NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488052714|ref|WP_002124111|]
View 

MULTISPECIES: spermidine N1-acetyltransferase [Bacillus cereus group]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 4-167 7.60e-98

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK15130:

Pssm-ID: 473072  Cd Length: 186  Bit Score: 280.14  E-value: 7.60e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   4 ELKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTE 83
Cdd:PRK15130   6 SVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  84 FQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNAIRMCMF 163
Cdd:PRK15130  86 FQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRMCIF 165


                 ....
gi 488052714 164 QKAY 167
Cdd:PRK15130 166 QHQY 169
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 4-167 7.60e-98

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 280.14  E-value: 7.60e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   4 ELKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTE 83
Cdd:PRK15130   6 SVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  84 FQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNAIRMCMF 163
Cdd:PRK15130  86 FQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRMCIF 165


                 ....
gi 488052714 164 QKAY 167
Cdd:PRK15130 166 QHQY 169
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-165 4.06e-43

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 140.90  E-value: 4.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   3 QELKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFvELQDLYDKHIHDQSERRF----IVEK-DNEMVGLVELVEIDY 77
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLE-EARAWLERLLADWADGGAlpfaIEDKeDGELIGVVGLYDIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  78 IHRRTEFQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNA 157
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ....*...
gi 488052714 158 IRMCMFQK 165
Cdd:COG1670  165 VLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 5-139 6.30e-28

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 101.27  E-value: 6.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714    5 LKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFvELQDLYDKHIHDQSERRF----IVEKDNEMVGLVELVEIDYIHR 80
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERGygwaIELKDTGFIGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488052714   81 RTEFQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFV 139
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 7-161 4.91e-13

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 63.15  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714    7 LRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTEFQI 86
Cdd:TIGR03585   3 FTPLNSEELELVLEWRNHPDVRANMYSDHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488052714   87 IIDPKYQGyGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEffvdGNYHNAIRMC 161
Cdd:TIGR03585  83 YANPFCKP-GVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG----GEYYDVLLMY 152
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-120 9.62e-04

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.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 9.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488052714  58 FIVEKDNEMVGLVELVEIDYIHRRTEFQ-IIIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYL 120
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRL 64
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 4-167 7.60e-98

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 280.14  E-value: 7.60e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   4 ELKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTE 83
Cdd:PRK15130   6 SVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  84 FQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNAIRMCMF 163
Cdd:PRK15130  86 FQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRMCIF 165


                 ....
gi 488052714 164 QKAY 167
Cdd:PRK15130 166 QHQY 169
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-165 4.06e-43

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 140.90  E-value: 4.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   3 QELKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFvELQDLYDKHIHDQSERRF----IVEK-DNEMVGLVELVEIDY 77
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLE-EARAWLERLLADWADGGAlpfaIEDKeDGELIGVVGLYDIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  78 IHRRTEFQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNA 157
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ....*...
gi 488052714 158 IRMCMFQK 165
Cdd:COG1670  165 VLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 5-139 6.30e-28

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 101.27  E-value: 6.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714    5 LKLRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFvELQDLYDKHIHDQSERRF----IVEKDNEMVGLVELVEIDYIHR 80
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERGygwaIELKDTGFIGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488052714   81 RTEFQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFV 139
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 30-138 2.60e-15

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 67.93  E-value: 2.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   30 YWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTE-FQIIIDPKYQGYGYAAEATRLAMDY 108
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEiEGLAVAPEYRGKGIGTALLQALLEW 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 488052714  109 AFSvLNMHKLYLVVDKENEKAVHVYKKVGF 138
Cdd:pfam00583  88 ARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-160 2.38e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 66.56  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   4 ELKLRPLEREDLKFVHELNNNA---HIMSYWFEEPYEAfvELQDLYDkHIHDQSERRFIVEKDNEMVGLVELV---EIDY 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAiaeGTATFETEPPSEE--EREAWFA-AILAPGRPVLVAEEDGEVVGFASLGpfrPRPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  78 IHRRTEFQIIIDPKYQGYGYAaeatRLAMDYAFSVL---NMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNY 154
Cdd:COG1247   78 YRGTAEESIYVDPDARGRGIG----RALLEALIERArarGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRW 153


                 ....*.
gi 488052714 155 HNAIRM 160
Cdd:COG1247  154 LDLVLM 159
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 7-161 4.91e-13

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 63.15  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714    7 LRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRRTEFQI 86
Cdd:TIGR03585   3 FTPLNSEELELVLEWRNHPDVRANMYSDHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488052714   87 IIDPKYQGyGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEffvdGNYHNAIRMC 161
Cdd:TIGR03585  83 YANPFCKP-GVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG----GEYYDVLLMY 152
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-149 2.34e-09

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.17  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   7 LRPLEREDLKFVHELNNNAhimsywFEEPYEAfvELQDLYDKHIHDqsERRFIVEKDNEMVGLVELVEIDYIHRRTEFQI 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA------FGPGREA--ELVDRLREDPAA--GLSLVAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488052714  87 ---IIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYLVVDkenEKAVHVYKKVGFVVEGELQDEFF 149
Cdd:COG3153   71 gplAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 58-140 1.07e-08

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   58 FIVEKDNEMVGLVELVEIDYIHRRTEFQIIIDPKYQGYGYaaeATRLaMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVG 137
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGI---GRAL-LEAAEAAAKEGGIKLLELETTNRAAAFYEKLG 81


                  ...
gi 488052714  138 FVV 140
Cdd:pfam13508  82 FEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-155 2.46e-08

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.88  E-value: 2.46e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488052714  77 YIHRrtefqIIIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYLVVDKENEKAVHVYKKVGFVVEGElQDEFFVDGNYH 155
Cdd:COG0456   15 EIED-----LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGE-RPNYYGDDALV 86
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
7-154 4.33e-07

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 46.98  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714    7 LRPLEREDLKFVHELNNNAHIMSYWFEEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRR---TE 83
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLSPGEIVFGVAESDRLIGYATLRQFDYVKTHkaeLS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488052714   84 FQIIIDPKYqgyGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNY 154
Cdd:pfam13420  81 FYVVKNNDE---GINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRW 148
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
86-144 6.23e-07

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.28  E-value: 6.23e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488052714  86 IIIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYLVVDKENEKAVHVYKKVGFVVEGEL 144
Cdd:COG3393   21 VYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVGEY 78
PRK10140 PRK10140
N-acetyltransferase;
83-160 9.52e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 43.43  E-value: 9.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488052714  83 EFQIIIDPKYQGYGYAAEATRLAMDYAFSVLNMHKLYLVVDKENEKAVHVYKKVGFVVEGELQDEFFVDGNYHNAIRM 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-162 1.05e-05

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 42.67  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   5 LKLRPLEREDLKFVHELnnnahIMSYWFEEPYEAFvelqdlydkhihdqserrFIVEKDNEMVGLVELVEID----YIHR 80
Cdd:COG1246    1 MTIRPATPDDVPAILEL-----IRPYALEEEIGEF------------------WVAEEDGEIVGCAALHPLDedlaELRS 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714  81 rtefqIIIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYLVVdkeNEKAVHVYKKVGFvVEGELQDEFFVDGNYHNAIRM 160
Cdd:COG1246   58 -----LAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGF-EEIDKEDLPYAKVWQRDSVVM 127


                 ..
gi 488052714 161 CM 162
Cdd:COG1246  128 EK 129
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 13-145 1.04e-04

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 433280  Cd Length: 145  Bit Score: 40.20  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   13 EDLKFVHELNNNAHIMSYWfeEPYEAFVELQDLYDKHIHDQSERRFIVEKDNEMVGLVEL--VEIDYIHRRTEFQ----- 85
Cdd:pfam13523   4 ADLELLHRWMNDPRVAFWW--MLAGPLEQVREYLARLAADPHSHPYIGLLDGEPFGYFEIywAKEDRLGEYYDARpgdrg 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488052714   86 ---IIIDPKYQGYGYAAEATRLAMDYAFsvLNMHKLYLVV--DKENEKAVHVYKKVGFVVEGELQ 145
Cdd:pfam13523  82 ihlLIGEPAFRGRGFTTALLRALVHYLF--ADPRTRRVVVepDVRNERAIRLLERAGFRKVKEID 144
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 34-145 3.09e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 38.79  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488052714   34 EPYEAFVELQDLYdKHIHDQSERRFIVEKDNEMVGLVELVEIDYIHRrtefqIIIDPKYQGYGYAAEATRLAMDYAfSVL 113
Cdd:pfam13673  11 ETFYEFISPEALR-ERIDQGEYFFFVAFEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYA-EKD 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 488052714  114 NMHKLYLVVDKENEkAVHVYKKVGFVVEGELQ 145
Cdd:pfam13673  84 GIKLSELTVNASPY-AVPFYEKLGFRATGPEQ 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-120 9.62e-04

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.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 9.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488052714  58 FIVEKDNEMVGLVELVEIDYIHRRTEFQ-IIIDPKYQGYGYAAEATRLAMDYAFSvLNMHKLYL 120
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRL 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH