ID A0A068SCY1_9FUNG Unreviewed; 471 AA.
AC A0A068SCY1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=LCOR_09920.1 {ECO:0000313|EMBL:CDH59086.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH59086.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH59086.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH59086.1}.
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DR EMBL; CBTN010000065; CDH59086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068SCY1; -.
DR STRING; 1263082.A0A068SCY1; -.
DR VEuPathDB; FungiDB:LCOR_09920.1; -.
DR OrthoDB; 203742at2759; -.
DR Proteomes; UP000027586; 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; 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; PTHR45867; PURPLE ACID PHOSPHATASE; 1.
DR PANTHER; PTHR45867:SF10; PURPLE ACID PHOSPHATASE; 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:UP000027586};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 18..471
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005103863"
FT DOMAIN 62..166
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 175..379
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 402..459
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 471 AA; 52815 MW; E2FF2060F4744B37 CRC64;
MKRLLFILGA WAVSAIASPS LLGRADKEQE EPAGSPGLMT VPDKFNTALG VDWNRTYGQT
EPQQIHLSFG SDSKYARIQF ATLSPIDQAV LKYWPKSRHV STSSKKPVTH LRGESWTFTD
GGALQRELYM HMIKTKNLKA ATVYAYQVGA TTCNGTEWGP ELEFHTASKE DEFSFLSIGD
MGVNNAVSMP HLVDFAKTHK YDFVTLSGDQ AYDMADFNGI KGDEYMNMVQ ELFARVPYMG
VPGNHERAYN FSHYINRYAT LPHKESHFAN PLMYSFDYKS LHLISFSTEI YFYGTPEEVQ
TAINWLEADL VEANKHRQQR PWIVLITHHP LYCSAPSEDC TSKAQLIRDG FNNTGFGALE
PLLLKYNVDV VIAGHVHNYE RTLPIAKGQV TSQSYHQPKS YMQVIVGNVG QPEGAESFNT
TGPWADWSAK RYDGNGFSTV KVTSETFSMT HHQANHDGTL GSVIDSFTIS K
//