ID A0A0A2VA75_BEABA Unreviewed; 1263 AA.
AC A0A0A2VA75;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=BBAD15_g11771 {ECO:0000313|EMBL:KGQ02990.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ02990.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ02990.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ02990.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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}.
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:KGQ02990.1}.
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DR EMBL; ANFO01001300; KGQ02990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VA75; -.
DR STRING; 1245745.A0A0A2VA75; -.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_264615_0_0_1; -.
DR Proteomes; UP000030106; 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; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
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; PTHR42678; AMIDASE; 1.
DR PANTHER; PTHR42678:SF30; PUTATIVE-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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:UP000030106};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 22..1263
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005109109"
FT DOMAIN 76..174
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 275..507
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 538..600
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
FT DOMAIN 775..1176
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 675..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 135936 MW; 9B0B9DF7CDAC34C6 CRC64;
MARMKIAVTA VVGLLSALVE AVPTVDEIYP YSGPEIPIGD WVNPTVKGNG RGYMRLVEPP
AVKPASSDPT NNINVISLSY AGSTGVNIHY QTPFGLGSTP SVRWGASRDA LDQTAHGVSH
SYDRTPPCSE VAVTQCSQHY HDVQIKGLKP ETTYYYFITA ANGTTASDVL SFQTARPAGS
KKSFTIGVLN DMGYTNAGGT YKQLNKAIDE GLVFAWHGGD ISYADDWYSG IIPCQSSWPV
CYNGSSTQLP SGITPDYDKP LPEGEIPTEG TPNGGDMSVL YESNWDLWQQ WMTPITSKVP
YMVLPGNHEA ACAEFDGPGQ ILAAYLNHNK PNSTAPKSDK LTYYSCPPSQ RFRDSNYTAY
QHRFRMPGGE SDGVSNFWYS FDYGLAHFIS FNGETDYPNS PEASFARDIK GDEKALKANE
TYITDSGPFG TVDGDITKKE SYEQYKWLQN DLAKVNRTKT PWVIAMSHRP MYSSQVSGYQ
QHMRNAFEDL FLKYGVDAYL SGHIHWYERT FPLSRNGTID KSAIINNNTF YANEGVSITH
IINGMAGNIE SHAELSKAKK PLDITAIFDQ THYGFSKLTV VNETVLTWSF VKGGDGSSGD
DLTLIRKAAN HSATSSTPTS TQSGAVAVIT ETVSSYTTYC PGPTTITEGT HTYVVSKATT
LTISDCPCTR VVTSSVTGGN NTAPAQTSKA QPMSRASQSS SARPVAPVTG AASASHHSVI
VCSSGACHTA TEVPGRLIVV DKGTVAHTGS FPPLLDATLD ELRRGLDGGQ FTSVDLTKAY
IARINDVSEQ LHAVNEINPD ALKIAAELDQ ERAKGKVGPL HGIPILIKDN IATDDKMNNT
AGSFALIGAK VPEDSTVAAK LRKAGAIILG KANLSQWAYF RSNNGSSGWT SVGGQTIGAY
FPGQDPSGSS SGSGVASSIG LAWACLGTET FGSIISPSQY NNLVGIKPTV GLTSRYLVVP
ISEHQDTVGP MARTVKDAAH LLGAIAGKDN HDKYTSAIPF GDEVPDYVAA CKESGLKDKR
IGIPRDVANE RDFDPAVVKS FREAIEILRS SGAVIVENID FPGVTKYRSA NDIVLKADFF
TGLPELYLKN LVTNPNNIHS LADLRAFTHQ DSREDWPERD TGVWDSALER GYGNDSPQFQ
QAYKEQLLYA GQEGLAGALK NHSLDAVFAP SAIASNLAAP LGHPAITLPI GRMPEGTLVT
QNDFGNLNAT SPNQPFGVGF AGDHFSEEAL IGMAYALEQQ TQVRTKIEPI VVLKTELKDV
VGK
//
