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Database: UniProt
Entry: F9FFH1_FUSOF
LinkDB: F9FFH1_FUSOF
Original site: F9FFH1_FUSOF 
ID   F9FFH1_FUSOF            Unreviewed;       862 AA.
AC   F9FFH1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=FOXB_05150 {ECO:0000313|EMBL:EGU84334.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU84334.1};
RN   [1] {ECO:0000313|EMBL:EGU84334.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU84334.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU84334.1}.
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DR   EMBL; AFQF01001679; EGU84334.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FFH1; -.
DR   STRING; 660025.F9FFH1; -.
DR   PaxDb; 5507-FOXG_15252P0; -.
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          155..319
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          335..436
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          441..780
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          782..849
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
FT   NON_TER         862
FT                   /evidence="ECO:0000313|EMBL:EGU84334.1"
SQ   SEQUENCE   862 AA;  95508 MW;  9D9BA63F76356D23 CRC64;
     MESETTITIV HVSFDHHHSG IGVATSRPSI SWRFGGTTVG WTQESCDIEV CLRQQASYPA
     ADAIQIFTLD TTDSVNVPWP ARELSSGEQA TVRVRSRGQS IETTWSEPFR VEAGLLKATD
     WTCDLIETPF LVETTETHPP TLFRRSFVLK QVPCKVRLYI TSHGIHEAEI NGIKVSDQVL
     APGWTAYDHE LQYQVHDVGQ LLRQGTENVI GIHVAEGWYC GRLGFGGGRH NIWGSRLGVI
     AQLVLTFQEE ITQTIGSDSD WTCHRSPIET AGLYDGETYD MAKEQVGWSS AGFNDEGWSA
     VKVCGYDPER LTCSDGPPIL PTQSLPAIQI THSINGNAIL DFGQNLVGWV QFRVPKGTAG
     HKITLVHAET LENGECVTRT LRHAKATDVV VLGQSSSPEE VYWNPRFTFH GFRYVEVIDW
     PEAELQLDDF SAVVIHSDMQ RTGYLTCSDP LVSRLHENVV WSMRGNFVGI PTDCPQRDER
     LGYTGDIQIF SPTACFLYDC YSTLRSWLRN LAAEQKEGAN GSPPIFSPNA MPVPNFPLAI
     WGDATILVPW DLYWAYGDVE ILSTQYETMI GWIDHGIPRA ANGLWGQVRV QLGDWLDPMT
     PPDRPHLGIT DSQLVANAYL IRITDVMSEA SAYSKHAVEL RAAFASEYIT QTGRLVSDSQ
     TAYALAIQFE LFPTPAQRNH AVERLQHLIL HRSRCKIATG FAGTPAIGHA LSKAGKDQLF
     YMMLTNTKPP SWLYPVTMGA TTIWERWDSV LPDGTIHPSE MTSLNHYALG AVADWLHAYV
     GGLKPLLPGW KKFRIAPKPG GGITWASASF ECPYGEIVVD WKLDDGNLVV EVKVPPNTTA
     EVQLGTKECE VVGSGFSHIP SC
//
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