ID A0A2G5EEV7_AQUCA Unreviewed; 989 AA.
AC A0A2G5EEV7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=AQUCO_00900678v1 {ECO:0000313|EMBL:PIA54296.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA54296.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA54296.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; KZ305026; PIA54296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5EEV7; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
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:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13415; Kelch_3; 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; 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:UP000230069}.
FT DOMAIN 755..760
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 105361 MW; 13BFEB7479C740FE CRC64;
MEVDSSMMGP ETTTTINHQQ DQRGHQNHEV SSTPSISISS DELEQSNSST PSTSPTSVQQ
NNNNNNQLQQ QQAVGSGSAV VVAGPRPAPT YSIVNAVIEK KEDGPGPRCG HTLTAVAAVG
EEGTPGYIGP RLILFGGATA LEGNSAAAGP PSPAGSAGIR LAGATADVHC YDVLSNKWSR
LTPLGEQPSP RAAHVATAVG TMVVIQGGIG PAGLSAEDLH VLDLTQQRPR WHRVVVQGPG
PGPRYGHVMA LVGQRFLLAI GGNDGKRPLA DVWALDTAAK PYEWRKLEPE GDGPPPCMYA
TASARSDGLL LLCGGRDANS VVFVNARLHV SGGALGGGRM VEDSSSIAVL DTAAGVWCDT
KSVVTSPRTG RYSADAAGGD AAVELTRRCR HAAAAIGDLI FIYGGLRGGV LLDDLLVAED
LAAAETTSAA SQAAAVAASN NVQAGRLQGR YGFADDRTRQ TATDAVSDGA VVLGSPVAPP
VNGDMYTDIS TENAVLQGPR RLSKGVEYLV EAAAAEAEAI NATLAAAKAR QVNGDVEQLP
DRDRGAEATP SGKQISTLKT PDSAFSSITP PPGVRLHHRA VVVAAETGGA LGGMVRQLSI
DQFENEGRRV SYGTPESATA ARKLLDRQMS INSVPKKVIA HLLKPRGWKP PVRRQFFLDC
NEIADLCDST ERIFASEPSV LQIKAPVKIF GDLHGQFGDL MRLFDEYGSP STAGDIAYID
YLFLGDYVDR GQHSLETITL LLALKVEYPH NVHLIRGNHE AADINALFGF RIECIERMGE
RDGIWAWHRI NRLFNWLPLA ALIEKKIICM HGGIGRSINH VEQIESLQRP ITMEAGSVVL
MDLLWSDPTE NDSVEGLRPN ARGPGLVTFG PDRVMEFCNN NDLQLIVRAH ECVMDGFERF
AQGHLITLFS ATNYCGTANN AGAILVLGRD LVVVPKLIHP LPPAITSPEA SPERHIEDTW
MQELNANRPP TPTRGRPQVT NDRGSLAWI
//
