ID A0A1D6MVF8_MAIZE Unreviewed; 998 AA.
AC A0A1D6MVF8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
GN Name=103650267 {ECO:0000313|EnsemblPlants:Zm00001eb134690_P001};
GN ORFNames=ZEAMMB73_Zm00001d041307 {ECO:0000313|EMBL:ONM32800.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM32800.1};
RN [1] {ECO:0000313|EMBL:ONM32800.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb134690_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM32800.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb134690_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb134690_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) 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 ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR036363};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR036363};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036363}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671, ECO:0000256|PIRNR:PIRNR036363}.
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DR EMBL; CM007649; ONM32800.1; -; Genomic_DNA.
DR RefSeq; XP_008674098.1; XM_008675876.1.
DR AlphaFoldDB; A0A1D6MVF8; -.
DR SMR; A0A1D6MVF8; -.
DR IntAct; A0A1D6MVF8; 5.
DR STRING; 4577.A0A1D6MVF8; -.
DR PaxDb; 4577-GRMZM2G009593_P01; -.
DR EnsemblPlants; Zm00001eb134690_T001; Zm00001eb134690_P001; Zm00001eb134690.
DR GeneID; 103650267; -.
DR Gramene; Zm00001eb134690_T001; Zm00001eb134690_P001; Zm00001eb134690.
DR KEGG; zma:103650267; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; A0A1D6MVF8; -.
DR OMA; HDEAQSP; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000007305; Chromosome 3.
DR ExpressionAtlas; A0A1D6MVF8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011498; Kelch_2.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041758; MPP_BSL_C.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF13; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL2 HOMOLOG; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036363};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR036363};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR036363};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036363};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR036363};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6MVF8};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 763..768
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 105693 MW; 97A87EB69A299F7E CRC64;
MDVDSRMATE SDSDSDARGG GSGSGSETPT ASASASASPS TSAPAPGTPT AAAASPGLVA
GPRPAPGYTV VDAAMDKKED GPGCRCGHTL TAVPAVGEEG SPGYVGPRLI LFGGATALEG
NSATPPSPAG SAGIRLAGAT ADVHCYDVLS NKWTRLTPLG EPPSPRAAHV ATAVGTMVVI
QGGIGPAGLS AEDLHVLDLT QQRPRWHRVV VQGPGPGPRY GHVMALVGQR FLLTIGGNDG
KRPLADVWAL DTAAKPYEWR KLEPEGEGPP PCMYATASAR SDGLLLLCGG RDANSVPLSS
AYGLAKHRDG RWEWAMAPGV SPSPRYQHAA VFVNARLHVS GGALGGGRMV EDSSSVAVLD
TAAGVWCDTK SVVTTPRTGR YSADAAGGDA SVELTRRCRH AAAAVGDLIF VYGGLRGGVL
LDDLLVAEDL AAAETTSAAN HAAAAAASTN GQREPGRYAY NDEQSGQTVT VSSPDGAVVL
GTPVAPPVNG DMYTDISPEN AIIQGQRKMS KGVDYLVEAS AAEAEAISAT LAAVKARQVN
GEMEHSPDRE QSPDAAPSTK QNSSLIKPDV ALVNNSTAPP GVRLHHRAVV VAAETGGALG
GMVRQLSIDQ FENEGRRVIY GTPENATAAR KLLDRQMSIN SVPKKVIASL LKPRGWKPPV
RRQFFLDCNE IADLCDSAER IFSSEPSVLQ LKAPIKIFGD LHGQFGDLMR LFDEYGAPST
AGDIAYIDYL FLGDYVDRGQ HSLETISLLL ALKVEYPHNV HLIRGNHEAA DINALFGFRI
ECIERMGERD GIWTWHRVNR LFNWLPLAAL IEKKIICMHG GIGRSINHIE QIENLQRPIT
MEAGSVVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD RVMEFCNNND LQLIVRAHEC
VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV VVPKLIHPLP PAITSPETSP
EHHIEDTWMQ ELNANRPPTP TRGRPQAPNN DRGSLAWI
//
