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Conserved domains on  [gi|446063018|ref|WP_000140873|]
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MULTISPECIES: 50S ribosomal protein L7/L12-serine acetyltransferase [Enterobacteriaceae]

Protein Classification

50S ribosomal protein L7/L12-serine acetyltransferase( domain architecture ID 10013440)

50S ribosomal protein L7/L12-serine acetyltransferase which acetylates the N-terminal serine of ribosomal protein L7/L12, similar to Escherichia coli RimL

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.10e-128

50S ribosomal protein L7/L12-serine acetyltransferase;


:

Pssm-ID: 182270  Cd Length: 179  Bit Score: 358.30  E-value: 1.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   1 MTETIKVSESLELHAVAENHVKPLYQLICKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  81 VISFNRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*....
gi 446063018 161 FLNDAYDDVNLYARIIDSQ 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.10e-128

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 358.30  E-value: 1.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   1 MTETIKVSESLELHAVAENHVKPLYQLICKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  81 VISFNRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*....
gi 446063018 161 FLNDAYDDVNLYARIIDSQ 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-177 2.72e-39

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: 131.66  E-value: 2.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   8 SESLELHAVAENHVKPLYQLiCKNKTWLQQslnWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFK--EDELIGVISFN 85
Cdd:COG1670    5 TERLRLRPLRPEDAEALAEL-LNDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  86 RIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAEFLNDA 165
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|..
gi 446063018 166 YDDVNLYARIID 177
Cdd:COG1670  161 YRDHVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-150 1.45e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 90.48  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   11 LELHAVAENHVKPLYQlICKNKTWLQQSLNWPQfvqSEEDTRKTVQGNVMLHQRGYAKMFMIF-KEDELIGVISFNRIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFE-LLSDPEVMRYGVPWPL---TLEEAREWLARIWAADEAERGYGWAIElKDTGFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446063018   90 LNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGF 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 69-125 9.53e-07

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: 44.19  E-value: 9.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446063018  69 MFMIFKEDELIGVISFNRIEPLNKTAEIGY-WLDESHQGQGIISQALQALIHHYAQSG 125
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERG 58
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 61-158 1.68e-04

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: 40.03  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   61 LHQRGYAKMFMIFKEDELIGVISFNRIEPLNKTAEIGYW---LDESHQGQGIISQALQalihhYAQSgELRRFVIKCRVd 137
Cdd:TIGR03585  45 LKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLEEAALE-----YAFE-HLGLHKLSLEV- 117

                          90       100
                  ....*....|....*....|....*
gi 446063018  138 nPQSNQVALR----NGFILEGCLKQ 158
Cdd:TIGR03585 118 -LESNNKALKlyekFGFEREGVFRQ 141
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.10e-128

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 358.30  E-value: 1.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   1 MTETIKVSESLELHAVAENHVKPLYQLICKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  81 VISFNRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160

                        170
                 ....*....|....*....
gi 446063018 161 FLNDAYDDVNLYARIIDSQ 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-177 2.72e-39

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: 131.66  E-value: 2.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   8 SESLELHAVAENHVKPLYQLiCKNKTWLQQslnWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFK--EDELIGVISFN 85
Cdd:COG1670    5 TERLRLRPLRPEDAEALAEL-LNDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  86 RIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGFILEGCLKQAEFLNDA 165
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|..
gi 446063018 166 YDDVNLYARIID 177
Cdd:COG1670  161 YRDHVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-150 1.45e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 90.48  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   11 LELHAVAENHVKPLYQlICKNKTWLQQSLNWPQfvqSEEDTRKTVQGNVMLHQRGYAKMFMIF-KEDELIGVISFNRIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFE-LLSDPEVMRYGVPWPL---TLEEAREWLARIWAADEAERGYGWAIElKDTGFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446063018   90 LNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPQSNQVALRNGF 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 70-150 1.32e-13

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: 63.69  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   70 FMIFKEDELIGVISFNRIEPLNKTAEI-GYWLDESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPQSNQVALRN 148
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKL 114


                  ..
gi 446063018  149 GF 150
Cdd:pfam00583 115 GF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
75-176 1.83e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  75 EDELIGVISFNRI---EPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPQSNQVALRNGFI 151
Cdd:COG1247   60 DGEVVGFASLGPFrprPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFE 138

                         90       100
                 ....*....|....*....|....*
gi 446063018 152 LEGCLKQAEFLNDAYDDVNLYARII 176
Cdd:COG1247  139 EVGTLPEVGFKFGRWLDLVLMQKRL 163
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
70-153 4.95e-07

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 47.21  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  70 FMIFKEDELIGVISFnRIEpLNKTAE-----IGYWLDESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPQSNQV 144
Cdd:COG3981   66 WLVDEDGRIVGAINL-RHE-LNEFLLrvgghIGYGVRPSERGKGYATEMLRLALEEARELG-LDRVLITCDKDNIASRKV 142


                 ....*....
gi 446063018 145 ALRNGFILE 153
Cdd:COG3981  143 IEANGGVLE 151
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 69-125 9.53e-07

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: 44.19  E-value: 9.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446063018  69 MFMIFKEDELIGVISFNRIEPLNKTAEIGY-WLDESHQGQGIISQALQALIHHYAQSG 125
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERG 58
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
61-157 1.02e-05

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 43.96  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018  61 LHQRGYAKMFMIF--KEDELIGVISF-NRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVD 137
Cdd:PRK10809  69 FHKQGSAFYFALLdpDEKEIIGVANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPH 148

                         90       100
                 ....*....|....*....|
gi 446063018 138 NPQSNQVALRNGFILEGCLK 157
Cdd:PRK10809 149 NKRSGDLLARLGFEKEGYAK 168
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
77-154 1.13e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.12  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446063018  77 ELIGVISFNRiePLNKTAEIGY-WLDESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPQSNQVALRNGFILEG 154
Cdd:COG3393    1 ELVAMAGVRA--ESPGVAEISGvYTHPEYRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYERLGFRPVG 76
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 61-158 1.68e-04

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: 40.03  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446063018   61 LHQRGYAKMFMIFKEDELIGVISFNRIEPLNKTAEIGYW---LDESHQGQGIISQALQalihhYAQSgELRRFVIKCRVd 137
Cdd:TIGR03585  45 LKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLEEAALE-----YAFE-HLGLHKLSLEV- 117

                          90       100
                  ....*....|....*....|....*
gi 446063018  138 nPQSNQVALR----NGFILEGCLKQ 158
Cdd:TIGR03585 118 -LESNNKALKlyekFGFEREGVFRQ 141
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 75-150 6.29e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 38.11  E-value: 6.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446063018  75 EDELIGVISFNRIEPlnKTAEIG--YWLDEsHQGQGIISQALQALIhHYAQSGELRRFVIKCRVDNPQSNQVALRNGF 150
Cdd:COG0454   42 KGEPIGFAGLRRLDD--KVLELKrlYVLPE-YRGKGIGKALLEALL-EWARERGCTALELDTLDGNPAAIRFYERLGF 115
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 67-131 2.02e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.89  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446063018   67 AKMFMIFKEDELIGVISFNRIEPLNKTAEIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFV 131
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL 67
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-154 6.87e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 34.25  E-value: 6.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446063018  80 GVISFnRIEPLNKTAEIGY-WLDESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPQSNQVALRNGFILEG 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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