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Conserved domains on  [gi|1934310481|ref|WP_195519970|]
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GNAT family N-acetyltransferase [Streptococcus salivarius]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-143 4.67e-20

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 80.90  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   3 IRHAREDDWADVVRIEQDNFSPE-EAATPEAIAERLKtiSDTFLIAEIDGVVAGYIegpviaeryltddLFHKVvPNASQ 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGrEAELVDRLREDPA--AGLSLVAEDDGEIVGHV-------------ALSPV-DIDGE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934310481  82 GGFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDYLIAYYEMNGFTDEGE 143
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGE 126
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-143 4.67e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 80.90  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   3 IRHAREDDWADVVRIEQDNFSPE-EAATPEAIAERLKtiSDTFLIAEIDGVVAGYIegpviaeryltddLFHKVvPNASQ 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGrEAELVDRLREDPA--AGLSLVAEDDGEIVGHV-------------ALSPV-DIDGE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934310481  82 GGFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDYLIAYYEMNGFTDEGE 143
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGE 126
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 22-159 3.48e-12

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: 59.98  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  22 FSPEEAAT------PEAIAERLKTISDTFLIAEIDGVVAGYIEgpviaeryltddlfhkvvpnASQGGFIavTSLSISKD 95
Cdd:pfam13673   5 YSEEGIETfyefisPEALRERIDQGEYFFFVAFEGGQIVGVIA--------------------LRDRGHI--SLLFVDPD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310481  96 FKGQGIGTALIAALKDLAIAQKRQGISLTCH--DYLIAYYEMNGFTDEGEsESNHGGSTWYNMVWE 159
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDGIKLSELTVNasPYAVPFYEKLGFRATGP-EQEFNGIRFVPMEKE 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-124 1.73e-07

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: 46.11  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  44 FLIAEIDGVVAGYIEgpviaeryltddlfhkVVPNASQGGFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISL 123
Cdd:cd04301     1 FLVAEDDGEIVGFAS----------------LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64


                  .
gi 1934310481 124 T 124
Cdd:cd04301    65 E 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-141 1.57e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   1 MLIRHAREDDWADVVRIEQDNFSPEEAATPEA-IAERLKTISDTFLIAEIDGVVAGYIegpviaeryltddlfhkvvpna 79
Cdd:PRK03624    3 MEIRVFRQADFEAVIALWERCDLTRPWNDPEMdIERKLNHDPSLFLVAEVGGEVVGTV---------------------- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934310481  80 sQGGFI----AVTSLSISKDFKGQGIGTALIAALKDLAIAQ---KRQGISLTCHDYLIAYYEMNGFTDE 141
Cdd:PRK03624   61 -MGGYDghrgWAYYLAVHPDFRGRGIGRALVARLEKKLIARgcpKINLQVREDNDAVLGFYEALGYEEQ 128
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-143 4.67e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 80.90  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   3 IRHAREDDWADVVRIEQDNFSPE-EAATPEAIAERLKtiSDTFLIAEIDGVVAGYIegpviaeryltddLFHKVvPNASQ 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGrEAELVDRLREDPA--AGLSLVAEDDGEIVGHV-------------ALSPV-DIDGE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934310481  82 GGFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDYLIAYYEMNGFTDEGE 143
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGE 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-158 2.46e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 71.56  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   1 MLIRHAREDDWADVVRIEQDNFS------PEEAATPEAIAERLKTISD---TFLIAEIDGVVAGYIEgpviAERYLTDDL 71
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAegtatfETEPPSEEEREAWFAAILApgrPVLVAEEDGEVVGFAS----LGPFRPRPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  72 FHkvvpnasqggFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDY---LIAYYEMNGFTDEGESES-N 147
Cdd:COG1247    78 YR----------GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGTLPEvG 147

                         170
                  ....*....|.
gi 1934310481 148 HGGSTWYNMVW 158
Cdd:COG1247   148 FKFGRWLDLVL 158
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 22-159 3.48e-12

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: 59.98  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  22 FSPEEAAT------PEAIAERLKTISDTFLIAEIDGVVAGYIEgpviaeryltddlfhkvvpnASQGGFIavTSLSISKD 95
Cdd:pfam13673   5 YSEEGIETfyefisPEALRERIDQGEYFFFVAFEGGQIVGVIA--------------------LRDRGHI--SLLFVDPD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310481  96 FKGQGIGTALIAALKDLAIAQKRQGISLTCH--DYLIAYYEMNGFTDEGEsESNHGGSTWYNMVWE 159
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDGIKLSELTVNasPYAVPFYEKLGFRATGP-EQEFNGIRFVPMEKE 127
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-159 2.11e-11

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: 58.08  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   1 MLIRHAREDDWADVVRIEQdnfspeeaatPEAIAERlktiSDTFLIAEIDGVVAGyiegpVIAERYLTDDLFHkvvpnas 80
Cdd:COG1246     1 MTIRPATPDDVPAILELIR----------PYALEEE----IGEFWVAEEDGEIVG-----CAALHPLDEDLAE------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  81 qggfiaVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDYLIAYYEMNGFTDEGESES-NHGGSTWYNMVWE 159
Cdd:COG1246    55 ------LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLpYAKVWQRDSVVME 128
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-138 8.56e-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: 55.99  E-value: 8.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  11 WADVVRIEQDNFS-PEEAATPEAIAERLKTISDTFLIAEIDGVVAGYIEGpviaeryltddlfhkvVPNASQGGFIAVTS 89
Cdd:pfam00583   1 LEALYELLSEEFPePWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASL----------------SIIDDEPPVGEIEG 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934310481  90 LSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCH---DYLIAYYEMNGF 138
Cdd:pfam00583  65 LAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAadnLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-139 2.27e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  41 SDTFLIAEIDGVVAGYIEGPVIAERYltddlfhkvvpnasqggFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQG 120
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEG-----------------ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKL 64

                          90
                  ....*....|....*....
gi 1934310481 121 ISLTCHDYLIAYYEMNGFT 139
Cdd:pfam13508  65 LELETTNRAAAFYEKLGFE 83
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-143 1.30e-08

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.57  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  45 LIAEIDGVVAGYIegpviaeRYLTDDlfhkvvPNASQGGFIAVtslsiSKDFKGQGIGTALIAALkdLAIAQKRQGISLT 124
Cdd:COG2153    37 LLAYDDGELVATA-------RLLPPG------DGEAKIGRVAV-----LPEYRGQGLGRALMEAA--IEEARERGARRIV 96

                          90       100
                  ....*....|....*....|.
gi 1934310481 125 CH--DYLIAYYEMNGFTDEGE 143
Cdd:COG2153    97 LSaqAHAVGFYEKLGFVPVGE 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 87-159 1.04e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.34  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310481  87 VTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDY---LIAYYEMNGFTDEGESEsNHGGSTWYNMVWE 159
Cdd:COG0456    16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERP-NYYGDDALVMEKE 90
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-124 1.73e-07

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: 46.11  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  44 FLIAEIDGVVAGYIEgpviaeryltddlfhkVVPNASQGGFIAVTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISL 123
Cdd:cd04301     1 FLVAEDDGEIVGFAS----------------LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64


                  .
gi 1934310481 124 T 124
Cdd:cd04301    65 E 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-141 1.57e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   1 MLIRHAREDDWADVVRIEQDNFSPEEAATPEA-IAERLKTISDTFLIAEIDGVVAGYIegpviaeryltddlfhkvvpna 79
Cdd:PRK03624    3 MEIRVFRQADFEAVIALWERCDLTRPWNDPEMdIERKLNHDPSLFLVAEVGGEVVGTV---------------------- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934310481  80 sQGGFI----AVTSLSISKDFKGQGIGTALIAALKDLAIAQ---KRQGISLTCHDYLIAYYEMNGFTDE 141
Cdd:PRK03624   61 -MGGYDghrgWAYYLAVHPDFRGRGIGRALVARLEKKLIARgcpKINLQVREDNDAVLGFYEALGYEEQ 128
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-158 1.59e-05

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: 42.68  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481   1 MLIRHAREDDWADVVRIEQD----NFSPEEAATPEAIAERLKTISDTF---------LIAEIDGVVAGYIEgpviaeryl 67
Cdd:COG1670     8 LRLRPLRPEDAEALAELLNDpevaRYLPGPPYSLEEARAWLERLLADWadggalpfaIEDKEDGELIGVVG--------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934310481  68 tddlFHKVVPNASQGGFiavtSLSISKDFKGQGIGTALIAALKDLAIAQKR-QGISLTCHDY---LIAYYEMNGFTDEGE 143
Cdd:COG1670    79 ----LYDIDRANRSAEI----GYWLAPAYWGKGYATEALRALLDYAFEELGlHRVEAEVDPDntaSIRVLEKLGFRLEGT 150

                         170
                  ....*....|....*.
gi 1934310481 144 SESN-HGGSTWYNMVW 158
Cdd:COG1670   151 LRDAlVIDGRYRDHVL 166
PTZ00330 PTZ00330
acetyltransferase; Provisional
 75-138 5.37e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 38.28  E-value: 5.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934310481  75 VVPNASQGGFIA--VTSLSISKDFKGQGIGTALIAALKDLAIAQKRQGISLTCHDYLIAYYEMNGF 138
Cdd:PTZ00330   71 VEPKFTRGGKCVghIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGF 136
 
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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