ID K3Y553_SETIT Unreviewed; 859 AA.
AC K3Y553;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK98203, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQK98203, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK98203,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQK98203}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK98203};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
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|ARBA:ARBA00001482};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AGNK02004439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3Y553; -.
DR STRING; 4555.K3Y553; -.
DR EnsemblPlants; KQK98203; KQK98203; SETIT_009341mg.
DR Gramene; KQK98203; KQK98203; SETIT_009341mg.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_010333_0_0_1; -.
DR InParanoid; K3Y553; -.
DR OMA; EYQSTLC; -.
DR Proteomes; UP000004995; Chromosome VII.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081:SF34; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 134..386
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 692..758
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 525..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96054 MW; 6AA3866638F60056 CRC64;
MIKSVVYYGN IPVGEAELWP KGETDLAWAR EIRVDRLSPP SERCPPLAVL HAVAAGARCL
VMESRPTSTA DEPPPPLVAM HTACLSGNKT AVFPLGAEEI HLVAMTSKRN LPNHACFWGY
KVPLGLYNSC LTMLNLRCLG IVFDLDETLV VANTSRSFED KIDAVQRKLS NETDPQRISG
MLAEIKRYQD DKSILKQYIE SDQVIDGGEV YKAQSEVIPP LADNHQQPMT RPIIRLQEKH
IILTRINPSI RDTSVLVRLR PAWDDLRNYL IARGRKRFEV YVCTMAERDY ALEMWRLLDP
DSKLINSVQL LDRLVCVKSG SRKSLLNVFH DGSCHPRMAL VIDDRLKVWN EKDQHRVHVV
PAFAPYYAPQ AEANFPIPVL CVARNVACNV RGGFFKEFDE GILPQISEVR YEDEMDGIPS
APDVSNYLIS EDENSAIINI NKDPHAIDGM ADAEVEKRMK EASSCFQATN PITTDIDVMS
VAAKQHFVTP TSSSTPIAAP PGIIMPLNNE HLPQPPSFSW PVTLSGLVDP SQGSPAREEG
EVPESELDPD TRRRLLILQH GQDTREAAQP FPDRPPAQVS VPPVQSHGNW LSLEDEMNPR
NLNKASTEFH LESDSVNYDN KQPQHPSYFP DGDNPISADR HSYKNQRYPP RPLHNEDHRM
LHNHAPATYR SFSGIQRSRQ MESGRYFIQH GGILGVLEEI AVKCGFKVEY RSTLCDTTDL
QFSIEVWIFG EKIGEGFGKT RKEAQCQAAD TSLRNLADKF LSWDPDKMTV AKENGFNSNP
NSHRYPGSNR DDMLPAASTS DESRYTNDRI DNLRKPGGSV AALKELCKVE GYNLAFQDQP
SIDGSAGKEV CAQVSTSSG
//
