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Database: UniProt
Entry: A0A0D9MQJ1_ASPFA
LinkDB: A0A0D9MQJ1_ASPFA
Original site: A0A0D9MQJ1_ASPFA 
ID   A0A0D9MQJ1_ASPFA        Unreviewed;       915 AA.
AC   A0A0D9MQJ1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=AFLA70_390g001150 {ECO:0000313|EMBL:KJJ29003.1};
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392242 {ECO:0000313|EMBL:KJJ29003.1, ECO:0000313|Proteomes:UP000032444};
RN   [1] {ECO:0000313|Proteomes:UP000032444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70 {ECO:0000313|Proteomes:UP000032444};
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 flavus AF70.";
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:KJJ29003.1}.
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DR   EMBL; JZDT01000912; KJJ29003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9MQJ1; -.
DR   OrthoDB; 5488371at2759; -.
DR   Proteomes; UP000032444; 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}.
FT   DOMAIN          159..331
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          341..444
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          449..798
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          800..881
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   REGION          895..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  102061 MW;  48545DF4A7C9E247 CRC64;
     MAKISALRFE QHSTGLGIQC SSPRISWTFC AIDDSICDWT QSQYQISVYR ETGSSVEVVV
     DSHVSSLVPW PATPLQSRER ASVRVRVYGI WMDRATKRQH SGWSAWSSWA IVECSLLSRQ
     DWSAVPISSS SIPASHEDEP LRPLLFRKSF VLPATFTSLH RARLYITALG VYRAYINGSR
     VGDHEMAPGW SSYRHRLAYQ VFDVDSLINP SCNNVLSVEV AEGWFAGRLG FSGGKRNIYG
     SCMAVMAQLE VDGVGGERFQ VTSDSSWKCH RSPIISSEIY NGEVYDARAE VGDWNRHGPL
     YLDENWEKVS ILDFPSARLY APNAPPARIT EYLAPQKIFT TPSGRLILDF GQNLVGKLLI
     HSMTLPVDAT VSFTHAEVME NDGELGTRPL RGARCVDTII SSGQKLVDWS PKDTFHGFRY
     VQVDGWDPRT VPFWRTNIRA LVIHTDFKRT GLFECSNSLI NQLHKNACWS MRGNFLSLPT
     DCPQRDERLG WTGDIQIFGP SATFLYDSIG MLSEWIEDVA CEQSDYHGVP PLVVPNILNH
     VWPSMPQAVW GDVVIILPWT LYLSSGDRDM LHRQYSSMAL WLDQGIRRGK DGLWDPELWQ
     LGDWLDPQAP PDEPGDCRTR GTLVADAYLV YVTSLMGNIS AIIGRDAESA HYRQTAQRLR
     TLFQNKYITS SGLVVGDSQT AYSLALVFGL LSTKEQLATA RSQLAERVRI AKFRVATGFA
     GTPIILRALT ESDNLSLAYR MLLEERCPSW LYPITMGATT VWERWDSMLP DGAINPGEMT
     SFNHYALGSV VAWLHETVGG LRPLQAGWKS ALVSPKPGGS LTHATVSYES VYGHWSCAWK
     LVPDGARDER MTLCLDLIVP PNCHAVVQIQ AGADGSGNRE ERVGSGRHQW KIPFSPGPWP
     PKATAPFIKN PGQGL
//
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