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Database: UniProt
Entry: F8QGU1_SERL3
LinkDB: F8QGU1_SERL3
Original site: F8QGU1_SERL3 
ID   F8QGU1_SERL3            Unreviewed;       509 AA.
AC   F8QGU1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SERLA73DRAFT_191032 {ECO:0000313|EMBL:EGN92524.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; GL945503; EGN92524.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QGU1; -.
DR   STRING; 936435.F8QGU1; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   HOGENOM; CLU_030431_3_1_1; -.
DR   InParanoid; F8QGU1; -.
DR   OMA; SWPPFTS; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063}.
SQ   SEQUENCE   509 AA;  57172 MW;  480270841EB911AB CRC64;
     MTILLATYFQ EFQLRYGTLR ILLLLFMLTS FVPLYSNSAQ QSSNFFVEGM AIGLGTNNAN
     NTATIHPPYT LKPPQTPLDV DDYPVAPEEL ELAQVHVYVR HGERTPVGVR MSEPPGSIPE
     NWIMCRDANE FGSAMAANLT SIQSGLDVPK NARRAVERRD GTSTLGLCLL GQLTDLGRQS
     TFDYGAALRK LYVERLHFLP DTLEREEEVY FRSTNVPRTI ESLQQIKHGL YPELKYAAHA
     APSILIRNGL DDNLIGNTYA CKRLQILQLG FARAAAAAIN PTLEPLNGKL SKYINGNPVL
     LDGQPKASGI LDTIRAATAH GVPVPPEFME DDVMDLLEKS VATEWFEDKT EEVRRLGMGP
     LLSDLMKKIQ RKVDPESHDM MKILVHSTHD STLAALLATL DAYDGRWPPF TSSVTFELFK
     LREARSRGTM FQNVFSGLWK STPNINDYYI RARYKNKNLM LPLCADEGKH LSGFPEFCTL
     SAFQKRVEEL TPRDWESECS HRGNKTTNR
//
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