ID A0A0F0ILI5_ASPPU Unreviewed; 512 AA.
AC A0A0F0ILI5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:KJK67602.1};
GN ORFNames=P875_00116963 {ECO:0000313|EMBL:KJK67602.1};
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:KJK67602.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK67602.1, 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KJK67602.1}.
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DR EMBL; JZEE01000186; KJK67602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0ILI5; -.
DR STRING; 1403190.A0A0F0ILI5; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002443345"
FT SITE 180
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 512 AA; 54904 MW; 1431B97D3D688BF3 CRC64;
MFLLLIKLAT YAAAVAAQVD SSSPFSFTSS GNPILSNGSW YSGDPAPLVV NDTLYIITGR
DSAPPDENAF VMNQWGMLAS SSAKPEGGTW TLYPDVADPQ AVFAWAEPGS AYAAQVVQGH
DSRFYMYAPV TQADSANEDA FAIGVAVSDS PTGPFQDAHP SGPIISQSVP PPGNTIQNID
PTALVDDDGH VYIYFGTFGQ LLGYQLDPDM VTVASNVTQF TSLTGYFEAP WLMKRQGVYY
MLFAANNAGA DSPCTPTSYH ACIAYGTASS PMGPWTFQDV ILPIVSSTTS HPGAVEWNGE
WYLVYHTADA VGGGHFRRSV AFDKLTWDDS QAPAKINVVQ QTFGPKSPAP PTHNVAPQAV
ASSVHSTPIQ YWVQALNDGI IRENPLPPDY WCSYEATDSP QTSTLVYTWN ETVQLNGTSM
VFFADHAAGA NEGVAPPQEW YIEYKDGSGT WQRAANTSSY PLEVTDTPDV VAFGTVDTVA
IRAILVASGA QGQYAGVGVK EWEALSTTLH SY
//
