ID K0KR56_WICCF Unreviewed; 280 AA.
AC K0KR56;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Lipid phosphate phosphohydrolase 1 {ECO:0000313|EMBL:CCH43768.1};
DE EC=3.1.3.4 {ECO:0000313|EMBL:CCH43768.1};
GN ORFNames=BN7_3322 {ECO:0000313|EMBL:CCH43768.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH43768.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH43768.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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:CCH43768.1}.
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DR EMBL; CAIF01000089; CCH43768.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KR56; -.
DR STRING; 1206466.K0KR56; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_6_1_1; -.
DR InParanoid; K0KR56; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:CCH43768.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..245
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 280 AA; 32529 MW; 896752AA752199E4 CRC64;
MVLFNSIKKF SPEWALVVSF TLYYAIIGSK QPPFLREFLI NDPTIQHPFT QFETIDDKKC
ILISSLVPLV LICLVTLGKH NWKFNKIINN NKFFNFLHLS ILGLALSLSI TGFITFFLKN
MIARPRPDFI DRCKPDLLKI KPNKFLYSID ICTNDNYELI LEGLRSTPSG HASIAFSGLH
YVTLFLFAQL SVWSNRKRIH LLLLSVLPEF IALFIALSRT QDYRHHFGDI FMGTLIGVGI
SYITYRKIFP SFADENYQDV YYLKEHSEIL PLYQERERSV
//
