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Database: UniProt
Entry: R0M5W9_NOSB1
LinkDB: R0M5W9_NOSB1
Original site: R0M5W9_NOSB1 
ID   R0M5W9_NOSB1            Unreviewed;       256 AA.
AC   R0M5W9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Lipid phosphate phosphatase 1 {ECO:0000313|EMBL:EOB13364.1};
GN   Name=LPP1 {ECO:0000313|EMBL:EOB13364.1};
GN   ORFNames=NBO_80g0027 {ECO:0000313|EMBL:EOB13364.1};
OS   Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS   (Pebrine of silkworm).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB13364.1, ECO:0000313|Proteomes:UP000016927};
RN   [1] {ECO:0000313|EMBL:EOB13364.1, ECO:0000313|Proteomes:UP000016927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX   PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA   Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA   Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA   Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA   Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT   "Comparative genomics of parasitic silkworm microsporidia reveal an
RT   association between genome expansion and host adaptation.";
RL   BMC Genomics 14:186-186(2013).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   EMBL; KB908988; EOB13364.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0M5W9; -.
DR   STRING; 578461.R0M5W9; -.
DR   EnsemblFungi; EOB13364; EOB13364; NBO_80g0027.
DR   VEuPathDB; MicrosporidiaDB:NBO_80g0027; -.
DR   HOGENOM; CLU_021458_6_1_1; -.
DR   OMA; CTEMYEN; -.
DR   Proteomes; UP000016927; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF35; RE23632P; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..235
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   256 AA;  29450 MW;  35EA10C401CDBC86 CRC64;
     MTLFNKQLIF IFVYREQPMR IGSSMILIST ISLLFILLSL IVDPRIVQPN FEDQSISKKF
     IEKEMISIAL VTFISVTIPF FIFFSCFRYL NLDITNEIQF YVVFLTNFFM VSAIIENLKN
     LVGRLRPDFL ERCIPIKGVC TGKLGRIKEG RKSFPSGHTG TSVAGFLFLC LFLNFYISTN
     TQRDTRSKIF KCTLICFILL IPTAIGLSRF YDNRHFISDV LSGALISILT SLFLFNFYGL
     KLIKTQTPET QIKNLD
//
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