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Conserved domains on  [gi|1622874665|ref|XP_028691327|]
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N-acetyltransferase 9 isoform X3 [Macaca mulatta]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 12134272)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
60-187 1.09e-10

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


:

Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665  60 VVLVPYTSEHVPRYHEWMKSEELQRLTASEPLTLEQEYA-MQRSWREDADK--CTFIVLDAekwqaqpgateESCMVGDV 136
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREwLARIWAADEAErgYGWAIELK-----------DTGFIGSI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665 137 NLFLTDlEDPTLGEIEVMIA-------------------GMTTLGLTKFEAKIGQENEPSIRMFQKLHFE 187
Cdd:pfam13302  71 GLYDID-GEPERAELGYWLGpdywgkgyateavralleyAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
60-187 1.09e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665  60 VVLVPYTSEHVPRYHEWMKSEELQRLTASEPLTLEQEYA-MQRSWREDADK--CTFIVLDAekwqaqpgateESCMVGDV 136
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREwLARIWAADEAErgYGWAIELK-----------DTGFIGSI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665 137 NLFLTDlEDPTLGEIEVMIA-------------------GMTTLGLTKFEAKIGQENEPSIRMFQKLHFE 187
Cdd:pfam13302  71 GLYDID-GEPERAELGYWLGpdywgkgyateavralleyAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
53-190 1.63e-10

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: 58.09  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665  53 TMLLGKKVVLVPYTSEHVPRYHEWMKSEELQRLTASEPLTLEQEYAMQRSWREDADKCTFIVLDAEKwqaqpgaTEESCM 132
Cdd:COG1670     1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIED-------KEDGEL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622874665 133 VGDVNLFLTDLEDPTlGEIEVMIA-------------------GMTTLGLTKFEAKIGQENEPSIRMFQKLHFEQVA 190
Cdd:COG1670    74 IGVVGLYDIDRANRS-AEIGYWLApaywgkgyatealralldyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149
 
Name Accession Description Interval E-value
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
60-187 1.09e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665  60 VVLVPYTSEHVPRYHEWMKSEELQRLTASEPLTLEQEYA-MQRSWREDADK--CTFIVLDAekwqaqpgateESCMVGDV 136
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREwLARIWAADEAErgYGWAIELK-----------DTGFIGSI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665 137 NLFLTDlEDPTLGEIEVMIA-------------------GMTTLGLTKFEAKIGQENEPSIRMFQKLHFE 187
Cdd:pfam13302  71 GLYDID-GEPERAELGYWLGpdywgkgyateavralleyAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
53-190 1.63e-10

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: 58.09  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622874665  53 TMLLGKKVVLVPYTSEHVPRYHEWMKSEELQRLTASEPLTLEQEYAMQRSWREDADKCTFIVLDAEKwqaqpgaTEESCM 132
Cdd:COG1670     1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIED-------KEDGEL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622874665 133 VGDVNLFLTDLEDPTlGEIEVMIA-------------------GMTTLGLTKFEAKIGQENEPSIRMFQKLHFEQVA 190
Cdd:COG1670    74 IGVVGLYDIDRANRS-AEIGYWLApaywgkgyatealralldyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149
 
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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