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Database: UniProt
Entry: A0A179FGY1_METCM
LinkDB: A0A179FGY1_METCM
Original site: A0A179FGY1_METCM 
ID   A0A179FGY1_METCM        Unreviewed;       480 AA.
AC   A0A179FGY1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:OAQ64786.1};
GN   ORFNames=VFPPC_13940 {ECO:0000313|EMBL:OAQ64786.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ64786.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ64786.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ64786.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(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:OAQ64786.1}.
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DR   EMBL; LSBJ02000005; OAQ64786.1; -; Genomic_DNA.
DR   RefSeq; XP_018142100.1; XM_018291712.1.
DR   AlphaFoldDB; A0A179FGY1; -.
DR   STRING; 1380566.A0A179FGY1; -.
DR   GeneID; 28855706; -.
DR   KEGG; pchm:VFPPC_13940; -.
DR   OrthoDB; 2315929at2759; -.
DR   Proteomes; UP000078397; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd12087; TM_EGFR-like; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..480
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008101715"
FT   TRANSMEM        428..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          460..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  51637 MW;  169E951313C029ED CRC64;
     MHTGTIFVLT GLASSAAAAT VHGALVFTRH GDRTTKWYKA QALTSLGAEQ NRQVGGGYRE
     RYLSSSSPDR ILGISQDKYV SSQVFATAPD QGILMNTATA FLQGFYPPLG DIAPEIASQT
     LNNGTNSTAP LDGYQYVILH GINDNSPDTI WIKGDDECPA YTNSSKKFTK STEFRQRDTS
     TRDFYAGFYD VLSSGVYNLK KEDMTYAHAF DIFDLVNVAR IHNATSPARN VSDTNLDQLR
     TLADSAELGL NYNASETIRS VGAQTLSGVV LRQLNTTVSS RGKAPKFSLL AGSYDTFLAF
     FGLTGLLDVS PDFHGLPEYA SSMAFELFTE DNADMFPSSV DSNLRVRWLF RNGTAGNLTG
     FPLFGSGEMS LPWPRFVSEM QKRAIVDVGD WCTKCSSKAD FCAAYGDNVG AKDNEKSDGG
     SSGGMSNAVA GVVGAMVTLG VVAIVGAVAF VLLRRKTAAK TSADKTSVRS GSTDERENKV
//
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