ID T1EDB2_HELRO Unreviewed; 286 AA.
AC T1EDB2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00039357};
DE EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
GN Name=20194564 {ECO:0000313|EnsemblMetazoa:HelroP102728};
GN ORFNames=HELRODRAFT_102728 {ECO:0000313|EMBL:ESN95134.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP102728, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN95134.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP102728}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; AMQM01006931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097542; ESN95134.1; -; Genomic_DNA.
DR RefSeq; XP_009026782.1; XM_009028534.1.
DR AlphaFoldDB; T1EDB2; -.
DR STRING; 6412.T1EDB2; -.
DR EnsemblMetazoa; HelroT102728; HelroP102728; HelroG102728.
DR GeneID; 20194564; -.
DR KEGG; hro:HELRODRAFT_102728; -.
DR CTD; 20194564; -.
DR eggNOG; KOG3040; Eukaryota.
DR HOGENOM; CLU_043473_4_1_1; -.
DR InParanoid; T1EDB2; -.
DR OMA; GPCIDVG; -.
DR OrthoDB; 2876640at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006355; LHPP/HDHD2.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
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 Pfam; PF13242; Hydrolase_like; 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:UP000015101}.
SQ SEQUENCE 286 AA; 31504 MW; 81849AF2CC8BB834 CRC64;
MTSRGGSCND GASSNSNVSN STNWTKGVKG FLLDVYGVAY NCGQTFSLID GSVEAVSKLR
KAGIPFRFCS NTSTKTPEKV LERLLEFGFD VKPGEIFTPI PVVKNYLRKH GYRPFILVDP
CVDQEFAEFD QSDPNCVVLG DAKHRFSYEN LNKAFQMLTD KKDSAIITLG TGKYYKETEG
MFLDCGVFAK ALEFATDKQS VCIGKPSKEF FTAAMNSMGL KPEETVMVGD DIIGDVQGAQ
QAGLKGVQVR TGKYRQLVDE PHSYVRPDAY VDNLLQAIEI YLAGKI
//
