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Database: UniProt
Entry: A0A1S3V2M1_VIGRR
LinkDB: A0A1S3V2M1_VIGRR
Original site: A0A1S3V2M1_VIGRR 
ID   A0A1S3V2M1_VIGRR        Unreviewed;       491 AA.
AC   A0A1S3V2M1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN   Name=LOC106771139 {ECO:0000313|RefSeq:XP_014512545.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014512545.1};
RN   [1] {ECO:0000313|RefSeq:XP_014512545.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014512545.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC       1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC       carbohydrate moieties of glycoproteins.
CC       {ECO:0000256|ARBA:ARBA00004071}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951}.
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DR   RefSeq; XP_014512545.1; XM_014657059.2.
DR   AlphaFoldDB; A0A1S3V2M1; -.
DR   STRING; 3916.A0A1S3V2M1; -.
DR   EnsemblPlants; Vradi08g19330.1; Vradi08g19330.1; Vradi08g19330.
DR   GeneID; 106771139; -.
DR   Gramene; Vradi08g19330.1; Vradi08g19330.1; Vradi08g19330.
DR   KEGG; vra:106771139; -.
DR   OrthoDB; 2955544at2759; -.
DR   Proteomes; UP000087766; Chromosome 8.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF37; ALPHA-L-FUCOSIDASE; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..491
FT                   /note="alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010349988"
SQ   SEQUENCE   491 AA;  56389 MW;  1C3DD1C44B516E14 CRC64;
     MVRLRLWWCS FLITLTVLFE QVRICSCWNE QTPTPPLPIL PLPTYSQIKW QQREIIMFLH
     FGVNTFTDRE WGTGHENPAI FNPTRLNTTQ WATVAADAGI SLMILTAKHH DGFCLWPSKY
     TNHSVIRSPW QGGKGDVVRD FVNAATAHGI DVGIYLSPWD RHDPRYGNDL LYNQYYLAQL
     QELLKKYQNV REIWFDGAKG AQAKNMSYYF SDWFSMVKEL QSSINIFSDA GPDVRWVGEE
     TGSAGYTCWS TINRTSLSIG NSSITEYLSS GDPKGTDWLP AECDVSIRPG WFWHESESPK
     RLSKLLDIYY NSVGRNCVLL LNVPPNKSGL ITDVDAQRLK EFRSAINTIF QHNLAEDSFV
     KVSSQRGGFG PENMLDTDHL WSYWTPKDDG GEKDHWIEIW AKDESFLRFN VISIQEAIGL
     GQRIKRHEIY ADDKLIVKAT TVGYKRLHRL DRGEVQARVV RITIRESKAV PLISSIGLYF
     DPFWHSKFTV T
//
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