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Database: UniProt
Entry: J7SBQ9_9APHY
LinkDB: J7SBQ9_9APHY
Original site: J7SBQ9_9APHY 
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
//
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