ID A0A151R954_CAJCA Unreviewed; 1075 AA.
AC A0A151R954;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=KK1_039652 {ECO:0000313|EMBL:KYP39067.1};
OS Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP39067.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP39067.1, ECO:0000313|Proteomes:UP000075243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX PubMed=22057054; DOI=10.1038/nbt.2022;
RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT of resource-poor farmers.";
RL Nat. Biotechnol. 30:83-89(2012).
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|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671}.
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DR EMBL; KQ483941; KYP39067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151R954; -.
DR STRING; 3821.A0A151R954; -.
DR OMA; WDWVLAP; -.
DR Proteomes; UP000075243; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 2.
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|RuleBase:RU004273};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000075243}.
FT DOMAIN 842..847
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 623..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 114475 MW; 820037BC47402012 CRC64;
MDVDSSMVPE ADHDPAAQNH AERDQLGESP SSPPSGGGSP AQLPAQQQQQ PPPATAAQVQ
HSPVVGPRLA PTYSVVNAIL EKKEDGPGPR CGHTLTAVAA VGEEGTPGYI GPRLILFGGA
TALEGNSAAS GTPSSAGNAG IRLAGATADV HCYDVITNKW SRITPIGEPP TPRAAHVATA
VGTMVVIQGG IGPAGLSAED LHVLDLTQQR PRWHRVGVPG PGPGPRYGHV MALVGQRYLM
AIGGNDGKRP LADVWALDTA AKPYEWRKLE PEGEGPPPCI LICSGVNFIF NFVSFEFIFG
CEQGSCPSFK LFHAPGCLAL VKTEFFVIFN ISAMSSMLSS GLLLCCIFGL VYLYATASAR
SDGLLLLCGG RDANSVPLAS AYGLAKHRDG RWEWAIAPGV SPSPRYQHAA VFVNARLHVS
GGALGGGRMV EDSSSVAVLD TAAGVWCDTK SVVTSPRTGR YSADAAGGDA SVELTRRCRH
AAAAIGDLIF IYGGLRGGVL LDDLLVAEDL AAAETTTAAS HAAAAAASNA QAGRLPGRYG
FVDDRTRQTM PEAVPDGSVV LGNPVAPPVN GDMYTDISTE NAMLPGSRRT SKGVEYLVEA
SAAEAEAISA TLAAAKARQV NGEVELPDRD RGAEATPSGK QISSLIKPDS VGSNSIPPGG
VRLHHRAVVV AAETGGALGG MVRQLSIDQF ENEGRRVSYG TPESATAARK LLDRQMSINS
VPKKVVAHLL KPRGWKPPVR RQFFLDCNEI ADLCDSAERI FSSEPSVLKL RAPIKIFGDL
HGQFGDLMRL FDEYGAPSTA GDIAYIDYLF LGDYVDRGQH SLETITLLLA LKVEYPNNVH
LIRGNHEAAD INALFGFRIE CIERMGERDG IWAWHRINRL FNWLPLAALI EKKIICMHGG
IGRSINHVEQ IENIQRPITM EAGSIVLMDL LWSDPTENDS VEGLRPNARG PGLVTFGPDR
VMEFCNNNDL QLIVRAHECV MDGFERFAQG HLITLFSATN YCGTANNAGA ILVLGRDLVV
VPKLIHPLPP AISSPETSPD HIEDTWMQEL NANRPPTPTR GRPQVANDRG SLAWI
//
