ID A0A453CG32_AEGTS Unreviewed; 853 AA.
AC A0A453CG32;
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:AET2Gv20835000.17, 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:AET2Gv20835000.17}
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}.
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 AlphaFoldDB; A0A453CG32; -.
DR EnsemblPlants; AET2Gv20835000.17; AET2Gv20835000.17; AET2Gv20835000.
DR Gramene; AET2Gv20835000.17; AET2Gv20835000.17; 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; 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: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 704..770
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 853 AA; 95221 MW; F662BB409F8B59A7 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 RSFSGEDMAT QRFHPGNRSS QMESGRQFVQ YTETSGAVLE EIAAKCGFKV
EYRSTLCDTT ELRFSIQIWI VGEKVGEGMG RTRKEAQRQA ANISLRNLAD KFLSFDPDKM
TVPMDDGFSS NPNSFKYTGI DGDNIVPVAS TSDGSRYMHE RVDNSTKSAG SVAALKELVS
SCFNCQLLIK CAL
//
