ID G0MVD3_CAEBE Unreviewed; 391 AA.
AC G0MVD3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=CAEBREN_16610 {ECO:0000313|EMBL:EGT44791.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; GL379814; EGT44791.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MVD3; -.
DR STRING; 135651.G0MVD3; -.
DR EnsemblMetazoa; CBN16610.1; CBN16610.1; WBGene00155335.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_864172_0_0_1; -.
DR InParanoid; G0MVD3; -.
DR OMA; GSDCRAH; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03384; PAP2_wunen; 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 InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165:SF102; ACIDPPC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 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:UP000008068};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..293
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 352..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 45512 MW; C02600FF1831E60A CRC64;
MSVPPSRAHS EVFSASQYGG VTTVPPPRPR SYINYFIFPS AVLHVVGIAC LAALWYYLRF
TSVFPYHHRV FYCRDVHLYK PNFVPEDFNV YVSYPLLYTL AFTIPPLVIL IGEVMFWLFS
TKPRKIVYAN CGECPVHLFT RRLFRFVIIY LAGLLIVQIF VDTIKLMTGY QRPYFLSLCN
VSITACTAPL EHSPSPSPHL ACNYRGADEL RYAWLTFPSL HAVVSSYAAC FASLYIYYMI
NLRGAPLLRP LLIFGFIGLC IVDSFSRING YKNHWRDIWV AWVIGVFMAW FLCYCVLCFQ
EVYHVTVERT PIVQEERVSP FFSWFRLPRV QAPSVKEEYV VYEEDVERAD GTMPRHRRNR
DRQYEVTTTT ESFHRTISPP QQNQQNGGYQ Y
//
