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Database: UniProt
Entry: V2XJM1_MONRO
LinkDB: V2XJM1_MONRO
Original site: V2XJM1_MONRO 
ID   V2XJM1_MONRO            Unreviewed;       579 AA.
AC   V2XJM1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:ESK93932.1};
GN   ORFNames=Moror_12951 {ECO:0000313|EMBL:ESK93932.1};
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:ESK93932.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK93932.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK93932.1,
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:ESK93932.1}.
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DR   EMBL; AWSO01000162; ESK93932.1; -; Genomic_DNA.
DR   RefSeq; XP_007846751.1; XM_007848560.1.
DR   AlphaFoldDB; V2XJM1; -.
DR   STRING; 1381753.V2XJM1; -.
DR   KEGG; mrr:Moror_12951; -.
DR   HOGENOM; CLU_013967_2_0_1; -.
DR   OrthoDB; 55429at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   PANTHER; PTHR43606:SF6; ALKALINE PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G03860); 1.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..536
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
SQ   SEQUENCE   579 AA;  66182 MW;  9BD354EFE5AFD957 CRC64;
     MRNVMVRRSS PDFPQATIIG KIAAFLLFKT DARQSEENYS LNLDPNPSLN AMSTSLLRFS
     GVIASAYLKY NTWLFLRKLP LGYRFIPRLI AAFGVFAASF LLQPRSRTKN TALPVVLGFR
     GRNNLVDAVT ILLNTLFLMS CADFIYRGQV LYPVHKLSTS RVGWTNSTTT RIVVSYPGPS
     SFNFSYTNDI TNWTVIISNL EIQNEATTIT LAFLEPSTRY TYSTSLGHSG SFLTSAPESM
     PTTVRFISTS CMKPFFPYSP FKHPFALQGL QHLSSYLSRN TSYSQDFILF LGDFIYTDLP
     IVSAPLTREY YTNLYRQIYA SPDYTPILRN TPWLHMFDDH EIINDFWPGM DVSSKTFAEA
     IQPFLLYQNN ANPPPLYEDV FYYTFRRGDA SFFVLDTRSY RDQPADLESG GHGKRSMLGL
     RQLEALKAWI RSEKGWKVVV SGVPMTQNWS KGSDAMDSWG GYLDEREEIF RELWAVGGGI
     IVSGDRHEHA TVKFPPPAGE YPENNAIIEF STSPLSFFYQ PFARDYEDVH ETDVTVYQHW
     KGTSKFGAFE LEKEVARFQL VVDGEVVWEY NHRRTNYHT
//
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