ID R9P6E1_PSEHS Unreviewed; 770 AA.
AC R9P6E1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=PHSY_001240 {ECO:0000313|EMBL:GAC93675.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC93675.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000256|ARBA:ARBA00038324}.
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DR EMBL; DF238778; GAC93675.1; -; Genomic_DNA.
DR RefSeq; XP_012187262.1; XM_012331872.1.
DR AlphaFoldDB; R9P6E1; -.
DR STRING; 1305764.R9P6E1; -.
DR GeneID; 24106541; -.
DR eggNOG; KOG2822; Eukaryota.
DR HOGENOM; CLU_019266_1_0_1; -.
DR OrthoDB; 2958177at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03388; PAP2_SPPase1; 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 PANTHER; PTHR14969:SF28; DIHYDROSPHINGOSINE 1-PHOSPHATE PHOSPHATASE LCB3-RELATED; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..400
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 79..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 84210 MW; A36BF7AF402BEA8C CRC64;
MVGGPKVETV SVSRWKGSCK GYNANQDLRL LENVDRAGCI EKQRRRGLSL LCSPKANRYR
CRLAQTRLAD GFDTIQEELR VGRPSTSSNL HQRRAPAARE ASSSSVEEDR KISGSQINHT
ISPSSSSTPA SSKSNRPALS VNTDHSTQPT DGTLQKHKRG HVQKHEKIER IGLLRGSSYV
KSNDKDSVGE HELTTSIGLQ DDAVYDAYLP RPIAFLRRCI VAILRREAPL HERHQRLVRR
PWLDRYFVNT SLLGTHSFFL VFLPMVFWLG SPRFGRGLIN VLAFGVYLSS AIKDLFCVPR
PYSPPVTRLT VGTHHLEYGF PSTHSTNSVS IALYIYLWVR KMREAADPSD SSLFDSYLWE
AGLLFYATSV VYGRIYAGMH SVIDCIAGSA LGAGITAVQW TFFDHIEQFV KVNSWGVPAV
IVPAGLLMVS VHPQPVDDCP CFEDAIAFVS VAMGVALARW CLRFGVVLHT DPLLHPFSTF
FDPAAEYSTV NTTATTSGTP LIQIPVAGAA EIWIKRGLVM AIGLVNVLLL RVIVKTACKV
ILPPTFRLVD QLIGFSLPRR HYTPASDYNK IPLADLSAVP SVIDLPSQII VTDESGKQQT
IQSPILSPTS SSRRGSADVR NGAAIGGGAF SPSLLGRSPL HSPIPSRTPS PNPLEMRRSL
ASTGKSPKKK IQFTIGGGAA DETDADSTPD TATDLPIPLT QSRAHPNFIP PDEQLARNLA
ADIKGSTPKD VEQQVKHYDA DVLTKVIVYT NIGLFSAGFI PALFQHLGLC
//
