ID A0A495ECJ3_9FLAO Unreviewed; 520 AA.
AC A0A495ECJ3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:RKR14349.1};
GN ORFNames=CLV91_0424 {ECO:0000313|EMBL:RKR14349.1};
OS Maribacter vaceletii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR14349.1, ECO:0000313|Proteomes:UP000269412};
RN [1] {ECO:0000313|EMBL:RKR14349.1, ECO:0000313|Proteomes:UP000269412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR14349.1,
RC ECO:0000313|Proteomes:UP000269412};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-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:RKR14349.1}.
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DR EMBL; RBIQ01000007; RKR14349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495ECJ3; -.
DR OrthoDB; 1095333at2; -.
DR Proteomes; UP000269412; 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; 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; IPR000933; Glyco_hydro_29.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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 PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000269412};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..520
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019869577"
FT DOMAIN 420..498
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
SQ SEQUENCE 520 AA; 59699 MW; A9D409D6A0BFE840 CRC64;
MRIVPLKSLF FCTFLFLSAI SFSQENPPKK FEQNWESLSK INETPDWFLD AKFGIYAHWG
PVSSAFVGAD PDKHYAGWHG MKMYDNGKLD KTKKGQPTNN YIHHRKKYGN PSKYGYKHII
EQFDPSGFNA KEWANLFALS GAKFAGPVAM HHDNFAMWDS KATRWNSMNY GGIDPSAELK
KEIEAKGLKY MGSFHHAFTW KYFSTAHAYG GVKAKDYDLY TNPHSLDSDV PDEQFYKDWW
AKLKEFIDVY QPDLIWFDWW LENMTDESRQ KFLAYYYNKG IEWNKEVAVC YKESTFPEDT
AIKDYERGRP NQPKEQAWLT DTSPGAWFYR PNAEFKTPNE LVDILIDIVS KNGNMLLNVP
PNPDGSIPPV MVNLLTEMGQ WLKINGDAIY GTRPWTVFGE GPTRLPEGGH KVEKIKIEYT
DKDIRFTKKS DKEFYAIVMA EANGETVIKT LSTDIGVLNS KITKIELLGS SEKVVWERNS
KGLVIKAPKK TPSTYAHAYK ILLEGYTENN IGGDQNAHTE
//
