ID G1UA82_CANAX Unreviewed; 306 AA.
AC G1UA82;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein CaJ7.0292 {ECO:0000313|EMBL:BAE44764.1};
GN Name=CaJ7.0292 {ECO:0000313|EMBL:BAE44764.1};
GN ORFNames=CaO19.6459 {ECO:0000313|EMBL:BAE44764.1};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476 {ECO:0000313|EMBL:BAE44764.1};
RN [1] {ECO:0000313|EMBL:BAE44764.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; AP006852; BAE44764.1; -; Genomic_DNA.
DR AlphaFoldDB; G1UA82; -.
DR EnsemblFungi; C7_02500C_A-T; C7_02500C_A-T-p1; C7_02500C_A.
DR VEuPathDB; FungiDB:C7_02500C_A; -.
DR VEuPathDB; FungiDB:CAWG_05594; -.
DR PhylomeDB; G1UA82; -.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:EnsemblFungi.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165:SF202; DIACYLGLYCEROL PYROPHOSPHATE PHOSPHATASE 1; 1.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..258
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 306 AA; 35484 MW; E07E7712EAA1E342 CRC64;
MALYDIINYF YGSNSKFNRI TWGFKSPTFI KWRITDFILI IVLIVLFFVT SQAEPFHRQF
YLNDMTIQHP FAEHERVTNI QLGLYSTVIP LSVIIIVALI STCPPKYKLY NTWVSSIGLL
LSVLITSFVT NIVKNWFGRL RPDFLDRCQP ANDTPKDKLV SIEVCTTDNL DRLADGFRTT
PSGHSSISFA GLFYLTLFLL GQSQANNGKT SSWRTMISFI PWLMACYIAL SRTQDYRHHF
IDVFVGSCLG LIIAIWQYFR LFPWFGGNQA NDSFNNRIMI EEIKRKEEIK QDENNYRRIS
DISTNV
//
