ID V2YMY2_MONRO Unreviewed; 559 AA.
AC V2YMY2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ESK93059.1};
GN ORFNames=Moror_8962 {ECO:0000313|EMBL:ESK93059.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK93059.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK93059.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK93059.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK93059.1}.
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DR EMBL; AWSO01000229; ESK93059.1; -; Genomic_DNA.
DR RefSeq; XP_007847697.1; XM_007849506.1.
DR AlphaFoldDB; V2YMY2; -.
DR STRING; 1381753.V2YMY2; -.
DR KEGG; mrr:Moror_8962; -.
DR HOGENOM; CLU_015982_0_0_1; -.
DR OrthoDB; 5487555at2759; -.
DR Proteomes; UP000017559; 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:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..559
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004713071"
FT DOMAIN 40..137
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 156..509
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
SQ SEQUENCE 559 AA; 61295 MW; BD8832E608763861 CRC64;
MLMNMKTTLL LVLLCVTVNA TRLLDRNLVY RSPFLDDLKG DPFDTSVLLW TRAVPVSPDG
TNELPDQSVP ACLSFKISSN SDLSGTPLDA GEVFTSYDVD WTAKVEASGL APDTKYFFQF
SDCTNPSIVS PIGATRTLPS PDTPADEVNG GKGLTLAVFS CSQYQAGYFN AYGFAAHNTT
ADIFVHLGDY IYESLGNGAR IGRQTLGREL ATIHDYRQRL NQYRTDTSLA FAHQNAPWVT
DDHEVADNAW KAGTADSNDT AVGCSFSPSG ACFTDRKLAA VRAYHEWMPI RQVAADDQFR
IWRNFQVGQL MDLSMLDTRQ YDRDLTDVYY NTVVNTISSF PNRSLMGAAQ ESWLYDTLSE
SKERGAVWRV IGQQIVFTQL NESDSFDLDA WDGYRANRQR VLDHLYNNEI DNTVILAGDS
HANWVSDLAH PNDSTTYDPI TGEGAIGVEF AGTAVTSSGF GTSLTPEASD ALSRILVATE
SNLNLQWSEG HFRGFFTLEV KPQTVNATYY AMRNTSNPNL DGFSTANFIV EAGANKLSRP
VGGGVGNIKA GALKINGTN
//
