ID A0A1M6IW52_9ACTN Unreviewed; 1213 AA.
AC A0A1M6IW52;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SHJ38680.1};
GN ORFNames=SAMN02745244_02394 {ECO:0000313|EMBL:SHJ38680.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ38680.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ38680.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ38680.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZG01000044; SHJ38680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6IW52; -.
DR STRING; 1123357.SAMN02745244_02394; -.
DR Proteomes; UP000184512; 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-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:UP000184512};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1213
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012341711"
FT DOMAIN 366..437
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1043..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 129344 MW; 67055554A605913A CRC64;
MTPRSHQRRR KIIPLALVGV LASASVPNAV AATTEVEPNE LEIAGAALSR HAATQGMVLL
ENSDSALPLA RTGNVAVFGV GSYVTVKGGT GSGSVNNRYT VNVLTGLEDA GYLLTTSPGY
STPMRAAADA AVSGTTGIFG GVDYAGAEVA LTPETVLPTA PTDTALFVIA RNSGEFNDRR
SGKGDYQLND IERANIALLG KTYAKVIVVL NTGGIMDTSW YSAINAASED PAGGQPLDAL
LLMSQAGQES GHALVDVLTG DVAPSGKLTD TWASSYTYYP ASQTFASNDG DSLHEAYTEG
LYVGYRYFDS MYEKLAKNPD DVVRYPFGFG LSYTTFDIRA GKVEADSDTV TVRAKVTNTG
TSAGAEVVQV YVSAPQKGLD KPYQELEGFA KTDVLDPGQS QEVTIEFKLA ELASYSESRA
SWVLEGGDYI IRVGNSSRST HVATKLNVSS TVITERLSNQ LDGATFDELT SNPANFYSYE
GEATEIAAAQ TVNLNAASVK TVNNASDRAQ RIQVPTTSPL YPIDGTLVSS TTALIDPAQT
DWSGSGAPYV AKEGEKIKHV QTDPGATLYD VAKGELTMEQ FVAGLSNEQL ANIVEGAGTT
GSTLMLATGS GGYTTSRYEN LGIPGLGLQD GPAGLRLTQS STSRGVTTYQ WATAFPIGTM
LAQTFDPDLI TEVGEAIGKE MAEYGTTLWL APSLNIHRDP LNGRNFEYYS EDPFVSGIAS
VATTLGIQKT PGRGVAIKHY AANNQETTRT TSDSQISERT LREIYLKGFE MSVKGAAPMS
VMTSYNYVNG TYAAANYDLI EDVLRGEWGF EGLVMTDWGA GPRAGAPAVM YAGNDLIMPG
NNPTEVVTAV QKLNVDIDGS GLPVYISRTT ASNGRTSYTW QWGSFSPSAT GTETVSTVVN
STSDLTALKS QFVDVDVINN ETVTAHPGFA SVDAAYTEVT TLLGGSALTA AQRAAITVTD
VVRQDPADTA SPVVSYTVNV RGGYPARGVA MRLGDLQRSA VNILTVISQS APFEQLAETQ
GVDGISVAPY ADQFDLTRFL DSQVGEPTTE PTPKPTPTPT PTPKPTQSAT PWTPSAPYTI
PGTHQINGRT WLTTCSRYSQ TERCRTEIWA STVARDASGR FSMKQGWAFN NQTYLPYMTR
AQWAKNPLGH AGEWRATDGR QWRTECDTAA TGRGACRSYT MTTVYKATPK AGGGYTFSQQ
NEWVFNNIVM FRR
//