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Conserved domains on  [gi|15225174|ref|NP_180763|]
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Acyl-CoA N-acyltransferases (NAT) superfamily protein [Arabidopsis thaliana]

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
PubMed:  27367672|26818562|15581578|10940244
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, ...
 23-185 9.49e-48

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: 153.62  E-value: 9.49e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  23 EKIHLRPMTLSDVDDFMVWATDSNVTRFCTWEPYTsREAAIAYLNDAL----LPHPWLRAICL-DNDRPIGSISVTPVDE 97
Cdd:COG1670   6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYS-LEEARAWLERLLadwaDGGALPFAIEDkEDGELIGVVGLYDIDR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  98 I--RGEIGYVLGSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRD 175
Cdd:COG1670  85 AnrSAEIGYWLAPAYWGKGYATEALRALLDYAFEE-LGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163

                       170
                ....*....|
gi 15225174 176 MVMFSFLPSD 185
Cdd:COG1670 164 HVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 23-185 9.49e-48

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: 153.62  E-value: 9.49e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  23 EKIHLRPMTLSDVDDFMVWATDSNVTRFCTWEPYTsREAAIAYLNDAL----LPHPWLRAICL-DNDRPIGSISVTPVDE 97
Cdd:COG1670   6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYS-LEEARAWLERLLadwaDGGALPFAIEDkEDGELIGVVGLYDIDR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  98 I--RGEIGYVLGSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRD 175
Cdd:COG1670  85 AnrSAEIGYWLAPAYWGKGYATEALRALLDYAFEE-LGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163

                       170
                ....*....|
gi 15225174 176 MVMFSFLPSD 185
Cdd:COG1670 164 HVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 27-158 2.89e-35

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 120.53  E-value: 2.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174    27 LRPMTLSDVDDFMVWATDSNVTRFCTWEPYT---SREAAIAYLNDALLPHPWLRAICLDNDRPIGSISVTPVDEIRG--E 101
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTleeAREWLARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPEraE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225174   102 IGYVLGSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFV 158
Cdd:pfam13302  84 LGYWLGPDYWGKGYATEAVRALLEYAFEE-LGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
102-178 2.96e-04

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 39.72  E-value: 2.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225174  102 IGYVLGSKYWGKGIATEAVRlVAGEIFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRDMVM 178
Cdd:PRK10809 107 LGYSLGQKWQGQGLMFEALQ-AAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 23-185 9.49e-48

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: 153.62  E-value: 9.49e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  23 EKIHLRPMTLSDVDDFMVWATDSNVTRFCTWEPYTsREAAIAYLNDAL----LPHPWLRAICL-DNDRPIGSISVTPVDE 97
Cdd:COG1670   6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYS-LEEARAWLERLLadwaDGGALPFAIEDkEDGELIGVVGLYDIDR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  98 I--RGEIGYVLGSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRD 175
Cdd:COG1670  85 AnrSAEIGYWLAPAYWGKGYATEALRALLDYAFEE-LGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163

                       170
                ....*....|
gi 15225174 176 MVMFSFLPSD 185
Cdd:COG1670 164 HVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 27-158 2.89e-35

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 120.53  E-value: 2.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174    27 LRPMTLSDVDDFMVWATDSNVTRFCTWEPYT---SREAAIAYLNDALLPHPWLRAICLDNDRPIGSISVTPVDEIRG--E 101
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTleeAREWLARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPEraE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225174   102 IGYVLGSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFV 158
Cdd:pfam13302  84 LGYWLGPDYWGKGYATEAVRALLEYAFEE-LGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
25-179 3.00e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 64.25  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  25 IHLRPMTLSDVD---DFMVWATDSNVTRFCTwEPYTSREAAiAYLNDALLP-HPWLraICLDNDRPIGSISVTPVDEIRG 100
Cdd:COG1247   2 MTIRPATPEDAPaiaAIYNEAIAEGTATFET-EPPSEEERE-AWFAAILAPgRPVL--VAEEDGEVVGFASLGPFRPRPA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174 101 -----EIGYVLGSKYWGKGIATEAVRLVAgEIFKEKPeMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRD 175
Cdd:COG1247  78 yrgtaEESIYVDPDARGRGIGRALLEALI-ERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLD 155


                ....
gi 15225174 176 MVMF 179
Cdd:COG1247 156 LVLM 159
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 55-157 4.59e-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: 57.53  E-value: 4.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174    55 PYTSREAAIAYLNDALLPHPWLRAICLDNDRPIGSISVTPVDE--IRGEI-GYVLGSKYWGKGIATEAVRLVAgEIFKEK 131
Cdd:pfam00583  13 PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDepPVGEIeGLAVAPEYRGKGIGTALLQALL-EWARER 91

                          90       100
                  ....*....|....*....|....*.
gi 15225174   132 pEMQRLEALVDVDNVGSQKVLEKVGF 157
Cdd:pfam00583  92 -GCERIFLEVAADNLAAIALYEKLGF 116
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
24-158 4.84e-10

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 55.69  E-value: 4.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  24 KIHLRPMTLSDVDDFMV----WAtDSNVTRFCTWEPYTSREAAIAYLND----ALLPHPWLRAICL----DNDRPIGSIS 91
Cdd:COG3981   1 MMELVRPTLEDEESYLEylaeFL-KEHIDGSGYLVSFEDFEAWLERLLDeekgEELPEGWVPATTYwlvdEDGRIVGAIN 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225174  92 V----TP-VDEIRGEIGYVLGSKYWGKGIATEAVRLVageifkeKPEMQRL---EALV--DVDNVGSQKVLEKVGFV 158
Cdd:COG3981  80 LrhelNEfLLRVGGHIGYGVRPSERGKGYATEMLRLA-------LEEARELgldRVLItcDKDNIASRKVIEANGGV 149
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 34-161 5.55e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 41.35  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174    34 DVDDFMVWATDSNVTRFctWEPYTSREAAIAYLnDALLPHPWLRA--ICLDnDRPIGSISVTPVDEIRGEIGY------- 104
Cdd:pfam13523   5 DLELLHRWMNDPRVAFW--WMLAGPLEQVREYL-ARLAADPHSHPyiGLLD-GEPFGYFEIYWAKEDRLGEYYdarpgdr 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225174   105 ---VL--GSKYWGKGIATEAVRLVAGEIFKEkPEMQRLEALVDVDNVGSQKVLEKVGFVKEG 161
Cdd:pfam13523  81 gihLLigEPAFRGRGFTTALLRALVHYLFAD-PRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
102-178 2.96e-04

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 39.72  E-value: 2.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225174  102 IGYVLGSKYWGKGIATEAVRlVAGEIFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRDMVM 178
Cdd:PRK10809 107 LGYSLGQKWQGQGLMFEALQ-AAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
27-178 4.63e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 38.89  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174    27 LRPMTLSDVDDFMVWATDSNVTRFCTWEpytSREAAIAYLNDALLPHPWLRAI---CLDNDRPIGSISVTPVDEIR---G 100
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQE---YAHSSIEEFETFLAAYLSPGEIvfgVAESDRLIGYATLRQFDYVKthkA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174   101 EIGY--VLGSKywgKGIATEAVRLVAgEIFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRDMVM 178
Cdd:pfam13420  78 ELSFyvVKNND---EGINRELINAII-QYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
84-179 5.28e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 38.97  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174   84 DRPIGSIS---VTPVDEIrGEIGYVLGSKYWGKGIATEAVRLVAGEiFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKE 160
Cdd:PRK10151  76 DELIGVLSfnrIEPLNKT-AYIGYWLDESHQGQGIISQALQALIHH-YAQSGELRRFVIKCRVDNPASNQVALRNGFTLE 153

                         90
                 ....*....|....*....
gi 15225174  161 GVMRKFMYLKGNVRDMVMF 179
Cdd:PRK10151 154 GCLKQAEYLNGAYDDVNLY 172
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 88-166 6.17e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 37.33  E-value: 6.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174  88 GSISVTPVDEIR-GEIG--YVLgSKYWGKGIATEAVRLVAgEIFKEKpEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMR 164
Cdd:COG0456   1 GFALLGLVDGGDeAEIEdlAVD-PEYRGRGIGRALLEAAL-ERARER-GARRLRLEVREDNEAAIALYEKLGFEEVGERP 77


                ..
gi 15225174 165 KF 166
Cdd:COG0456  78 NY 79
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 20-179 2.37e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 37.08  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174   20 SPPEKIHLRPMTLSDVDdfMVWATDSN--VTRFCTWEPYTsreaAIAYLNDALLPH----PWLRAICLDNDRPIGSISVT 93
Cdd:PRK15130   2 PSAHSVKLRPLEREDLR--FVHQLDNNasVMRYWFEEPYE----AFVELSDLYDKHihdqSERRFVVECDGEKAGLVELV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174   94 PVDEI--RGEIGYVLGSKYWGKGIATEAVRLVAGEIFKEKpEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKG 171
Cdd:PRK15130  76 EINHVhrRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVL-NLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFING 154

                        170
                 ....*....|.
gi 15225174  172 NVRD---MVMF 179
Cdd:PRK15130 155 EYRNtirMCIF 165
PRK10140 PRK10140
N-acetyltransferase;
65-175 3.45e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 36.50  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225174   65 YLNDALLPHP----WLRAI-----------CLDNDrPIGSISVTPVDEIR----GEIGYVLGSKYWGKGIATEAVRLVAg 125
Cdd:PRK10140  27 YHNTLQVPHPsdhmWQERLadrpgikqlvaCIDGD-VVGHLTIDVQQRPRrshvADFGICVDSRWKNRGVASALMREMI- 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15225174  126 EIFKEKPEMQRLEALVDVDNVGSQKVLEKVGFVKEGVMRKFMYLKGNVRD 175
Cdd:PRK10140 105 EMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVD 154
 
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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