ID A0A1J9QKT1_9PEZI Unreviewed; 507 AA.
AC A0A1J9QKT1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pap2 domain protein {ECO:0000313|EMBL:OJD29486.1};
GN ORFNames=BKCO1_7900015 {ECO:0000313|EMBL:OJD29486.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29486.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD29486.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29486.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD29486.1}.
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DR EMBL; MNUE01000079; OJD29486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QKT1; -.
DR STRING; 236234.A0A1J9QKT1; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
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:UP000183809};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 129..272
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 355..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 56019 MW; B9F36D700108C59B CRC64;
MDSWNQQKLP FSKKRLSKTV IVSYVFDYVI IVILIIAFYA LDHVEPHHQE FSLRNYTLQY
KYAVKERIPV FDLCIIAVLA PALIIAFYTL VIDGLFSSNR GAAAGPGRRK LLGKYRMKDR
LWELNCGVLG LMLSVGAAFT ITGSLKNAVG KPRPDLIDRC QPNTFEDPQP FGLSNHSICT
QDNNAILKDG FRSFPSGHSS TAFGGLYYLS IYLAGKLHVL DSKGEVWKSF IVMVPTLGAA
LVAASRIMDA RHHPFDVLSG SLLGILTAWG SYRQYFPPVS ETWRKGRAFP IRSWGKEPEI
PADAYPINHE GREPLRDAAS LKTIDEEQPM RGADTGATDI DASDPAANVF RQQISNSQRH
RQQLAAQAYG DARPTPSSVY TADLNRTPTA TTYSSQLPSS NPYAQTYGAR RRRGDNYEES
SSEEETDEFE LQRTYTLSNP HQGQTAAPVA YNPVNDTFGD TSYRAQTTSP FVAPHEEADL
GAGAARTLPP QVPPHAAPYG SGRGADY
//
