ID   A0A0F0IJW4_ASPPU        Unreviewed;       527 AA.
AC   A0A0F0IJW4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Histidine phosphatase superfamily branch 2 {ECO:0000313|EMBL:KJK67441.1};
GN   ORFNames=P875_00117134 {ECO:0000313|EMBL:KJK67441.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67441.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK67441.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK67441.1}.
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DR   EMBL; JZEE01000194; KJK67441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IJW4; -.
DR   STRING; 1403190.A0A0F0IJW4; -.
DR   Proteomes; UP000033540; 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; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR20963:SF43; PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01240)-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:UP000033540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002443461"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        382
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        71..435
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        288..301
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   527 AA;  57280 MW;  8357E0811C5ED914 CRC64;
     MQQLLQSAAA LLAFQAVVGD AAPTSSSSAA APGPTGASYP SGFDMSTSWG NLSPYKDQPG
     FEVPNGVPRG CELSQVHVLH RHAQRYPTSW KLDGGVIEDF AQKLKNYTKR HDNATVGKGA
     LSFLNEWEYV LGEDLLLVSG AATEATSGAN VWSKYGRALY HAPVGVASYD SSLNVYSNGT
     ERPKPIFRTT DQARILESAR WWLSGFFGNT GANSSYSEYD LVITHEGTGF NNTLASDGSC
     PGDLEEGDDS GEKFIPNLTK DALKRLSHFL PSDFNLTAYD VVGMFSLCPY ETAALGSSSF
     CSLFTEQEWR DFEYFVDLQF YGNYGFGAPT GRAQGIGYVL ELAARLEGKR IETSDTSINT
     TIDSKPATFP LNQPLYMDMS HDDVIVGVLA ALGLKYFNYG SKGLPDDVAH AVPRNFKLNE
     VTPFGAHLIS EIWTCPEKTN FHQLDGALYK NPDLSSTSDT TDVIRFVLNG SPVSQEGLDG
     CESSINGFCG VEDFLKGVPK LKEKAEYQYA CFGNYTAGHQ VGDGRPE
//