ID A0A0M2CS33_9MICC Unreviewed; 841 AA.
AC A0A0M2CS33;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:EYT49237.1};
GN ORFNames=H488_0114685 {ECO:0000313|EMBL:EYT49237.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT49237.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT49237.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT49237.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(2013).
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:EYT49237.1}.
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DR EMBL; AOSQ01000034; EYT49237.1; -; Genomic_DNA.
DR RefSeq; WP_017834021.1; NZ_AOSQ01000034.1.
DR AlphaFoldDB; A0A0M2CS33; -.
DR HOGENOM; CLU_004542_4_0_11; -.
DR Proteomes; UP000033173; 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 764..831
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 296..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 88002 MW; 8F9E4803FBE7ED45 CRC64;
MTDATRTSGR AARLMELVDR LSLAEKVHLL TGETAFTLPG NERIGLAALA FSDGPTGVRG
LTFVGGDAVA LFPSATLIAG AFDDGIAEEV GRMLAEEAQR QHIHVVLGPT INLHRTPLGG
RLFEAYSEDP YLTGRTAAAY VRGMQERGTA ACLKHLVANE SETLRNFMDS RVPETALREL
YLLPFEMAVQ DAGAWSMMAA YNDVNGVAAT EHDHVQNGIV KGEWAWDGLI MSDWFATKRT
AASASGGLDL VMPGPGGPWG ERLVTAVRAG EVAEETIDDH VLRLLHLAER VGGLTPPGRQ
SRPWAQDLPA VDSPQRKEQL RRIAVRGMTV VANDGVLPLA VEGDAGQDVA LIGRHAIDTV
DMGGGSAVVN PPYLSTIAEG LAALLGDRVR VADGPAVRTR PVPADPAFLT DPATGTPGMQ
VVLLGADGTE LTRYHSDSPA ISLDGHDDLG EVPATAVLTT ILANDAGPVR LGAVGAGRWD
LVAEGQELSA ELRLEGQDPG EAMLRPPAFA ETVELPAAAT LTATVAPAPV DWREVLLGDP
GLGLAEESHL LQMTTAGKTA LVAAPAPRPD DDLLAAAEAA AAAAGTAVVV VGLTEEQETE
AADKTTLVLP GRQDELVRRV ATAAERTVVV VNAATPVLMP WLDQVDAVLV AGLPGQEGGH
AVAAALTGAL EPTGRLVTSW PAADGAAPAW DVVPDGDRAL SYDDGTFIGH RGYHAGHAPA
PLFWFGHGLG YGTWEYGTVR ARAGEGGPVV DVELTNTSSR ASRETVQVYL DPAEDDQPIR
LIGYQGVDVP SGATAAVRVR CDDRLLRRWD DAAGTWAPLA GGGELVLARG LGDVRARVPL
A
//