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
//