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Database: UniProt
Entry: A0A0S8EDP6_9BACT
LinkDB: A0A0S8EDP6_9BACT
Original site: A0A0S8EDP6_9BACT 
ID   A0A0S8EDP6_9BACT        Unreviewed;       640 AA.
AC   A0A0S8EDP6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN   ORFNames=AMK72_09675 {ECO:0000313|EMBL:KPK46536.1};
OS   Planctomycetes bacterium SM23_25.
OC   Bacteria; Planctomycetota.
OX   NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK46536.1, ECO:0000313|Proteomes:UP000052058};
RN   [1] {ECO:0000313|EMBL:KPK46536.1, ECO:0000313|Proteomes:UP000052058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_25 {ECO:0000313|EMBL:KPK46536.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK46536.1}.
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DR   EMBL; LJTY01000207; KPK46536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8EDP6; -.
DR   PATRIC; fig|1704028.3.peg.2008; -.
DR   Proteomes; UP000052058; Unassembled WGS sequence.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; 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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..640
FT                   /note="CBM6 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006645067"
FT   DOMAIN          510..632
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   640 AA;  71675 MW;  E5325FB16AF17B3A CRC64;
     MVKHVLTIAA LMTAGGGVAA CGQGKPFTAD WASLKRHEAA PKWFRDAKFG IYFHWGVYSV
     PAFGSEWYPR NMHLKNHREY KHHVQKYGDP TKFGYHDFVP MFKAEKFDAD EWAALFTKAG
     ARFAGPVAEH HDGFAMWASK LTPWNVKDTG PKRDITGELA KAVRKRGMKF VVTFHHARNS
     LHEVERRGGK AWTGHYDGVR SNFPSLLEDP KRAILYGYMP REKFLELWLG KLKEVIDNYQ
     PDLMWFDSWL NEIPEKHQMA YLAYYFNKAR QWGKDVVVTR KQRDLPLELS VEDFEKGRLD
     RLSDHAWLTD DTISRGSWCY TESLRIKPTR EVLHVLIDIV SKNGCLLLNI SPKADGTIPN
     NQKEVLLGVG AWLGKFGEAI YQTRPWVVFG EGPTRMKRGG HFVGSLSYTA ADVRFTTKGD
     VLYAIFLGAP KGAARITSLA KGSGLFGGEV ERVSLLGRDG AVKHKQDEKG LHVTFPARLP
     HELAVALKIE GLKLAGFKPD LSIRFSDGKA VLDASRAALH GPGIATERRD DGKANIGFWD
     DPSAWASWEV RFPKAGTYEV HGRFAALRQG TFTVQVGHAA LKGQPPVTGN WGEFKTVSLG
     TITVAKAGRQ EVKVVPVRSG WAAMNLAWLE LRQSAATRRP
//
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