ID D2VCD2_NAEGR Unreviewed; 373 AA.
AC D2VCD2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=NAEGRDRAFT_66530 {ECO:0000313|EMBL:EFC45631.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC45631.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC45631.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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|RuleBase:RU361203};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|RuleBase:RU361203}.
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DR EMBL; GG738862; EFC45631.1; -; Genomic_DNA.
DR RefSeq; XP_002678375.1; XM_002678329.1.
DR AlphaFoldDB; D2VCD2; -.
DR EnsemblProtists; EFC45631; EFC45631; NAEGRDRAFT_66530.
DR GeneID; 8849190; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_66530; -.
DR eggNOG; KOG1378; Eukaryota.
DR InParanoid; D2VCD2; -.
DR OMA; TAHEHCY; -.
DR OrthoDB; 203742at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR22953:SF153; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 28..373
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005126206"
FT DOMAIN 31..130
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 172..371
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 373 AA; 43051 MW; 8352B616176E84BE CRC64;
MSLQGWTLSN NIIFFLLLLV STTFVYCDFQ PRELHLAFTN NPNELVVSFH TSNYSEQLLG
KPLITFSTSE NLANYETASI GSVVTSYGDS SKTGFDFHVL LTNLKFATKY YYKCGFEKAE
FLSETFFFYT RTDPMSDESK ETTIVIYGDQ GTTNSKYVIA QTQGFVSNFL QKSKNKNLFI
YHLGDIGYAD DFAGAMYQPI WTKYMQMMNR IMPYVPYMVC VGNHENGPQN KPYDEFEAGF
QAYNHRFFMP SRNDSSIGHN MWYTFKQGLI TFIATDTETN FPQSFFPQYD NLFSGNKNQL
IWLEETLKNV DRKETPFLII VGHRPIYSSD YAFSDIPGNI IGESLRLQAA FEDLLYKYHV
DIAFYGHVHS YGK
//
