ID W3WJW6_PESFW Unreviewed; 812 AA.
AC W3WJW6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN ORFNames=PFICI_14024 {ECO:0000313|EMBL:ETS74158.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS74158.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI912120; ETS74158.1; -; Genomic_DNA.
DR RefSeq; XP_007840796.1; XM_007842605.1.
DR AlphaFoldDB; W3WJW6; -.
DR STRING; 1229662.W3WJW6; -.
DR GeneID; 19279037; -.
DR KEGG; pfy:PFICI_14024; -.
DR eggNOG; KOG3340; Eukaryota.
DR HOGENOM; CLU_002934_4_1_1; -.
DR InParanoid; W3WJW6; -.
DR OMA; HRDTYGE; -.
DR OrthoDB; 2955544at2759; -.
DR Proteomes; UP000030651; 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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR000933; Glyco_hydro_29.
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 PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..812
FT /note="alpha-L-fucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004833601"
SQ SEQUENCE 812 AA; 89386 MW; 2F68413FA20C6CF6 CRC64;
MGRSRWVPCL TAILSTALAQ VYNPLYTSAQ LSAVSSLPID ISGLIDNKAF GTLPGDADFD
GKQSSYPAQY QPGANLTYGG VQYEFQGNGT YDNFVAQGQN LSFPPGKYSS INLLAAAESS
PTEGQITISY KGEPEVLAGV SVPPWWQWAF PPGGDIVLPF YFTNESTNYN KSHIYQRTLW
LDSSKELVGL QVPESDVGNR LHIFAATLTP TTTSANDTGT KLEVVYARST KKYAEASTTQ
IYEVAVSNVD DRAWVTANDS VQVTIESDGV TTTKAGIIKR LRPGDRVVVQ VEVENKQGVE
PGTVGVATAR LTSGAVDVKH DFEATFGIAP YEPTYESIFS HESPDWYNNA KFGIFIHWGL
YSIPAWGNTG SNETYAEWYW WNLNGGPDTS DRTYEYHLET YGPNFVYDDF ISNFSAAGFD
AKEWVDLFAD AGATYFVHVS KHHDGYALFD LPANVSQRTS VALFPHRDFI QETFAAAETY
QPQLHRAVYY SLPEFFHPDY VPYGFGRWPG GNATNPFTNE TLPYTGYVPV DDYVRDLVLP
EMQTLASLGT EIMWCDIGGP NLTTEFAAEW YNEAITQNRH VVMNNRCGVP GDFDTPEYAT
ISATQQRKWE SSAGMDPFSY GYNRATPPEG YMNASTIITN LVDIVSKNGN YLLDIGPVGN
GSILDIEAQH LRQAGSWIKD HGEAIFNTTS YFITPQEGDD VRFTTTTDAF YILVMNQLNS
TLTLTSAIPW IEGDVVTVLG GDLSGTAVPI QEVTVQGQPA LQLDISKDIQ DADQWTWVFK
ISYTPNVVDA AQAHVVDRAT AEAIIGPLVG AV
//
