ID S9PYR5_SCHOY Unreviewed; 276 AA.
AC S9PYR5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phosphatidic acid phosphatase {ECO:0000313|EMBL:EPX74236.1};
GN ORFNames=SOCG_03448 {ECO:0000313|EMBL:EPX74236.1};
OS Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS (Octosporomyces octosporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX74236.1};
RN [1] {ECO:0000313|EMBL:EPX74236.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX74236.1};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [2] {ECO:0000313|EMBL:EPX74236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX74236.1};
RG The Broad Institute Genome Sequencing Platform;
RA Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Birren B.;
RL Submitted (AUG-2012) 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; KE503206; EPX74236.1; -; Genomic_DNA.
DR RefSeq; XP_013017390.1; XM_013161936.1.
DR AlphaFoldDB; S9PYR5; -.
DR EnsemblFungi; EPX74236; EPX74236; SOCG_03448.
DR GeneID; 25032420; -.
DR VEuPathDB; FungiDB:SOCG_03448; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_6_1_1; -.
DR OMA; WFSYRRY; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000016088; Unassembled WGS sequence.
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 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..240
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 276 AA; 31245 MW; 1F7586BB10ACA9B3 CRC64;
MSPGNNEKYE RFKELWIIYG DYGVLLLVAL CYFILDVTML PFQREFSLED LTISHPYAKH
ERVPTMYLGI IALPLPGLIL YGFGRFRKSP LLFWKSLMGL LYSTMLSGLI VTVIKNTVGR
PRPDFIARCN PLSSSPHTGL VDLHVCTTSW ESHILQDGLR SFPSGHTAFS FAGLGYLSLF
IASQLRMFRK KTSSWAIIIT VLPLMLATWI GISRNEDYRH HVEDIVVGGF LGMAIAYVCY
RQIFPPVDDA LANIPYAQLE IDDGNSDSRR VVEEMV
//
