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Database: UniProt
Entry: A0A179H0Q5_PURLI
LinkDB: A0A179H0Q5_PURLI
Original site: A0A179H0Q5_PURLI 
ID   A0A179H0Q5_PURLI        Unreviewed;       488 AA.
AC   A0A179H0Q5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:OAQ83288.1};
GN   ORFNames=VFPFJ_09091 {ECO:0000313|EMBL:OAQ83288.1};
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ83288.1, ECO:0000313|Proteomes:UP000078340};
RN   [1] {ECO:0000313|EMBL:OAQ83288.1, ECO:0000313|Proteomes:UP000078340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ83288.1};
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT   Phytophthora in bio-control Purpureocillium lilacinum.";
RL   Submitted (FEB-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:OAQ83288.1}.
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DR   EMBL; LSBI01000008; OAQ83288.1; -; Genomic_DNA.
DR   RefSeq; XP_018175916.1; XM_018326164.1.
DR   AlphaFoldDB; A0A179H0Q5; -.
DR   GeneID; 28891213; -.
DR   KEGG; plj:VFPFJ_09091; -.
DR   OMA; REWAQAC; -.
DR   OrthoDB; 2315929at2759; -.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078340};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..488
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008103139"
FT   TRANSMEM        438..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          466..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  51778 MW;  71FDF00BF0206D96 CRC64;
     MHSATLLAAA VAGLAGSAAA VTVHGALVFT RHGDRTTKWY KAQALTSLGA EQNYQVGGSY
     RQRYLSSSSP DAIRGISQDK YVSSQVFASA PDQGILMNTA TAFLQGLYPP LEDVAPDVAS
     QGLNNGTNST SPLGGYQYVV LHGVNDNSPD AIWIKGDDEC PAYTASSKGF SRSDEFRARD
     DATRGFYERF YDVLAPGVYN LKREDVSYAR AFDVFDLVNV ARIHNATSPA RNVSDEDLAQ
     LRTLADSAEL GLNWNASEPM RAVGAKTLSG VVLRQLNATV SSRGATPKLS LLAGSYDTFL
     AFFGLTGLLD TGADFHGLPE YASSMAFELF TDGNDDKSFP ADPAANLRVR WLFRNGTAGT
     LKGFPLFGTG EASLPWPRFV SEMQKRAITD VGDWCDKCDS KAGFCAAYRD DDGEAGGAEK
     NSGGGGGDGG ISKAVAGLIG AMVTLAVVAV VGGLAWMVLR RKRKGAGRQQ GDKTSVRSGS
     TDERTDTV
//
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