ID G0N9D2_CAEBE Unreviewed; 274 AA.
AC G0N9D2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=Cbn-scpl-2 {ECO:0000313|EMBL:EGT55705.1};
GN ORFNames=CAEBREN_00716 {ECO:0000313|EMBL:EGT55705.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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 -!- SIMILARITY: Belongs to the dullard family.
CC {ECO:0000256|ARBA:ARBA00038346}.
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DR EMBL; GL379852; EGT55705.1; -; Genomic_DNA.
DR AlphaFoldDB; G0N9D2; -.
DR STRING; 135651.G0N9D2; -.
DR EnsemblMetazoa; CBN00716.1; CBN00716.1; WBGene00139441.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; G0N9D2; -.
DR OMA; RIWGFFM; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblMetazoa.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0031468; P:nuclear membrane reassembly; IEA:EnsemblMetazoa.
DR GO; GO:0051783; P:regulation of nuclear division; IEA:EnsemblMetazoa.
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 NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..248
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 274 AA; 31539 MW; 8218C1C3DAE418F4 CRC64;
MYDPNRTFAG GAQDRRRDQK NSNWIARGMT SITQSLFGII LACFNFIILY FRKANRAYCK
YQVVKYHSKI PMSPLTTHRL LAVKRKILVL DLDETLIHSH HDGVLRQTVK PGTPSDFTIR
VVIDRHPVKF SVHERPHVDY FLSVVSQWYE LVVFTASMEV YGTSVADKLD RGRGILKRRY
FRQHCTMEVG GYTKDLSAIH PDLSSICILD NSPGAYRKFP QNAIPIPSWF SDPNDTALLN
LLPFLDALRF TADVRSVLSR NTMVLPEPQQ VQYY
//
