ID B3RSV4_TRIAD Unreviewed; 326 AA.
AC B3RSV4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_22320 {ECO:0000313|EMBL:EDV27113.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV27113.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV27113.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV27113.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; DS985243; EDV27113.1; -; Genomic_DNA.
DR RefSeq; XP_002111109.1; XM_002111073.1.
DR AlphaFoldDB; B3RSV4; -.
DR EnsemblMetazoa; TriadT22320; TriadP22320; TriadG22320.
DR GeneID; 6752322; -.
DR KEGG; tad:TRIADDRAFT_22320; -.
DR CTD; 6752322; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_1_1_1; -.
DR InParanoid; B3RSV4; -.
DR OMA; CKPTAIK; -.
DR OrthoDB; 5489935at2759; -.
DR PhylomeDB; B3RSV4; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV27113.1"
SQ SEQUENCE 326 AA; 37705 MW; 68DE0E67A7587002 CRC64;
VYRHGDRAPM VIYPNSPNRA KVWPQGTGQL TQRGMRQEAA LGKFLKIRYI ENFRFLNRSY
IRKEVSIRST NVDRTLMSAE SQLSSLYPPH GRQVWNKNLA WQPVPIHTVP KAEDTLLLAY
NLPCKRYMDL KKQYRMSAEY KNFSNKYEDF LKNVSKLAGY KKPLNLSNSW KLYDSLFCEQ
QHDLTLPKWA TNETIETLHH ISNFGMMALF HGKPAQQIAA GVLVYRIIND MKLVRAGKKD
RPIKMMMYSS HDTTVMALLC ALSIANGLQP PYSAAVLIEL YVDNKKDYFV QILYRNSTNS
PYVLTIPGCS TYCPLDKFIK LVFQLK
//
