ID A0A1Z5SA71_SORBI Unreviewed; 516 AA.
AC A0A1Z5SA71;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SORBI_3001G421000 {ECO:0000313|EMBL:OQU92821.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU92821.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU92821.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|EMBL:OQU92821.1}
RP NUCLEOTIDE SEQUENCE.
RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F.,
RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A.,
RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N.,
RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S.,
RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K.,
RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.;
RT "WGS assembly of Sorghum bicolor.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 EMBL; CM000760; OQU92821.1; -; Genomic_DNA.
DR EMBL; CM000760; OQU92822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5SA71; -.
DR EnsemblPlants; OQU92821; OQU92821; SORBI_3001G421000.
DR EnsemblPlants; OQU92822; OQU92822; SORBI_3001G421000.
DR Gramene; OQU92821; OQU92821; SORBI_3001G421000.
DR Gramene; OQU92822; OQU92822; SORBI_3001G421000.
DR Proteomes; UP000000768; Chromosome 1.
DR ExpressionAtlas; A0A1Z5SA71; baseline.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR13832:SF349; PROTEIN PHOSPHATASE 2C 31-RELATED; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 216..516
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 55488 MW; 54B2511C158D4971 CRC64;
MGNGITKNPC FSGDPYAAAV ASDPLPDDSQ GHSFTYVPSG AAFEQPPTAA ATSSAESSFF
SLSGAAISAN PATSASMPSF QVLNEMTWPQ STACTFESSR SFAAVPLQAA PPRLSMSGPV
QSTSGRFSET SGSASTISGP PSDSPFMSGP LDLAVGLQPS VSQLIAERRA ARSRLRDERS
LLRFFVGTAS KLRLGSRRYR RRPQEPAEPI KVSFSDGDYR SPPNGNVEWA QGMAGEDRFH
VAVSEEHGWV FVGIYDGFNG PDATDYLFAN LYGVVHNELK GVLWDDIQAG DDARCGQQEA
AAGNAERLCL AEADGDSSEA KRRRTEVPVP GNNATPVHRD VLRALARALK KTEDAFFAAA
EERAAESPEL GLVGSCVLVM VMKGTDVYVM NVGDSRAVLA RRPEPDLKNV LGKASQDLQQ
FKAEIMRELE AHDMDGLQAV QLTAEHSTAV HEEVMRIKGQ HLNDRNAIVN GRVKGKINVT
RAFGVAYLKQ CYGLELRLRV TNHVVVGPTL QIIMAD
//
