ID A0A453SJU2_AEGTS Unreviewed; 1077 AA.
AC A0A453SJU2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:AET7Gv20964800.8, 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:AET7Gv20964800.8}
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};
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DR AlphaFoldDB; A0A453SJU2; -.
DR STRING; 200361.A0A453SJU2; -.
DR EnsemblPlants; AET7Gv20964800.8; AET7Gv20964800.8; AET7Gv20964800.
DR Gramene; AET7Gv20964800.8; AET7Gv20964800.8; AET7Gv20964800.
DR Proteomes; UP000015105; Chromosome 7D.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF26; PROTEIN PHOSPHATASE 2C 50-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..1077
FT /note="protein-serine/threonine phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019078290"
FT DOMAIN 84..442
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 617..1073
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 122401 MW; 4D0A751A3270022C CRC64;
LPLFCSGDSP MSLPPSGHRT ILLLILIELL SPLLCTGESA TCLAVYREGG APAVYQSAHC
PRWTILSAGE GDGDKGPSSP QPRRCHVAAH RGRRRSQEDR AVCALGIRIP FIEQMRIKEV
DVGVMAIFDG HNGDEASEMA SKLLLEYLLL HVYFLLDGIY SIMFRNSTGK LTHKEVTILN
SVLNLYKEDQ SNHGQRSCWI SPTILDRSFH MEILKESLLR AVQDIDLTFS KEALRKKFKS
GSTATVVLIA DGQIITANVG DSKAFLCSQS HASYRQKRKR RRKRNSSNHE DFALANYGGP
LYNVKELTRD HHPDREDERR RVEAAGGYVL EWAGVYRVNG ELALSRAIGD VPFKRYGVIS
TPELTGWQLL SANDSFLIAS SDGVFEKMSM QDVCDMMLYA KYGVNQDFEP LAVVQQNLAD
FIVHLALQKG TTDNVAAVIV PLGSPSSSGA RIEDWHHLEE NSVTSVLPLQ TIPYQHKSDD
GVSSAVIEME YFKRSSTKFQ RFLVDAKLKR LGCFYLSESL DEDMDFIFRV PKDYQHEGVH
DFNHMPTENV LSSDGNLEKY KDRNFCWHLV HQDDEMGRCT SPEGFANYFG LLDSVSHNGS
RSSSSHAFGY KIADIRYKLK RRFDRGSYGE VWLAFRWNCS DDVDVHKDPS HFNTILTPDS
YNCTSSNTTS SSDENHGSDM IDGDLFILKR IMVERGNAAY LSGLREKHFG ELFSNASKTL
EILSRMESSS ATFPMDMQFI EYSFPEQNIS AVEESLKHVA RFIESFESES REIWLVYRNE
GRSLSKLLYA AEDTKLVTGD DNERVRYIQV LQPSKWWYWL RTTKAGQRQM QNLLWQLLMG
LKACHDRNIT HRDIKPENMI ICFEDLKTGK CLREIPSEAT ENKLNLRLID FGSAIDDFTL
KHLYGSGPTR SEQTFEYTPP EALLNSSWFQ GSKSARLKYD IWSVGVVMLE LIVGSPHVFQ
ISDRARILMD QRLEGWSEET KELAYKLRSY MELCILVPGI STQQQGSINS ERGHGGLASW
KCSEESFARQ VKILDPLKMG FPNLWALRLA RQLLVWHHED RLSIDEALNH PYFQEPP
//
