ID A0A2T7DFL1_9POAL Unreviewed; 642 AA.
AC A0A2T7DFL1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=GQ55_5G125800 {ECO:0000313|EMBL:PUZ54363.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ54363.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ54363.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) 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|ARBA:ARBA00008723,
CC ECO:0000256|RuleBase:RU361203}.
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DR EMBL; CM009753; PUZ54363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7DFL1; -.
DR STRING; 1504633.A0A2T7DFL1; -.
DR Gramene; PUZ54363; PUZ54363; GQ55_5G125800.
DR OrthoDB; 45007at2759; -.
DR Proteomes; UP000244336; Chromosome 5.
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; IPR040974; Fn3_PAP.
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:SF3; PURPLE ACID PHOSPHATASE; 1.
DR PANTHER; PTHR45778; PURPLE ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF17808; fn3_PAP; 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:UP000244336};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 24..642
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5015375588"
FT DOMAIN 74..204
FT /note="Purple acid phosphatase Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF17808"
FT DOMAIN 210..311
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 321..533
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 565..623
FT /note="Purple acid phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 642 AA; 69673 MW; D692E9C580B5A4AB CRC64;
MGFFSSGVVP PLLVLLGLFG AAASPSPPPP EMLHGSYAGK SEFRTVNRKE LQSCLNPSPY
LAINVSTGGA PLPDEALLEV TVAGVLRPDA SDWVAMITPS NSSVSGCPLS GVNYVETGDL
ANLPLLCHYP VKAQYLTSDP GYMGCKNAGC GKRDASGACK ARTCAATLTF HVVNFRTDVE
FVLFSGGFKT PCLLKRSGAL RFANPSSPLY GHLSSTDSKA TSMRLTWVSG DGNPQQVQYG
DGKSSTSEVA TFTQEDMCSI SVLPSPAKDF GWHDPGYIHS SVMTGLQPSQ SYSYRYGSDS
VGWSDTIKFR TPPAAGSDEL SFVIYGDMGK APLDPSVEHY IQPGSISVAK AVAKEIQTGK
IDSIFHIGDI SYATGFLVEW DFFLHLITPL ASQVSYMTAI GNHERDYANS ASVYVTPDSG
GECGVAYESY FPMPAVSKDK PWYSIEQGSV HFIVMSTEHE WSEKSEQYNW MDEDLSSIDR
SRTPWVIFIG HRPMYSSHGG ILPNVDSNFV ASVEPLLLNY QVDLVFFGHV HNYERTCAVY
QGNCNGMPTK DANGIDVYDN SNYTAPVHAI VGAGGFSLDN FPNNGETWSL SRVSEFGYAR
VHATRTDMLV QFVNSSTMEV RDQFRIVKGS SAKKSPSLII QQ
//
