Species | Batrachochytrium salamandrivorans | |||||||||||
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Lineage | Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans | |||||||||||
CAZyme ID | OON08241.1 | |||||||||||
CAZy Family | GT21 | |||||||||||
CAZyme Description | alpha-1,2-Mannosidase [Source:UniProtKB/TrEMBL;Acc:A0A1S8W133] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.113:6 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH47 | 105 | 538 | 6e-150 | 0.9955156950672646 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396217 | Glyco_hydro_47 | 1.78e-160 | 105 | 539 | 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 | 1.39e-86 | 99 | 542 | 73 | 521 | glycoside hydrolase family 47 protein; Provisional |
271199 | LanC_SerThrkinase | 0.003 | 198 | 362 | 88 | 235 | 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 |
---|---|---|---|---|---|
5.29e-194 | 105 | 539 | 1 | 437 | |
1.44e-169 | 95 | 565 | 67 | 552 | |
3.08e-166 | 95 | 539 | 67 | 527 | |
2.26e-165 | 91 | 588 | 28 | 526 | |
4.62e-162 | 95 | 592 | 9 | 537 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.72e-50 | 97 | 517 | 12 | 415 | Structure of 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] |
|
2.03e-48 | 104 | 539 | 11 | 451 | Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens] |
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2.30e-48 | 104 | 539 | 16 | 456 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens] |
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2.39e-48 | 104 | 539 | 16 | 456 | 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] |
|
2.87e-48 | 99 | 539 | 23 | 467 | Structure of 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.13e-161 | 95 | 592 | 122 | 650 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1 |
|
1.17e-159 | 95 | 592 | 127 | 655 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1 |
|
7.16e-156 | 98 | 539 | 35 | 477 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2 |
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1.94e-146 | 98 | 539 | 40 | 473 | Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1 |
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7.35e-139 | 98 | 578 | 37 | 525 | Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000018 | 0.000015 |
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