ID Q0CW13_ASPTN Unreviewed; 577 AA.
AC Q0CW13;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_02121 {ECO:0000313|EMBL:EAU37083.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37083.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476596; EAU37083.1; -; Genomic_DNA.
DR RefSeq; XP_001211299.1; XM_001211299.1.
DR AlphaFoldDB; Q0CW13; -.
DR STRING; 341663.Q0CW13; -.
DR EnsemblFungi; EAU37083; EAU37083; ATEG_02121.
DR GeneID; 4317264; -.
DR VEuPathDB; FungiDB:ATEG_02121; -.
DR eggNOG; ENOG502SM2K; Eukaryota.
DR HOGENOM; CLU_023111_0_1_1; -.
DR OMA; STQEWCL; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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:UP000007963};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 451..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 512..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63189 MW; 0E1BDD3EE97F532A CRC64;
MLVPRPYLAA LAATLHTSIV SGQEMKEQVW GVFAYTLHGD TVPSSVSRPQ TLTPYGSNQL
YQAGSAFRNR YVAIHEDDSA PSTRIESLSR NMLDPEDIEI FSTTDASVVA SAQAFMQGLY
PPLNDSYGAT YYDPSFELAN GSLAEAPLNG YQYPPILTYG SSDYQSIVVE GHSSCLMHRV
ADDEYKFTQE FEQMKEETEA FYQSIYDQVL SGIMNRSEAT YANAYYISEF LEYQSVHNDS
LLHQLNQGDI ESARYFADHY IFATNGNTST SGVGTPDVRT VAGKTLAASI VNVFGTNIDA
RGTSGKMTFM FGSHEPVVAL TSLMGLASPE HASFYSRPAH GASIVLELYS LENDTYPTYP
DPSQLYVRFA LRNGTGSPES PEFQTYPLFG LGPSNIGIPY SEFESEMKQI ALNSTEEWCH
LCNTDIAFCS PFSDKTHKDH QGSGHKGMAP GVAGVIGAVV TLVTVGVVAV VGFLLCGVRL
GRIRKRSLGG FKGNSKMASD TDVAFRNTTW SDAKEAGTNE GEAGARTHER HGSWEMRGGA
TLASRGPDEN ARSPFDDEMD DWRIHTLQQP VQAREHV
//
