ID G0VGW4_NAUCC Unreviewed; 304 AA.
AC G0VGW4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN Name=NCAS0F02510 {ECO:0000313|EMBL:CCC70735.1};
GN OrderedLocusNames=NCAS_0F02510 {ECO:0000313|EMBL:CCC70735.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70735.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC70735.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; HE576757; CCC70735.1; -; Genomic_DNA.
DR RefSeq; XP_003677090.1; XM_003677042.1.
DR AlphaFoldDB; G0VGW4; -.
DR STRING; 1064592.G0VGW4; -.
DR GeneID; 11527650; -.
DR KEGG; ncs:NCAS_0F02510; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_6_1_1; -.
DR InParanoid; G0VGW4; -.
DR OMA; WFSYRRY; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000001640; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..248
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 304 AA; 34570 MW; DB9D8DD1AA9C7EF8 CRC64;
MAVDRLTLVG NPTSFANRNP KWRLTDVILL FTMMILCYPV YYQEPFQRQF YLNDLTISHP
YADPQRVSDF MLFVYSLFLP LVAIIIFGLI LADPKHRGFL IYISVLGLFV SWFSTTLITN
FIKNWIGRLR PDFLARCQPK PDLPTDVLFT ASEVCTTENR AILMDGFRTT PSGHSSQSFA
GLGYLYLWLC GQLLTENILT GYWRKVFALM PLLGASLIAL SRTQDYRHHF VDVLIGSILG
YVIAHFCYRR NFPAIDEEIP FKPLLDDSDV TLNIPPAPAP LPDEELHPLT EGATAVPDEI
QANN
//
