ID A0A1S2PDZ4_9ACTN Unreviewed; 643 AA.
AC A0A1S2PDZ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alpha-fucosidase {ECO:0000313|EMBL:OIJ91837.1};
GN ORFNames=BIV23_39225 {ECO:0000313|EMBL:OIJ91837.1};
OS Streptomyces monashensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIJ91837.1, ECO:0000313|Proteomes:UP000179642};
RN [1] {ECO:0000313|EMBL:OIJ91837.1, ECO:0000313|Proteomes:UP000179642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 1 {ECO:0000313|EMBL:OIJ91837.1,
RC ECO:0000313|Proteomes:UP000179642};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 1.";
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}.
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:OIJ91837.1}.
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DR EMBL; MLYO01000082; OIJ91837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S2PDZ4; -.
DR OrthoDB; 5526311at2; -.
DR Proteomes; UP000179642; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF00754; F5_F8_type_C; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SMART; SM00231; FA58C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000179642};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..643
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039297446"
FT DOMAIN 492..635
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 507..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 69666 MW; 9B9F20F6383343D0 CRC64;
MPESTSRRSV LAAMAAMTVA AAGGSVTVAA PADAAPDAPL PLPLPALRIP RTDMGVEQQP
DSAIEWLQDA KLGMFIHWGV YSGPAKGEWW MHSAPITPAD YRKYVTDATD EQFTADAYDP
TAWARLAKDF GARYVTLTTR HHDGFALWPL NHPNSWNSGQ APLGRDFVGE YVAAVRAAGL
KVGLYYSPID WRYPGYYDVR GTHCAPNPWN YTTDPAHKEN ARVMKTEVYQ SVKELVTRYG
PIDDLWWDGG WLAEQGSDAD AAFFWEPGRY RDPANEWPVD AAYGETDGDG RPLGLMGMVR
KHQPGIVATS RSGWTGDYAS DEGPSVPSGA IRTGLVEKVF TVDGTWGYNS GATVMSYGTA
MDILVNCWVR NMTAMVNVGP DRHGTVSDAQ AGLLRRIGTF MASCGRSVYG TRGGPWHPVD
GQYGFTCKDD TFYVHLLPGY SGTSFTIPPL GDARIVRAFD VRTGAALAYS AGGDGRVTIN
GIDRTAHAED SVVGVTLDRS VQPADIAAGR TATADSEESS KGNTAARAVD GSTSTRWCAN
DGGTGHWLKV DLGSPRSLTG TRIAWELDGV NYRYSIEGSV DNRRWNTLAD DTATTSTSQV
QVALFRSRAR YVRVTVTGLP SGAWASIRTF EVYDRPFSTD LGS
//
