ID A0A1V9ZEX7_9STRA Unreviewed; 600 AA.
AC A0A1V9ZEX7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=ACHHYP_15413 {ECO:0000313|EMBL:OQR96543.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR96543.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR96543.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR96543.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR96543.1}.
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DR EMBL; JNBR01000141; OQR96543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZEX7; -.
DR STRING; 1202772.A0A1V9ZEX7; -.
DR OrthoDB; 63847at2759; -.
DR Proteomes; UP000243579; 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_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR45778:SF51; 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:UP000243579};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 17..600
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5011810777"
FT DOMAIN 161..270
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 281..508
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 529..587
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 600 AA; 64614 MW; 0D3B01A24B7B0D7A CRC64;
MKLATCLLAL TTAAIATDDK WVGGLGMLHD TPDHCRHSNG THICEYEAHD GRRLDTPAAT
ISVSATSINH LAQVEVSYTA VSPSAGDRIA AYCASPVTTA ADSDYMDFQL TSGVSGTLTF
GPLVNMRCDY QFRYQKAVAP KQFVTQATSA VVTMAKGPTQ PLQVHLALTG NAGEMRVKWT
SAAVTNPTVR YGIVHDNCGD PDLSLEAAAT ADTYAAVDMC GAPATTVSAI TYIPVGTFYD
AVLTQLPPNA HIKYQVGDAV AGWSDVFTFK MPDLGSRRDS RFFVFGDMGT WTTATGGLGL
DGRSLSTAKR VAADAATADY AAVLHVGDLS YADSVGYTWE QWMALIEPIA AQLPYMVSVG
NHEYAYTTST HAVDVSGASQ CFFPTPAFAK ASSGGECGVP TAKRFHMPGN GNGVFWYSFD
MGLVHQVVVS SEHDFNTGSR MRQWLEADLA AVDRTKTPWV FFHVHRPMYV SINTSNDQAY
NTLSRAAYEP LLAKYVVDAV FTGHVHNYER TCPVFGGMCN TAADGKAKAP VHIMIGSAGK
LLDTGANLAF DWSAKWLHEY GYGRVHVPNA THAHFEFVQD VDGVVADDVW IVSDHQWGSV
//
