logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: KNZ61972.1

You are here: Home > Sequence: KNZ61972.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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
Protein Length CGC Molecular Weight Isoelectric Point
999 113816.86 8.6400
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PsorghiRO10H11247 21769 N/A 691 21078
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KNZ61972.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT90 747 987 1.7e-44 0.664

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]

Swiss-Prot Hits      download full data without filtering help

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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.996864 0.003170

TMHMM  Annotations      help

There is no transmembrane helices in KNZ61972.1.