ID W6QN32_PENRF Unreviewed; 523 AA.
AC W6QN32;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase {ECO:0000313|EMBL:CDM31062.1};
GN ORFNames=PROQFM164_S02g001212 {ECO:0000313|EMBL:CDM31062.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM31062.1};
RN [1] {ECO:0000313|EMBL:CDM31062.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM31062.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792016; CDM31062.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QN32; -.
DR STRING; 1365484.W6QN32; -.
DR OMA; ADDCPCY; -.
DR OrthoDB; 2958177at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase 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 Oxidoreductase {ECO:0000313|EMBL:CDM31062.1};
KW Peroxidase {ECO:0000313|EMBL:CDM31062.1};
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..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..210
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 399..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58265 MW; 3993C6CECF38DED0 CRC64;
MGTSKKDQPD AGLKSLNHYS NRLPLWRYWP RQKLIPLIRY ETPYLAWVQE KVRTPTLDSY
FAFTANLGTH TFFMVFLPFL FWCGSPSMGR GLVHILASGV FWSGFLKDLL CLPRPLSPPL
QRITMSGSAA LEYGFPSTHS TNAVSVAVYA LALLGSPDST LGTQVTLLLQ AVTYVYVVSI
VLGRLYCGMH GMLDCVVGCA MGAAIGLIQF HYGPAFEEFI LSASPKEISL LGLLIIFLVR
IHPEPADDCP CFDDSVAFAG VMLGVDVSSW HFADIWVGYP SGSIPYDLAT VGWIKTVIRL
FMGVLCVFAW RIATKPALLR ILPPIFRTLE KLGLLLPRRF FTTASKYTTV PYNLKDHDVF
PNFSDIPDIL TTMRHPRRRA ISIGPQSEAD AYETLAYREK RRRQSQSGSN HPSPVAEDQN
KLNGTPVRPR KTASLDDYED MMGRGSPMSS AANVNFDIPT TPFPSLDIQA GERDEQEVFS
QIKKPRVRYD VEVVTKLVVY AGIPWVVIEV APLLFDLIGL GTR
//
