ID A0A2V4N8M6_9ACTN Unreviewed; 744 AA.
AC A0A2V4N8M6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:PYC79555.1};
GN ORFNames=C7C46_14480 {ECO:0000313|EMBL:PYC79555.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC79555.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC79555.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC79555.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL Submitted (MAR-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 -!- 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:PYC79555.1}.
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DR EMBL; PYBW01000043; PYC79555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4N8M6; -.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000248039; 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:UP000248039};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..744
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015955277"
FT DOMAIN 608..742
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 744 AA; 79920 MW; 829A2A026079D3A7 CRC64;
MAISRRAFLS SAAGIVAAAT ANLTIGTARA LAAPSSYSPT WASVDQHPAA PEWFQDAKFG
IYFHWGAFSV PAYGSEWYPR NMYIGGSDVN NHHIATYGDP SVWPYNNFLD GARDKAGNWV
QFAPKLASQG GSFDPDAWAQ LFVDAGARFA GPVAEHHDGF SMWNSSVNEW NSVQRGPKLN
LLQIFRDSIR GKGLKLLVAM HHAYNFNGYY DHAPAQPTAS LQKLFGQLGS TAENQLWYAK
LKEVIDLAQP DILWEDFDLS RVDETQRLNF LSYYYNQALG WGREVVATYK DGYDNLGEVF
DYERGGPGDI ANPYWLTDDS ISSSSWCYTV GIGYYSTQQM LHSLIDRISK NGNMLLNIAP
MADGTIPQGQ KDVLLGIGDY LGRFGESLYA TRAWTVYGEG PTKMGGGSFT TPVAGTNKDF
RFTRNKAGTV LYATVLGWPG SSTTISTLAS GRIDLSSLTS VQLLNSTTGT YLGLPAPTQG
SDGLHVTLPS SSAPFGALAY VLKFTFSGQI PVLQAGGTGV VTAYSDVSYA GTAAGLVLGT
YTAAQLQSAG LSPRTISSLR VPAGYQVTGY SGDNFTGTAW TFGADNADLR NTGNNDAITS
LKVAFDPAAY FRISNVTDGL ALDSGGNVAS GSNLKQWSWN GSTNLQWQAV DLGNGYYKLV
NRTNGMVADG WGSTADGSPA QQAAWNGGNN QQWQITNRGS GLYSIANRTT GLVLDGGGQV
ASGSVTKQWS WNGSPNLQWS FIAQ
//
