ID A0A1U8A8R4_NELNU Unreviewed; 1015 AA.
AC A0A1U8A8R4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LOC104601422 {ECO:0000313|RefSeq:XP_010263036.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010263036.1};
RN [1] {ECO:0000313|RefSeq:XP_010263036.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_010263036.1; XM_010264734.2.
DR AlphaFoldDB; A0A1U8A8R4; -.
DR STRING; 4432.A0A1U8A8R4; -.
DR GeneID; 104601422; -.
DR KEGG; nnu:104601422; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; A0A1U8A8R4; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000189703; Unplaced.
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; IPR006652; Kelch_1.
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:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF01344; Kelch_1; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT DOMAIN 781..786
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 108384 MW; 71DDD053EF5C2D4C CRC64;
MEVDSSMMPE SDQDHGQNHD PGAISSMDSS RHGEQLGGGE QSASSVTPTS QPQQAQVQQP
QAQPQQQPPQ VQQAPVAGPR PAPTYSVVEA NIEKKEDGPG PRCGHTLTAV AAVGEEGTAG
YIGPRLILFG GATALEGNSA ASGPPSSAGS AGIRLAGATA DVHCYDVNSN KWSRLTPLGE
PPSPRAAHVA TAVGTMVVIQ GGIGPAGLSA EDLHVLDLTQ QRPRWHRVVV QGPGPGPRYG
HVMALVGQRF LLAIGGNDGK RPLADVWALD TAAKPYEWRK LEPEGEGPPP CMYATASARS
DGLLLLCGGR DANSVPLAQA YGLAKHRDGR WEWAIAPGVS PSPRYQHAAV FVNARLHVSG
GALGGGRMVE DSSSVAVLDT AAGVWCDTKS VVTSPRTGRY SADAAGGDAA VELTRRCRHA
AAAVGDLIYI YGGLRGGVLL DDLLVAEDLA AAETTSAASH AAAAAAATNI QAGRLPGRYF
DDRTRQTIPE AVPDGAVVLG SPVAPPANGD MYTDLSTENA MLQGPRRLSK DVDYLVKASA
AEAEAISAAL AAAKARQVNG EVEQMPERDR GAEATPSGKQ ISTLIKTPDS SLSNNNPPGV
RLHHRAVVVA AETGGALGGM VRQLSIDQFE NEGRRVSYGT PESATAARKL LDRQMSINSV
PKKVIEHLLK PRGWKPPVRR QFFLDCNEIA DLCDSAERIF ANEPSVLQIK APVKIFGDLH
GQFGDLMRLF DEYGAPSTAG DIAYIDYLFL GDYVDRGQHS LETITLLLAL KVEHPHQVHL
IRGNHEAADI NALFGFRIEC IERMGERDGI WAWHRINRLF NWLPLAALIE KKIICMHGGI
GRSINHIEQI ENLQRPITME TGSVVLMDLL WSDPTENDSV EGLRPNARGP GLVTFGPDRV
MEFCNNNDLQ LIVRAHECVM DGFERFAQGH LITLFSATNY CGTANNAGAI LVLGRDLVVV
PKLIHPLPPA VASPQTSPEH HIEDTWMQEL NANRPPTPTR GRPQVANDRG SLAWI
//
