YY06_CAEEL
ID YY06_CAEEL Reviewed; 454 AA.
AC P48460;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative serine/threonine-protein phosphatase C27B7.6;
DE EC=3.1.3.16;
GN ORFNames=C27B7.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z54236; CAA90981.4; -; Genomic_DNA.
DR PIR; T19505; T19505.
DR RefSeq; NP_501547.3; NM_069146.4.
DR AlphaFoldDB; P48460; -.
DR SMR; P48460; -.
DR STRING; 6239.C27B7.6; -.
DR PaxDb; P48460; -.
DR EnsemblMetazoa; C27B7.6.1; C27B7.6.1; WBGene00007763.
DR GeneID; 182956; -.
DR KEGG; cel:CELE_C27B7.6; -.
DR UCSC; C27B7.6; c. elegans.
DR CTD; 182956; -.
DR WormBase; C27B7.6; CE43510; WBGene00007763; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00970000196421; -.
DR HOGENOM; CLU_004962_0_3_1; -.
DR InParanoid; P48460; -.
DR OMA; TEIHELC; -.
DR OrthoDB; 995797at2759; -.
DR PhylomeDB; P48460; -.
DR PRO; PR:P48460; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007763; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..454
FT /note="Putative serine/threonine-protein phosphatase
FT C27B7.6"
FT /id="PRO_0000058916"
FT REGION 414..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 51597 MW; 425C550C7B010E0B CRC64;
MLETEHANTE VHELCRQMIA RIEKYGTLEG FSDSDILEVL KTIKEILEPL PCLIEIIAPV
VVFGDIHGQL GDLLQFTNEV GRPPDFQYLF LGDYVDRGPN SLEVTVWLFC MKILFSKKVH
LLRGNHEVRR VNTMYGFKEE MMRKRNSHLW KVFNDVFAEL SICASINRKI LCMHGGISPK
IESWDSLTGM TKPRVHGDCE HGLIVDLIWS DPNRKDDTIQ FNKMRGISTL FGKSVVDNLC
TTLAIDLIIR AHEMKEKGHT FEFDNRLLTV FSAPYYSGHN SNLGSVATIS KSLKLRIVTL
KPNKGYDRSK LDKRTLHDFE KNFQPLDENP RKNISCQFNV PPNGQKMSPF LGEYSMFAHE
TQFCKKDNET PVKKPYSSNQ DEDHSVLDMI RKTQKGYGVE VSLKDKVMSL ESIRKKLGMT
TSTTPPPPRT PSPDAPLAQS PPIPRSPPSS TENA
