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Conserved domains on  [gi|489932797|ref|WP_003836113|]
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MULTISPECIES: 50S ribosomal protein L7/L12-serine acetyltransferase [Citrobacter]

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

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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 ...
 1-177 2.50e-124

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 PRK10151:

Pssm-ID: 473072  Cd Length: 179  Bit Score: 347.52  E-value: 2.50e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   1 MSEIIIVSDALELRAVEEQHVTPLHQLVLKNKVWLQQSLNWPQFVTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQGEVAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  81 VISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGCLRQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*..
gi 489932797 161 FLNGDYYDVNLYARIID 177
Cdd:PRK10151 161 YLNGAYDDVNLYARIID 177
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-177 2.50e-124

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 347.52  E-value: 2.50e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   1 MSEIIIVSDALELRAVEEQHVTPLHQLVLKNKVWLQQSLNWPQFVTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQGEVAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  81 VISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGCLRQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*..
gi 489932797 161 FLNGDYYDVNLYARIID 177
Cdd:PRK10151 161 YLNGAYDDVNLYARIID 177
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-178 3.79e-41

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: 136.28  E-value: 3.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   4 IIIVSDALELRAVEEQHVTPLHQLVLKNKVWLQqslnWPQFVTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQ--GEVAGV 81
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARY----LPGPPYSLEEARAWLERLLADWADGGALPFAIEDKedGELIGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  82 ISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGCLRQAEF 161
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156

                        170
                 ....*....|....*..
gi 489932797 162 LNGDYYDVNLYARIIDD 178
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-151 1.80e-21

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 85.09  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   11 LELRAVEEQHVTPLHQLVLKNKVWlQQSLNWPqfvTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQGE-VAGVISFNQIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVM-RYGVPWP---LTLEEAREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489932797   90 LNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQ 151
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 69-132 9.65e-08

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: 46.89  E-value: 9.65e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489932797  69 MFLIFEQGEVAGVISFNQIEPLNRAAYIGY-WLDEDHQGKGILSQALQALIQhYAQRQEIRRFVI 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEE-EARERGAKRLRL 64
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 61-173 5.28e-07

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: 46.97  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   61 LHQRGYAKMFLIFEQGEVAGVISFNQIEPLNRAAYIGYW---LDEDHQGKGILSQALQaliqhYAQRQeIRRFVIKCRVd 137
Cdd:TIGR03585  45 LKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLEEAALE-----YAFEH-LGLHKLSLEV- 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489932797  138 nVKSNQVALR----NGFQLEGCLRQaeflNGDYYDVNLYA 173
Cdd:TIGR03585 118 -LESNNKALKlyekFGFEREGVFRQ----GGEYYDVLLMY 152
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-177 2.50e-124

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 347.52  E-value: 2.50e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   1 MSEIIIVSDALELRAVEEQHVTPLHQLVLKNKVWLQQSLNWPQFVTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQGEVAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  81 VISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGCLRQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*..
gi 489932797 161 FLNGDYYDVNLYARIID 177
Cdd:PRK10151 161 YLNGAYDDVNLYARIID 177
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-178 3.79e-41

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: 136.28  E-value: 3.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   4 IIIVSDALELRAVEEQHVTPLHQLVLKNKVWLQqslnWPQFVTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQ--GEVAGV 81
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARY----LPGPPYSLEEARAWLERLLADWADGGALPFAIEDKedGELIGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  82 ISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGCLRQAEF 161
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156

                        170
                 ....*....|....*..
gi 489932797 162 LNGDYYDVNLYARIIDD 178
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-151 1.80e-21

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 85.09  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   11 LELRAVEEQHVTPLHQLVLKNKVWlQQSLNWPqfvTSVEDTRKNVQGNMMLHQRGYAKMFLIFEQGE-VAGVISFNQIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVM-RYGVPWP---LTLEEAREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489932797   90 LNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQ 151
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
74-176 1.52e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 62.32  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  74 EQGEVAGVISFNQIEPLNRAAYIGYW---LDEDHQGKGILSQALQALIQHyAQRQEIRRFVIKCRVDNVKSNQVALRNGF 150
Cdd:COG1247   59 EDGEVVGFASLGPFRPRPAYRGTAEEsiyVDPDARGRGIGRALLEALIER-ARARGYRRLVAVVLADNEASIALYEKLGF 137

                         90       100
                 ....*....|....*....|....*.
gi 489932797 151 QLEGCLRQAEFLNGDYYDVNLYARII 176
Cdd:COG1247  138 EEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 70-150 1.89e-12

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: 60.99  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   70 FLIFEQGEVAGVISFNQIEPLNRAAYI-GYWLDEDHQGKGILSQALQALIQhYAQRQEIRRFVIKCRVDNVKSNQVALRN 148
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLE-WARERGCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 489932797  149 GF 150
Cdd:pfam00583 115 GF 116
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
61-173 5.39e-09

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 53.20  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  61 LHQRGYAKMFLIF--EQGEVAGVISF-NQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVD 137
Cdd:PRK10809  69 FHKQGSAFYFALLdpDEKEIIGVANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPH 148

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489932797 138 NVKSNQVALRNGFQLEGCLRQAEFLNGDYYDVNLYA 173
Cdd:PRK10809 149 NKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTA 184
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 69-132 9.65e-08

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: 46.89  E-value: 9.65e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489932797  69 MFLIFEQGEVAGVISFNQIEPLNRAAYIGY-WLDEDHQGKGILSQALQALIQhYAQRQEIRRFVI 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEE-EARERGAKRLRL 64
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 61-173 5.28e-07

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: 46.97  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   61 LHQRGYAKMFLIFEQGEVAGVISFNQIEPLNRAAYIGYW---LDEDHQGKGILSQALQaliqhYAQRQeIRRFVIKCRVd 137
Cdd:TIGR03585  45 LKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLEEAALE-----YAFEH-LGLHKLSLEV- 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489932797  138 nVKSNQVALR----NGFQLEGCLRQaeflNGDYYDVNLYA 173
Cdd:TIGR03585 118 -LESNNKALKlyekFGFEREGVFRQ----GGEYYDVLLMY 152
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
70-153 9.78e-07

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 46.44  E-value: 9.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  70 FLIFEQGEVAGVISF----NQIePLNRAAYIGYWLDEDHQGKGILSQALQALIQHyAQRQEIRRFVIKCRVDNVKSNQVA 145
Cdd:COG3981   66 WLVDEDGRIVGAINLrhelNEF-LLRVGGHIGYGVRPSERGKGYATEMLRLALEE-ARELGLDRVLITCDKDNIASRKVI 143


                 ....*...
gi 489932797 146 LRNGFQLE 153
Cdd:COG3981  144 EANGGVLE 151
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
70-171 1.59e-06

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 45.82  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   70 FLIFEQGEVAGVISFNQIEPL-NRAAYIGYWLDEDHQgKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRN 148
Cdd:pfam13420  52 FGVAESDRLIGYATLRQFDYVkTHKAELSFYVVKNND-EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAI 130

                          90       100
                  ....*....|....*....|...
gi 489932797  149 GFQLEGCLRQAEFLNGDYYDVNL 171
Cdd:pfam13420 131 GFEWLGIERNAIKKNGRWIDMMW 153
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 70-166 4.80e-05

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 42.09  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  70 FLIFEQGEVAGVISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNG 149
Cdd:PRK15130  60 FVVECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLG 139

                         90
                 ....*....|....*..
gi 489932797 150 FQLEGCLRQAEFLNGDY 166
Cdd:PRK15130 140 FEVEGELIHEFFINGEY 156
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 42-151 1.14e-04

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.42  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  42 PQFVTSVEDTRKNVQGnmMLHQRGYAKMFLIFEQGEVAGVISFNQIEPlnRAAYIG--YwLDEDHQGKGILSQALQALIQ 119
Cdd:COG0454   11 INFILLIEALDAELKA--MEGSLAGAEFIAVDDKGEPIGFAGLRRLDD--KVLELKrlY-VLPEYRGKGIGKALLEALLE 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489932797 120 hYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQ 151
Cdd:COG0454   86 -WARERGCTALELDTLDGNPAAIRFYERLGFK 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
77-161 2.24e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 38.35  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  77 EVAGVISFNQiePLNRAAYIGY-WLDEDHQGKGILSQALQALIQHyAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLEGC 155
Cdd:COG3393    1 ELVAMAGVRA--ESPGVAEISGvYTHPEYRGRGLASALVAALARE-ALARGARTPFLYVDADNPAARRLYERLGFRPVGE 77


                 ....*.
gi 489932797 156 LRQAEF 161
Cdd:COG3393   78 YATVLF 83
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 67-151 1.35e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 36.28  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797   67 AKMFLIFEQGEVAGVISFNQIEPLNRAAYIGYWLDEDHQGKGILSQALQALIQHYAQRqeirrfviKCRVDNVKSNQVAL 146
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEG--------GIKLLELETTNRAA 74


                  ....*....
gi 489932797  147 ----RNGFQ 151
Cdd:pfam13508  75 afyeKLGFE 83
PRK10140 PRK10140
N-acetyltransferase;
76-175 2.24e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 36.88  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932797  76 GEVAGVISFNQIEPLNRA--AYIGYWLDEDHQGKGILSQALQALIQHYAQRQEIRRFVIKCRVDNVKSNQVALRNGFQLE 153
Cdd:PRK10140  60 GDVVGHLTIDVQQRPRRShvADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIE 139

                         90       100
                 ....*....|....*....|..
gi 489932797 154 GCLRQAEFLNGDYYDVNLYARI 175
Cdd:PRK10140 140 GTGKKYALRNGEYVDAYYMARV 161
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-154 2.58e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.79  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489932797  80 GVISFnQIEPLNRAAYIGY-WLDEDHQGKGILSQALQALIQHYAQRQeIRRFVIKCRVDNVKSNQVALRNGFQLEG 154
Cdd:COG0456    1 GFALL-GLVDGGDEAEIEDlAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVG 74
 
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.
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