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Conserved domains on  [gi|503994342|ref|WP_014228336|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-200 2.80e-30

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: 110.47  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342  27 TALNGRFCRLEPLdTERHAADLFAAYAlgDDSDWTWLASTcPQSVESTANWI---TGKVMDDGLVPYAVIDLRAERAVGL 103
Cdd:COG1670    1 PTLETERLRLRPL-RPEDAEALAELLN--DPEVARYLPGP-PYSLEEARAWLerlLADWADGGALPFAIEDKEDGELIGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342 104 VSYMAIERAMGTVEIGHVTwSRAMKNTPLGTEAVWLLLQNGFAH-GYRRLEWKCDSMNLASRRAADRLGFTWEGRLRQRM 182
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 503994342 183 VRKGRTRDSDMLSIIDSE 200
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-200 2.80e-30

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: 110.47  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342  27 TALNGRFCRLEPLdTERHAADLFAAYAlgDDSDWTWLASTcPQSVESTANWI---TGKVMDDGLVPYAVIDLRAERAVGL 103
Cdd:COG1670    1 PTLETERLRLRPL-RPEDAEALAELLN--DPEVARYLPGP-PYSLEEARAWLerlLADWADGGALPFAIEDKEDGELIGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342 104 VSYMAIERAMGTVEIGHVTwSRAMKNTPLGTEAVWLLLQNGFAH-GYRRLEWKCDSMNLASRRAADRLGFTWEGRLRQRM 182
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 503994342 183 VRKGRTRDSDMLSIIDSE 200
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-173 2.16e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 65.06  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342   35 RLEPLdTERHAADLFAAYAlgdDSDWTWLASTCPQSVESTANWITGKVMDDGLVPYA--VIDLRAERAVGLVSYMAIERA 112
Cdd:pfam13302   3 LLRPL-TEEDAEALFELLS---DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYgwAIELKDTGFIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994342  113 MGTVEIGHVTWsRAMKNTPLGTEAVWLLLQNGFAH-GYRRLEWKCDSMNLASRRAADRLGFT 173
Cdd:pfam13302  79 PERAELGYWLG-PDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
42-200 2.25e-06

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 46.29  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342  42 ERHAADLFAAyaLGDDSDWTWLASTCPQSV---ESTANWITGKVM--DDGLVPYAVIdLRAERAVGLVSYMAIERAMGTV 116
Cdd:PRK10151  18 ESHVTPLHQL--VCKNKTWLQQSLNWPQFVqseEDTRKTVQGNVMlhQRGYAKMFMI-FKEDELIGVLSFNRIEPLNKTA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342 117 EIGHvtWsraMKNTPLGTEAVWLLLQnGFAHGY------RRLEWKCDSMNLASRRAADRLGFTWEGRLRQRMVRKGRTRD 190
Cdd:PRK10151  95 YIGY--W---LDESHQGQGIISQALQ-ALIHHYaqsgelRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNGAYDD 168
                        170
                 ....*....|.
gi 503994342 191 SDMLS-IIDSE 200
Cdd:PRK10151 169 VNLYArIIDSD 179
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-200 2.80e-30

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: 110.47  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342  27 TALNGRFCRLEPLdTERHAADLFAAYAlgDDSDWTWLASTcPQSVESTANWI---TGKVMDDGLVPYAVIDLRAERAVGL 103
Cdd:COG1670    1 PTLETERLRLRPL-RPEDAEALAELLN--DPEVARYLPGP-PYSLEEARAWLerlLADWADGGALPFAIEDKEDGELIGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342 104 VSYMAIERAMGTVEIGHVTwSRAMKNTPLGTEAVWLLLQNGFAH-GYRRLEWKCDSMNLASRRAADRLGFTWEGRLRQRM 182
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 503994342 183 VRKGRTRDSDMLSIIDSE 200
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-173 2.16e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 65.06  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342   35 RLEPLdTERHAADLFAAYAlgdDSDWTWLASTCPQSVESTANWITGKVMDDGLVPYA--VIDLRAERAVGLVSYMAIERA 112
Cdd:pfam13302   3 LLRPL-TEEDAEALFELLS---DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYgwAIELKDTGFIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994342  113 MGTVEIGHVTWsRAMKNTPLGTEAVWLLLQNGFAH-GYRRLEWKCDSMNLASRRAADRLGFT 173
Cdd:pfam13302  79 PERAELGYWLG-PDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
42-200 2.25e-06

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 46.29  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342  42 ERHAADLFAAyaLGDDSDWTWLASTCPQSV---ESTANWITGKVM--DDGLVPYAVIdLRAERAVGLVSYMAIERAMGTV 116
Cdd:PRK10151  18 ESHVTPLHQL--VCKNKTWLQQSLNWPQFVqseEDTRKTVQGNVMlhQRGYAKMFMI-FKEDELIGVLSFNRIEPLNKTA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342 117 EIGHvtWsraMKNTPLGTEAVWLLLQnGFAHGY------RRLEWKCDSMNLASRRAADRLGFTWEGRLRQRMVRKGRTRD 190
Cdd:PRK10151  95 YIGY--W---LDESHQGQGIISQALQ-ALIHHYaqsgelRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNGAYDD 168
                        170
                 ....*....|.
gi 503994342 191 SDMLS-IIDSE 200
Cdd:PRK10151 169 VNLYArIIDSD 179
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
59-172 2.89e-05

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: 42.12  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994342   59 DWTWLASTCPQSVESTANWITGKVMDDGLVPYAVIDLRAERAVGLVSYMAIERAMGTVEIGHVTWSRAMKNTPLGTEAVW 138
Cdd:pfam00583   3 ALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQ 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503994342  139 LLLQNGFAHGYRRLEWKCDSMNLASRRAADRLGF 172
Cdd:pfam00583  83 ALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
146-194 3.03e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.28  E-value: 3.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 503994342 146 AHGYRRLEWKCDSMNLASRRAADRLGFTWEGRLRQRMVRKGRTRDSDML 194
Cdd:COG1247  111 ARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159
 
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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