ID A0A168F879_9HYPO Unreviewed; 623 AA.
AC A0A168F879;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Alkaline phosphatase D-related protein {ECO:0000313|EMBL:KZZ99585.1};
GN ORFNames=AAL_02157 {ECO:0000313|EMBL:KZZ99585.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ99585.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ99585.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ99585.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ99585.1}.
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DR EMBL; AZGY01000003; KZZ99585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168F879; -.
DR STRING; 1081109.A0A168F879; -.
DR OrthoDB; 5487555at2759; -.
DR Proteomes; UP000078544; 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:UP000078544};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..623
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007896798"
FT DOMAIN 65..184
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 197..547
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
SQ SEQUENCE 623 AA; 70318 MW; 7916E543ACBB7478 CRC64;
MRLHGLWCAV TFLAGFAIAR FDGNVNYQSP SRRHEWLGID VSLVERRSLK RSNVPYKPAQ
LHFTHGVASG DPWPESVILW TRIAPFNESD ASEVTVSGTV PLWNHDNDKY IKADAHPICA
EWKVFRANGT RLHDVVVAGK AYTTSDIDFT VKVEATGLKP LTQYHYQFSV CGSNNKSPVG
RTKTSPAKDD AVSELSFAVF SCSNYPYGYF NAYGNAARKD KHDFVIHLGD YLYESGERGE
RASKPSKTLF SLGDYRTRHG QYRSDPDLQL ISKDFAWIST WDDHEFADNG YKDGFAQLNN
TEDSFLKAGA GVSVDQRKVH AVRAYFEWMP IRQTDLDDGL RVWRSFQMGK LVDLIILDTR
NYDRSITDLY WNEHYISRIA DEPSRTLMGA RQESWFYRSL SQSKKRGAAW RIIGNQIMFS
RIYLNDNLRL NGDAWDGYVA NRNRTLAHMY ENSIDNNIFL AGDTHQNWVS DLAWLGSKPY
DKTSGRGAIG VEFGGTAVSS TGQKGPIEPV AGDSARSLVR RNDELAWQEG YYRGYFLLTV
TPSTARALYF GCPTVASRNG WEIPLANFTI NAGANHLERP IGGGRVESGA LRDGQVQHTN
LTLNTNTGKW EVVGYEKMYL LSR
//