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Database: UniProt
Entry: A0A2K6KH31_RHIBE
LinkDB: A0A2K6KH31_RHIBE
Original site: A0A2K6KH31_RHIBE 
ID   A0A2K6KH31_RHIBE        Unreviewed;       212 AA.
AC   A0A2K6KH31;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00039357};
DE            EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
GN   Name=LHPP {ECO:0000313|Ensembl:ENSRBIP00000010587.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000010587.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000010587.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000010587.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-
CC       phosphohistidine and 6-phospholysine. Has broad substrate specificity
CC       and can also hydrolyze inorganic diphosphate, but with lower
CC       efficiency. {ECO:0000256|ARBA:ARBA00037258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000926};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00007958}.
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DR   AlphaFoldDB; A0A2K6KH31; -.
DR   Ensembl; ENSRBIT00000034218.1; ENSRBIP00000010587.1; ENSRBIG00000029121.1.
DR   GeneTree; ENSGT00940000159002; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006355; LHPP/HDHD2.
DR   NCBIfam; TIGR01458; HAD-SF-IIA-hyp3; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF44; PHOSPHOLYSINE PHOSPHOHISTIDINE INORGANIC PYROPHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180}.
SQ   SEQUENCE   212 AA;  22927 MW;  CBE8047AA2E0133C CRC64;
     MAPWAERLAG VRGVLLDISG VLYDSGAGGG TAIAGSVEAV ARLKGSRLKV RFCTNESQKS
     RAELVGQLRR LGFDISEREV TAPAPAACQI LKERGLRPYL LIHDGVRSEF DQIDTSNPNC
     VVIADAGESF SYQNMNNAFQ VLMELENPVL ISLGKGRYYK ETSGLMLDVG PYMKALEYAC
     GIKAEVVGKP SPEFFKSALQ AIGVEAHQLL SM
//
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