ID J7SBQ9_9APHY Unreviewed; 564 AA.
AC J7SBQ9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=FIBRA_00035 {ECO:0000313|EMBL:CCL98041.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCL98041.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCL98041.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCL98041.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE796867; CCL98041.1; -; Genomic_DNA.
DR RefSeq; XP_012177324.1; XM_012321934.1.
DR AlphaFoldDB; J7SBQ9; -.
DR STRING; 599839.J7SBQ9; -.
DR GeneID; 24092952; -.
DR HOGENOM; CLU_019266_1_0_1; -.
DR InParanoid; J7SBQ9; -.
DR OrthoDB; 2958177at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:UP000006352};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..290
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63020 MW; 653C095F4B361678 CRC64;
MPPQTSDPYT ANAFPVAADA HRNHLNNVPN RSASPYDSRS STPDPIEFTA RRWDEATKAN
GTSLSVDEVR KEEDCEGISE VGAGLRPEEV YDRTMSGWRA AIRRRVRKNV IWESVILGKM
QEFVRHPILD GYFVYTSSLG THTFFMISLP ALVFFGYTQV STGLILVLAM GVYASSFLKD
LVCSPRPFAP PVTRLTIGTH HLEYGFPSTH STNSVSIALY FYSILREAYT RSAESEHAHG
LSSTSYYILS GVLLFYVFSI VYGRLYTGMH SITDCVVGVL LGAGIWAVNL VCNDLLHAWI
RDSGWIVPAV TIPLCLLLVH RHPQPVDDCP CFEDAIAFIS VIMGEILSRW YMLHNGYDEN
YFVLVMPGKM WGNWFEMCTW WSVATIKMTF GILIIFMWRI FAKTIMHIVL PPIFRLLSQA
FTLPHRRFYT PATDYKNVPA EKGLHPIPSV IDLTSMMEME TDVGNASASG FGVGLQYGGI
YGERNVKLRG AKGRDRSANP IFHGRGEKSG ILLSADESDR NREDVKHYDA DVLTKVVVYS
GIGMFACGVI PVLFEAVGLG LRIS
//