Species | Enterococcus_G italicus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_G; Enterococcus_G italicus | |||||||||||
CAZyme ID | MGYG000000335_01422 | |||||||||||
CAZy Family | GH170 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 691; End: 1755 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH170 | 1 | 347 | 1.7e-120 | 0.9942857142857143 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3589 | COG3589 | 1.03e-111 | 1 | 351 | 3 | 360 | Uncharacterized protein [Function unknown]. |
pfam19200 | DUF871_N | 1.70e-101 | 3 | 230 | 2 | 233 | DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown. |
pfam05913 | DUF871 | 1.06e-36 | 242 | 348 | 7 | 116 | Bacterial protein of unknown function (DUF871). This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown. |
cd06565 | GH20_GcnA-like | 0.005 | 64 | 135 | 5 | 72 | Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEA60502.1 | 2.29e-117 | 1 | 351 | 1 | 350 |
AIS03849.1 | 2.29e-117 | 1 | 351 | 1 | 350 |
ALS00837.1 | 2.37e-117 | 1 | 350 | 1 | 351 |
QRZ11657.1 | 1.86e-116 | 1 | 351 | 1 | 350 |
QIT58302.1 | 1.06e-115 | 1 | 351 | 1 | 351 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2P0O_A | 4.74e-102 | 2 | 350 | 5 | 360 | Crystalstructure of a conserved protein from locus EF_2437 in Enterococcus faecalis with an unknown function [Enterococcus faecalis V583] |
1X7F_A | 1.57e-33 | 3 | 349 | 30 | 385 | Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A0A0H2XHV5 | 2.86e-51 | 1 | 346 | 1 | 342 | 6-phospho-N-acetylmuramidase OS=Staphylococcus aureus (strain USA300) OX=367830 GN=mupG PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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