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Database: UniProt
Entry: A0A1M3EMU0_9CELL
LinkDB: A0A1M3EMU0_9CELL
Original site: A0A1M3EMU0_9CELL 
ID   A0A1M3EMU0_9CELL        Unreviewed;       860 AA.
AC   A0A1M3EMU0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:OJV60133.1};
GN   ORFNames=BGO38_00875 {ECO:0000313|EMBL:OJV60133.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV60133.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV60133.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV60133.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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   -!- 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:OJV60133.1}.
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DR   EMBL; MKTI01000004; OJV60133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3EMU0; -.
DR   STRING; 1895739.BGO38_00875; -.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 1.
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}.
FT   DOMAIN          766..841
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          299..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  89660 MW;  3B1928E3B3E8B7C2 CRC64;
     MALDTAQQPS TGTDALVALA GTLTLEEKVA LVVGAGLWTT TAIPRIGLRA MVLSDGPAGV
     RGVGPDAGTS ASFPAPTALA ATWDVELAGR VGTLFAAEAH RHGVDVVLAP QVNLQRTPVG
     GRHFECFSED PLLTSLLTVP LVDAAQRAGV AMCVKHYVAN DSETDRTRYV SHVDERTLRE
     VYLPPFEAAV RAGAWSVMGA YSGVDDGVEA APVLEHRHLL TEVLKEEWGF DGVVLSDWVA
     TRSVAGAVRG GLDLQMPGPD GPWGDGLLDA VRTGVVAESE LDDKVLRLLR LAQRVGALAA
     ADDDEAPDDE ARDDDEAHDD GEAALPLPDP AQVAAQLRAL VTASMVVLRD DGLLPLTGTR
     GVPAAGPAPT RVALIGANAV EPFLQGGGSS MVAPDRRAVL ADRLADALGA PVDVHVGARS
     RLVPPDLDLV ACTTPDGTPG LRVELFDADG AVLDVQDVTA WDGWLREPPA AAASVRLRAA
     IRLTEPGLHQ VGVGTVGAHR LVVDGVTVSS SDHLVGAEVI LDSTVNHPVP AMLSVAGPAT
     VHLDATVQAV HPVGYDSFAR ALLVHRVPGP SAAQLRDEAV AAAAAADVAI VVVGTTEEVE
     SEGWDRTSLA LPGEQDALVD AVLAANPRTV VVVNAGAPVL LPWLDRAPCV VWGWLGGQEW
     PDAVADVLAG RAEPAGRLPW TLPARAQDVP VPDAVPVDGV VEYREGVHVG HRSWDLLGRT
     PAAPFGHGLG WTTWEHLSAT LAGQQADGSV ELAVTVRNAG PRPGREVVQV YVEPPEGTPR
     GERPVRALGG FAVVDAEPGV TTTVRVPVAV QAFRTWQAGD AGRGGWTVPA GTYRLRIGRS
     SRDLRLALDV VQPTRAAEPQ
//
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