ID   UBCP_ARATH              Reviewed;         340 AA.
AC   Q8W3M6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ubiquitin-like domain-containing CTD phosphatase;
DE            EC=3.1.3.16;
DE   AltName: Full=Nuclear proteasome inhibitor UBLCP1;
GN   OrderedLocusNames=At4g06599; ORFNames=T11G11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11853315; DOI=10.1093/dnares/8.6.285;
RA   Kumekawa N., Hosouchi T., Tsuruoka H., Kotani H.;
RT   "The size and sequence organization of the centromeric region of
RT   Arabidopsis thaliana chromosome 4.";
RL   DNA Res. 8:285-290(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing
CC       their proteolytic activity. The dephosphorylation may prevent assembly
CC       of the core and regulatory particles (CP and RP) into mature 26S
CC       proteasome (By similarity). {ECO:0000250}.
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC       nuclear proteasomes. {ECO:0000250}.
CC   -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC       proteasomes. {ECO:0000250}.
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DR   EMBL; AB073160; BAB83612.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82552.1; -; Genomic_DNA.
DR   RefSeq; NP_849320.1; NM_178989.3.
DR   AlphaFoldDB; Q8W3M6; -.
DR   SMR; Q8W3M6; -.
DR   STRING; 3702.AT4G06599.1; -.
DR   PaxDb; Q8W3M6; -.
DR   PRIDE; Q8W3M6; -.
DR   ProteomicsDB; 228626; -.
DR   EnsemblPlants; AT4G06599.1; AT4G06599.1; AT4G06599.
DR   GeneID; 826068; -.
DR   Gramene; AT4G06599.1; AT4G06599.1; AT4G06599.
DR   KEGG; ath:AT4G06599; -.
DR   Araport; AT4G06599; -.
DR   TAIR; locus:1005716300; AT4G06599.
DR   eggNOG; KOG1605; Eukaryota.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_046931_1_0_1; -.
DR   InParanoid; Q8W3M6; -.
DR   OMA; DSNAMIS; -.
DR   OrthoDB; 1376145at2759; -.
DR   PhylomeDB; Q8W3M6; -.
DR   PRO; PR:Q8W3M6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8W3M6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1000; -; 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   Pfam; PF03031; NIF; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02245; HAD_IIID1; 1.
DR   PROSITE; PS50969; FCP1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Ubiquitin-like domain-containing CTD phosphatase"
FT                   /id="PRO_0000305941"
FT   DOMAIN          24..101
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          151..312
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          151..312
FT                   /note="Phosphatase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38956 MW;  1B9D23EF3E424382 CRC64;
     MASSSSSPTP SAAAAVSPLT EEELTLTVKW NGKEYTVRIC ADDSVAELKR RICLLTTVLP
     KRQKLLYPKI GNKLSDDSLL LSSISFKPSL KMTMIGTVED DIIVDQAESP EIVDDFELGK
     EEAVDVKDKE VNKQKLRRRI DQYKINLRTP CRQGKKLLVL DIDYTLFDHR STAENPLQLM
     RPYLHEFLTA AYAEYDIMIW SATSMKWVEL KMTELGVLNN PNYKVTALLD HLAMITVQSD
     TRGIFDCKPL GLIWALLPEF YNPGNTIMFD DLRRNFVMNP QNGLTIKPFR KAHANRDTDQ
     ELVKLTQYLL TIAELSDLSS LHHSRWESFS QDNVKRRRQE