ID F9YQI4_CAPCC Unreviewed; 737 AA.
AC F9YQI4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Beta-D-glucoside glucohydrolase {ECO:0000313|EMBL:AEK23523.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:AEK23523.1};
GN OrderedLocusNames=Ccan_14070 {ECO:0000313|EMBL:AEK23523.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23523.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23523.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; CP002113; AEK23523.1; -; Genomic_DNA.
DR RefSeq; WP_013997511.1; NC_015846.1.
DR AlphaFoldDB; F9YQI4; -.
DR STRING; 860228.Ccan_14070; -.
DR KEGG; ccm:Ccan_14070; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_4_1_10; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000008895; Chromosome.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:AEK23523.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEK23523.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..737
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003392296"
FT DOMAIN 655..725
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 737 AA; 81778 MW; FA41FDF7DE6814DE CRC64;
MKKITIKTIF LFCAIGFLSA QEKSPIYLDN SQPIEKRVED ALSRMTLEEK VAMCHAQSKF
SSPGVPRLGI PENWMTDGPH GIRPEVLWDE WNQAGWTNDA CTAFPALTCL AASWNPEMSL
LYGKAIGEEA RYRNKNVLLG PGVNIYRTPL NGRNFEYMGE DPYLASKMVV PYIQGVQSNG
VAACVKHFAL NNQEINRHTV NVKLSDRALY EIYLPAFKAA VQEGKTWSIM GAYNKYKDQW
ASQNKYLLVD ILRNEWGFDG AVVSDWGAVN NTDHAAHHGL DMEFGTWTDG LTENKANAYD
HYYLAQPFLQ KLKSGEIKEE VVNEKVRNIL RLVFRTNMAP NRPFGSFASP EHFAVARKIG
QEGIVLLKNE RNVLPLNLKK AKRIAVIGEN AIKVMTVGGG SSSLKAVHEI LPFDGLKKRI
GNEAEVVFAR GYASDDYKDQ DGLSAGQNIA DKRPASEMIA EAVNVAKSAD YVIFIGGLNK
HDGQDCEGND RKSYGLPYGQ DAVISALSKV NKNLIVVMIS GNAVAMPWVN EVPAIVQNWY
LGSEAGNALA DILAGDVNPS GKLPFTFPVK LQDNGAHAMG EYPGGENETY HEGILVGYRW
ADTKKIKPLF AFGHGLSYTT FEYGKVSANK KTMSANDKIT FSVSVKNIGN RDGAEVVQLY
IRDVKSSVVR PYKELKGFEK VYLKAEESKI VKFTIDKEAL SFFDEKKHDW VAEKGEFEAI
IGSSSADIKT RISFSLK
//