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Database: UniProt
Entry: A0A117E3R5_ASPNG
LinkDB: A0A117E3R5_ASPNG
Original site: A0A117E3R5_ASPNG 
ID   A0A117E3R5_ASPNG        Unreviewed;       791 AA.
AC   A0A117E3R5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=ABL_10244 {ECO:0000313|EMBL:GAQ47583.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ47583.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ47583.1}.
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DR   EMBL; BCMY01000032; GAQ47583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117E3R5; -.
DR   VEuPathDB; FungiDB:An10g00290; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1165677; -.
DR   VEuPathDB; FungiDB:ATCC64974_63320; -.
DR   VEuPathDB; FungiDB:M747DRAFT_289043; -.
DR   OMA; NCRHETY; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR34987:SF2; B, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G05040)-RELATED; 1.
DR   PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
FT   DOMAIN          47..195
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          382..704
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
SQ   SEQUENCE   791 AA;  89661 MW;  DD37FF2353475183 CRC64;
     MASPDWTRAA PWIWLPHYLE EENRPGRFFL FRKAFQWHPS DNPQDLSVHV SADSRYRLFV
     NGHRVSWGPC KSYPGKWYYE TVDIRPYLRD GENVISARVL RYSTLVPGSS SIVSMPLPGF
     MLYSPHPELA ISTDPSWTCI EQRSVKIIPQ TEWNYLLGPP FLSNNERAEE DQTITGWQMP
     GYDDATWDKA VFQSNAVKML PIVSPWKLAP RPIPDLPEIE GRFDGIVKAT GSVSEDQWKL
     LIREDRAVVI PANAQVTVDL SVEALMTAFV NFAFSGGGGA KISILYSECY EKDLGVEAAP
     FPMPRTKSNR SDASGRLYGV KDFYTVTSGQ DTHSFEPFWF RCFRYVQLEI TTTSNPITLT
     SISLRETSYP LEIATKVDAG AELNKIWEIS LRTLQNCRHE TYEDCPFYEQ NQFASDSRLQ
     LLFTYQLSPD DRLARKTLEE FHASRTPDGL IVAQYPTGIA SKQIPQFSLF WILMVHDHMM
     YLADRTLVRR YLSTVDSIIQ HFEDRLDDRG LVGQFDPDTW PFVDWVQDWF VPGQIFKSCM
     PPAYHNAGAA TVNSLMYAYA LLHAAELCEF VGRISTAEEY RARVHSIRSA VNQRCTSNSQ
     LYLDGPGVEQ YSQHTQVFAI LSETVTGDAA KQLLRQTVTD SSLAQCSYAM KFYVFRAAEK
     TGIYSELFSS MLDPWRSMMA NNLTTWAEDE VNARSDCHGW SASPVNEIVT QLFGVKPAEP
     GFERVRIVPR RELVAGADGV LHTSRGNIKV QWAPEQPLSV EATSKIHVEI VVNGRVVERV
     LGPGEPVIFA E
//
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