ID D7FIS9_ECTSI Unreviewed; 1153 AA.
AC D7FIS9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=Esi_0123_0062 {ECO:0000313|EMBL:CBJ28896.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ28896.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ28896.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN647892; CBJ28896.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FIS9; -.
DR STRING; 2880.D7FIS9; -.
DR EnsemblProtists; CBJ28896; CBJ28896; Esi_0123_0062.
DR eggNOG; KOG0374; Eukaryota.
DR InParanoid; D7FIS9; -.
DR Proteomes; UP000002630; Chromosome LG08.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF385; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 120..125
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 254..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 117820 MW; 50E7014EDB8D5658 CRC64;
MNSISLNVDG LIEELLSVRG KGPARQVNLY EDDIRSLCLV ARDVFLDQPC LLQLATPMKI
CGDIHGQYYD LLRLFDHGGH PPHSNYLFLG DYVDRGKHSL ETICLLLCYK VKYPANFFLL
RGNHESASIN KMYGFYDECK RRYSTKLWRT FTDCFNCLPI AAIVDDKIFC AHGGLSPELF
DMEQINRVSR PTDVPDTGLL CDLLWSDPDR DIIGWGENDR GVSFTFGEDI VRDFLATHDL
DLICRAHQIL QSSEKKRRLP RRSTATRALL SKGPIAGPRD SPSPPLGEDP LSAPPAQAEE
EEEEEEEGGD YGVGETGAFP SPAPETLVPP LSHAAAAAAS AATAPRTSLL DASVSAFAAA
GAAKLAGNGG APFNSDGSLS SSASDYDSGP PSFGSLPGDH NRSARGANGG GGARDGTGSP
PTGLGRALVA PTNDFDGAGA ATAAGLACSP DIMAGDGGSF VDEGRLGGGS EAGGLERIPV
VRLPPPPPTT LSDALATRKL ADIDGVGGAA GALPGDGAAV EGPPLNKQTS SGRSRGGGGG
GGGGGSERSG RGGGRQYSSP PPGGELVDRD GDWVNSSIGG GGDRVDKRRR QRWLNTAASR
RGDGGFTTAP ANGGGAGKAA AAAAGPPSSR DTQASGGDRG ARIGVATAVA GRGVGVAGQA
AAADGGGPAV PLPEFGGDGD GVGGGRGVSG AATMSPGDVG GGAGAAGERG GGQQLVVFPV
AKALDESDLA VLSSDEDSVY AASSDTYEVT SDTSLDLNVD RRLTGGLGAD EDSDDYYSAS
DEEDEEEEEK WGGGRSGGDL QRRRMMMTGG DGEATSGSAE RRGEQRQANA RAREKAAAAA
TAAYAGGGSR ADVVGGGAID PAMLPYAAYG LATPPAGTGE SDSPGVGGSS SGTSFEAAAA
AAERSSGSER KSEECDDGGA RRTTRSTREA APTHRGGGGG GRDDDHDHDD GNGGITGYSR
FDDGGGGGGG RDDASGYGRT RSLTAEASSP EDTIRANRGD SEDFGRRRGR EKSMAGRKLG
GWRLGKPMTG SRKRGATTGM GADGGEEEKA RGPADLDSSS RSSACSCSLR SDGGDSLTES
EKRSRREGAT RLLGSVKKGA SVVWSKVTSD HPEPLPIDKG PSARALAAWA TRRRVAEVAE
QASCTAGLLQ FSD
//
