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CAZyme Information: MGYG000002216_01566

You are here: Home > Sequence: MGYG000002216_01566

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ;
CAZyme ID MGYG000002216_01566
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1899 212495.85 4.9599
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002216 3003083 MAG Spain Europe
Gene Location Start: 450;  End: 6149  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 34 690 5.6e-201 0.8292682926829268

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15979 Glyco_hydro_115 1.46e-147 189 560 1 333
Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
pfam17829 GH115_C 1.89e-38 823 1018 2 172
Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
sd00036 LRR_3 8.49e-15 1766 1866 14 127
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036 LRR_3 8.91e-15 1785 1866 1 81
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036 LRR_3 2.52e-12 1769 1851 63 136
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUC17495.1 7.93e-233 31 1189 21 1197
APZ46852.1 7.93e-233 31 1189 21 1197
AFO77172.1 2.43e-201 29 1028 44 982
ADJ45460.1 2.43e-201 29 1028 44 982
AGT84300.1 2.43e-201 29 1028 44 982

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZMH_A 2.68e-127 34 1019 13 933
Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
4C90_A 2.30e-109 35 681 44 640
Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
5BY3_A 5.12e-104 44 741 27 694
Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482]
6NPS_A 8.13e-101 56 1020 32 964
Crystalstructure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]
7PUG_A 1.61e-100 35 689 17 633
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000264 0.999044 0.000209 0.000156 0.000148 0.000135

TMHMM  Annotations      download full data without filtering help

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