ID A0A498JK21_MALDO Unreviewed; 569 AA.
AC A0A498JK21;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=DVH24_024941 {ECO:0000313|EMBL:RXH95257.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH95257.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH95257.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH95257.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH95257.1}.
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DR EMBL; RDQH01000333; RXH95257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498JK21; -.
DR STRING; 3750.A0A498JK21; -.
DR Proteomes; UP000290289; Chromosome 7.
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:SF589; PROTEIN PHOSPHATASE 2C 57; 1.
DR Pfam; PF00481; PP2C; 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:UP000290289}.
FT DOMAIN 228..527
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 141..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 62074 MW; 8CF143BCC90F8BDF CRC64;
MNLKTVEGGG GDNTTANASA TIPFFTLSPP SPVTLSLSKI IWTKIKFSIR EFPVLNFLLI
TFTFILSTTE GAAESGKFDA FELFPEAEGG FPNAERWRRA ASVAAKKIGT KEKYPIELSL
IFLLEVQLHS LFILHNNNST STTIPPSSEL TRPNSPTQLS TSSATTAGDK MTLTSPQLQR
FVLTKYHGGL YKTAAAKSSF NIRARSRSCS AIAIDTPGSS LTDVAGIRWG STSLQGAREE
MEDAVVVRSE GLDEFSFAAV FDGHAGFNSV KFLRDELYKE CCAALQGGLL LRGNDFKAIR
EALLETFEKV DSKLLNWLES NGEKDESGST ATLMFVGNDT LVISHVGDSC VVQSCSGKAE
VLTHPHRPYG SNKASLQEIK RIREEGGWIS NGRICGDIAV SRAFGDMRFK TKKNEVQFNG
DLVTASPDVF QVTFGTDSEF VLLASDGLWD YINRSVGLNT LSKRMPCFLM KLIAHVKFGH
SFSSDAVTFV RNQLRKHGDV QLACDALAEA ALDQRSQDNI SIVIADLGRT DWQGLPFQQQ
NVVYEFGQAF ATVGIVSLGI WISTSLLST
//
