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Database: UniProt
Entry: A0A1M6IW52_9ACTN
LinkDB: A0A1M6IW52_9ACTN
Original site: A0A1M6IW52_9ACTN 
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}.
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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
//
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