ID A0A0D3A7E2_BRAOL Unreviewed; 851 AA.
AC A0A0D3A7E2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE AltName: Full=Nuclear proteasome inhibitor UBLCP1 {ECO:0000256|ARBA:ARBA00032039};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g052910.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g052910.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g052910.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A0D3A7E2; -.
DR EnsemblPlants; Bo1g052910.1; Bo1g052910.1; Bo1g052910.
DR Gramene; Bo1g052910.1; Bo1g052910.1; Bo1g052910.
DR eggNOG; KOG1605; Eukaryota.
DR eggNOG; KOG1872; Eukaryota.
DR HOGENOM; CLU_335368_0_0_1; -.
DR OMA; YNEERSY; -.
DR Proteomes; UP000032141; Chromosome C1.
DR ExpressionAtlas; A0A0D3A7E2; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd01813; Ubl_UBLCP1; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR011943; HAD-SF_hydro_IIID.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR008545; Web.
DR NCBIfam; TIGR02245; HAD_IIID1; 1.
DR PANTHER; PTHR48405; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1.
DR PANTHER; PTHR48405:SF1; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF05701; WEMBL; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 21..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 148..309
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT COILED 420..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 528..706
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 851 AA; 98052 MW; 7E7DA22416ACF005 CRC64;
MASSSSSSPT PDAVTAMDEE LTLIVKWSGK EYTLRICADD SVAELKRRIC FLTNVLPKRQ
KLLYPKVGNK LSDDSLLLSQ IPLKPSLKMT MIGTTEDDII VDQVTSDDVV DDFELGKEEV
VDIEDKEINK QKLRRRIDQY KIKLVNPCRK GKKLLVLDID YTLFDHRSTA ENPLQLMRPY
LHEFLTAAYA EYDIIIWSAT SMKWVELKMG ELGVLNNPNY KITALLDHLA MITVQSDTRG
IFDCKPLGLI WALLPELYNA QNTIMFDDLR RNFVMNPQNG LKIRPFRKAH VNRDKDDELV
LLTRYLLTIA ELDDLSSLDH SRWETFTEDS MIRADAPVMP LETPPRSSEV GEIDTHPPFQ
SVRAAVSLFR QVSFSKQQPP SLSSSSQDST DVPDKETQLL LAEQEMNRVH LCRDSSVNAK
ARALSDLDSA QRKAADLRDK LETTKQSRKC AIQTKHTMNQ RLEKLQSQSQ ETESVRESYI
LATAELFMAK EKLTEIGQEF SISVEERLSE LQRAEEAECS SMVNSQKIND MLKEIAEMRD
TAERLNSDAD KKKEEEAKIN EKSIDAKETY ADMKREAEKR LEDLRQDCDP ELRKEIDELA
EISAENESLQ REIKLSRDLK EAKSAMQEIY NEERSYKSLV ISLTVELDGM QRENRDLKEK
EKDREEVEEG EWVEERLKVE ETMRVAERTR QEAEETRMHV DELRREAAAT HTVMGEAAKQ
LEIVRRAVKK AKTAEKRAVE DMTVLTEKKE SLTHDDPDKK IRISLKEHEE LRGKHEESER
MVQYKAETVD AQLEEINESR VEGESMLEEK MKEMEQVKEA TDTALRSAEI AEEAHCIVDA
ELRKWKPEEL Q
//
