ID A5DRJ4_PICGU Unreviewed; 462 AA.
AC A5DRJ4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=PGUG_05895 {ECO:0000313|EMBL:EDK41797.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK41797.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK41797.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CH408162; EDK41797.2; -; Genomic_DNA.
DR RefSeq; XP_001482132.1; XM_001482082.1.
DR AlphaFoldDB; A5DRJ4; -.
DR STRING; 294746.A5DRJ4; -.
DR GeneID; 5123955; -.
DR KEGG; pgu:PGUG_05895; -.
DR VEuPathDB; FungiDB:PGUG_05895; -.
DR eggNOG; ENOG502QPKA; Eukaryota.
DR HOGENOM; CLU_047580_1_0_1; -.
DR InParanoid; A5DRJ4; -.
DR OMA; PMAPPWF; -.
DR OrthoDB; 1423352at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF8; INOSITOLPHOSPHOTRANSFERASE 1; 1.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..416
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 462 AA; 52953 MW; 633A3AB9BE8FA343 CRC64;
MPSFFAVQAK GMNILRVLVR PFLFIFQFLY RVFWSGLNEK SLIQLVVSFW INFAPVFVWL
MIFKNAGLIP KKIRPPIHVK LAMNMDIFMF DFMKKPIGSL ITLTGLAAVS WLLYKKFYRP
SAYAELSSIS DDNSFEMSSG GSSDLEDQVS TFDLAKYHSS TPSAPGDFQD DVHHGDLVFF
HKLSHRRIAA RTAEINRKIV EHLQTTGSYR PYNCWHLSPI LLTAASWVLL NIAHYFRVEV
YTAKDLFAWA SYVLGHFFVP LFTAIWLYVF HAPGALKLFS FGLGMQNIAG VLTHLLLPTA
PPWFIHLNGE NSTANYDMPG YAAGLTRIDV EMGTHLHSKG FHASPIVFGA VPSLHSAMAV
MAFYFVSYYS RWTILKIMAL SFVCIQWWAT IYLDHHWRLD LIVGMFYSLV AITILRTWSK
GFNKVDKDFL DARLRFDFIR GSTMGMRVFR NTRLQSFFDP LS
//
