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Conserved domains on  [gi|491530200|ref|WP_005387823|]
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MULTISPECIES: GNAT family N-acetyltransferase [Vibrio]

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, ...
6-180 8.93e-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: 130.50  E-value: 8.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   6 EIIAPRLALKLIPAEEAHSLQRLLAeSPSLHQWLDWCDknVTLKTAQDFLLATRLNWVKTEAFGFGIYERQSNTLVGMAA 85
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN-DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  86 VNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARNRFIFQ 165
Cdd:COG1670   79 LYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 491530200 166 GKPKDGVVFSLLPTD 180
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
6-180 8.93e-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: 130.50  E-value: 8.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   6 EIIAPRLALKLIPAEEAHSLQRLLAeSPSLHQWLDWCDknVTLKTAQDFLLATRLNWVKTEAFGFGIYERQSNTLVGMAA 85
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN-DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  86 VNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARNRFIFQ 165
Cdd:COG1670   79 LYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 491530200 166 GKPKDGVVFSLLPTD 180
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-153 4.20e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 89.33  E-value: 4.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   11 RLALKLIPAEEAHSLQRLLAEsPSLHQWldWCDKNVTLKTAQDFLLATRLNWVKTEAFGFGIYERQSNtLVGMAAVNELY 90
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD-PEVMRY--GVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDID 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491530200   91 HTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQ 153
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
5-166 1.97e-06

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 45.91  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   5 FEIIAPRLALKLIPAEEAH--SLQRLLAESPS-LHQWLDW----CDKNVTLKTAQDFLLATRLNWVKTeafgFGIYerQS 77
Cdd:PRK10151   2 TEIIPVSESLELHAVDESHvtPLHQLVCKNKTwLQQSLNWpqfvQSEEDTRKTVQGNVMLHQRGYAKM----FMIF--KE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  78 NTLVGMAAVNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALiesvgAQkeai 157
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQV-----AL---- 146

                 ....*....
gi 491530200 158 aRNRFIFQG 166
Cdd:PRK10151 147 -RNGFTLEG 154
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
6-180 8.93e-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: 130.50  E-value: 8.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   6 EIIAPRLALKLIPAEEAHSLQRLLAeSPSLHQWLDWCDknVTLKTAQDFLLATRLNWVKTEAFGFGIYERQSNTLVGMAA 85
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN-DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  86 VNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARNRFIFQ 165
Cdd:COG1670   79 LYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 491530200 166 GKPKDGVVFSLLPTD 180
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-153 4.20e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 89.33  E-value: 4.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   11 RLALKLIPAEEAHSLQRLLAEsPSLHQWldWCDKNVTLKTAQDFLLATRLNWVKTEAFGFGIYERQSNtLVGMAAVNELY 90
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD-PEVMRY--GVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDID 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491530200   91 HTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQ 153
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
98-153 4.08e-12

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 61.08  E-value: 4.08e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491530200  98 IGYWVADRYQRQGYAQEAVKALAEFCfAKLSLTRLEIVCDPDNEASQALIESVGAQ 153
Cdd:COG3981   95 IGYGVRPSERGKGYATEMLRLALEEA-RELGLDRVLITCDKDNIASRKVIEANGGV 149
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
33-151 1.29e-11

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: 58.68  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   33 PSLHQWLDWCdknvTLKTAQDFLLATRLNWVKTEAFGFGIYERqSNTLVGMAAVNELYHTFNMASI-GYWVADRYQRQGY 111
Cdd:pfam00583   2 EALYELLSEE----FPEPWPDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 491530200  112 AQEAVKALAEFCFaKLSLTRLEIVCDPDNEASQALIESVG 151
Cdd:pfam00583  77 GTALLQALLEWAR-ERGCERIFLEVAADNLAAIALYEKLG 115
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
5-166 1.97e-06

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 45.91  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   5 FEIIAPRLALKLIPAEEAH--SLQRLLAESPS-LHQWLDW----CDKNVTLKTAQDFLLATRLNWVKTeafgFGIYerQS 77
Cdd:PRK10151   2 TEIIPVSESLELHAVDESHvtPLHQLVCKNKTwLQQSLNWpqfvQSEEDTRKTVQGNVMLHQRGYAKM----FMIF--KE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  78 NTLVGMAAVNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALiesvgAQkeai 157
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQV-----AL---- 146

                 ....*....
gi 491530200 158 aRNRFIFQG 166
Cdd:PRK10151 147 -RNGFTLEG 154
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
67-176 1.20e-05

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 43.96  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  67 AFGFGIYERQSNTLVGMAAV-NELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQA 145
Cdd:PRK10809  75 AFYFALLDPDEKEIIGVANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGD 154
                         90       100       110
                 ....*....|....*....|....*....|.
gi 491530200 146 LIESVGAQKEAIARNRFIFQGKPKDGVVFSL 176
Cdd:PRK10809 155 LLARLGFEKEGYAKDYLLIDGQWRDHVLTAL 185
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
102-177 3.68e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 41.90  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491530200 102 VADRYQRQGYAQEAVKALAEFCfAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARNRFIFQGKPKDGVVFSLL 177
Cdd:COG1247   88 VDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
101-160 1.72e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 38.87  E-value: 1.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200 101 WVADRYQRQGYAQEAVKALAEFCfAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARN 160
Cdd:COG0456   20 AVDPEYRGRGIGRALLEAALERA-RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 5.38e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 35.81  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200   14 LKLIPAEEAHSLQRLLAESPSLHQWldwcdKNVTLKTAQDfLLATRLNWVKTE-AFGFGIYErqSNTLVGMAAVNEL-YH 91
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAF-----TQEYAHSSIE-EFETFLAAYLSPgEIVFGVAE--SDRLIGYATLRQFdYV 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491530200   92 TFNMASIGYWVADRYQRqGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARNRFIFQGKPKD 170
Cdd:pfam13420  73 KTHKAELSFYVVKNNDE-GINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
81-167 9.83e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 35.16  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491530200  81 VGMAAVNELYHTFNMASIGYWVADRYQRQGYAQEAVKALAEFCFAKLSLTRLEIVCDPDNEASQALIESVGAQKEAIARN 160
Cdd:PRK15130  69 AGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIH 148

                 ....*..
gi 491530200 161 RFIFQGK 167
Cdd:PRK15130 149 EFFINGE 155
 
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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