ID A0A0T2KY36_9MICO Unreviewed; 760 AA.
AC A0A0T2KY36;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KRA24590.1};
GN ORFNames=ASD65_09345 {ECO:0000313|EMBL:KRA24590.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA24590.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA24590.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24590.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA24590.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24590.1,
RC ECO:0000313|Proteomes:UP000051216};
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, ECO:0000256|RuleBase:RU361161}.
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:KRA24590.1}.
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DR EMBL; LMGU01000001; KRA24590.1; -; Genomic_DNA.
DR RefSeq; WP_056221563.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KY36; -.
DR STRING; 1736570.ASD65_09345; -.
DR OrthoDB; 3187421at2; -.
DR Proteomes; UP000051216; 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; IPR019800; Glyco_hydro_3_AS.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216}.
FT DOMAIN 588..658
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 760 AA; 80492 MW; CD1298420DBEC6D2 CRC64;
MTDTTIQDAA AAAVADLTLE EKASLTSGAS FWYTKGVERA GIPSVMVTDG PHGLRKQRGS
ADHLGIGDSV PATCFPPAVG LGSSWDTELA YRVGEALGVE SSIEDVAVIL GPGVNIKRSP
LCGRNFEYFS EDPIASSVMA TALVQGTQST GVGTSLKHFA ANNQEHDRMR SSSDIDPRPL
REIYLRSFQR VVEDAQPYTV MCAYNRVNGV FASEDPFLLT QVLRNEWGFE GLVVSDWGAV
NDRIASIAAG MDLEMPSSGG ITDAQIVAAV QDGSLNESVV DVSATRIAKL ALRWKETPRV
AGPLDVDAHH ALAREVAGRS IVLLKNDGDL LPLQGQKSVA LIGAFVDQPR YQGAGSSMIN
PTRIDSVALE IVAKAGEDFV FQAPGFTLNG SGDAAALRAD AVALAAKNDV AVVFLGLPAA
AESEGYDREH IDLPAVQLEL LDAVLEVNPN TVVVLSNGSV VALPFADRVP AILEGWLLGQ
AGGGAIADVL YGDVNPSAKL TETIPVRLED TAAFLNFPGE DGHVRYGEGL FVGYRWYDAR
KIDVTFPFGH GLSYTTFGYG DAAASVNADG DVEVRVTVTN TGKRAGREVV QAYTGLASEA
VQRPERELKA FALVSLEAGE SREVLLTVRR ADLAYWNVRA DRWVVEGGAY TVDVAASSRD
IRSSTTVEVA GDAVVMLLNR ESSLAEVFAH PVAGPIMQQA MAQMASAMEG ASSIMPEGVD
MQKMMGSFPI GRIGMLAGDD FRPEQVDQLL AMANAATAGA
//