ID A0A179URG0_BLAGS Unreviewed; 573 AA.
AC A0A179URG0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Sphingosine-1-phosphate phosphohydrolase {ECO:0000313|EMBL:OAT10696.1};
GN ORFNames=BDBG_06506 {ECO:0000313|EMBL:OAT10696.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT10696.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657461; OAT10696.1; -; Genomic_DNA.
DR RefSeq; XP_002623067.1; XM_002623021.1.
DR AlphaFoldDB; A0A179URG0; -.
DR STRING; 559298.A0A179URG0; -.
DR GeneID; 8509096; -.
DR KEGG; bgh:BDBG_06506; -.
DR VEuPathDB; FungiDB:BDBG_06506; -.
DR OrthoDB; 2958177at2759; -.
DR Proteomes; UP000002038; 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:UP000002038};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..210
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 401..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 63253 MW; 5B6FC46433B7DC2C CRC64;
MTKGKADQPD AGLKGLDHYQ QKLPKWRYKL RTALLPLVRW ETPYLAWFQA RMRTPSLDSW
FAITANLGTH TFYMVMLPIL FWCGYTEVGR GLVHLLASGV FISGWFKDML CLPRPLSPPL
HRITMSGSAA LEYGFPSTHS TNAISVVVYA LHLLNSPDST ASPVTNTIFR IVLYIFGTSI
VIGRLYCGMH GFFDVIIGSF LGALLGFLRC SYGETYDEII YSGSINTVFA VVVVVLALVR
MHPEPADSCP CFDDSVAFAG VLMGAEFGNW HFAQTTFAWG DPYPGTVPYD LAKVGWIKTI
LRIILGVVIV FLWREIMKPS LHRILPPIFR VIERLGLNLP RRFFTLASEY EQVPGHLKDD
DIIPNVSEIP SILTSIRHPR RRAISIGPQS EADAYETLAY REKRRRESTS SNQSRSVSAG
RRLPPTIEDK QNMRDTSSAS SPAAGGSQRF GGGENNPVVR SPRKLDEYEH MMGTGTPVFS
AESTPNMDGA GGADGASGAS GTGANADVNV NVAADALEYQ LGAEEEKEMF SKITPPRVRY
DVEVVTKLVV YFGIGWLSVE VNPIIFQLIG LGP
//
