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Conserved domains on  [gi|446509370|ref|WP_000586898|]
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MULTISPECIES: GNAT family N-acetyltransferase [Streptococcus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-161 2.58e-63

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 2.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   1 MIIRPVLPSDAKELLAIYAPYVTDTTITFEYDIPSISEFTNRIKNI-SKSFPYLVAEENGKILGYAYASTYYARAAYDWT 79
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  80 CELSIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVWLQK 159
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 446509370 160 RL 161
Cdd:COG1247  162 RL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-161 2.58e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 2.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   1 MIIRPVLPSDAKELLAIYAPYVTDTTITFEYDIPSISEFTNRIKNI-SKSFPYLVAEENGKILGYAYASTYYARAAYDWT 79
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  80 CELSIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVWLQK 159
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 446509370 160 RL 161
Cdd:COG1247  162 RL 163
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
3-156 6.42e-24

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 90.89  E-value: 6.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370    3 IRPVLPSDAKELLAIYAPYVTDTTITFEYDIPSISEFTNRIKNIS--KSFPYLVAEeNGKILGYAYASTYyaRAAYDWTC 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLspGEIVFGVAE-SDRLIGYATLRQF--DYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446509370   81 ELSIYLDKDaRSKKISSQLYDTLEKELVS-QGYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVW 156
Cdd:pfam13420  78 ELSFYVVKN-NDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 3.47e-06

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: 42.65  E-value: 3.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446509370  52 YLVAEENGKILGYAyasTYYARAAYDWTCELS-IYLDKDARSKKISSQLYDTLEKELVSQGY 112
Cdd:cd04301    1 FLVAEDDGEIVGFA---SLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGA 59
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-161 2.58e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 191.75  E-value: 2.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   1 MIIRPVLPSDAKELLAIYAPYVTDTTITFEYDIPSISEFTNRIKNI-SKSFPYLVAEENGKILGYAYASTYYARAAYDWT 79
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  80 CELSIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVWLQK 159
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 446509370 160 RL 161
Cdd:COG1247  162 RL 163
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
3-156 6.42e-24

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 90.89  E-value: 6.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370    3 IRPVLPSDAKELLAIYAPYVTDTTITFEYDIPSISEFTNRIKNIS--KSFPYLVAEeNGKILGYAYASTYyaRAAYDWTC 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLspGEIVFGVAE-SDRLIGYATLRQF--DYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446509370   81 ELSIYLDKDaRSKKISSQLYDTLEKELVS-QGYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVW 156
Cdd:pfam13420  78 ELSFYVVKN-NDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-162 5.12e-14

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 65.01  E-value: 5.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   1 MIIRPVLPSDAKELLAIYAPYVTDTTITFeydipsiseftnriknisksfpYLVAEENGKILGYAYASTYYARaaydwTC 80
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE----------------------FWVAEEDGEIVGCAALHPLDED-----LA 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  81 EL-SIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLAcisLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDIVWLqK 159
Cdd:COG1246   54 ELrSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVME-K 129


                 ...
gi 446509370 160 RLK 162
Cdd:COG1246  130 DLE 132
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 52-135 1.65e-13

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: 63.31  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   52 YLVAEENGKILGYAYASTYYARaaYDWTCELSIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLACISLPNDISIAFHK 131
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYE 112


                  ....
gi 446509370  132 KRGF 135
Cdd:pfam00583 113 KLGF 116
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
3-138 2.83e-10

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 55.71  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   3 IRPVLPSDAKELLAI---YAPYVTDTTITFEYDIPSISEFTnriknisksfpyLVAEENGKILGY--AYAS-TYYARAAY 76
Cdd:COG3818    7 IRDAREHDLDAVLALnnaAVPAVSPLDAARLARLHEQAAYA------------RVAEVDGEVAGFllAFGPgADYDSPNY 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446509370  77 DWTCELS---IYLDK-----DARSKKISSQLYDTLEKELVSQGYvNLLAC-ISL--PNDISIAFHKKRGFNQV 138
Cdd:COG3818   75 RWFAERYdnfLYIDRivvapSARGRGLGRALYADVFSYARARGV-PRVTCeVNLepPNPGSLAFHARLGFREV 146
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-161 1.31e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.55  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   3 IRPVLPSDAKELLAIYApyvtdttitFEYDIPSISEFTNRIKNISKSFPYLVAEENGKILGYAYASTYYARAAYDWtCEL 82
Cdd:COG3153    1 IRPATPEDAEAIAALLR---------AAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPA-LLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  83 S-IYLDKDARSKKISSQLYDTLEKELVSQGYVnllACISLPNDISIAFHKKRGFNQVAHfpkigFKFEQWHDIVWLQKRL 161
Cdd:COG3153   71 GpLAVDPEYRGQGIGRALMRAALEAARERGAR---AVVLLGDPSLLPFYERFGFRPAGE-----LGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 52-135 4.26e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.22  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   52 YLVAEENGKILGYAyasTYYARAAYDWTCELSIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLAcisLPNDISIAFHK 131
Cdd:pfam13508   5 FFVAEDDGKIVGFA---ALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRAAAFYE 78


                  ....
gi 446509370  132 KRGF 135
Cdd:pfam13508  79 KLGF 82
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-157 1.22e-07

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: 48.84  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   1 MIIRPVLPSDAKELLAIYA-PYVTDTTITFEYDIPSISEFTNRIKNISKS---FPYLVAE-ENGKILGYAyasTYYARAA 75
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNdPEVARYLPGPPYSLEEARAWLERLLADWADggaLPFAIEDkEDGELIGVV---GLYDIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  76 YDWTCELSIYLDKDARSKKISSQLYDTLEKELVSQ-GYVNLLACISLPNDISIAFHKKRGFNQVAHFPKIGFKFEQWHDI 154
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ...
gi 446509370 155 VWL 157
Cdd:COG1670  165 VLY 167
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 3.47e-06

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: 42.65  E-value: 3.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446509370  52 YLVAEENGKILGYAyasTYYARAAYDWTCELS-IYLDKDARSKKISSQLYDTLEKELVSQGY 112
Cdd:cd04301    1 FLVAEDDGEIVGFA---SLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGA 59
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-162 1.88e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 41.18  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370  63 GYAYASTYYAraayDWTCEL-SIYLDKDARSKKISSQLYDTLEKELVSQGYVNLLACISLPNDISIAFHKKRGFNQVAHF 141
Cdd:COG0456    1 GFALLGLVDG----GDEAEIeDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76

                         90       100
                 ....*....|....*....|.
gi 446509370 142 PkigfKFEQWHDIVwLQKRLK 162
Cdd:COG0456   77 P----NYYGDDALV-MEKELA 92
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-135 3.91e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.18  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370    2 IIRPVLPSDAKELLAIYA-PYVTDTTITFEYDIPSISEFTNRI---KNISKSFPYLVAEENGKILGYAyasTYYARAAYD 77
Cdd:pfam13302   3 LLRPLTEEDAEALFELLSdPEVMRYGVPWPLTLEEAREWLARIwaaDEAERGYGWAIELKDTGFIGSI---GLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446509370   78 WTCELSIYLDKDARSKKI----SSQLYDTLEKELvsqGYVNLLACISLPNDISIAFHKKRGF 135
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYateaVRALLEYAFEEL---GLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-135 9.84e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 37.25  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509370   36 ISEFTNRIKN-------ISKSFPYLVAEENGKILGYAYAST--YYARaaydwtcelsIYLDKDARSKKISSQLYDTLEKE 106
Cdd:pfam13673  10 IETFYEFISPealreriDQGEYFFFVAFEGGQIVGVIALRDrgHISL----------LFVDPDYQGQGIGKALLEAVEDY 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 446509370  107 LVSQGY-VNLLACISLPNdiSIAFHKKRGF 135
Cdd:pfam13673  80 AEKDGIkLSELTVNASPY--AVPFYEKLGF 107
 
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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