ID W2Y097_PHYPR Unreviewed; 1231 AA.
AC W2Y097;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=F442_22159 {ECO:0000313|EMBL:ETP28535.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP28535.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP28535.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP28535.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|RuleBase:RU004273}.
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:ETP28535.1}.
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DR EMBL; ANIY01004594; ETP28535.1; -; Genomic_DNA.
DR AlphaFoldDB; W2Y097; -.
DR EnsemblProtists; ETP28535; ETP28535; F442_22159.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00303; S100_CABP; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 168..223
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 746..781
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 922..957
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 986..1021
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1120..1155
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 1231 AA; 140752 MW; 301FBD041535240F CRC64;
MDTEGFTSRA WLGHWVSGEE EPVNNYYEDH KLMEGALIKL GDYAHFRYFL LFRNGRFCYY
ELPMPAAAPG GGSEGPRRVH LTLTSKHLRG VMMLNASVNA KDLAKSEDEY DADLIKRGLV
FNRKKLEMQL TGYSPTGQLM CWKLRAGKDA VYLKWERAFR LALRPIWVQN SKCCMVCKKE
FSFFIRPHHC RKCGTCMCDE CSVFVPRLPM QGYYDEVRIC RDCSPIKIQR SSLKMGTRVL
VYGILVGRVV QVDAADDSVD GSAFVNVELV KKNNQLRRFA LEHVELYSDA VLSANRIKNA
IRQHLSYAVF RTQLNFNTWN LLETVQEQRT VQMVRILNKS TSINELQSMV PMLGSLDTMQ
FPDDDISEKD RVKESLSHYR GVHVSFPLRL DTVKKLINQF RNGILLHRVF VRQILDESEK
LFRKMHGSPM NEIEIPMGVQ LVVVGDLHGQ LEDLLTIMDK NGVPNSKTWY LFNGDFVDRG
SHGIEVILLL LIFKLLYPEY VFLNRGNHEE RMINEVFGFE DEVYTKYGTD NDEVAGWSGL
GTSMNYSPMK LFQMFETVFG LFPIFALLNK RVFIVHGGLS NHENVTIEEL LQLDHRREIP
TQGTSRADEV FTHLLWSDPR DENGWKPSSR GAGVEFGPDI TKAFCAQNGI SLIIRSHECR
EEGFDIVHDG LLLTVFSASS YCGSQTNKGA YVQLELGEDN EVKPHVVQFS SQPLQKLKDA
GRNEWRKKAQ RLERRTLMSL VEIICEKKHA LLAAFNELDS TGSGRVTKLE WKATLQKVLG
IEASFLSYFH QLAEEEQDGG VDYQKFLNRY TVELDGGNVE WRRNLIRKVW KGFCQALPHP
SESDAEKMTL QDKLHFAFNL FQSSPAGAAK AATPLSKIEE SGPLSTCGYG DKPKESYMRN
SLVTYEVFRN TIQGKLQLGD TLSEQQIFEL MQHLDQNHDG VVDYQEFCSF FAEFSRTDYL
QEIFEVDDTK AISLLNRCAA LLQNPNKFKS LREAFDAFDH SKTGKLTVDD ILKGTQELNM
VPELDNEEAQ LLFNSILLSY YGINQRHQWD KRGLDWVVFE DTFSPDSTFQ RRLWLASLGA
SNTNLAALDI GDDDVQDGQA SKNQAWADTF VDSVKQSLHE QRLYIKFLFR ILDRKRHGYV
TKQQFVATMQ AINEEHGAPL KLSQLEQLAD AFAHRKTVRR MSNAGEETEE TRTYVSYPEF
LRSLRIIDSG PTEGTAVFPE MQEVTDASSG E
//
