Species | Pyricularia oryzae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae | |||||||||||
CAZyme ID | mRNA_M_BR32_EuGene_00127361-p1 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.55:10 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH51 | 152 | 664 | 5.1e-71 | 0.8047619047619048 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
236919 | tynA | 0.0 | 596 | 1232 | 26 | 641 | primary-amine oxidase. |
395938 | Cu_amine_oxid | 0.0 | 818 | 1222 | 2 | 403 | Copper amine oxidase, enzyme domain. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ). This family corresponds to the catalytic domain of the enzyme. |
226256 | TynA | 1.94e-162 | 596 | 1222 | 42 | 649 | Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism]. |
184793 | tynA | 8.10e-61 | 612 | 1220 | 117 | 714 | primary-amine oxidase. |
215306 | PLN02566 | 8.76e-56 | 600 | 1220 | 38 | 645 | amine oxidase (copper-containing) |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 599 | 48 | 646 | |
2.47e-191 | 1 | 593 | 50 | 634 | |
9.71e-191 | 1 | 593 | 50 | 634 | |
9.71e-191 | 1 | 593 | 50 | 634 | |
9.71e-191 | 1 | 593 | 50 | 634 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.53e-138 | 612 | 1226 | 31 | 633 | Chain A, copper amine oxidase [Ogataea angusta],3LOY_B Chain B, copper amine oxidase [Ogataea angusta],3LOY_C Chain C, copper amine oxidase [Ogataea angusta] |
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1.48e-103 | 601 | 1222 | 24 | 641 | Chain A, COPPER AMINE OXIDASE [Ogataea angusta],1EKM_B Chain B, COPPER AMINE OXIDASE [Ogataea angusta],1EKM_C Chain C, COPPER AMINE OXIDASE [Ogataea angusta] |
|
3.79e-103 | 601 | 1222 | 40 | 657 | Chain A, Peroxisomal primary amine oxidase [Ogataea angusta],3SX1_B Chain B, Peroxisomal primary amine oxidase [Ogataea angusta],3SX1_C Chain C, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_A Chain A, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_B Chain B, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_C Chain C, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_D Chain D, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_E Chain E, Peroxisomal primary amine oxidase [Ogataea angusta],3SXX_F Chain F, Peroxisomal primary amine oxidase [Ogataea angusta],3T0U_A Chain A, Peroxisomal primary amine oxidase [Ogataea angusta],3T0U_B Chain B, Peroxisomal primary amine oxidase [Ogataea angusta],3T0U_C Chain C, Peroxisomal primary amine oxidase [Ogataea angusta] |
|
1.93e-102 | 601 | 1222 | 23 | 640 | Chain A, METHYLAMINE OXIDASE [Ogataea angusta],1A2V_B Chain B, METHYLAMINE OXIDASE [Ogataea angusta],1A2V_C Chain C, METHYLAMINE OXIDASE [Ogataea angusta],1A2V_D Chain D, METHYLAMINE OXIDASE [Ogataea angusta],1A2V_E Chain E, METHYLAMINE OXIDASE [Ogataea angusta],1A2V_F Chain F, METHYLAMINE OXIDASE [Ogataea angusta] |
|
2.20e-102 | 601 | 1222 | 28 | 645 | Chain C, Peroxisomal copper amine oxidase [Ogataea angusta],2OOV_D Chain D, Peroxisomal copper amine oxidase [Ogataea angusta],2OOV_E Chain E, Peroxisomal copper amine oxidase [Ogataea angusta],2OOV_F Chain F, Peroxisomal copper amine oxidase [Ogataea angusta],2OQE_C Chain C, Peroxisomal copper amine oxidase [Ogataea angusta],2OQE_D Chain D, Peroxisomal copper amine oxidase [Ogataea angusta],2OQE_E Chain E, Peroxisomal copper amine oxidase [Ogataea angusta],2OQE_F Chain F, Peroxisomal copper amine oxidase [Ogataea angusta] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.96e-171 | 1 | 593 | 50 | 628 | Alpha-L-arabinofuranosidase A OS=Penicillium canescens OX=5083 GN=abfA PE=1 SV=1 |
|
1.50e-154 | 600 | 1232 | 20 | 657 | Copper amine oxidase 1 OS=Aspergillus niger OX=5061 GN=AO-I PE=1 SV=2 |
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1.44e-123 | 1 | 593 | 58 | 625 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfA PE=3 SV=1 |
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1.48e-123 | 1 | 593 | 58 | 626 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abfA PE=3 SV=2 |
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4.08e-122 | 1 | 593 | 58 | 626 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abfA PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000048 | 0.000000 |
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