ID A0A101S1T0_9ACTN Unreviewed; 740 AA.
AC A0A101S1T0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:KUN65884.1};
GN ORFNames=AQJ54_19465 {ECO:0000313|EMBL:KUN65884.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN65884.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN65884.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN65884.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-2015) 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:KUN65884.1}.
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DR EMBL; LMWV01000016; KUN65884.1; -; Genomic_DNA.
DR RefSeq; WP_062238976.1; NZ_KQ948737.1.
DR AlphaFoldDB; A0A101S1T0; -.
DR Proteomes; UP000054375; 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; 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; PF14200; RicinB_lectin_2; 2.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00458; RICIN; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054375};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..740
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007105618"
FT DOMAIN 604..738
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 740 AA; 80072 MW; 3FF1247E7F1DD879 CRC64;
MISRRQFLAS ATGVAAAAAV GNVLTAGTAR AATTYTPTWA SVDQHTASPE WFKDAKFGIY
YHWGVFSVPA YDSEWYPRNM YISGSKANTH HIATYGDPSA WPYHNFINGA NDLNGNFNKF
APKLKSAGGN FDPDEWAQLF ADAGARFAGP VAEHHDGFSM WNSSVNEWNS VAKGPQLNLL
QLFTDSIRAK GLKLLVAMHH AFNFNGFYDH APAQSDPSLQ KLYGQLGTTA ENQLWYDKLK
EVIDLAKPDI IWQDFDLNKV NQTQQLNFLS YYYNQAEAWG REVVATYKDG FNGHGEVFDY
ERGGPGDITA PYWLTDDSIS SSSWCYTNGI GYYSTQQMLH SLIDRVSKNG NMLLNIAPMA
DGTIPQAQKD ILLGIGDYLK RFGESVYSTR AWTTYGEGPT HMGGGAFTAP KVGTAQDIRF
TRSKNNTVLY ATVLGWPGSA LNISTLNSAR INVGSLTSAQ LLNPTAGTYT SLPTPTQDSA
GLHVTLPSSS APFSALAYVV KLTFSGQIPT LKPQSGAVAY QDVNYLGGSA VLQIGTYTAD
QLSLAGLPSR TLSSLKLAPG HQIIGYSGDN FTGTAWTFTA DTADLRPSGT NDAVVSMKVQ
LNPSAWFRIT NVTDGLVLDS GGNVPSGSNL KQWTWNGSTN LQWQAVELGT GYYKLVNRAN
GMVADGGGAT TNGSPALEAT WDGSTKQQWQ LRYQGGGRYW ITNRATGLVL DGGGNVPSGS
VTKQWSGNSS TNVQWTFTAV
//