ID A0A453CG05_AEGTS Unreviewed; 883 AA.
AC A0A453CG05;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20835000.19, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20835000.19}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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 AlphaFoldDB; A0A453CG05; -.
DR EnsemblPlants; AET2Gv20835000.19; AET2Gv20835000.19; AET2Gv20835000.
DR Gramene; AET2Gv20835000.19; AET2Gv20835000.19; AET2Gv20835000.
DR Proteomes; UP000015105; Chromosome 2D.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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; IEA:InterPro.
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; 2.
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:UP000015105};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 139..390
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 693..759
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 503..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 98393 MW; B15AC6AB2C71F146 CRC64;
MIKSMVYFGH ISIGEVELWP KGETNVAAAP WVREIRVDRL SPPSERCLPL AVLHTVSSGA
LCFVMESRPS PATADDEPPS SLVAMHTACL RDNKTAVFPL GAEEIHLVAM KPKSNLPNHA
CFWGYKVPLG LYNSCLSMLN LRCLGIVFDL DETLIVANTT RSFEDRIDAL QRKLSKETDP
QRISGMLAEI KRYQEDRTML KQYIDGDQVI DGGKMYKVQS EVVPPLADNH QPMIRPVIRL
QEKSIILTRI NPSIRDTSVL VRLRPAWDDL RSYLIARGRK RFEVYVCTMA ERDYALEMWR
LLDPDSRLIN SVQLPHRLVC VKSGFKKSLL NVFHDGSCHP GMALVIDDRL KVWEEKDQCR
VHVVPAFSPY YAPQAEANFP IPVLCVARNV ACNVRGSFFK EFDEGLLPSI SEVHFDDELD
HVPSSPDVGN YLISEDENAA SLNVNKDPMA FDGMADAEVE RRMKEAVCSV QAADPVTTNV
DVISAAANQQ FATSSSIPLA PPLGMVPLNN DQGPQPPSVS WSDAQSGMVD PLQGSPAREE
GEVPESELDP DTRRRLLILQ HGQDTRDPTP PFAAEPSVQA SVPPVQSQGN WFPVEDEMDP
RNLNRTSTDF HVESDAVHSD KSQPPHQPYF PARDNPVFSD RFNHQNQRYS SQLPHSEDRQ
MLQNQAPTTY RSFSGNRSSQ MESGRQFVQY TETSGAVLEE IAAKCGFKVE YRSTLCDTTE
LRFSIQIWIV GEKVGEGMGR TRKEAQRQAA NISLRNLADK FLSFDPDKMT VPMDDGFSSN
PNSFKYTGID GDNIVPVAST SDGSRYMHER VDNSTKSAGS VAALKELCTA EGYNLVFQAQ
PSPLDSLTRK EVHAQIEIGG QILGKGVGVT WEEAKVQVAT IRF
//
