ID A0A485L406_9STRA Unreviewed; 595 AA.
AC A0A485L406;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN Name=Aste57867_15825 {ECO:0000313|EMBL:VFT92613.1};
GN ORFNames=As57867_015769 {ECO:0000313|EMBL:KAF0693178.1},
GN ASTE57867_15825 {ECO:0000313|EMBL:VFT92613.1};
OS Aphanomyces stellatus.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniomycetes;
OC Saprolegniales; Verrucalvaceae; Aphanomyces.
OX NCBI_TaxID=120398 {ECO:0000313|EMBL:VFT92613.1, ECO:0000313|Proteomes:UP000332933};
RN [1] {ECO:0000313|EMBL:VFT92613.1, ECO:0000313|Proteomes:UP000332933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 568.67 {ECO:0000313|EMBL:VFT92613.1};
RA Gaulin E., Dumas B.;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0693178.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 578.67 {ECO:0000313|EMBL:KAF0693178.1};
RA Gaulin E.;
RT "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT effector associated with host adaptation.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|RuleBase:RU361203}.
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DR EMBL; VJMH01005756; KAF0693178.1; -; Genomic_DNA.
DR EMBL; CAADRA010005777; VFT92613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485L406; -.
DR OrthoDB; 45007at2759; -.
DR Proteomes; UP000332933; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR025733; PAPs_C.
DR InterPro; IPR015914; PAPs_N.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR PANTHER; PTHR45778:SF7; PURPLE ACID PHOSPHATASE; 1.
DR PANTHER; PTHR45778; PURPLE ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 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|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000332933};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..595
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033437308"
FT DOMAIN 159..267
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 282..504
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 525..584
FT /note="Purple acid phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 595 AA; 65320 MW; 8C623D58A9CB5C30 CRC64;
MKLFAVLALA AVAAAHSDSG EWIGATHHLH AAQDACKDGA CAFPSSGRRL KDSSNSIKVS
QTTIPHMTKV DVTFAVQGAS KNDRVAAYCT SENVDATDDK EYIDFQPVSG KDTDKLTFGP
LLNMRCDYQF RYQKAVTNTT FETVAKSKVV KMKRGDTEPL QIHIALTQND DEMNVAWTSA
EIDNPTLRVT IQSKNGKAGP VQTIDATSKS YSAEDMCSAP ANLTTAQRYI PSGVHYDGVI
SHIPAGATVV YQVGSDASGW SEKKSFVMPD LLPSDKPSSY FVFGDMGTWV TATNGTGLPG
RSLGTINRVA EDLAKGDRNY HAALHVGDLS YADSIGYIWE QFGDLIQPVA SKIPYMVSVG
NHEYCYLNST KEVDVSGESA AFYADKPKAS SNGECGVPIA NRFNVPDNGN GVFWYSFDAG
MTHQIILSSE HDFNHGSKLR QWLEADLAGI DRDARPWVFI HYHRPMYVSM DSSAKYTKIL
RTALEPLLKQ YSVDAFFTGH THAYERTLPV YNQTVQVGAN GQAKGTVHVM IGSAGKAMDT
DDWLNTTWSA KQLKEFGYGR VHVQNRTHTQ IEFVLNSDHS VADTTWIVSD HKWGN
//
