Species | Puccinia sorghi | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi | |||||||||||
CAZyme ID | KNZ61972.1 | |||||||||||
CAZy Family | GT22 | |||||||||||
CAZyme Description | N-acetyltransferase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0L6VN22] | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
214773 | CAP10 | 1.50e-11 | 852 | 976 | 136 | 241 | Putative lipopolysaccharide-modifying enzyme. |
310354 | Glyco_transf_90 | 2.95e-07 | 859 | 986 | 213 | 321 | Glycosyl transferase family 90. This family of glycosyl transferases are specifically (mannosyl) glucuronoxylomannan/galactoxylomannan -beta 1,2-xylosyltransferases, EC:2.4.2.-. |
173926 | NAT_SF | 0.004 | 132 | 210 | 3 | 56 | N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.77e-116 | 374 | 997 | 154 | 752 | |
3.33e-82 | 442 | 998 | 171 | 695 | |
4.14e-82 | 437 | 991 | 166 | 693 | |
1.87e-81 | 442 | 987 | 114 | 631 | |
1.18e-78 | 441 | 999 | 175 | 711 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.06e-12 | 134 | 292 | 50 | 150 | Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA [Homo sapiens],3TFY_B Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA [Homo sapiens],3TFY_C Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA [Homo sapiens],4X5K_A Human NAA50 complex with coenzyme A and an acetylated peptide [Homo sapiens],6PPL_A Cryo-EM structure of human NatE complex (NatA/Naa50) [Homo sapiens],6PW9_A Cryo-EM structure of human NatE/HYPK complex [Homo sapiens] |
|
1.11e-12 | 134 | 292 | 52 | 152 | Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF3_B Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF3_C Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF3_D Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF3_E Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF3_F Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1) [Homo sapiens],6WF5_A Crystal structure of human Naa50 in complex with a truncated cofactor derived inhibitor (compound 2) [Homo sapiens],6WF5_B Crystal structure of human Naa50 in complex with a truncated cofactor derived inhibitor (compound 2) [Homo sapiens],6WFG_A Crystal structure of human Naa50 in complex with an inhibitor (compound 3) identified using DNA encoded library technology [Homo sapiens],6WFG_C Crystal structure of human Naa50 in complex with an inhibitor (compound 3) identified using DNA encoded library technology [Homo sapiens],6WFG_E Crystal structure of human Naa50 in complex with an inhibitor (compound 3) identified using DNA encoded library technology [Homo sapiens],6WFK_A Crystal structure of human Naa50 in complex with CoA and an inhibitor (compound 4a) identified using DNA encoded library technology [Homo sapiens],6WFK_B Crystal structure of human Naa50 in complex with CoA and an inhibitor (compound 4a) identified using DNA encoded library technology [Homo sapiens],6WFK_C Crystal structure of human Naa50 in complex with CoA and an inhibitor (compound 4a) identified using DNA encoded library technology [Homo sapiens],6WFN_A Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4a) identified using DNA encoded library technology [Homo sapiens],6WFO_A Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4b) identified using DNA encoded library technology [Homo sapiens],6WFO_B Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4b) identified using DNA encoded library technology [Homo sapiens],6WFO_C Crystal structure of human Naa50 in complex with AcCoA and an inhibitor (compound 4b) identified using DNA encoded library technology [Homo sapiens] |
|
1.72e-11 | 134 | 292 | 51 | 151 | Human MAK3 homolog in complex with Acetyl-CoA [Homo sapiens],2OB0_B Human MAK3 homolog in complex with Acetyl-CoA [Homo sapiens],2OB0_C Human MAK3 homolog in complex with Acetyl-CoA [Homo sapiens],2PSW_A Human MAK3 homolog in complex with CoA [Homo sapiens],2PSW_B Human MAK3 homolog in complex with CoA [Homo sapiens],2PSW_C Human MAK3 homolog in complex with CoA [Homo sapiens] |
|
3.18e-11 | 134 | 292 | 53 | 153 | Chain A, N-alpha-acetyltransferase 50 [Arabidopsis thaliana],6Z00_A Chain A, Acyl-CoA N-acyltransferases (NAT) superfamily protein [Arabidopsis thaliana],6Z00_B Chain B, Acyl-CoA N-acyltransferases (NAT) superfamily protein [Arabidopsis thaliana] |
|
1.76e-06 | 815 | 991 | 196 | 345 | human POGLUT1 in complex with Notch1 EGF12 and UDP [Homo sapiens],5L0S_A human POGLUT1 in complex with Factor VII EGF1 and UDP [Homo sapiens],5L0T_A human POGLUT1 in complex with EGF(+) and UDP [Homo sapiens],5L0U_A human POGLUT1 in complex with EGF(+) and UDP-phosphono-glucose [Homo sapiens],5L0V_A human POGLUT1 in complex with 2F-glucose modified EGF(+) and UDP [Homo sapiens],5UB5_A human POGLUT1 in complex with human Notch1 EGF12 S458T mutant and UDP [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.20e-62 | 437 | 992 | 147 | 660 | Beta-1,2-xylosyltransferase 1 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CXT1 PE=1 SV=1 |
|
5.35e-12 | 134 | 292 | 49 | 149 | N-alpha-acetyltransferase 50 OS=Danio rerio OX=7955 GN=naa50 PE=1 SV=1 |
|
5.47e-12 | 134 | 292 | 50 | 150 | N-alpha-acetyltransferase 50 OS=Bos taurus OX=9913 GN=NAA50 PE=2 SV=1 |
|
5.47e-12 | 134 | 292 | 50 | 150 | N-alpha-acetyltransferase 50 OS=Pongo abelii OX=9601 GN=NAA50 PE=2 SV=1 |
|
5.47e-12 | 134 | 292 | 49 | 149 | N-alpha-acetyltransferase 50 OS=Xenopus tropicalis OX=8364 GN=naa50 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.996864 | 0.003170 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.