ID G8BQ58_TETPH Unreviewed; 279 AA.
AC G8BQ58;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN Name=TPHA0B04700 {ECO:0000313|EMBL:CCE62139.1};
GN OrderedLocusNames=TPHA_0B04700 {ECO:0000313|EMBL:CCE62139.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62139.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62139.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
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).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; HE612857; CCE62139.1; -; Genomic_DNA.
DR RefSeq; XP_003684573.1; XM_003684525.1.
DR AlphaFoldDB; G8BQ58; -.
DR STRING; 1071381.G8BQ58; -.
DR GeneID; 11535096; -.
DR KEGG; tpf:TPHA_0B04700; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_4_0_1; -.
DR OMA; YGLDICQ; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF35; RE23632P; 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:UP000005666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..261
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 279 AA; 31679 MW; 4F35E3FD8DAA4835 CRC64;
MKLNLQQVTS YLSVFILQYL YVLIGFVFFF YSEYGLVPRT TDMKFNIKNG SIAKAHVADE
VVSGVECLSI AFLLPTVVII VHCLVGRISK KRLSVSEAGD KKGNSYMLSR LSFIPPQLHV
LQLSLLCLGL ILTVNGTITN ILKLSIGNAR PDFLDRCQPD IPAEMKDQEW FTLDICKQAN
HDFLYEGLKS TPSGHSSFIS CSMAYLFWWQ TYFLSTSKSK HFWCLLLAAV VIVSRLTDHR
HHWYDLLFGT VVGLASFFFA RTLIFDNKKV DQLLPTTKN
//