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Conserved domains on  [gi|1983701695|ref|WP_203452781|]
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AAC(6')-Ib family aminoglycoside 6'-N-acetyltransferase, partial [Lelliottia sp. RWM.1]

Protein Classification

N-acetyltransferase( domain architecture ID 11500359)

N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-180 7.82e-143

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


:

Pssm-ID: 275224  Cd Length: 184  Bit Score: 394.25  E-value: 7.82e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   1 NDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSG 80
Cdd:TIGR04431   5 NDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVALGSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  81 DGWWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPD 160
Cdd:TIGR04431  85 DGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTITTPD 164

                         170       180
                  ....*....|....*....|
gi 1983701695 161 GPAVYMVQTRQAFERTRSDA 180
Cdd:TIGR04431 165 GPAVYMVQTRQAFERARSAA 184
 
Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-180 7.82e-143

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


Pssm-ID: 275224  Cd Length: 184  Bit Score: 394.25  E-value: 7.82e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   1 NDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSG 80
Cdd:TIGR04431   5 NDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVALGSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  81 DGWWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPD 160
Cdd:TIGR04431  85 DGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTITTPD 164

                         170       180
                  ....*....|....*....|
gi 1983701695 161 GPAVYMVQTRQAFERTRSDA 180
Cdd:TIGR04431 165 GPAVYMVQTRQAFERARSAA 184
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-158 6.25e-46

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 147.67  E-value: 6.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  11 EHDLAMLYEWLNRSHIVEWWGGEearPTLADVQEqYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGWwEEETDP 90
Cdd:pfam13523   3 EADLELLHRWMNDPRVAFWWMLA---GPLEQVRE-YLARLAADPHSHPYIGLLDGEPFGYFEIYWAKEDRLGE-YYDARP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983701695  91 GVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 158
Cdd:pfam13523  78 GDRGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVKEIDL 145
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-156 3.04e-22

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: 87.75  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   2 DSVTLRLMTEHDLAMLYEWLNRSHIVEWWGG-----EEARPTLADVQEQYlpsvlAQESVTPYIAML--NGEPIGYAqsy 74
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGppyslEEARAWLERLLADW-----ADGGALPFAIEDkeDGELIGVV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  75 valgsgdGWWEEETDPGVRGIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQG 154
Cdd:COG1670    78 -------GLYDIDRANRSAEIGYWLAPAYW-GKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149


                  ..
gi 1983701695 155 TV 156
Cdd:COG1670   150 TL 151
AlcB smart01006
Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the ...
 11-54 3.40e-04

Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the proteins of a complex which mediates alcaligin biosynthesis in Bordetella and aerobactin biosynthesis in E. coli and other bacteria. The protein appears to catalyse N-acylation of the hydroxylamine group in N-hydroxyputrescine with succinyl CoA - an activated mono-thioester derivative of succinic acid that is an intermediate in the Krebs cycle.


Pssm-ID: 198074  Cd Length: 48  Bit Score: 36.78  E-value: 3.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1983701695   11 EHDLAMLYEWLNRSHIVEWWGGEEarpTLADVqEQYLPSVLAQE 54
Cdd:smart01006   6 EQDLPLLHRWMNRPHVAAFWGMGG---PLEEV-RAYLRAQLADP 45
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 7.74e-03

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: 33.79  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1983701695  59 YIAMLNGEPIGYAQSYVALGSGDGWWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLFN 123
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDlaVLPEYRG------------KGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-180 7.82e-143

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


Pssm-ID: 275224  Cd Length: 184  Bit Score: 394.25  E-value: 7.82e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   1 NDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSG 80
Cdd:TIGR04431   5 NDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVALGSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  81 DGWWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPD 160
Cdd:TIGR04431  85 DGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTITTPD 164

                         170       180
                  ....*....|....*....|
gi 1983701695 161 GPAVYMVQTRQAFERTRSDA 180
Cdd:TIGR04431 165 GPAVYMVQTRQAFERARSAA 184
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-158 6.25e-46

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 147.67  E-value: 6.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  11 EHDLAMLYEWLNRSHIVEWWGGEearPTLADVQEqYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGWwEEETDP 90
Cdd:pfam13523   3 EADLELLHRWMNDPRVAFWWMLA---GPLEQVRE-YLARLAADPHSHPYIGLLDGEPFGYFEIYWAKEDRLGE-YYDARP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983701695  91 GVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 158
Cdd:pfam13523  78 GDRGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVKEIDL 145
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-156 3.04e-22

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: 87.75  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   2 DSVTLRLMTEHDLAMLYEWLNRSHIVEWWGG-----EEARPTLADVQEQYlpsvlAQESVTPYIAML--NGEPIGYAqsy 74
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGppyslEEARAWLERLLADW-----ADGGALPFAIEDkeDGELIGVV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  75 valgsgdGWWEEETDPGVRGIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQG 154
Cdd:COG1670    78 -------GLYDIDRANRSAEIGYWLAPAYW-GKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149


                  ..
gi 1983701695 155 TV 156
Cdd:COG1670   150 TL 151
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-151 4.33e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 65.83  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   4 VTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEarPTLADVQEQYLPSVLAQESVTPY---IAMLNGEPIGYAqSYVALGSG 80
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWP--LTLEEAREWLARIWAADEAERGYgwaIELKDTGFIGSI-GLYDIDGE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983701695  81 DGWWEeetdpgvrgIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFE 151
Cdd:pfam13302  79 PERAE---------LGYWLGPDYW-GKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-150 5.06e-14

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: 64.85  E-value: 5.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  14 LAMLYEWLNRSHIVEWwggeeaRPTLADVQEQYLPsvlaQESVTPYIAMLNGEPIGYAQSYValgsgdgWWEEetdPGVR 93
Cdd:pfam00583   1 LEALYELLSEEFPEPW------PDEPLDLLEDWDE----DASEGFFVAEEDGELVGFASLSI-------IDDE---PPVG 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1983701695  94 GIDQLLANASQLGKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGF 150
Cdd:pfam00583  61 EIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-156 2.07e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 59.24  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   3 SVTLRLMTEHDL---AMLYEWLNRSHIVEWwggEEARPTLADVQEQYlpSVLAQESVTPYIAMLNGEPIGYA--QSYVAL 77
Cdd:COG1247     1 EMTIRPATPEDApaiAAIYNEAIAEGTATF---ETEPPSEEEREAWF--AAILAPGRPVLVAEEDGEVVGFAslGPFRPR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  78 GSGDGWWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLFNDPeVTKIQTDPSPSNLRAIRCYEKAGFERQGT 155
Cdd:COG1247    76 PAYRGTAEESiyVDPDARG------------RGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGT 142


                  .
gi 1983701695 156 V 156
Cdd:COG1247   143 L 143
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-167 3.04e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.08  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695   6 LRLMTEHDLAMLYEWLNRShiveWWGGEEARpTLADVQEQYLPSVLaqesvtpYIAMLNGEPIGYAQ-SYVALGSGDGWW 84
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA----FGPGREAE-LVDRLREDPAAGLS-------LVAEDDGEIVGHVAlSPVDIDGEGPAL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  85 EEE---TDPGVRGidqllanasqlgKGLGTKLVRALVELL--FNDPEVTkIQTDPSPSNLraircYEKAGFERQGTVTTP 159
Cdd:COG3153    69 LLGplaVDPEYRG------------QGIGRALMRAALEAAreRGARAVV-LLGDPSLLPF-----YERFGFRPAGELGLT 130


                  ....*....
gi 1983701695 160 DGP-AVYMV 167
Cdd:COG3153   131 LGPdEVFLA 139
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 106-167 1.06e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983701695 106 GKGLGTKLVRALVELLFnDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT-PDGPAVYMV 167
Cdd:COG0456    27 GRGIGRALLEAALERAR-ERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNyYGDDALVME 88
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
106-158 1.27e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.51  E-value: 1.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1983701695 106 GKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 158
Cdd:COG3393    29 GRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 59-152 5.91e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.83  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  59 YIAMLNGEPIGYAqSYVALGSGDGWWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLfNDPEVTKIQTDpsp 136
Cdd:pfam13508   6 FVAEDDGKIVGFA-ALLPLDDEGALAELRlaVHPEYRG------------QGIGRALLEAAEAAA-KEGGIKLLELE--- 68

                          90
                  ....*....|....*.
gi 1983701695 137 SNLRAIRCYEKAGFER 152
Cdd:pfam13508  69 TTNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 13-154 7.01e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 40.78  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  13 DLAMLYEWLNRSHIVEWwggeearptladvQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDgwweeetdpgv 92
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPW-------------TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAH----------- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983701695  93 rgIDQLLANASQLGKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGFERQG 154
Cdd:TIGR01575  57 --ILNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 26-161 2.50e-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: 39.18  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  26 IVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAqsyvALGSGdgwweeetdpgvRGIDQLLANASQL 105
Cdd:pfam13673   1 EAPDYSEEGIETFYEFISPEALRERIDQGEYFFFVAFEGGQIVGVI----ALRDR------------GHISLLFVDPDYQ 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1983701695 106 GKGLGTKLVRALVELLFND-PEVTKIQTDPSPSnlrAIRCYEKAGFERQGTVTTPDG 161
Cdd:pfam13673  65 GQGIGKALLEAVEDYAEKDgIKLSELTVNASPY---AVPFYEKLGFRATGPEQEFNG 118
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
59-167 3.13e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.01  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  59 YIAMLNGEPIGYAqsyVALGSGDGWWEEE---TDPGVRGidqllanasqlgKGLGTKLVRALVELLFNDPeVTKI----Q 131
Cdd:COG2153    37 LLAYDDGELVATA---RLLPPGDGEAKIGrvaVLPEYRG------------QGLGRALMEAAIEEARERG-ARRIvlsaQ 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1983701695 132 TdpspsnlRAIRCYEKAGFERQGTVTTPDG-PAVYMV 167
Cdd:COG2153   101 A-------HAVGFYEKLGFVPVGEEFLEAGiPHIDMR 130
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 33-161 3.39e-04

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: 38.82  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  33 EEARPT-LADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAqSYVALGSGDGWweeetdpgvrgIDQLLANASQLGKGLGT 111
Cdd:COG1246     4 RPATPDdVPAILELIRPYALEEEIGEFWVAEEDGEIVGCA-ALHPLDEDLAE-----------LRSLAVHPDYRGRGIGR 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1983701695 112 KLVRALVELLfNDPEVTKIQTDpspSNLRAIRCYEKAGFERQGTVTTPDG 161
Cdd:COG1246    72 RLLEALLAEA-RELGLKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYA 117
AlcB smart01006
Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the ...
 11-54 3.40e-04

Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the proteins of a complex which mediates alcaligin biosynthesis in Bordetella and aerobactin biosynthesis in E. coli and other bacteria. The protein appears to catalyse N-acylation of the hydroxylamine group in N-hydroxyputrescine with succinyl CoA - an activated mono-thioester derivative of succinic acid that is an intermediate in the Krebs cycle.


Pssm-ID: 198074  Cd Length: 48  Bit Score: 36.78  E-value: 3.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1983701695   11 EHDLAMLYEWLNRSHIVEWWGGEEarpTLADVqEQYLPSVLAQE 54
Cdd:smart01006   6 EQDLPLLHRWMNRPHVAAFWGMGG---PLEEV-RAYLRAQLADP 45
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 23-167 5.28e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 38.50  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983701695  23 RSHIVEWWGGEEARPTLADVQEQYLPSVLaqesvtpYIAMLNGEPIGYAqsyvalgsgdgwWEEETDPGVRGIDQLLANA 102
Cdd:COG0454     8 PEDINFILLIEALDAELKAMEGSLAGAEF-------IAVDDKGEPIGFA------------GLRRLDDKVLELKRLYVLP 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983701695 103 SQLGKGLGTKLVRALVELLfNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPDGPAVYMV 167
Cdd:COG0454    69 EYRGKGIGKALLEALLEWA-RERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKE 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 7.74e-03

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: 33.79  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1983701695  59 YIAMLNGEPIGYAQSYVALGSGDGWWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLFN 123
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDlaVLPEYRG------------KGIGSALLEAAEEEARE 56
 
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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