ID   A0A100ISP6_ASPNG        Unreviewed;       477 AA.
AC   A0A100ISP6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:GAQ46622.1};
GN   ORFNames=ABL_09283 {ECO:0000313|EMBL:GAQ46622.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ46622.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ46622.1}.
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DR   EMBL; BCMY01000022; GAQ46622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100ISP6; -.
DR   PaxDb; 5061-CADANGAP00012404; -.
DR   VEuPathDB; FungiDB:An16g01730; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1145506; -.
DR   VEuPathDB; FungiDB:ATCC64974_72850; -.
DR   VEuPathDB; FungiDB:M747DRAFT_79146; -.
DR   OMA; YIFHRHG; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..477
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007087702"
FT   TRANSMEM        429..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          404..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  51048 MW;  3A3DF79FB4898ABE CRC64;
     MRTSSQSSGL CLALMVMSLA LPASAEKVLG AYIFARHGDR TAKVLKDTEL TDLGYREVYT
     TGTYWRSRYI DSDSSLQIQN ISEDIVKLSQ ISASTPSDDV LQNSATGFLQ GVYPPVGSSA
     NETLADGTVV DSPLDGYQLI PLSMTDSGSN SEDTTWLQSA TNCQNAEVSS NNYYSSSLYN
     SLLNSTSDFY QSLSSLLNST FSESSMSFKN AYTIFDYLNV GSIHNTTNVP TAEQLHQAFL
     LANIEQYNLA YNSSEPVRAV AGAMLAGDVL QGLNKTITSK GKTKLNIQFG SYGTFLSYFG
     LAQLPTADVN FTGIPDYASS MAWELVTNST SSEFPSTSDI SVRFVFHNGT LNESKNDSPT
     EYPLYGRSSA TISWSDFERL STKIAVTSQS QWCQACGNTD GQCASYSTGS NTTSTSTPQQ
     KSSSGISRAV AGVIGAMVTL AVILGAEALL LLVGGFRITK KGAVAQNAAA DEEDKTS
//