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Database: UniProt
Entry: A0A0F0ILS2_ASPPU
LinkDB: A0A0F0ILS2_ASPPU
Original site: A0A0F0ILS2_ASPPU 
ID   A0A0F0ILS2_ASPPU        Unreviewed;       893 AA.
AC   A0A0F0ILS2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=P875_00075737 {ECO:0000313|EMBL:KJK68759.1};
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:KJK68759.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK68759.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
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:KJK68759.1}.
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DR   EMBL; JZEE01000026; KJK68759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0ILS2; -.
DR   STRING; 1403190.A0A0F0ILS2; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR33307:SF6; ALPHA-RHAMNOSIDASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF05592; Bac_rhamnosid; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          146..317
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          328..420
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          433..787
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          789..866
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   893 AA;  100924 MW;  114F4B62F87935ED CRC64;
     MALVTNVQFE HYHPPNTLGV QERKPRISWG FKNVPRHFRQ EGYDIEIFDS EHTVLSTVKR
     TSQQSYLVPW PSDQPLKSRQ KISLRVRVWD GEGYISPWSE EAYLETGLLE RSNWQCERIA
     APWGPETTGP VPEDLYRKEF SLRGPVRQAR LYVTAEGVYE AEINGQRVGD YFMAPGWTTY
     DGRLQYQTYD VTSMLSADRN CIGVRVAEGW FCGRIGFEGG HRNIWGPHTA LMAQLEVTYT
     DGRVDAISSD RSWLVTTGPI RLAEIYDGEK YDATREIPCW SSPAMTLDTA WEPVLLMDPL
     PDSVALTAGF SEPVRRTEVF QPIQKVVTPS GKIILDFGQN LVGYVRLKDI KGPRGHIVRL
     SHAEVLEHKE LGTRPLRICQ AIDEYTLKGG SEGEHYEPRF TFHGFRYVQI DGWRGDLELE
     TSAEAVVCHT DMKQVGTFSC SDSLLNQLYK NVCWGMRGNF LSVPTDCPQR DERLGWSGDL
     ALFAPTATLI YDCFNMLRNW LVDVEHDQNI LGGVPAMVTP NATLPDPIWC RRIPCAIWHD
     VTILAPWALY EETGDESILF QQYASMTTWL KRLPRNPTGS THLWDTTVFQ LGDWLDPAAP
     PDAPWKGATD AKLVANAFLI RSLDYMSRIA GILGKDDDRE QFAAELKEAW KEFQDEYVTP
     NGRITSDSQA AYALAICFDL LTPNQRVHAG NRLVELVRKN EFKIGTGFAG TPYLCEALTL
     SGHIQVAYSM LLEKKCPSWL YPVTMGATTV WERWDSMLPD GTINPGEMTS FNHYAFGAIA
     KFLFERVAGL QRLEPGWKHF RVAPSIGAEL TYASASHATP YGQASCSWET SRVEKGLDKI
     QLRVSVPHGT TCEVVYPSGS GEETEIVGYG EWSFEAIFKR EYEWPIKPLP PKS
//
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