ID A0A370B662_9ACTN Unreviewed; 489 AA.
AC A0A370B662;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:RDG36152.1};
GN ORFNames=DVH02_21580 {ECO:0000313|EMBL:RDG36152.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG36152.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG36152.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG36152.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-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:RDG36152.1}.
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DR EMBL; QQNA01000175; RDG36152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370B662; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000253741; 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; -; 3.
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; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 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, ECO:0000313|EMBL:RDG36152.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253741};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016563123"
FT DOMAIN 350..425
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT DOMAIN 433..488
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT SITE 159
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 489 AA; 52221 MW; EF497F2F3CFE6FEC CRC64;
MSRTERQPAL LIAVLLVVLA GLVAAVAPTA GAAEGRPYTN PVKDRKGADP WIEFYDGDYY
LITTSWTSEL TMRKSPTLAG LATAPSVQVW SDSTSSRCCN MGAPEIHFRD GRWYLYYVAG
QGIADYNPTQ RVHVLESAGS DPMGPYTYRN QLGATRILDA GLLTLNGSLY LLGSASGGGT
RNLVIAPMSN PYTLSGGFST ISTPTYGWER SGGTVNEAPE VIQHAGKTFV VYSASGCWTP
DHRLGRLTFT GTDPLSASSW TKKSTPVFGR SDAAGVYGPG HNGFFTSPDG TENWIVYHAN
NSASGGCDNG RTTRAQKFTW NADGTPDLGT PLALGTTRPG PSGESAATPT GYTLVNRDSG
KCLEVEGGSA ADGAHVIQWS CDGGTNQRWR VEDLGNDTSR LVNAASGKVL DTADCSVVDG
AELRQSSWLN NLCQAYRFVV TDRGGWIRLV NARSGKVADV ENCSTADGAD VRQWSWLGNA
CQQWQLRPV
//
