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Database: UniProt
Entry: A0A226H6W9_9FLAO
LinkDB: A0A226H6W9_9FLAO
Original site: A0A226H6W9_9FLAO 
ID   A0A226H6W9_9FLAO        Unreviewed;       686 AA.
AC   A0A226H6W9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Ricin B lectin domain-containing protein {ECO:0000259|SMART:SM00458};
GN   ORFNames=B0A66_13740 {ECO:0000313|EMBL:OXA90059.1};
OS   Flavobacterium hercynium.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=387094 {ECO:0000313|EMBL:OXA90059.1, ECO:0000313|Proteomes:UP000198345};
RN   [1] {ECO:0000313|EMBL:OXA90059.1, ECO:0000313|Proteomes:UP000198345}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18292 {ECO:0000313|EMBL:OXA90059.1,
RC   ECO:0000313|Proteomes:UP000198345};
RA   Stine C., Li C., Tadesse D.;
RT   "Whole genomes of Flavobacteriaceae.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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:OXA90059.1}.
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DR   EMBL; MUGW01000026; OXA90059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226H6W9; -.
DR   Proteomes; UP000198345; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09004; GH43_bXyl-like; 1.
DR   CDD; cd00161; RICIN; 2.
DR   Gene3D; 2.80.10.50; -; 6.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 3.
DR   SMART; SM00458; RICIN; 2.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198345};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   DOMAIN          304..441
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   DOMAIN          450..587
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            129
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   686 AA;  76534 MW;  929891AA5EBA9B9D CRC64;
     MLIGIVIPAH AQLSGNPLFT GADPEIHYFN NKYYIYTTAI YGTQFHAYSS NDLTNWHDEG
     LIFDLFPDSP WAQYNGWAPA VVFRNNKYYF YYTAETKIGL AVGNTPIGPF TDIGAPLIAT
     DPYTDDIIDA NVFIDDDGQA YIYYGGSGKS RMVVRKLNAD MISLATGPTD ITPQNYTEGP
     YMVKRKGIYY MMYSNGAWFN DSYNVQYSTS NSPMGPWTYR GKVLSSNAED KGPGHHGVLK
     IGNCDEYYMV YHRYENGTSG ERKIAIDRMY FNSNDLIEPV NMTNYGVAPR VPDQSCPTQN
     ITSGGIYKLT HKGTNQCLDV VNNASQSGIN VQQSTDNGND AQRWVITLEA DGYYKLTHKG
     TNQCLDVANN SNQPGANVQQ WVDNNNDAQR WKIELMSDGY CKLTHKGTNQ CLDVKDNSNQ
     SGANVQQWTD LGTDAQRWKL DLIEVPIVSG GVYKLTHKGT NQCLDVSDGS TQQGANVQQY
     TGNDTDAQRW VITKESDGFY KLTHKGTNQC LDVDNNSSQP GANVQQWSDL GTDAQRWKIE
     LMSDGYFKLT HKGTNQCLDV ANNSAEPGTN VHQWTDNNND AQRWKLDLIK PVTPSSTAKS
     SKSIVGNQDE ALANTVTIYP NPVKNRLFIN SEIKDMKISI FSQTGSLVKV QRNIDNSVDV
     SGLTSGIYFA VFEKDNTKIT KQFIKE
//
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