ID A0A452XYQ3_AEGTS Unreviewed; 657 AA.
AC A0A452XYQ3;
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=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
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:AET1Gv20217900.18, 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:AET1Gv20217900.18}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A452XYQ3; -.
DR EnsemblPlants; AET1Gv20217900.18; AET1Gv20217900.18; AET1Gv20217900.
DR Gramene; AET1Gv20217900.18; AET1Gv20217900.18; AET1Gv20217900.
DR Proteomes; UP000015105; Chromosome 1D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF6; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL1-RELATED; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT DOMAIN 585..590
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 295..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 71926 MW; 4E750CC6A808EE9C CRC64;
GLAGVTNTVH SYDVDKRRWT RLHPAGDPPS PRAAHSAAAV GTMVVFQGGI GPAGHSTDDL
YVLDLTNDKF KWHRVVVQGA GPGPRYGHCM DLVAQRYLVS VSGNDGKRVL SDAWALDTAQ
KPYKWQKLNP DGDRPSARMY GTASARSDGM LLLCGGRDAS GTPLSDAYGL LMHTNGQWEW
TLAPGISPSP RYQHAAVFVG ARLHVTGGVL RGGRAIEGEG AIAVLDTAAG VWLDKNGIVT
SRTLKSSNEH DASSDLLRRC RHAAASVGSQ IYIYGGLRGD ILLDDFLIAE NAPFQSETDR
VPRSENQNRN HNFNSDSRPF EQYTNNSHET APGFSTDKKS IDMLTEASAA EAEAVSAVWR
AAKEASHASS EDSLSDGIGS ESPLSETSPM ADDLDDGGSM EPDVKLHSRA VVVAKEAVGD
LGCLVRQLSL DQFENESRRM HPANNDQSYS SKKALNRQRS PQGLHKKVIS LLLRPRNWNA
PADRTFFLDS YEVGELCYAA EQIFMQEPTV LQLKAPVKVF GDLHGQFGDL MRLFDEYGYP
STAGDITYID YLFLGDYVDR GQHSLETITL LLALKIEYPE HVHLIRGNHE AADINALFGF
RLECIERMVV TIVLHISLGI EILDALVDLI PLCRVKVMVY GLGLDSTNYL IISLWLL
//
