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Database: UniProt
Entry: A0A1Y1HVG9_KLENI
LinkDB: A0A1Y1HVG9_KLENI
Original site: A0A1Y1HVG9_KLENI 
ID   A0A1Y1HVG9_KLENI        Unreviewed;       502 AA.
AC   A0A1Y1HVG9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN   ORFNames=KFL_001180090 {ECO:0000313|EMBL:GAQ82630.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ82630.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ82630.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ82630.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
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}.
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DR   EMBL; DF237067; GAQ82630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1HVG9; -.
DR   STRING; 105231.A0A1Y1HVG9; -.
DR   OrthoDB; 11009at2759; -.
DR   Proteomes; UP000054558; 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   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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; PF07228; SpoIIE; 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:UP000054558}.
FT   DOMAIN          268..501
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          203..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  52770 MW;  A685B96E6D0D8189 CRC64;
     MQSAAALALG REYVLLRHSR CGPSGSPLKA PEGSLSLWPC SRRGGAALHV PSAETCPGVC
     LAAARRHCHL PDLHGQSRQT AGPGCQARRS LQQTAQVCIG RRGRAHIERL QARELGTGRQ
     GPSASTSAVA ALAQEGRSKS EGATEEAVHQ LEDHVVESRP LEENETGPVI IRVRECADGS
     FIFDFGDAAE RPEQDPLDAF VRGAPSAEEA PPESIAASTE LQASQGVDEA EEDLPVEADA
     AQSSLTASSE GGSVVESSGP SLRLNSGGSS LPHPAKVEKG GEDAFFCTEN GKSSYVGVSD
     GVGGWATLGI NAGLYSRELM YHCQRLAGDD ILPRSMLIRA HKMTKATGSA TAMVARLRGN
     RLRVANLGDS GFLLVRDGQV ALASTQMQHA FNFPFQIGSK GGDDPDAAKD YEVEVERGDL
     LILGTDGLHD NLFEREIAEA AAILKSKGVS PQLASQQIAA FAQQRSVLKG GLSPFAVQAD
     AAGYKHLGGK PDDITVVVAY IE
//
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