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pycom17g11550.1
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pyrus_communis |
-
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The RING-variant domain is a C4HC3 zinc-finger like motif found in a number of cellular and viral proteins. Some of these proteins have been shown both in vivo and in vitro to have ubiquitin E3 ligase activity. |
Detail
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pycom17g11560.1
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pyrus_communis |
-
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Endoplasmic reticulum-Golgi intermediate compartment protein |
Detail
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pycom17g11570.1
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pyrus_communis |
-
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F-box kelch-repeat protein |
Detail
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pycom17g11590.1
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pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11600.1
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pyrus_communis |
-
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strictosidine synthase activity |
Detail
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pycom17g11650.1
|
pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11670.1
|
pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11680.1
|
pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11690.1
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pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11700.1
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pyrus_communis |
-
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Amidase |
Detail
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pycom17g11710.1
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pyrus_communis |
-
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Peptidyl-prolyl cis-trans isomerase |
Detail
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pycom17g11730.1
|
pyrus_communis |
-
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None |
Detail
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pycom17g11740.1
|
pyrus_communis |
-
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TMV resistance protein |
Detail
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pycom17g11750.1
|
pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11760.1
|
pyrus_communis |
-
|
UDP-Glycosyltransferase |
Detail
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pycom17g11770.1
|
pyrus_communis |
-
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Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand |
Detail
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pycom17g11780.1
|
pyrus_communis |
-
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UDP-Glycosyltransferase |
Detail
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pycom17g11800.1
|
pyrus_communis |
-
|
UDP-Glycosyltransferase |
Detail
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pycom17g11820.1
|
pyrus_communis |
-
|
UDP-Glycosyltransferase |
Detail
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pycom17g11830.1
|
pyrus_communis |
-
|
UDP-Glycosyltransferase |
Detail
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