ID A0A395MKY5_9HYPO Unreviewed; 609 AA.
AC A0A395MKY5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN ORFNames=FIE12Z_7286 {ECO:0000313|EMBL:RFN48477.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN48477.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN48477.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN48477.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RFN48477.1}.
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DR EMBL; PXXK01000208; RFN48477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MKY5; -.
DR STRING; 2594813.A0A395MKY5; -.
DR OrthoDB; 2955544at2759; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.20.10; Crystallins; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR011024; G_crystallin-like.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF16757; Fucosidase_C; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49695; gamma-Crystallin-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..609
FT /note="alpha-L-fucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017367025"
FT DOMAIN 427..514
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
SQ SEQUENCE 609 AA; 67752 MW; 053803DE9FB2D4EF CRC64;
MMTLSNKATA LVALACTLFP LDTTAQAKGP YEATWESTDK HHAAPEWYRD AKFGVYWHWG
AFTTAQYASE WYPRNMYEPD SDQKKHHTET YGPPEEWGYE NFIKGAKDKK GNFVQFKPVL
KSKGGEFDPE AIMKVVKASG ARFAGPVAEH HDGYSMWDSK VNEWNSVKYG PKLDLVKLWA
DLVRQNDMKL VVAMHQAYNY NGFFQWAPKT NDTSLQKLLG QLPREEEDQL WFDKHREMLD
HVKPDIIWND FSLDSPGECG SAEGPCAVDE KKRLEFLAYY FNRGEEWGKE VVTTYKHHDH
GFRNTSAVDD WERGGPANLV RPYWQTDDAI SASSWSYTVG IKYYSSKAMV HSLIDRVSKN
GNMLLNISPK ANGVLPEEQI KVLEDIGDFL GRYGEAIYDT RAWDLYGEGP NQVEGGAFTA
PLQGNSSDIR FTRNQDDDTL YVTVLGWPED KLVSIKNLGS DTLVDLKSLK SIELLGDKAG
DYVKVSDWDQ GKDALEITLP SQPAESLAYV LKMTFDGGIP VPLPKGGAAV FSGADATGTG
VSLEAGTFDT VFLTEAGLEP KKIGSIRVAE GAKATVFTGF RFTGESKELK AGEHKLDAGS
VGSIVVSKA
//
