQVVEPGK RGSPPRKQKP KFDEQEEGES
     GSGRRWTGHS SVIALVHNAT ASKDKFYGHK YKVTPIVVDP EGTFIYGASI AAVNWETKQA
     LVGGPLMKGV VMCEWPETVP ADEAGKGKGK GK
//
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