ID A0A2P5CS58_PARAD Unreviewed; 608 AA.
AC A0A2P5CS58;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=PanWU01x14_128620 {ECO:0000313|EMBL:PON63885.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON63885.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU366020};
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:RU366020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU366020}.
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:PON63885.1}.
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DR EMBL; JXTB01000100; PON63885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5CS58; -.
DR STRING; 3476.A0A2P5CS58; -.
DR OrthoDB; 11009at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366020};
KW Magnesium {ECO:0000256|RuleBase:RU366020};
KW Manganese {ECO:0000256|RuleBase:RU366020};
KW Metal-binding {ECO:0000256|RuleBase:RU366020};
KW Protein phosphatase {ECO:0000256|RuleBase:RU366020};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT DOMAIN 365..603
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 113..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 65561 MW; D5CD7CF999FEA9DA CRC64;
MAEFCPYPLR PWRPLSSLFV PSRVVLSKPY HHFSYSIRTL KRRTRFRILS KLESDSSSSS
SDFGLLSAAE CPDGSFVFRF GRVGDNGTSV SGMDFDKVDE DDDAAIEGSV NENGEQLNKG
LGPDSGLEHV QSHSRRRGRS YLARVAREDS SVRNRDCNEV ESVTGAISRL SESLLEETTF
EIETTDLFSV NDDEGVIAAR NTAPQVDVVL SEEVHSHIEE NTASISENEV LNGLISSELH
SMIEVSDNCA STVSTEESAG VEVADLANDD DDCNPFEAAC VSATVPVQAS LDEETSPSAY
VGANETETSL ALGYSASSTN CEEERANKAH GTNVAGVSIS EVVEFHSIED TTRREEISTA
SLVLSTGAAS LPHPSKAFTG EEDAYFVAYQ NWLGVADGVG QWSLEGTSDG LYARELMKNC
KKIVSDCEGI PVNEPEEVLV RSVAETQSPG SSTILVAYFD GQTFHVANIG DSGFIIIRNG
AIFQRASSMV HEFNFPLHIE RGDDPSGLIE GYKIDLDEGD VIVTATDGLF DNLYGQEIAS
IVSKSVEAGS KPQDIAKFLA KRAQEVGHSS SSRSPYADEA RVAGYVGYAG GKLDNVVVIV
SLVQKKST
//
