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Database: UniProt
Entry: G2YFE0_BOTF4
LinkDB: G2YFE0_BOTF4
Original site: G2YFE0_BOTF4 
ID   G2YFE0_BOTF4            Unreviewed;       909 AA.
AC   G2YFE0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=BofuT4P142000003001 {ECO:0000313|EMBL:CCD50488.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD50488.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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};
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DR   EMBL; FQ790326; CCD50488.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2YFE0; -.
DR   STRING; 999810.G2YFE0; -.
DR   eggNOG; ENOG502QW2K; Eukaryota.
DR   HOGENOM; CLU_002926_1_1_1; -.
DR   InParanoid; G2YFE0; -.
DR   Proteomes; UP000008177; Unplaced contigs.
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; 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:SF5; CELLULOSE-BINDING SDE182 NUCLEOSIDE HYDROLASE-LIKE DOMAIN-CONTAINING PROTEIN-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   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCD50488.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT   DOMAIN          164..340
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          352..446
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          467..806
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          808..875
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   909 AA;  103409 MW;  560A75EA65E9E983 CRC64;
     MKITSCGIHG FHETVGIDSD VLLFHWKLEG DLEGEKQDAY QVIVRKGADS GEVLWDSGRC
     HGPQQRNIRC EPQGGFESCT YYVWEVTSWN QHGETCKKSA DFFTAYPRSD HLPPLSMNQT
     YMPHTALIFR TWFEDIENKW KAWWIGDGGE KPLYLRKTIT LERKPTRAVA FVCGLGHHQF
     RVNGQAASEH VLDPGWTDYH TTVQYVAHDV TERLSVGENV LGAHIGNGFY AGDQGDRFFW
     PKYEDNTYVR YGNELCFFAE LHLFYEDGSH VVEISDDKWR VAPSATLLAN IYASETHDRR
     LYPIGWDAPG FDDSSWKPAK GLTGPRGALK YQSQPPVILH ETFRPIKETS PRPGIICIDL
     GQNSSIMTEI EVEGETGSEI IIRYGETTYE DGTICMPDPL FHEFETKVYS KFILAGTGGK
     EHWTPDFCFT SARYIQIEGV CNGKDTESKL PILHSVCGRH VSSASPRLGT MKTDKEDVNA
     LLSALKWTFS SNLFSYHTDC PQIEKFAWLE VTHLLAPATQ YMWNMESLYT KILDDILDSQ
     ERSGLIPTMA PEMRYMCGPL HDTITWGCAL ILIPDILQRY YGTTKSIAKM YRAGERYMAY
     MKGKERFGGL IEHGLGDWGR GIAHGNAQAN IETAIYHECL LCMSRFASHL NLDDEKKGWE
     KEAQRVYDVY NKHLLVTDDP SRPHAYYTSR DDYPNRDCDA VCQALALQFN MVPEAHISAV
     QASFLSDVSD GKLRSGEIGL RYLFNTLGDL GRSDLVLQMA RQEEHPSYMR FLRRGETTLL
     EFWQDECRSK CHDMLGSILE WFYVYVLGLK VGEKGWKTFT VAPDYHSEFG TVEGEFESPY
     GKIGLKWSKI GCGIELELSV PVGSTATVVL PKDNCHVEIH RHRVGDKKWV QQSKRVELEH
     GAYTLNFSI
//
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