ID A0A024U1U6_9STRA Unreviewed; 915 AA.
AC A0A024U1U6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=H310_07593 {ECO:0000313|EMBL:ETW00195.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW00195.1};
RN [1] {ECO:0000313|EMBL:ETW00195.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW00195.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-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}.
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DR EMBL; KI913965; ETW00195.1; -; Genomic_DNA.
DR RefSeq; XP_008871220.1; XM_008872998.1.
DR AlphaFoldDB; A0A024U1U6; -.
DR STRING; 157072.A0A024U1U6; -.
DR EnsemblFungi; H310_07593-t26_1; H310_07593-t26_1-p1; H310_07593.
DR EnsemblProtists; ETW00195; ETW00195; H310_07593.
DR GeneID; 20084643; -.
DR VEuPathDB; FungiDB:H310_07593; -.
DR eggNOG; KOG0377; Eukaryota.
DR OrthoDB; 46665at2759; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 3.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF13499; EF-hand_7; 3.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00054; EFh; 6.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00018; EF_HAND_1; 6.
DR PROSITE; PS50222; EF_HAND_2; 6.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 608..643
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 644..679
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 740..775
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 776..811
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 837..872
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 877..912
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 915 AA; 102986 MW; 5E5E68459183D4B4 CRC64;
MSGDSGNEFH GANDIAVGLR VLVFGKHAGI VRFVPDTRSA LLGVELDRSV GDCDGIAADG
RQHFKCRPLH GIYVREENLA PYTAEDAAAV RIQSAWRRRK TVLAFTTVVL SSMWNMLDNN
QEQLNMKRAE KTKSASQALS LLAKQSSKGE IKISHSVSSI TDDYSGPRLA FPLRLHNVLD
MLEQFKKGVV LHSKYVMDVL SEAKKVFTAL PTLQEIAVTE GEKLTVVGDI HGQLKDLFTI
FTTNGLPSGK NKYLFNGDFV DRGAYGTEVM MTLLCFKLLY PDGVYLNRGN HESRNQNSWM
GFEEEIWAKY DGTMDGDPCR ASTVYDAFQG LFDSLPLCAL VLKKIFVVHG GLFSCDNVTL
AHIKAINRKR EPPLHQTGFE DKIYEDMLWS DPRTIAGRQP SERGAGTEFG HEVTNNFCAV
NRVALVIRSH ECVPEGYDVL HGGRLITLFS ASRYCGTQMN KGAFLTLGSD LQPEIQQFYG
NPLNESEWER PEDEQAKMQE NLEGDALRMI AERICDHKAD LFWYFTQHEH EYKGTVPRLV
WAEALKSILG IDLPFLLYQT KLADSEPDNT INYSKFLSRY RIENPAVDAS GWQESIISII
CKKLYRAMGA GSIEQAFKVF DTDDNGTIEY DEFMNILKSM DTGLSDQQMF ELMRTADTND
DGRLDFKEFF SRFDVIFTDV RLANSQSFIS PPPAPTSLSA PSKLVRKKSE RAAPLTPAPK
QDVDKDTMAA LVAIGRAFFQ LEGTLLDNFH RFDTNRDGVL QKDEFFQALR HLNLNYPDEL
LAKIMEAVDL DGGNTIDYKE FLAAFTVKDA SEQVALEKGD MTWQQSVLQQ VSNMFYQHRI
HIRAAFRLFD VDNSGTISID EFRTGIATFN AIMDSPLTDE QIDALLAHLD SDSDGIISYK
EFLEGFQVVD VRLHE
//
