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P2C75_ORYSJ
ID   P2C75_ORYSJ             Reviewed;         432 AA.
AC   Q2R637; A0A0P0Y256; Q0IT39;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable protein phosphatase 2C 75;
DE            Short=OsPP2C75;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=Os11g0417400, LOC_Os11g22404;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; DP000010; ABA93159.2; -; Genomic_DNA.
DR   EMBL; AP008217; BAF28126.2; -; Genomic_DNA.
DR   EMBL; AP014967; BAT13771.1; -; Genomic_DNA.
DR   EMBL; AK070536; BAG92015.1; -; mRNA.
DR   RefSeq; XP_015617585.1; XM_015762099.1.
DR   RefSeq; XP_015617586.1; XM_015762100.1.
DR   RefSeq; XP_015617587.1; XM_015762101.1.
DR   RefSeq; XP_015617588.1; XM_015762102.1.
DR   RefSeq; XP_015617589.1; XM_015762103.1.
DR   RefSeq; XP_015617590.1; XM_015762104.1.
DR   RefSeq; XP_015617591.1; XM_015762105.1.
DR   RefSeq; XP_015617592.1; XM_015762106.1.
DR   RefSeq; XP_015617593.1; XM_015762107.1.
DR   RefSeq; XP_015617594.1; XM_015762108.1.
DR   RefSeq; XP_015617595.1; XM_015762109.1.
DR   RefSeq; XP_015617596.1; XM_015762110.1.
DR   RefSeq; XP_015617598.1; XM_015762112.1.
DR   RefSeq; XP_015617599.1; XM_015762113.1.
DR   RefSeq; XP_015617600.1; XM_015762114.1.
DR   AlphaFoldDB; Q2R637; -.
DR   SMR; Q2R637; -.
DR   STRING; 4530.OS11T0417400-01; -.
DR   PaxDb; Q2R637; -.
DR   PRIDE; Q2R637; -.
DR   EnsemblPlants; Os11t0417400-01; Os11t0417400-01; Os11g0417400.
DR   GeneID; 9268201; -.
DR   Gramene; Os11t0417400-01; Os11t0417400-01; Os11g0417400.
DR   KEGG; osa:9268201; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_6_0_1; -.
DR   InParanoid; Q2R637; -.
DR   OMA; ANETWRF; -.
DR   OrthoDB; 1344250at2759; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   Genevisible; Q2R637; OS.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..432
FT                   /note="Probable protein phosphatase 2C 75"
FT                   /id="PRO_0000363322"
FT   DOMAIN          44..356
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          372..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  47110 MW;  D438E3AC09386086 CRC64;
     MGTCLTTAEQ RAMEVPAASV KGGGGRRSDE EAPGRIAGNG AGNVACLFTR QGKKGTNQDA
     MVAWENYNGR SDTVFCGVFD GHGPHGHLIA RKVRDILPSR LCDLIYEDCG DSPTSNSDVS
     TLEENLSPYA DAECRSPTLA GQKEHQEFFN AMKESFRKAF KNVDKELKLQ RNIDSICSGT
     TAVTLIKQGH DLIVGNLGDS RAVLGTRDQN DKLVAHQLTV DLKPDHPREA RRIRRCNGRV
     FAHQDEPDVA RLWLPNCNSP GLAMARAFGD FCLKDFGLIS VPDVTYRQIT EKDEFIVLAT
     DGVWDVLSNQ EVVDVVASCS GRFAAARSVV DLANETWRFK YPTSKTDDCA VVCLFLNKYE
     VTGGLSGQPG YSPRMPALSG ITRPNSKRVT PDDVDDGSDS NVSGDERSLD GFTRLNTLLA
     LPKFGDTSPT KK
 
 
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