ID H6C6B1_EXODN Unreviewed; 577 AA.
AC H6C6B1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:EHY59257.1};
GN ORFNames=HMPREF1120_07250 {ECO:0000313|EMBL:EHY59257.1};
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:EHY59257.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY59257.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY59257.1};
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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; JH226135; EHY59257.1; -; Genomic_DNA.
DR RefSeq; XP_009159718.1; XM_009161470.1.
DR AlphaFoldDB; H6C6B1; -.
DR STRING; 858893.H6C6B1; -.
DR GeneID; 20311889; -.
DR VEuPathDB; FungiDB:HMPREF1120_07250; -.
DR eggNOG; ENOG502SM2K; Eukaryota.
DR HOGENOM; CLU_023111_0_1_1; -.
DR InParanoid; H6C6B1; -.
DR OMA; STQEWCL; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000007304; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
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..577
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005683338"
FT TRANSMEM 445..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 513..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 61574 MW; A0E4C787509D0EA1 CRC64;
MAHLPTSIVF LFALFVVAGA QTAIQQQLLS TFIYTLHGDR TPLVLPTSPS LTPLGAEQLF
AAGDSFRERY VAPSESNSFT IRGISAYQLE DDQLTVLSTT DQFVAASAQA FLQGLYPPLQ
TDSNSANTAQ NDTTMVAPLR GYQYADIMTV SSNDFNSIWL RGSKSCPAYL ASSSDYYETE
AFETLQNSTE DFYRSIQPDF LDGILSDASV GYFNAYQIYD YLNYVSIHNT SASGLLAPEV
LAKAKILADD LVFALNTDIS PSGSSFDDYI RTIAGRTLAA RITQAFSATI NTQGASDKMT
LVFGSYEPVV ALAALAGLVV PQHSAFYNVP APGASYVFEL ISMQGNDTDA YPEVSDLFVR
FLYKNGTGSD SSLVPYPLFG LSPSQTLISF ADFVAGLDRF SVSNVQDWCT ACNSFSVFCP
AFATTNGSLD YTGSGSPYGK RLSPVIGGVI GAVVTLAATA LIYGAAMLFG GVRMHRVRDK
RRSALGGFKG AEKLASDPDL SVAKGSAGAV VIASQGPAGT GGHERTGSWE MKDQGKAVEA
QRQALGAGAP SPRSPSYEDD DMPIEPHAFP VQPRSHV
//
