ID D4AXB4_ARTBC Unreviewed; 496 AA.
AC D4AXB4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARB_00842 {ECO:0000313|EMBL:EFE32319.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE32319.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE32319.1}.
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DR EMBL; ABSU01000016; EFE32319.1; -; Genomic_DNA.
DR RefSeq; XP_003012959.1; XM_003012913.1.
DR AlphaFoldDB; D4AXB4; -.
DR STRING; 663331.D4AXB4; -.
DR GeneID; 9523038; -.
DR KEGG; abe:ARB_00842; -.
DR eggNOG; ENOG502RCH9; Eukaryota.
DR HOGENOM; CLU_023111_1_0_1; -.
DR OMA; YIFHRHG; -.
DR OrthoDB; 2315929at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_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:UP000008866};
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..496
FT /note="Histidine acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003054059"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 53024 MW; B5E32CEC736EFA16 CRC64;
MLNSASLLAV SLLAQAATAE TVLGAYIFSR HGDRTSKSTP PTVLTDLGYS QVYSSGRYYR
DRYISSSSSS QVLGISPNII SPGEITASAP QDEVLQKSAL AFFQGLYPPA GKEAKTTLRN
GTVVEAPMDG YQLVAIEQVK SGSNSENVAW LQSASACKNA KISSNDYFAS KEYKDLLKSS
EGFYEDVAPL VKDTIVAEKV NFKNAYTVFD LLNVASIHNS SDSFPSLSSE VYSQLQSLAN
IHEFGLAYNA SEPIRAVSGA LLAGEVLNSF MDTIKAPKTK PKVNVQFGAY ATFLSFFGLT
KLPTANHDFN GIPDYASTMV FELVTNASTS SGSFPAESEI SVRFLFHNGT TIAGSPETEP
TAYPLFGQEK ALLPWFEFVS HMKEIAITSQ DQWCQACGTA SEGCPGAPSS SGASGHSTSS
NSDSGVSRPV AGVIGALVTL SVILGVQALV FFVGGFTITR KTINDINEMI YINVTLKPYI
QIFYIDSTPV AMELGT
//
