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CAZyme Information: MGYG000002890_00194
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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 | Streptococcus oralis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus oralis | |||||||||||
| CAZyme ID | MGYG000002890_00194 | |||||||||||
| CAZy Family | GH92 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 16846; End: 17799 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3537 | COG3537 | 1.54e-128 | 1 | 315 | 35 | 374 | Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism]. |
| pfam07971 | Glyco_hydro_92 | 1.07e-19 | 221 | 315 | 1 | 96 | Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation. |
| pfam17678 | Glyco_hydro_92N | 5.48e-16 | 8 | 126 | 2 | 117 | Glycosyl hydrolase family 92 N-terminal domain. This domain is found at the N-terminus of family 92 glycosyl hydrolase proteins. |
| NF035929 | lectin_1 | 2.93e-04 | 211 | 312 | 257 | 362 | lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QLL96703.1 | 2.53e-219 | 1 | 315 | 1 | 315 |
| QXW61384.1 | 5.09e-219 | 1 | 315 | 1 | 315 |
| CBZ01551.1 | 1.18e-217 | 1 | 315 | 1 | 315 |
| QRO08003.1 | 4.77e-217 | 1 | 315 | 1 | 315 |
| QQL00240.1 | 4.77e-217 | 1 | 315 | 1 | 315 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5SWI_A | 3.40e-211 | 1 | 315 | 24 | 338 | Crystalstructure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_B Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_C Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_D Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae] |
| 6DWO_A | 1.29e-79 | 5 | 315 | 3 | 320 | Crystalstructure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_B Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_C Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_D Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583] |
| 7FE1_A | 1.29e-79 | 5 | 315 | 3 | 320 | ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100] |
| 7FE2_A | 1.29e-79 | 5 | 315 | 3 | 320 | ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100] |
| 2WVY_A | 6.73e-38 | 5 | 315 | 8 | 340 | StructureOf The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_B Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_C Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_A Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_B Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_C Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O86365 | 2.39e-09 | 5 | 315 | 42 | 376 | Uncharacterized glycosidase Rv0584 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv0584 PE=3 SV=1 |
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 |
|---|---|---|---|---|---|
| 1.000041 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |