ID G3AR07_SPAPN Unreviewed; 452 AA.
AC G3AR07;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGW31669.1};
GN ORFNames=SPAPADRAFT_62282 {ECO:0000313|EMBL:EGW31669.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31669.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; GL996503; EGW31669.1; -; Genomic_DNA.
DR RefSeq; XP_007376447.1; XM_007376385.1.
DR AlphaFoldDB; G3AR07; -.
DR STRING; 619300.G3AR07; -.
DR GeneID; 18874242; -.
DR KEGG; spaa:SPAPADRAFT_62282; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; G3AR07; -.
DR OMA; RGRSDWC; -.
DR OrthoDB; 1058279at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-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.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
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:UP000000709}.
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 60..374
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 254..267
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 394..402
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 452 AA; 51924 MW; D37EBB682FFA2803 CRC64;
MVSVKLNPSL LLAGQSIFQD VASPQQASTE QYNIIKYLGG SAPYRQRTGF GISTSIPEEC
SIEQVHLLSR HGERYPSKRD GVFFESVMKV FEEYPHKFQG ELEFLNDYTY FVSDKEYYEK
ETDVNNSKGP YSGTTTEFRH GQLFREKYGS LYDKDLVVFT SNSGRVHKSA QYFTEGFLGD
ISKAKFVIVD EDGKMGANSL TPRYACPKLD EHVNTDKINQ YDRTYLQDIL TRLQKSNPEL
PLSTQQVQSL FLWCAFEINV RGSSPFCNLF KNDEFIKDGY RNDLYNYNSI GEGNPYSKVV
GSPLVQAFMK LLKDENKIWL SFTHDSDMEI FLTSLGLIIP SRDLPTDYVP FPNMYNAAEL
FPQAARVYTE KLKCGEEYFI RFIMNDAVVP YPNCSNGPGF SCEMNQLFEI LNKRLEGVNF
VQQCSVPEDS PNEVTFYWDY KSKEYNAPLI DQ
//
