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Conserved domains on  [gi|635780969|gb|KDF62391|]
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hypothetical protein AF40_01169 [Enterobacter roggenkampii MGH 54]

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 ...
 3-176 6.27e-121

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: 338.66  E-value: 6.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   3 SEIIPVTQDIELRAVEERYTADLHNLVVKNRAFLQTAFDWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFKDDALVGV 82
Cdd:PRK10151   2 TEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  83 LSFNTIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEY 162
Cdd:PRK10151  82 LSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEY 161

                        170
                 ....*....|....
gi 635780969 163 LNGRFDDVNIYGRI 176
Cdd:PRK10151 162 LNGAYDDVNLYARI 175
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-176 6.27e-121

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 338.66  E-value: 6.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   3 SEIIPVTQDIELRAVEERYTADLHNLVVKNRAFLQTAFDWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFKDDALVGV 82
Cdd:PRK10151   2 TEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  83 LSFNTIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEY 162
Cdd:PRK10151  82 LSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEY 161

                        170
                 ....*....|....
gi 635780969 163 LNGRFDDVNIYGRI 176
Cdd:PRK10151 162 LNGAYDDVNLYARI 175
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 9-176 1.57e-32

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: 114.33  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   9 TQDIELRAVEERYTADLHNLVvKNRAFLQTafdWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFK--DDALVGVLSFN 86
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELL-NDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  87 TIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEYLNGR 166
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|
gi 635780969 167 FDDVNIYGRI 176
Cdd:COG1670  161 YRDHVLYSLL 170
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-152 3.02e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 66.22  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   12 IELRAVEERYTADLHNLVvKNRAFLQTAFDWAQhaiSEEDTRRNVQS--NQMLHQRGYAkmFLIF-KDDALVGVLSFNTI 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWPL---TLEEAREWLARiwAADEAERGYG--WAIElKDTGFIGSIGLYDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635780969   89 EPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFT 152
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 70-126 1.16e-05

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: 41.49  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 635780969  70 MFLIFKDDALVGVLSFNTIEPTNKAGYIGY-WLDEAHQGQGILSQSLQAFMRYYAERG 126
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERG 58
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-176 6.27e-121

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 338.66  E-value: 6.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   3 SEIIPVTQDIELRAVEERYTADLHNLVVKNRAFLQTAFDWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFKDDALVGV 82
Cdd:PRK10151   2 TEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  83 LSFNTIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEY 162
Cdd:PRK10151  82 LSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEY 161

                        170
                 ....*....|....
gi 635780969 163 LNGRFDDVNIYGRI 176
Cdd:PRK10151 162 LNGAYDDVNLYARI 175
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 9-176 1.57e-32

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: 114.33  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   9 TQDIELRAVEERYTADLHNLVvKNRAFLQTafdWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFK--DDALVGVLSFN 86
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELL-NDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  87 TIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEYLNGR 166
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|
gi 635780969 167 FDDVNIYGRI 176
Cdd:COG1670  161 YRDHVLYSLL 170
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-152 3.02e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 66.22  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   12 IELRAVEERYTADLHNLVvKNRAFLQTAFDWAQhaiSEEDTRRNVQS--NQMLHQRGYAkmFLIF-KDDALVGVLSFNTI 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWPL---TLEEAREWLARiwAADEAERGYG--WAIElKDTGFIGSIGLYDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635780969   89 EPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFT 152
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-151 1.39e-10

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: 55.99  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   36 LQTAFDWAQHAISEEDTRRNVQSNQMLHQRGYAKMFLIFKDDALVGVLSFNTIEPTNKAGYI-GYWLDEAHQGQGILSQS 114
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 635780969  115 LQAFMRYYAERGeIRRFVIKCRVANQHSNSVAVRNGF 151
Cdd:pfam00583  81 LQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
8-169 1.07e-08

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 52.43  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969   8 VTQDIELRAVEERYTADLHNLVVKNRAFL---QTAFDWAQHAISEEDTRRNVQSNqmLHQRGYAKMFLIF--KDDALVGV 82
Cdd:PRK10809  14 TTDRLVVRLVHERDAWRLADYYAENRHFLkpwEPVRDESHCYPSGWQARLGMINE--FHKQGSAFYFALLdpDEKEIIGV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  83 LSF-NTIEPTNKAGYIGYWLDEAHQGQGILSQSLQAFMRYYAERGEIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAE 161
Cdd:PRK10809  92 ANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYL 171


                 ....*...
gi 635780969 162 YLNGRFDD 169
Cdd:PRK10809 172 LIDGQWRD 179
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
32-176 4.80e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.99  E-value: 4.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635780969  32 NRAFLQTAFDWAQHAISEEDTRRNVQSnqmLHQRGYAkMFLIFKDDALVGVLSFNTIEPTNKAGYIGYW---LDEAHQGQ 108
Cdd:COG1247   20 NEAIAEGTATFETEPPSEEEREAWFAA---ILAPGRP-VLVAEEDGEVVGFASLGPFRPRPAYRGTAEEsiyVDPDARGR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635780969 109 GILSQSLQAFMRYYAERGeIRRFVIKCRVANQHSNSVAVRNGFTLEGCLREAEYLNGRFDDVNIYGRI 176
Cdd:COG1247   96 GIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 70-126 1.16e-05

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: 41.49  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 635780969  70 MFLIFKDDALVGVLSFNTIEPTNKAGYIGY-WLDEAHQGQGILSQSLQAFMRYYAERG 126
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERG 58
 
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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