ID D7LK41_ARALL Unreviewed; 355 AA.
AC D7LK41;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=ARALYDRAFT_344104 {ECO:0000313|EMBL:EFH56908.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; GL348716; EFH56908.1; -; Genomic_DNA.
DR RefSeq; XP_002880649.1; XM_002880603.1.
DR AlphaFoldDB; D7LK41; -.
DR STRING; 81972.D7LK41; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_4000446; fgenesh1_pg.C_scaffold_4000446; fgenesh1_pg.C_scaffold_4000446.
DR GeneID; 9314891; -.
DR Gramene; fgenesh1_pg.C_scaffold_4000446; fgenesh1_pg.C_scaffold_4000446; fgenesh1_pg.C_scaffold_4000446.
DR KEGG; aly:9314891; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_4_1_1; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000222; PP2C_BS.
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:SF631; PROTEIN PHOSPHATASE 2C 21-RELATED; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 23..329
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 330..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 39341 MW; A677C357E957D072 CRC64;
MGTYLSSPKT DKLSEDGEND KLRYGLSSMQ GWRATMEDAH AAILDLDDKT SFFGVYDGHG
GKVVAKFCAK YLHQQVISNE AYKAGDIETA LRRAFFRMDD MMQGQRGWRE LAVLGDKMNK
FSGMIEGFIW SPRSGDTNNQ PDNWPLEDGP HSDFTGPTSG CTACVALIKD KKLFVANAGD
SRCVISRNSQ AYNLSKDHKP DLEVEKERIL KAGGFIHAGR INGSLNLTRA IGDMEFKQNK
FLPSEKQMVT ADPDINTIDL CDDDDFLVVA CDGIWDCMSS QELVDFIHEQ LKSETKLSSV
CEKVVDKCLA PDTTSGEGCD NMTIILVQFK KLNPSETEPE ESKPEPSEDE PSSSS
//
