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Database: UniProt
Entry: B6HB86_PENRW
LinkDB: B6HB86_PENRW
Original site: B6HB86_PENRW 
ID   B6HB86_PENRW            Unreviewed;       413 AA.
AC   B6HB86;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Pc18g03180 protein {ECO:0000313|EMBL:CAP94542.1};
GN   ORFNames=Pc18g03180 {ECO:0000313|EMBL:CAP94542.1}, PCH_Pc18g03180
GN   {ECO:0000313|EMBL:CAP94542.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP94542.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP94542.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   EMBL; AM920433; CAP94542.1; -; Genomic_DNA.
DR   RefSeq; XP_002562158.1; XM_002562112.1.
DR   AlphaFoldDB; B6HB86; -.
DR   STRING; 500485.B6HB86; -.
DR   GeneID; 8316148; -.
DR   KEGG; pcs:Pc18g03180; -.
DR   VEuPathDB; FungiDB:PCH_Pc18g03180; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   HOGENOM; CLU_021458_9_0_1; -.
DR   OMA; DCASWNG; -.
DR   OrthoDB; 25293at2759; -.
DR   BioCyc; PCHR:PC18G03180-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c18.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03390; PAP2_containing_1_like; 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; 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:UP000000724};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..244
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          288..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  45452 MW;  F13AB37A4ABAA510 CRC64;
     MEIPAKLPFS KRRLRPRVVI SYIFDYVIII ACVAGFAILN TIEPYHQHFS LNNISIQYPY
     AVHERIPMAY AVCISCGFPL VLIIVYTLFI DGLLWELNCG VLGLLLAQGL AFVITQALKN
     ACGKPRPDLI DRCQPRAGSK DLFPGLSNSS ICTGDPHLLT DGFRSWPSGH SSSSFAGLVY
     ISLWLGGKLH VMDNRGEAWK ALLVMTPLLA ATLVAVSRIM DARHHPFDVI TGSMLGIACG
     FVAYRQYFPP LSEPWRKGRA YPIRTWGTEP AGPDSVRIKG PRGESMVALR NPEEERMNPP
     DIPSSEHTRP DASTYLDESN PYTSNVYNRR PHDHDDDGGA WSSSEDDVTN GYEMRHGNTM
     GQNPGAGHHV PQYDPSNAYV SQTQPLTADA GIHVPDGMAG QGRPLTGMPG RPM
//
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