ID H6BUM3_EXODN Unreviewed; 466 AA.
AC H6BUM3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:EHY54898.1};
GN ORFNames=HMPREF1120_03058 {ECO:0000313|EMBL:EHY54898.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY54898.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY54898.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54898.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH226132; EHY54898.1; -; Genomic_DNA.
DR RefSeq; XP_009155359.1; XM_009157111.1.
DR AlphaFoldDB; H6BUM3; -.
DR STRING; 858893.H6BUM3; -.
DR GeneID; 20307697; -.
DR VEuPathDB; FungiDB:HMPREF1120_03058; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; H6BUM3; -.
DR OMA; FPWVNAS; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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 InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF14; ACID PHOSPHATASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003603325"
FT DISULFID 57..379
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 196..440
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 244..257
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 409..417
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 466 AA; 51822 MW; C9DFE91E1917A919 CRC64;
MAFTTLLCLA ACVHSAFSFK QTIYDTYDFD PLQHLAGIAP YFEPADPPRN PNPPNGCAVT
RAAYLVRHAA INANDYDYES YIEPFVSKLK NHTNINWAQL PELAFLSAWS PPAFAEQEIL
TRVGKLEASQ LGVQLSFRYP NFRLPEKVWS STAERTVVSA ESFIHGYEMN NGSINLVEIY
ESEEGGANTL TPYDSCPAYS SSAGSKQSQQ YLKKWSAPYL SRLNAAFPSF NFTSSDIFGM
MELCGYETVI RGSSPFCSLD VFPPDAWLDF EYTNDIMYFY NTGYGQPVSG NIGLPWVNAS
ISLLTADTPS PDQDIFVSFT HRELPPTVLV AMGLFNNTEF GGGNANDSMP LDRINYNRAW
VSSYILPFLT NIAIERMNCS ARQGTYNDVT EDDYYRVLVN NAPQTLPGCY DGPDESCSFS
GLSKWLDERT VLFGGYSQAC NTTSQYKNST DIVTFYQNPG NGSSVP
//
