ID A0A0Q3E762_BRADI Unreviewed; 937 AA.
AC A0A0Q3E762;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=100832517 {ECO:0000313|EnsemblPlants:KQJ83718};
GN ORFNames=BRADI_5g16462v3 {ECO:0000313|EMBL:KQJ83719.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ83719.1};
RN [1] {ECO:0000313|EMBL:KQJ83719.1, ECO:0000313|EnsemblPlants:KQJ83718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ83719.1,
RC ECO:0000313|EnsemblPlants:KQJ83718};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ83719.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ83719.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ83718}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ83718};
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; CM000884; KQJ83718.1; -; Genomic_DNA.
DR EMBL; CM000884; KQJ83719.1; -; Genomic_DNA.
DR EMBL; CM000884; PNT61530.1; -; Genomic_DNA.
DR RefSeq; XP_003580187.1; XM_003580139.3.
DR AlphaFoldDB; A0A0Q3E762; -.
DR STRING; 15368.A0A0Q3E762; -.
DR EnsemblPlants; KQJ83718; KQJ83718; BRADI_5g16462v3.
DR EnsemblPlants; KQJ83719; KQJ83719; BRADI_5g16462v3.
DR EnsemblPlants; PNT61530; PNT61530; BRADI_5g16462v3.
DR GeneID; 100832517; -.
DR Gramene; KQJ83718; KQJ83718; BRADI_5g16462v3.
DR Gramene; KQJ83719; KQJ83719; BRADI_5g16462v3.
DR Gramene; PNT61530; PNT61530; BRADI_5g16462v3.
DR KEGG; bdi:100832517; -.
DR InParanoid; A0A0Q3E762; -.
DR OrthoDB; 1200617at2759; -.
DR Proteomes; UP000008810; Chromosome 5.
DR ExpressionAtlas; A0A0Q3E762; baseline and differential.
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; -; 2.
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; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 135..386
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 694..760
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 820..889
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 104595 MW; 5A6DCF3CF89DA854 CRC64;
MIKSVVYFGH IPIGDVDVWP KGETNLAAAA WVREIRLDRL SPPSERCPPL AVLHTVSSRC
LVMESRLTVT ADEPPPPLVD MHTACLRDNK TAVFPLGAEE IHLVAMKDKR NLPNHVCFWA
YKLPLGLYNS CLSMLNLRCL GIVFDLDETL IVANTTRSFE DRIDALQRKL SNETDPQRIS
GMLAEIKRYQ DDRSMLKQYI ESDQVIDGGK VYKVQSEVVP PLADNPQPMI RPIIRLQEKS
IIFTRINPSI RDTSVLVRLR PAWDDLRSYL IARGRKRFEV YVCTMAERDY ALEMWRLLDP
DSRLINSVQL PDRLVCVKSG SRKSLLNVFH DGSCHPGMAL VIDDRLKVWD EKDQGRVHVV
PAFSPYYAPQ AEENFPIPVL CVARNIACNV RGGFFKEFDE GLLPWISEVH FDDELNHVPS
APDVGNYLVS EDESASILSV NKDPLAFDGM AGPEVERRLK EAGHSVQTVG PITTNVDVMS
VASNQQLVTP SSIPLAPVLG MVPLNNVQGP QYQSAIVDPL QGSPAREEGE VPESELDPDT
RRRLLILQHG QDTRDPTPPF PAEPSVEVQV SVPPVQSQGN SFFMEDWMDP RSLDRTSMGF
PLESDSVHYD KKQPPQPSYF HGGDDHLSSD RFNYQNQRYT SQLPHSEDCR MLPNQAPTTY
RSFSGEGTAT QRLHSGQRSG QLESGHQFVQ YTETSGGVLQ EIAAKCGFKV EYQSTLCDTA
ELRFSIEVWV LGEKVGEGMG RTRKEAQRQA ADISLRNLAD KFLSFDPDKM TVLKDNGFSS
NPNVFRYTGS NRDNMLTPAN TSDDSRYMNE RLDNSSKSTG SVAALKELCT AEGYNLIFHA
QPSLSDSSTG KEVHAQVEIG GQILGQGVGA TWEEAKLQAA DGALGTLKYM LGQLGQKRSG
SPRSFPSNFG KRFKPDFQRT VQRVPSGRYA RNDGRVP
//
