Species | Colletotrichum graminicola | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola | |||||||||||
CAZyme ID | EFQ27216.1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | alpha-1,2-Mannosidase [Source:UniProtKB/TrEMBL;Acc:E3Q937] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.113:7 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH47 | 103 | 565 | 6.3e-163 | 0.9955156950672646 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396217 | Glyco_hydro_47 | 0.0 | 102 | 565 | 1 | 453 | 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). |
240427 | PTZ00470 | 1.23e-137 | 50 | 566 | 24 | 519 | glycoside hydrolase family 47 protein; Provisional |
271200 | LanM-like | 8.20e-04 | 184 | 275 | 598 | 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. |
271199 | LanC_SerThrkinase | 0.002 | 186 | 292 | 94 | 197 | 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 |
---|---|---|---|---|---|
0.0 | 1 | 567 | 1 | 590 | |
2.38e-256 | 3 | 565 | 5 | 570 | |
4.30e-256 | 3 | 565 | 5 | 567 | |
2.16e-255 | 4 | 565 | 11 | 569 | |
5.65e-255 | 3 | 565 | 25 | 590 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.20e-80 | 95 | 563 | 5 | 449 | Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens] |
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1.42e-80 | 95 | 563 | 10 | 454 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens] |
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1.49e-80 | 95 | 563 | 10 | 454 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens] |
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3.00e-80 | 59 | 563 | 61 | 532 | Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens] |
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7.11e-80 | 95 | 563 | 5 | 449 | Crystal structure 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 |
---|---|---|---|---|---|---|
1.39e-84 | 89 | 564 | 91 | 535 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 OS=Arabidopsis thaliana OX=3702 GN=MNS1 PE=1 SV=1 |
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2.99e-82 | 89 | 564 | 92 | 536 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 OS=Arabidopsis thaliana OX=3702 GN=MNS2 PE=1 SV=1 |
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5.88e-78 | 59 | 563 | 222 | 693 | Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Homo sapiens OX=9606 GN=MAN1B1 PE=1 SV=2 |
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2.15e-75 | 94 | 563 | 173 | 615 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC OS=Homo sapiens OX=9606 GN=MAN1C1 PE=1 SV=1 |
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2.38e-75 | 72 | 564 | 22 | 513 | Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CPSG_02648 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999909 | 0.000128 |
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