ID A0A0Q4KQ06_9SPHN Unreviewed; 770 AA.
AC A0A0Q4KQ06;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KQN24365.1};
GN ORFNames=ASF00_16120 {ECO:0000313|EMBL:KQN24365.1};
OS Sphingomonas sp. Leaf34.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN24365.1, ECO:0000313|Proteomes:UP000051932};
RN [1] {ECO:0000313|EMBL:KQN24365.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN24365.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN24365.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN24365.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KQN24365.1}.
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DR EMBL; LMLC01000005; KQN24365.1; -; Genomic_DNA.
DR RefSeq; WP_055881648.1; NZ_LMLC01000005.1.
DR AlphaFoldDB; A0A0Q4KQ06; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000051932; 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 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:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..770
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006224685"
FT DOMAIN 682..749
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 770 AA; 80772 MW; CAD2135922A45042 CRC64;
MIASGTKAPI GRRLAGSAVL ILAALSPAVA QTTNNAPAAA AARTQAPQAR PWMDTSLSAD
ARVDLLLKQM TLDEKLQLTF GYFATSADWL KTPIKNWVYP KDGLAASAGI VPGIPRLGIP
NQWQTDAGVG VASQRGPTPR LRTSLPSGIA TAATWNPELA QAGGAMIGRE AFLSGFNVQL
AGGMNLTREP RNGRNFEYGG EDPLLAGVIT GHEIKGIQSQ HVVSTMKHYA FNGQETNRNN
IDHRIGEQAA RQSDLLAFEI ANEVGQPGSV MCAYNRVNGH YACENDWLLN KVLKRDWGFK
GYVMSDWGAT HSTSEAANAG LDQQSGWAFD RSAYFADALR EAVNNGHVSE ARATDMARRV
LWGMVSVGAF DTVVTGDQAT KIDYAAHAAV TRADAEEGIV LLKTTAGLLP IAKTAKSILL
IGAHADVGVL SGGGSSQVYS HNAPTNGLVV PDAFPSGFPG PKTYHASSPM KALQARTGAT
VTYLDGKDVK AAAAAARTAD VVVVFGEQWT GESIDVPDLN LPDGQNALID AVARANKKTV
VVLETGGPVV MPWLGKVGAV LEAWYPGTAG GEAIARVLTG AVNPSGHLPA TFPASLAQTP
RPVLEGDPKL DRDSHPMGNY DIEGAAVGYK WFDKTGAKPL FPFGYGLSYT SFAMSGLTAA
ADGKGIKAGF NVKNTGAVQG KAVAQVYVSG AGWESPKRLG AFRKVDLAPG TEQTVSVTID
PRLLATFDVA SGGWRIAGGE YSVMLATSAA DVVQTVKVQI AAQTLDRTGK
//
