ID A0A319C4F9_9EURO Unreviewed; 620 AA.
AC A0A319C4F9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=BO82DRAFT_394208 {ECO:0000313|EMBL:PYH79051.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH79051.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH79051.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH79051.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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 -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|RuleBase:RU361203}.
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DR EMBL; KZ821723; PYH79051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319C4F9; -.
DR STRING; 1448315.A0A319C4F9; -.
DR VEuPathDB; FungiDB:BO82DRAFT_394208; -.
DR OrthoDB; 203742at2759; -.
DR Proteomes; UP000248340; 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; IPR014390; Acid_Pase_Asper.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR003961; FN3_dom.
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 InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR22953:SF159; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR PIRSF; PIRSF000900; Acid_Ptase_Asper; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR PROSITE; PS50853; FN3; 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:UP000248340};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 21..620
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5016194992"
FT DOMAIN 80..176
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 620 AA; 68119 MW; 2420E690D36533B3 CRC64;
MKTAAASALL VALSATLAQA RPVADERYPY TGPAVPVGDW VDPTVNGNGK GFPRLIEPPA
VRPASANPRN NVNVISLSYI PKGMHIHYQT PFGLGQTPSV MWGKSPHQLN KVARGYTHTY
ARTPSCSEIK IITQCSEYFH EVSLENLEPG TTYYYQIPAA NGTTTSEVLS FKTAREAGDK
GSFSVAVLND MGYTNAHGTQ KQLIKAANEG TAFAWHGGDI SYADDWYEGT LACESSWDVC
YNGTSTELPG NLPLPDEYKK PLPAGEIPNQ GGPQGGDVSV IYESNWDLWQ QWLSNVTVKI
PYMVMPGNHE AACAEFDGPG NILTAYLNDD IANGTAAEDK LNYYSCPPSQ RNFTAYQHRF
RMPGEETGGV GNFWYSFDYG LAHFVSIDGE TDFANSPEWP FAEDIKGNET HPTAEETFIT
DSGPFGAVDG SYKETKNYAQ YKWLRQDLAK VDRKKTPWVF VMSHRPMYSS AYSSYQLNVR
EAFEGLLLKY GVDAYFSGHI HWYERLYPLG ANQTIDTASV INNNTYIANN GKSITHIING
MAGNIESHSE FSEGQGLTNI TAVLDTVHYG FSKLTVKSET EVKWQFIRGD DGSVGDEVTL
LKPSAVKGKG SGKGYSGFRA
//
