ID   A0A317VHS2_ASPEC        Unreviewed;       525 AA.
AC   A0A317VHS2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:PWY73916.1};
GN   ORFNames=BO83DRAFT_359779 {ECO:0000313|EMBL:PWY73916.1};
OS   Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY73916.1, ECO:0000313|Proteomes:UP000246171};
RN   [1] {ECO:0000313|EMBL:PWY73916.1, ECO:0000313|Proteomes:UP000246171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY73916.1,
RC   ECO:0000313|Proteomes:UP000246171};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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:PWY73916.1}.
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DR   EMBL; MSFU01000011; PWY73916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VHS2; -.
DR   VEuPathDB; FungiDB:BO83DRAFT_359779; -.
DR   OrthoDB; 2681959at2759; -.
DR   Proteomes; UP000246171; 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:SF127; -; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..525
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016418029"
FT   TRANSMEM        458..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          504..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  56627 MW;  7DB2858A8681516A CRC64;
     MLSTRQFVAL AAILQAATQA SAQDLKEQVW AVFAYTLYGD RVPTALPRPN ILTPYGANTL
     YEAGSAFRDR YVAIHSTDVS PSTRIESIST YALEDEDLDI LSTTDPSVIA SAQAFMQGLY
     PPLNDTYDVQ YPDPSYLMAN GSFATAPMGG YQYPPIVTVS SDDPQSVVVA GQDNCFLHQI
     ANADYQASTE AQQMIQESDA LYNRLYIQVL SGDFDRSSVN YANSIAVSEF LEYQLLHNET
     LLHSVSQEDI RLARWYADQY TFATNGNSDT SLSSPIDSSA IRTIAGQTLA GSILDAFDTN
     VLYRGTSGKL TFVFGGYEPA VALTSLVQLA SPENGKFYGR PALGASLTFE LFSLENQSFP
     TYPDPSQLYV RFLLRNGTTS PEFQSYPLFG HSPSIIEVPY SDFKAEMQAF SLNSTQEWCL
     QCDSSSSAVF CPGVLDDEDD GPSSSAASSS GRKGISPAVG GVIGAIVTLV VVGLIAAAGF
     LLLGVRVQRG RRPSLEEIKG GIDLGSDSNL ALREHAAPPA KTARP
//