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Database: UniProt
Entry: A0A0F8CNN1_CERFI
LinkDB: A0A0F8CNN1_CERFI
Original site: A0A0F8CNN1_CERFI 
ID   A0A0F8CNN1_CERFI        Unreviewed;       491 AA.
AC   A0A0F8CNN1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Lysosomal acid phosphatase {ECO:0000313|EMBL:KKF92332.1};
DE            EC=3.1.3.2 {ECO:0000313|EMBL:KKF92332.1};
GN   Name=acp2 {ECO:0000313|EMBL:KKF92332.1};
GN   ORFNames=CFO_g5315 {ECO:0000313|EMBL:KKF92332.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF92332.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF92332.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF92332.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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:KKF92332.1}.
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DR   EMBL; LBBL01000453; KKF92332.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8CNN1; -.
DR   Proteomes; UP000034841; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF142; -; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KKF92332.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..491
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002528220"
FT   TRANSMEM        430..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   491 AA;  52440 MW;  C2AE878ED13B9F98 CRC64;
     MLGALKIAPL LALASSAAAE TVYGAAVFSR HGDRTTKHYK NQQLTTVGAN QNFVMGSAYR
     SRYLLSSSEH QIANISEDKY VSSQVYASAP DSGILLATAN YFLQGLYPPL DTINAAEAGT
     ALANGTKVAA PLAGYQYVTL HAEDANSPDT MWIKGDENCP AQAATISAWE ASPVFAQRVS
     DSKDFYESMY PALNEVYDYT DSAQLSYAQA YDIYDLINVA RIHNASSPAA NVTDEQLFQL
     RTLADSAEFG ANFNATNTDS AIHARTLIAA FVSQLNTTVI GKGKLKFSLF SGSYNTMLAF
     FGMLQLPEVS PDFYGLPDYA STMGFELFTA DNTSAFPADP NNDLRVRFLF RNGTEGTLQA
     FPLFGTGEDS LTWADFKSRM EAVSIPSTKD WCNACGSTQI FCLGYQQQES VAAAAAAGAS
     GDKDSMSNTV AGVIGAMVTL GVFSLAGLVT FILFRRKSKV AALPVVAVGA GNGSVHSSVD
     EKTHVSMESN V
//
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