ID A0A2U2PIN9_9SPHI Unreviewed; 522 AA.
AC A0A2U2PIN9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Ricin B lectin domain-containing protein {ECO:0000259|Pfam:PF14200};
GN ORFNames=DDR33_07775 {ECO:0000313|EMBL:PWG81265.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG81265.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG81265.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG81265.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:PWG81265.1}.
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DR EMBL; QEAS01000005; PWG81265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2PIN9; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000245647; 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:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
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 PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000245647}.
FT DOMAIN 95..181
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 321
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 522 AA; 56761 MW; 71F131EB92B138EA CRC64;
MKERSFTAIL AAFLLLTAAC QKETLKGEND SGDGGTKKNG AKTSDAPPLG TLIDGAVYRI
RGVSSLPGGP VVEVTGNSTA ENAKIQQWGW FPNSGQKWKL VKVDATYYKL INMTSNKCLE
SPSATSGDIL QQATDDGSDS QLWTIAYSSG STNLFSLTNK ATGMKMAVDP GDSTPGRKIR
QLSTISGTQD LFNFHNVNFR NPLINASRAD PYVAQKDGNY YFMYTRGSNL AIRKTTSMSL
LANATDVVVF TPPSGTDHSS NLWAPELHFL SGKWYIYFAA NDGNGDNHRM FVLENSNSDP
TTGTWTFKGK ITDPSDQWAI DGSVLTVGSS NYFIWSGWES VASRYKQYIY LAPMSNPWTI
SGPRVKISSP TNTWEKHEPS SIGAGVNEGP IMLQKDASSP VFVIFSASRY TSDDYCLGQI
QLKAGGDPTV AADWINKKQV FVRNDANSVY GPGHNGFFTS SYTDPNGVSK TENWFIYHAR
SAPNNTGSRT PRMQKLTWNS DGSPNFGTAV ANGVDIPIPV GE
//
