ID X6LYF8_RETFI Unreviewed; 656 AA.
AC X6LYF8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=RFI_31194 {ECO:0000313|EMBL:ETO06202.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO06202.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO06202.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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:ETO06202.1}.
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DR EMBL; ASPP01027371; ETO06202.1; -; Genomic_DNA.
DR AlphaFoldDB; X6LYF8; -.
DR EnsemblProtists; ETO06202; ETO06202; RFI_31194.
DR OMA; VWDHFFN; -.
DR OrthoDB; 9143at2759; -.
DR Proteomes; UP000023152; 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:UP000023152};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 207..314
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 350..547
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 565..623
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 656 AA; 74921 MW; 5E6A42DF029FE8D5 CRC64;
MFPLLARKNF LSFPNNKMAL CTGLKKIKYA LTFCLICAIY FCTVEPKTNV KLEQSQEIPS
FLWRVDSKNS KLWDSKLRLA SKSFRVAPKI NAEGGVQLTV YPSQLETPNG SGVVTLEWQN
VSSPTTQDWI GTPKKNKIRI RIYCPANSSN EDYIDYVWTN GIPDGSMNVT LWNMRDDYEL
RYFSDKDGNE YWLRATSNVV TVNKYQPLQG HLSLTENGCS EMRMMWVSSN VDEFVPRVRV
GAQNGVYTAE YVAKGHTYNT SQMCYSGASI ISPQWYRDPG TIYDALLTNL TCNTMYYFIF
GSDKEWSQQS TFITASNDPD DTFEFVMYGD MGISPPPGGV TTAANLAQYE PNLRLILHVG
DLSYALGHGY IWEQWSNLVT PIASKVPYMV SVGNHEYDHL QNSSSKDNED ISGAANNGYH
PDWGNFGDDS NGECGVPTAE RYHMPDNGNQ VFWYSFDFQS VHFVMLSSEH NLSQGSEAYQ
WLKQDLQMAD AQRDRFPWII VNLHRPLYVS ESYPSDLQVA EHLKLELETL LYEFGVDVVF
SGHFHAYQRT CAVYHDQCIG EKNGGITHIM IGTAGKTLDD QHFLPMQWNE FNDIQFGYGK
IFVNSSTLLF QFLRNSDRAV VDSVTLYKYD SVQKTFFIYT LYKKKIFFLI KNFDTG
//
