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Database: UniProt
Entry: I3MBM2_ICTTR
LinkDB: I3MBM2_ICTTR
Original site: I3MBM2_ICTTR 
ID   I3MBM2_ICTTR            Unreviewed;       238 AA.
AC   I3MBM2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=CTDSP1 {ECO:0000313|Ensembl:ENSSTOP00000007557.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000007557.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000007557.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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};
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DR   EMBL; AGTP01062674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MBM2; -.
DR   STRING; 43179.ENSSTOP00000007557; -.
DR   Ensembl; ENSSTOT00000008432.3; ENSSTOP00000007557.3; ENSSTOG00000008434.3.
DR   eggNOG; KOG1605; Eukaryota.
DR   GeneTree; ENSGT01040000240451; -.
DR   HOGENOM; CLU_020262_4_0_1; -.
DR   InParanoid; I3MBM2; -.
DR   TreeFam; TF313556; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:Ensembl.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF139; CARBOXY-TERMINAL DOMAIN RNA POLYMERASE II POLYPEPTIDE A SMALL PHOSPHATASE 1; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN          63..221
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   SITE            129
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT   SITE            167
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
SQ   SEQUENCE   238 AA;  26791 MW;  A9E078BB25CEF7EE CRC64;
     DQKSAASQKP RSRGILHSLF CCVCRDDGEA LPAHSGAPLL VEENGAIPKQ TPVQYLLPEA
     KAQDSDKICV VIDLDETLVH SSFKPVNNAD FIIPVEIDGV VHQVYVLKRP HVDEFLQRMG
     ELFECVLFTA SLAKYADPVA DLLDKWGAFR ARLFRESCVF HRGNYVKDLS RLGRDLRRVL
     ILDNSPASYV FHPDNAVPVA SWFDNMSDTE LHDLLPFFEQ LSRVDDVYSV LRQPRPGS
//
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