ID A0A183LDU9_9TREM Unreviewed; 525 AA.
AC A0A183LDU9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN ORFNames=SMRZ_LOCUS1974 {ECO:0000313|EMBL:VDO53490.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000197301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000197301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO53490.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO53490.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UZAI01000482; VDO53490.1; -; Genomic_DNA.
DR STRING; 48269.A0A183LDU9; -.
DR WBParaSite; SMRZ_0000197301-mRNA-1; SMRZ_0000197301-mRNA-1; SMRZ_0000197301.
DR Proteomes; UP000277204; 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; IPR018526; Glyco_hydro_29_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF2; TISSUE 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 PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 525 AA; 62279 MW; F9158728DA636C8D CRC64;
MNKFFYHILF IFIYYIIKIN CNINSKSINQ SIIYEPNWNS LDKRPLPKWY DEAKIGIFIH
WGVFSVPSYR TEWFWWMWQG DKTTMPEIPE YMRKYYEPDF AYANFAKQFH AEFFEPDKWA
DLFQKSGARY VVLTAKHHEG FCNWPSINSW QWNSMDIGPN RDLVGDLATS IRKRTKLRFG
VYHSLFEWFN PLYLYDKANN FTTQTFVEQK TMPELYDLVL RYKPEVIWSD GDAGPDTYWN
STQFLAWLYN ESPVKDTVVT NDRWGNGCLC KHGGYYSCDD RYHPGKLVRH KWENCMTLDC
CSWGFRREIT LDKILTPEQL ISEVIETVTF GGNILINVGP TSWGTILPIY EERLLQLGEW
LSINGEGIYA TQPWRIQKEP NYDFVWYTYK PALIDKNINE YMKMPFLYLL KIISSIKQNP
SIVYAHLTKW PNKYCHNLTE IINDQSIQTR TYCKRELHLT SINAHSNLSN FTLLDGSLTG
IQLSYRIMNK TTMNGVIINL PDLIMNNDNR NILNYAWTIR MINVF
//
