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Database: UniProt
Entry: A0A0E0G9N3_ORYNI
LinkDB: A0A0E0G9N3_ORYNI
Original site: A0A0E0G9N3_ORYNI 
ID   A0A0E0G9N3_ORYNI        Unreviewed;      1075 AA.
AC   A0A0E0G9N3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA02G26350.2};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA02G26350.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G26350.2};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA02G26350.2}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G26350.2};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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|ARBA:ARBA00001512};
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|ARBA:ARBA00001482};
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   AlphaFoldDB; A0A0E0G9N3; -.
DR   STRING; 4536.A0A0E0G9N3; -.
DR   EnsemblPlants; ONIVA02G26350.2; ONIVA02G26350.2; ONIVA02G26350.
DR   Gramene; ONIVA02G26350.2; ONIVA02G26350.2; ONIVA02G26350.
DR   eggNOG; KOG0654; Eukaryota.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_287070_0_0_1; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 3.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   InterPro; IPR015655; PP2C.
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:SF285; PROTEIN PHOSPHATASE 2C 22-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 2.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00385; CYCLIN; 3.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 4.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591}.
FT   DOMAIN          1..287
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          307..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..404
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..453
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  116372 MW;  064E9B6A760E1CA6 CRC64;
     MERIRELIEL DLDALRNTSF FGVYDGDGGA EVAMYCAKRF HAMLCEDENY LNNLPNAITS
     VCSRLDDDLQ RSNEWKESLY PRGNGECFQF LKTGVCANLW HSEELGFMLP QQAYRAPLYE
     GSTACVVIIR GNQITVGNVG DSRCVVSHNG QAIDLSIDHK PTVGSERERI LRAGGRVLVK
     RIPVMGSDGR LMRGWGYFEL KKNQNIPASQ QMVTCDPEFT IVDITADTEF LVIATDGIWG
     HMSSQDVVDF IRKELHSGEE NLRAICEKLL DHCLTSRDNV TVILVRFKPG AAVIPILSDI
     DEEPVLSDVE EEPHEPQQNP GDGGGGGGGQ QDIGGESEEL PLAHFPQEYS NSSAPLPMFD
     SFSGGGTPPI DTDTFLRAIG ALPPLAPPPE APLAPAPPDS PHQTALPLFH PFSGGATPQM
     VDTDTFLRAI GALPPLAPPP AAPLAPAPPD SPRTPHTYGS LLPVYGDLPP LTGAVVQEPL
     PLPEGGDHPE PPKKKIKVAP LLPERADQPV VTSNSATTTR PQLCAPYDDE IEATLRAMET
     NPAERPSPYF LETTQGGRMT ALVRASMIAF MDEFSQFHEL ADGTLQRAAY FLDRYLSVTP
     ESDDALQLRL VGATAVFLAA KYEDQYTLRK IDASMVAARC GYTSETRHKM VSIMETEMLA
     ALGFNLGGPT AYTFVEHFTR YYGDGKKEKL LKEAAHRFAD GSLLTYGFHR YLPSVVAASA
     IFLARLDVLG HEPWSQDLAE LTGYKAIDLM GCPYVADLLA DDITASMVEL LSGDGGAAQM
     DVGVLDAYLR AIGALPAHPA APGADLAAAA EVESMASNYD TNGVLYDWDT KVDVKVPCAL
     LPPPPGFPPL PVPGLADEPV YAAPARRLPP PPGFPPLPVP AKAEPVYAAP VDEGDAIRAF
     MQQLEWSEQY NGDNDAPAPD NSTASRPQLC APYDDDIDAN LRDMEKDAAQ RPSPDYLDTV
     QGGQISAAAR ASLVAWMGRL THRYELAAGT LHRAVSYFDR FLSVRALPCH VADRSLESYG
     CLGYLPSVVA AAVISIARWT LNPPGALPWS SELHELTGYS SQHISSCVLT VLNTQ
//
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