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Conserved domains on  [gi|15598466|ref|NP_251960|]
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hypothetical protein PA3270 [Pseudomonas aeruginosa PAO1]

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, ...
13-181 7.59e-31

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: 7.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  13 ITLQRGALRLEPLVEADIPELVSLAeANREALQYMDGPTRP-----DWYRQSLAEQREGRALPLAVRLGV--QLVGTTRF 85
Cdd:COG1670   1 PTLETERLRLRPLRPEDAEALAELL-NDPEVARYLPGPPYSleearAWLERLLADWADGGALPFAIEDKEdgELIGVVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  86 AEFLPALPACEIGWtWLDQAQHGSGLNRMIKYLMLKHAFDNLRMVRVQLSTAASNLRAQGAIDKLGAQREGVLRNHRRLa 165
Cdd:COG1670  80 YDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI- 157
                       170
                ....*....|....*.
gi 15598466 166 GGRLDDTFVYSITDHE 181
Cdd:COG1670 158 DGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
13-181 7.59e-31

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: 7.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  13 ITLQRGALRLEPLVEADIPELVSLAeANREALQYMDGPTRP-----DWYRQSLAEQREGRALPLAVRLGV--QLVGTTRF 85
Cdd:COG1670   1 PTLETERLRLRPLRPEDAEALAELL-NDPEVARYLPGPPYSleearAWLERLLADWADGGALPFAIEDKEdgELIGVVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  86 AEFLPALPACEIGWtWLDQAQHGSGLNRMIKYLMLKHAFDNLRMVRVQLSTAASNLRAQGAIDKLGAQREGVLRNHRRLa 165
Cdd:COG1670  80 YDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI- 157
                       170
                ....*....|....*.
gi 15598466 166 GGRLDDTFVYSITDHE 181
Cdd:COG1670 158 DGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
20-153 1.07e-16

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 72.76  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466    20 LRLEPLVEADIPELVSLAeANREALQYMDGPTRP-----DWYRQSLAEQREGRALPLAVRL-GVQLVGTTRFAEFLPALP 93
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWPLTleearEWLARIWAADEAERGYGWAIELkDTGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466    94 ACEIGWtWLDQAQHGSGLNRMIKYLMLKHAFDNLRMVRVQLSTAASNLRAQGAIDKLGAQ 153
Cdd:pfam13302  81 RAELGY-WLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
13-181 7.59e-31

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: 7.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  13 ITLQRGALRLEPLVEADIPELVSLAeANREALQYMDGPTRP-----DWYRQSLAEQREGRALPLAVRLGV--QLVGTTRF 85
Cdd:COG1670   1 PTLETERLRLRPLRPEDAEALAELL-NDPEVARYLPGPPYSleearAWLERLLADWADGGALPFAIEDKEdgELIGVVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  86 AEFLPALPACEIGWtWLDQAQHGSGLNRMIKYLMLKHAFDNLRMVRVQLSTAASNLRAQGAIDKLGAQREGVLRNHRRLa 165
Cdd:COG1670  80 YDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI- 157
                       170
                ....*....|....*.
gi 15598466 166 GGRLDDTFVYSITDHE 181
Cdd:COG1670 158 DGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
20-153 1.07e-16

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 72.76  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466    20 LRLEPLVEADIPELVSLAeANREALQYMDGPTRP-----DWYRQSLAEQREGRALPLAVRL-GVQLVGTTRFAEFLPALP 93
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWPLTleearEWLARIWAADEAERGYGWAIELkDTGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466    94 ACEIGWtWLDQAQHGSGLNRMIKYLMLKHAFDNLRMVRVQLSTAASNLRAQGAIDKLGAQ 153
Cdd:pfam13302  81 RAELGY-WLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
19-175 8.98e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.83  E-value: 8.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  19 ALRLEPLVEADIPELVSL-AEANREALQ-YMDGPTRPDWYRQSLAEQREGRALPLAVRLGVQLVGttrFAEFLPALPACE 96
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIyNEAIAEGTAtFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVG---FASLGPFRPRPA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598466  97 IGWTW-----LDQAQHGSGLNRmikyLMLKHAFDNLR---MVRVQLSTAASNLRAQGAIDKLGAQREGVLRNHRRLAGGR 168
Cdd:COG1247  78 YRGTAeesiyVDPDARGRGIGR----ALLEALIERARargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRW 153

                ....*..
gi 15598466 169 LDDTFVY 175
Cdd:COG1247 154 LDLVLMQ 160
 
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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