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Database: UniProt
Entry: G5ADQ9_PHYSP
LinkDB: G5ADQ9_PHYSP
Original site: G5ADQ9_PHYSP 
ID   G5ADQ9_PHYSP            Unreviewed;       523 AA.
AC   G5ADQ9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Calcineurin-like phosphoesterase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHYSODRAFT_531827 {ECO:0000313|EMBL:EGZ06312.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ06312.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ06312.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ06312.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; JH159164; EGZ06312.1; -; Genomic_DNA.
DR   RefSeq; XP_009538209.1; XM_009539914.1.
DR   AlphaFoldDB; G5ADQ9; -.
DR   STRING; 1094619.G5ADQ9; -.
DR   EnsemblProtists; EGZ06312; EGZ06312; PHYSODRAFT_531827.
DR   GeneID; 20661661; -.
DR   KEGG; psoj:PHYSODRAFT_531827; -.
DR   InParanoid; G5ADQ9; -.
DR   OMA; YTGLEGR; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          43..248
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          333..484
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  57145 MW;  7E7298F54BFB2477 CRC64;
     MTETTDPLPP SPTATDATPD QVPASAEPAK PPTGDQRAKL VILSVNDVYD MTPNEHGHGG
     MAEFATLLER QKAALPEDVT LLVTLNGDFL SGSEMGEHFK GAHMIELMNH LGIEYVVLGN
     HEFDFGADEL KARMRDSTAK WFGSNVLNAA TGALFDGVVD TELITLKDGL KLGVFGVCTE
     ETPTLSFPGS TVKFDDVFST SRRCVDELRA QGADFIVALT HLSISQDKKL ARSVPGIDVM
     LGGHDHEPFT MYEGKTFIHK SGQNAFWLAK LEFELYRSAD HPERGLSVLP QWSMIANARM
     PPQPACQQII YKYMREMESA NDPEQNERVL ATLATTLSTR TALLRAGESN AGNLVADALR
     SELAADIGFI NGGFIRGDKE YLAKSNVTVG ILKHEMPFPR PAVLVRIKGS DLRDAFIQHL
     YKYPQQSGSH PHVSGLKLTI DMQSNPPAVT KMLNDNGEPV DLDAELLVAT SKFVAGGGDG
     CSSWLKGEVL REAAKIPEVV ADFMMKKRLL AYPEHEGRIT ILE
//
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