ID A0A1I5CZ80_9ACTN Unreviewed; 743 AA.
AC A0A1I5CZ80;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:SFN92272.1};
GN ORFNames=SAMN04487980_10385 {ECO:0000313|EMBL:SFN92272.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN92272.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFN92272.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFN92272.1,
RC ECO:0000313|Proteomes:UP000198530};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOUV01000038; SFN92272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5CZ80; -.
DR Proteomes; UP000198530; 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; 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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR006311; TAT_signal.
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 Pfam; PF14200; RicinB_lectin_2; 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.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011516020"
FT DOMAIN 419..505
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT DOMAIN 653..728
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
SQ SEQUENCE 743 AA; 80862 MW; 1E2FE6DD015103E8 CRC64;
MPRPINRRAF LACATGVAAA AVAGGLLGSG SAYAAPATYT PSWDSVDQHP PAPEWFKDAK
FGIYFHWGVF SVPAFESEWY PRHMYQNNST AKQHHVATYG NPSSWPYHNF INGANDLAGN
HAEFAPKLKS AGGNFDPDEW AQLFVDAGAK FAGPVAEHHD GYSMWDSQVN EWNSVDKGPH
LDLLELFTDA IRARNLKLLV AMHHAYNYTG FFEFAPAQSD PSLKKLYGQL GSAQENQLWY
DKLKEVVDRA RPDILWQDFR LDHVDETQRL NFLSYYYNQA NSWGKEVVAT YKDGFNSHGA
VFDYERGGPS DLTAPYWLTD DSISSSSWCY TEGIGYYSVK QMVHSFIDRI SKNGNVLLNI
APKADGTIPQ AQRDILLGIG DHLGRFGESI YSTRAWTAYG EGPTKMGGGA FVQPTTGTAQ
DIRFTRNKAN TVLYATVLGW PGSSLEIKTL NSGRINLGSL TSVKLLDSTA GTYISLANPT
QNASGLQVTL PSSAPFSAHA YVLKLSFSGE IPGLKPLAGA VAYTNVGYAG DAAVLALGSY
TADQLTQAGV PPLSVSSLRV APGHQVIGYS ADDFGGTSWT FGADNSDLRN TGNNDRITSL
KVVLNPSAWL RITNVTNGLA LDSGGNVAGG SNLKQWTWDG SNNLQWHAID LGNGYYKVEN
RANGMVADGW GATTNGSACR QLEWNGHTNQ QWKITYRGDG RYSLTNRTTG MALDGGGNVA
SGSNAKQWRF DNSTNLLWTF TAL
//
