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Conserved domains on  [gi|878900967|emb|CIX53764|]
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acetyltransferase%2C gnat family [Streptococcus pneumoniae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10008168)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  9175471|10940244|15581578
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-164 3.63e-75

Predicted acetyltransferase [General function prediction only];


:

Pssm-ID: 443180  Cd Length: 170  Bit Score: 222.09  E-value: 3.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   1 MELRRPRLADKKAVLDMMTEFEKSQSAHDGGFWDTENFvyEEWLESNQEQEMGINLPEGWVPAIQLVAFSEKGQAVGFLN 80
Cdd:COG3981    2 MELVRPTLEDEESYLEYLAEFLKEHIDGSGYLVSFEDF--EAWLERLLDEEKGEELPEGWVPATTYWLVDEDGRIVGAIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967  81 LRLRLSNFLLEEGGHIGYSIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRAVILANGGIFED------A 154
Cdd:COG3981   80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDevvdeeD 159

                        170
                 ....*....|
gi 878900967 155 HNGVERYWIE 164
Cdd:COG3981  160 GRPVRRYWID 169
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-164 3.63e-75

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 222.09  E-value: 3.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   1 MELRRPRLADKKAVLDMMTEFEKSQSAHDGGFWDTENFvyEEWLESNQEQEMGINLPEGWVPAIQLVAFSEKGQAVGFLN 80
Cdd:COG3981    2 MELVRPTLEDEESYLEYLAEFLKEHIDGSGYLVSFEDF--EAWLERLLDEEKGEELPEGWVPATTYWLVDEDGRIVGAIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967  81 LRLRLSNFLLEEGGHIGYSIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRAVILANGGIFED------A 154
Cdd:COG3981   80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDevvdeeD 159

                        170
                 ....*....|
gi 878900967 155 HNGVERYWIE 164
Cdd:COG3981  160 GRPVRRYWID 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-148 3.50e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967    3 LRRPRLADKKAVLDMMTEFEKSQSahdGGFWDTENFVYEEWLESNQEQEmgiNLPEGWVPAIQLvafsEKGQAVGFLNLR 82
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRY---GVPWPLTLEEAREWLARIWAAD---EAERGYGWAIEL----KDTGFIGSIGLY 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 878900967   83 LRLSNfllEEGGHIGYSIRPSERGKGYAKETLRQGLQVA-KEKNIKKALVTCSVNNPASRAVILANG 148
Cdd:pfam13302  74 DIDGE---PERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLG 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 66-132 3.12e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 34.56  E-value: 3.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 878900967  66 LVAFSEKGQAVGFLNLRLRlsnFLLEEGGHIGY-SIRPSERGKGYAKETLRQGLQVAKEKNIKKALVT 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-164 3.63e-75

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 222.09  E-value: 3.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   1 MELRRPRLADKKAVLDMMTEFEKSQSAHDGGFWDTENFvyEEWLESNQEQEMGINLPEGWVPAIQLVAFSEKGQAVGFLN 80
Cdd:COG3981    2 MELVRPTLEDEESYLEYLAEFLKEHIDGSGYLVSFEDF--EAWLERLLDEEKGEELPEGWVPATTYWLVDEDGRIVGAIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967  81 LRLRLSNFLLEEGGHIGYSIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRAVILANGGIFED------A 154
Cdd:COG3981   80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDevvdeeD 159

                        170
                 ....*....|
gi 878900967 155 HNGVERYWIE 164
Cdd:COG3981  160 GRPVRRYWID 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-148 3.50e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967    3 LRRPRLADKKAVLDMMTEFEKSQSahdGGFWDTENFVYEEWLESNQEQEmgiNLPEGWVPAIQLvafsEKGQAVGFLNLR 82
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRY---GVPWPLTLEEAREWLARIWAAD---EAERGYGWAIEL----KDTGFIGSIGLY 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 878900967   83 LRLSNfllEEGGHIGYSIRPSERGKGYAKETLRQGLQVA-KEKNIKKALVTCSVNNPASRAVILANG 148
Cdd:pfam13302  74 DIDGE---PERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLG 137
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-152 1.86e-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: 56.55  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   1 MELRRPRLADKKAVLDMMT--EFEKSQSAHDGGFWDTENFVyEEWLESNQEQEMGInlpegWVpaiqlVAFSEKGQAVGF 78
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNdpEVARYLPGPPYSLEEARAWL-ERLLADWADGGALP-----FA-----IEDKEDGELIGV 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 878900967  79 LNLRLRLSNFlleEGGHIGYSIRPSERGKGYAKETLRQGLQVAKEK-NIKKALVTCSVNNPASRAVILANGGIFE 152
Cdd:COG1670   77 VGLYDIDRAN---RSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-142 2.17e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.07  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   1 MELRRPRLADKKAVLDMMTEFEKSQSAHdggfWDTENFVYEE---WLESNQEQEMGInlpegwvpaiqLVAfSEKGQAVG 77
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTAT----FETEPPSEEEreaWFAAILAPGRPV-----------LVA-EEDGEVVG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 878900967  78 FLnlrlRLSNFLLEEG----GHIGYSIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRA 142
Cdd:COG1247   66 FA----SLGPFRPRPAyrgtAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIA 130
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-143 6.43e-07

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: 45.97  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 878900967   32 FWDTENFVYEEWLESNQEQEMGINLPEGWVPAIQLVAFSEKGQAVGFLNLRLRlsNFLLEEGGHIGYSIRPSERGKGYAK 111
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSII--DDEPPVGEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 878900967  112 ETLRQGLQVAKEKNIKKALVTCSVNNPASRAV 143
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIAL 110
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-142 2.23e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.79  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 878900967  77 GFLNLRLRLSnfllEEGGHIGY-SIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRA 142
Cdd:COG0456    1 GFALLGLVDG----GDEAEIEDlAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIA 63
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 66-132 3.12e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 34.56  E-value: 3.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 878900967  66 LVAFSEKGQAVGFLNLRLRlsnFLLEEGGHIGY-SIRPSERGKGYAKETLRQGLQVAKEKNIKKALVT 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
101-143 8.25e-03

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 33.73  E-value: 8.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 878900967 101 RPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPASRAV 143
Cdd:COG3393   24 HPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRL 66
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
66-139 8.46e-03

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 34.68  E-value: 8.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 878900967  66 LVAFSEkGQAVGFLnlrlRLSNFLLEEGGHIGY----SIRPSERGKGYAKETLRQGLQVAKEKNIKKALVTCSVNNPA 139
Cdd:COG3153   42 LVAEDD-GEIVGHV----ALSPVDIDGEGPALLlgplAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP 114
 
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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