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CAZyme Information: MGYG000001693_02113

You are here: Home > Sequence: MGYG000001693_02113

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 Halorubrum lipolyticum
Lineage Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum; Halorubrum lipolyticum
CAZyme ID MGYG000001693_02113
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
949 104816.75 4.48
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001693 3425042 Isolate Canada North America
Gene Location Start: 184713;  End: 187562  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001693_02113.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 10 928 1.4e-236 0.9956958393113343

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15979 Glyco_hydro_115 0.0 163 508 1 334
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 7.50e-39 776 944 6 172
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.
cd14948 BACON 2.50e-05 702 759 26 80
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam19190 BACON_2 0.005 698 750 26 90
Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHG01349.1 0.0 1 947 1 946
AHG01821.1 0.0 1 948 2 948
ADB62762.1 0.0 1 945 6 959
QRV17780.1 0.0 1 945 1 955
AEH39042.1 0.0 3 945 25 982

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZMH_A 1.37e-150 20 948 23 936
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]
5BY3_A 9.79e-144 65 642 68 625
Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482]
6NPS_A 4.43e-108 28 945 26 963
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]
4C90_A 5.87e-107 5 631 38 639
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]
7PUG_A 8.32e-107 13 634 19 627
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.995209 0.004674 0.000099 0.000010 0.000006 0.000015

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001693_02113.