Species | Caulobacter sp903900155 | |||||||||||
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Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Caulobacter; Caulobacter sp903900155 | |||||||||||
CAZyme ID | MGYG000001261_00771 | |||||||||||
CAZy Family | GH47 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3247; End: 4632 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH47 | 43 | 456 | 1.8e-109 | 0.9932735426008968 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01532 | Glyco_hydro_47 | 1.07e-121 | 42 | 456 | 1 | 452 | Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). |
PTZ00470 | PTZ00470 | 1.19e-73 | 39 | 460 | 76 | 521 | glycoside hydrolase family 47 protein; Provisional |
cd04792 | LanM-like | 0.001 | 128 | 214 | 600 | 682 | Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB. |
cd04791 | LanC_SerThrkinase | 0.002 | 128 | 218 | 94 | 178 | Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ADG09297.1 | 7.15e-312 | 1 | 460 | 1 | 461 |
AVQ01103.1 | 7.15e-312 | 1 | 460 | 1 | 461 |
QTC92579.1 | 3.16e-260 | 6 | 459 | 6 | 461 |
QDH72853.1 | 1.52e-251 | 5 | 458 | 5 | 470 |
QNA83392.1 | 1.15e-179 | 5 | 460 | 2 | 461 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4AYO_A | 1.06e-290 | 31 | 461 | 9 | 439 | Structureof The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 [Caulobacter sp. K31],4AYP_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with thiomannobioside [Caulobacter sp. K31],4AYQ_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole [Caulobacter sp. K31],4AYR_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin [Caulobacter sp. K31],5MEH_A Crystal structure of alpha-1,2-mannosidase from Caulobacter K31 strain in complex with 1-deoxymannojirimycin [Caulobacter sp. K31],5NE5_A Crystal structure of family 47 alpha-1,2-mannosidase from Caulobacter K31 strain in complex with kifunensine [Caulobacter sp. K31] |
1NXC_A | 2.52e-50 | 37 | 460 | 22 | 471 | Structureof mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus] |
5KKB_A | 2.93e-50 | 37 | 453 | 24 | 463 | Structureof mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus] |
5KIJ_A | 5.75e-46 | 43 | 441 | 13 | 434 | Crystalstructure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens] |
5KK7_A | 6.10e-46 | 43 | 441 | 13 | 434 | Crystalstructure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9SXC9 | 1.43e-59 | 39 | 438 | 41 | 460 | Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1 |
Q9FG93 | 1.23e-51 | 38 | 435 | 43 | 445 | Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1 |
P53624 | 3.04e-51 | 39 | 455 | 204 | 645 | Mannosyl-oligosaccharide alpha-1,2-mannosidase IA OS=Drosophila melanogaster OX=7227 GN=alpha-Man-Ia PE=2 SV=2 |
P39098 | 4.13e-51 | 39 | 459 | 184 | 628 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Mus musculus OX=10090 GN=Man1a2 PE=1 SV=1 |
O60476 | 7.89e-51 | 39 | 455 | 184 | 624 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Homo sapiens OX=9606 GN=MAN1A2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000786 | 0.159402 | 0.000428 | 0.838633 | 0.000658 | 0.000084 |
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