ID R1G4B2_9PSEU Unreviewed; 657 AA.
AC R1G4B2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:EOD66323.1};
GN ORFNames=H480_22162 {ECO:0000313|EMBL:EOD66323.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD66323.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD66323.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD66323.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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 -!- 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:EOD66323.1}.
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DR EMBL; AOUO01000319; EOD66323.1; -; Genomic_DNA.
DR RefSeq; WP_003091424.1; NZ_AOUO01000319.1.
DR AlphaFoldDB; R1G4B2; -.
DR PATRIC; fig|1292037.4.peg.4205; -.
DR eggNOG; COG3669; Bacteria.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000014139; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 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; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
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; PF14200; RicinB_lectin_2; 2.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 521..592
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT DOMAIN 602..655
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
SQ SEQUENCE 657 AA; 71391 MW; 7D688F95A37B2673 CRC64;
MSSFELSRRK LLAVTGVAVT ASVFRVRTVW ATEGPGSYTP SWSSVDQHPP APEWFQDAKF
GIYYHWGVFS VPAFGNEWYP RNMYVGGSNE NNHHKAVYGD PSAWPYQNFI NGARDKAGNW
VQFAPKLKSA GGNFDPAEWA QLFADAGAKF AGPVAEHHDG YSMWNSTANE WNSVRTGPQL
DLLRLHADAI RGKGLKLVTA LHHAYHFNGY YDHVPNQPTE SLRRLFGQNG RTAENQLWYD
KLREVVDGYQ PDLVYQDFDL NLVDESQRLN FLSHYYNQAV AWNKDVVASY KDGFNTRGEV
FDFERGGPGD ILNPYWLTDD SISSSSWCYT VGIGYYSVKA MLHSLIDRVS KNGNMLLNIA
PMADGTIPSG QRSILLGIGD HLKRFGESIY ATRAWSVYGE GPTKMGGGSF TTPVEGTKTD
IRFTRSKDNT VLYATVLGWP GSTFTITTLG SNRINLATLT SVQLLGPAAG GVTNLPTRSQ
DGSGLHITMP SSNPPFDALA YVVKLTFSGP IPTPGSGPLP TGWARIANVS SGLVLDGGGS
VASGSHLKQW NWDGSTNLQW QLADAGGGYY RLVNRTNGLV ADSGGNSANG AACLEATSNG
STNQQWRLTS LGNGRYQIVN RGTGTALDGM GRTAAGSEAG LWAPNSSTNN QWTITGV
//
