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Database: UniProt
Entry: A0A0F8XA34_9EURO
LinkDB: A0A0F8XA34_9EURO
Original site: A0A0F8XA34_9EURO 
ID   A0A0F8XA34_9EURO        Unreviewed;       897 AA.
AC   A0A0F8XA34;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, 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};
DE   Flags: Fragment;
GN   ORFNames=ARAM_002171 {ECO:0000313|EMBL:KKK26410.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26410.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26410.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26410.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
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:KKK26410.1}.
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DR   EMBL; JZBS01000399; KKK26410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8XA34; -.
DR   STRING; 308745.A0A0F8XA34; -.
DR   OrthoDB; 5488371at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000034291; 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; IPR008979; Galactose-bd-like_sf.
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; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          152..320
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          333..431
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          435..794
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          796..880
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKK26410.1"
SQ   SEQUENCE   897 AA;  99116 MW;  C9AAF24276590E79 CRC64;
     SSIPDPNMAL SVSKVFFEHH RTALGIGETS PRISWRFDGK VSDWYQSAYE LEIRRVGQEP
     ATTFHIDSSD SVLVPWPSDP LNSGEEATVR VRSFGHKHQP STPWSDPVTV EPGLLSPDAW
     QGAAAIGSDR PTEVNRTHRP IYFRKEFILD EQVLAARLYI TALGLYEARL NGQRVGDHVL
     APGWQSYKHR HEYNTYDVTD LLRHGQNSVA VAVGEGWYSG RLTWASFRNI YGDTLGMLCL
     LAVTNSNGTR TYVPSDGTWK SSTGPLLTSE IYDGETYDSR LEMDGWDSPG FNDSSWLGTH
     EVPFSKQVLA APDAPPVRRV AEHKLVNVFP SASGKPVLDF GQNLVGWLRI RVKGPRGQTI
     RFLHTEVMEN GEVATRPLRT AKATDYFTLS GDAVQGWEPS FTYHGFRYVQ VDGWPAETEL
     NADSVTAIVV HSDMEQTAFF ECSDPLINRL HKNIVWSMRG NFLGIPTDCP QRDERLGWTG
     DINAFSRTAN FMYDTAGFLR GWLRDAYSEQ QENSCKFSES SFLYIFAPPQ TIPNVLGPSS
     PATSIWGDSI VGVPWQLFQS FGDKAMLQEQ YPGAKDWIDR GIIRNEVGLW NRSTFQYADW
     LDPKAPPDSP GAATTNSYLV SDAYLIHSTE MVANMSSALS LAQNAEGYAS SRAALTKAFQ
     DAWISDSGLV ANETQTGLTL PLYFKLFAKP AHYTAAIGRL VDMITQNEFK VGTGFAGTHL
     LGHTLSAYGA ADTFYNMLRQ KDVPGWLFQV IMNGTTTWER WDSMLANGSI NPGEMTSFNH
     YAVGSVGSWI HESIGGLSPQ EPGWKKFNVE IIPGGGLDEA STQFLSPYGL IATQWSVDAH
     KGEGCAKGTR NFQLALEVPP NTQATVKLPG NGKGKGKGKK ILVVGSGVYH YQACLTT
//
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