ID M4BB21_HYAAE Unreviewed; 889 AA.
AC M4BB21;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP803482, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP803482}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP803482};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; JH598083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BB21; -.
DR STRING; 559515.M4BB21; -.
DR EnsemblProtists; HpaT803482; HpaP803482; HpaG803482.
DR VEuPathDB; FungiDB:HpaG803482; -.
DR eggNOG; KOG0375; Eukaryota.
DR HOGENOM; CLU_017609_0_0_1; -.
DR InParanoid; M4BB21; -.
DR OMA; RWKKALH; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713}.
FT DOMAIN 312..317
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 99732 MW; 927AE2ECF167ABCF CRC64;
MASKLNAFLA AVPANASVSK SSPPALSVPQ SEPQATPEPI ESSLKIPQTH HCFSSLQRLQ
QDLSLSNSSD KAQDQPEDDR VIARPSLLKS FMATQAAAAK LKAYKDEMAP NLMHSSSCTE
LDAKSEAGPM RLTTVQGPHY RRVSTDTTLF NRYLRQQADR DIGQETVQHF TNVPIVTATA
VREDNVESET SEDCSDDTEH VEQVLDPQEI LARFRVGETI PVSSALEIIR RATSLMSLEQ
NVISIRAPYT LVGDLHGQFQ DMLELFRVHG FPAVDNPFLF LGDYVDRGVS SCEIILLLLA
FKVDVPESVH LLRGNHECRS LSTFYGFRAE CLQKYGPAVY NRMIKCFESM PLAARLETVH
GTFLAVHGGL SPDITFVEDI NAQVNRFMEP EPKGVLCDLL WSDPARGEAQ EYEWAPNSIR
GCSFTFNEHA CHEFLKRNNL LAIIRAHELE EDGYKEHFRH EADHPEDDTG GELVLPAVVT
VFSAPEYCNT NHNVGATLKI PWEKQNDRLL QYQQHKRSRY SEFNYARPSE DKAVKALLKE
HLPFLPIDFY DLVNVCRQLR FTLDRAANMS SSSRSSAIKP LRKKMSFVSS LCAPSTALET
TIREDVELPI SPPYFAPVSD LEIEHNAAGT SGDLLQDWEI VGESKSVETA GTINLTKYLK
NEKTDNKLKT KLEKKHKQQK DKKSWDTNRI VSGWKFSPAF VRFYDRYFAR DSVKKCDPDV
SSAPSHPGKR VPGIYRSPSS RSTSTGEVAL GLEANDTVVE TTGPSRRKSM TDWMPMPSFE
QVARLTNTLQ GHITIEGSGV NVFTKSQWQA LKLWFSILDL DGKGVLVEES FVVLLAEQDT
DAYATEDELS LLMEVMDCNA DSRVTEQDFL LFAYRALLQW KKSMHGSGK
//
