Species | Rhizophagus irregularis | |||||||||||
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Lineage | Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis | |||||||||||
CAZyme ID | FUN_008351-T1-p1 | |||||||||||
CAZy Family | GH15 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.14:25 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 783 | 1126 | 4.3e-84 | 0.9527027027027027 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
276817 | KISc_C_terminal | 1.74e-109 | 291 | 647 | 1 | 325 | Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. |
119365 | GH18_chitinase | 5.51e-107 | 785 | 1121 | 1 | 322 | The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. |
214753 | Glyco_18 | 2.31e-106 | 784 | 1121 | 1 | 334 | Glyco_18 domain. |
214526 | KISc | 4.34e-101 | 293 | 661 | 1 | 334 | Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. |
276812 | KISc | 4.37e-93 | 293 | 647 | 1 | 326 | Kinesin motor domain. Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.40e-136 | 776 | 1162 | 4 | 400 | |
6.75e-133 | 775 | 1166 | 2 | 400 | |
1.10e-124 | 787 | 1164 | 11 | 398 | |
4.57e-123 | 778 | 1165 | 1 | 390 | |
6.94e-123 | 783 | 1164 | 63 | 445 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.26e-122 | 788 | 1164 | 8 | 389 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL4_A Chain A, Chitinase 1 [Coccidioides immitis],1LL4_B Chain B, Chitinase 1 [Coccidioides immitis],1LL4_C Chain C, Chitinase 1 [Coccidioides immitis],1LL4_D Chain D, Chitinase 1 [Coccidioides immitis] |
|
8.89e-122 | 788 | 1164 | 8 | 389 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis] |
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1.74e-121 | 788 | 1164 | 8 | 389 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL6_B Chain B, CHITINASE 1 [Coccidioides immitis],1LL6_C Chain C, CHITINASE 1 [Coccidioides immitis],1LL6_D Chain D, CHITINASE 1 [Coccidioides immitis] |
|
2.30e-116 | 779 | 1166 | 1 | 394 | Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus] |
|
2.70e-116 | 787 | 1165 | 20 | 403 | Crystal structure of Aspergillus niger chitinase B [Aspergillus niger] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.00e-121 | 745 | 1164 | 9 | 424 | Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1 |
|
1.40e-121 | 779 | 1164 | 34 | 424 | Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1 |
|
1.96e-121 | 745 | 1164 | 9 | 424 | Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1 |
|
1.51e-115 | 779 | 1166 | 39 | 432 | Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1 |
|
1.51e-115 | 779 | 1166 | 39 | 432 | Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000045 | 0.000000 |
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