ID A0A2B7WHZ6_9EURO Unreviewed; 620 AA.
AC A0A2B7WHZ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Alkaline phosphatase D {ECO:0000313|EMBL:PGG96151.1};
GN ORFNames=GX51_07955 {ECO:0000313|EMBL:PGG96151.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGG96151.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGG96151.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGG96151.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGG96151.1}.
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DR EMBL; PDNC01000188; PGG96151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7WHZ6; -.
DR STRING; 2060905.A0A2B7WHZ6; -.
DR OrthoDB; 5487555at2759; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012021689"
FT DOMAIN 61..183
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 196..551
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 579..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 69658 MW; 15D119D42C106805 CRC64;
MLRSTTVLLA LASTSLAFYA GNLNYRSPSH NHPGLGISIP KVAKRSDTVQ EYSADELEFT
HGIASGDPYP NSVILWTRCA PSTENVKEPV DPERGGELYD SVPIYGDNEG NAPVSKAPVC
VEYSVSPDKD FKKITDHGTV YTSSDVDFTV KVEASHMKPF TTYYYKFNIC GSDKSSPVGR
AKTSPTEHDE VTDISLAVYS CSNFANGYFN AYGNTARKDS VDYVVHLGDY IYELGGDGSG
IGRTQYPKKM IYTLYEYRKR HATYKTDEDL LLSHRTFTWI PVWDDHEVAD NSYRDGSSLL
RNIEGSFIVD GGVSVDQRKM NAVRAYFEWM PIRQVAMDDN LRIWRNFKIG NLLDLIMLDT
RHYDRSITDL YLNHGYIKKI ADDIGRSMMG PRQEHWFYEN LKSSAKRQAT WRVIGSQTVF
SRVDEFGSIG LGVNLDSWDG YRSNLNRTLR TLYENNIGNN IVIAGDSHAN WVSDLTWLDE
YPYDPVTGEG AIGAEFAGTA VTSSGPAGNV GIGNLQSKTL IKKNRELQWS ELYYRGYFEM
TLSHTRTDAQ FFAIPDIKKR SPYEIPMANF TVIAGENRLS RTNGSPTTDG QGVHNGALKN
GKLEKQTVQY NTETKEWTGI
//
