ID A0A0D2FR09_9EURO Unreviewed; 232 AA.
AC A0A0D2FR09;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|Pfam:PF01569};
GN ORFNames=PV04_10607 {ECO:0000313|EMBL:KIW62434.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62434.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW62434.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62434.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) 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; KN846963; KIW62434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FR09; -.
DR STRING; 5601.A0A0D2FR09; -.
DR HOGENOM; CLU_1194762_0_0_1; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000054266; 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:SF84; PHOSPHATIDIC ACID PHOSPHATASE BETA; 1.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..225
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
SQ SEQUENCE 232 AA; 25288 MW; B7628B791EE46F28 CRC64;
MSDLRSAPVG PPHTPLSTSI YQFLSDSIPH RASFRRLGRY SKAFFLDHWP DILLVLLVTA
IAGAVFLIPT RPPLLFPLLD PTGAVYNPSL AYPYRPAILN SLTAGLLSSL IPLATILLSQ
FSIRSFADFW AATLGLLYAL ATGTCFQAIL KKTIGGFRPH FLSVCKPRPM AVGSGVGFNG
IMYRVQDVCT GSAKEIEWGI QSFPSGHSEI AFAGFGYLTI YLFTHLHSGD HD
//
