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Conserved domains on  [gi|488976685|ref|WP_002887560|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

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];
12-152 3.13e-23

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.37  E-value: 3.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDIALLPAIERSAaqafrqipslaWLADSEVISVARHHDYLETEHSLLAVAAGQPVGFILTEPLD-----DALF 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDidgegPALL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFrevPWNAPFYTRLGFAMLDELTLPAG 152
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-152 3.13e-23

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.37  E-value: 3.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDIALLPAIERSAaqafrqipslaWLADSEVISVARHHDYLETEHSLLAVAAGQPVGFILTEPLD-----DALF 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDidgegPALL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFrevPWNAPFYTRLGFAMLDELTLPAG 152
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 59-141 3.49e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.09  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   59 ETEHSLLAVAAGQPVGFILTEPLDDALFIVE--VAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREvpwNAPFY 136
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAElrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFY 77


                  ....*
gi 488976685  137 TRLGF 141
Cdd:pfam13508  78 EKLGF 82
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 63-124 8.48e-12

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: 57.67  E-value: 8.48e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976685  63 SLLAVAAGQPVGFILTEPLD---DALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLT 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
65-150 5.39e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 52.12  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  65 LAVAAGQPVGF----ILTEPLDDalfIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAV-TLTtfrevpWNAPFYTRL 139
Cdd:PRK07757  45 VAEEEGEIVGCcalhILWEDLAE---IRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVfALT------YQPEFFEKL 115

                         90
                 ....*....|.
gi 488976685 140 GFAMLDELTLP 150
Cdd:PRK07757 116 GFREVDKEALP 126
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 64-142 1.82e-08

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 50.41  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   64 LLAVAAGQPVGFILT-EPLDDAlFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLttfrEV-PWNAP---FYTR 138
Cdd:TIGR01575  34 LLARIGGKVVGYAGVqIVLDEA-HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL----EVrVSNIAaqaLYKK 108


                  ....
gi 488976685  139 LGFA 142
Cdd:TIGR01575 109 LGFN 112
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-152 3.13e-23

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 89.37  E-value: 3.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDIALLPAIERSAaqafrqipslaWLADSEVISVARHHDYLETEHSLLAVAAGQPVGFILTEPLD-----DALF 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDidgegPALL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFrevPWNAPFYTRLGFAMLDELTLPAG 152
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 12-148 5.33e-19

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 78.17  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDIALLPAIERSAAQAFRQIPSLAwladsevisvarhhdyleTEHSLLAVAAGQPVGFILTEPLDD-ALFIVEV 90
Cdd:COG0454    3 IRKATPEDINFILLIEALDAELKAMEGSLA------------------GAEFIAVDDKGEPIGFAGLRRLDDkVLELKRL 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488976685  91 AVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREVPWNAPFYTRLGFAMLDELT 148
Cdd:COG0454   65 YVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYV 122
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 64-157 1.10e-16

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: 72.33  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  64 LLAVAAGQPVGFI-LTEPLDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREVpwnAPFYTRLGFA 142
Cdd:COG1246   31 WVAEEDGEIVGCAaLHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAA---IHFYEKLGFE 107

                         90
                 ....*....|....*
gi 488976685 143 MLDELTLPAGLAAKR 157
Cdd:COG1246  108 EIDKEDLPYAKVWQR 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 59-141 3.49e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.09  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   59 ETEHSLLAVAAGQPVGFILTEPLDDALFIVE--VAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREvpwNAPFY 136
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAElrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFY 77


                  ....*
gi 488976685  137 TRLGF 141
Cdd:pfam13508  78 EKLGF 82
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-141 6.62e-15

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: 67.16  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   32 QAFRQIPSLAWLADSEVISVARHHDY--LETEHSLLAVAAGQPVGFILTEPLDDA---LFIVEVAVHQAWQQQGIGRMLL 106
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWdeDASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488976685  107 ERVIESARQMGYPAVTLTTFREVPWNAPFYTRLGF 141
Cdd:pfam00583  82 QALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-146 3.56e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 3.56e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976685  74 GFIL--TEPLDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREVPWNAPFYTRLGFAMLDE 146
Cdd:COG0456    1 GFALlgLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
11-147 5.63e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 65.79  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  11 VLRLTQESDIALLPAIERSAaqafrqIPSLAWLADSEVISVARHHDYLETEHS-----LLAVAAGQPVGFI-----LTEP 80
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEA------IAEGTATFETEPPSEEEREAWFAAILApgrpvLVAEEDGEVVGFAslgpfRPRP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  81 LDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFrevPWNAP---FYTRLGFAMLDEL 147
Cdd:COG1247   77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVL---ADNEAsiaLYEKLGFEEVGTL 143
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 63-124 8.48e-12

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: 57.67  E-value: 8.48e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976685  63 SLLAVAAGQPVGFILTEPLD---DALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLT 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
59-141 4.97e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 54.81  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  59 ETEHsLLAVAAGQPVGFILTEPLDDALFIVE-VAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLttfrevpwNA---- 133
Cdd:COG2153   33 DARH-LLAYDDGELVATARLLPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL--------SAqaha 103


                 ....*....
gi 488976685 134 -PFYTRLGF 141
Cdd:COG2153  104 vGFYEKLGF 112
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 59-153 7.97e-10

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: 54.20  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   59 ETEHSLLAVAAGQPVGFILtepLDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGyPAVTLTTFREVPWNAPFYTR 138
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIA---LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPYAVPFYEK 104

                          90
                  ....*....|....*
gi 488976685  139 LGFAMLDELTLPAGL 153
Cdd:pfam13673 105 LGFRATGPEQEFNGI 119
PRK07757 PRK07757
N-acetyltransferase;
65-150 5.39e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 52.12  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  65 LAVAAGQPVGF----ILTEPLDDalfIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAV-TLTtfrevpWNAPFYTRL 139
Cdd:PRK07757  45 VAEEEGEIVGCcalhILWEDLAE---IRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVfALT------YQPEFFEKL 115

                         90
                 ....*....|.
gi 488976685 140 GFAMLDELTLP 150
Cdd:PRK07757 116 GFREVDKEALP 126
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 64-142 1.82e-08

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 50.41  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   64 LLAVAAGQPVGFILT-EPLDDAlFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLttfrEV-PWNAP---FYTR 138
Cdd:TIGR01575  34 LLARIGGKVVGYAGVqIVLDEA-HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL----EVrVSNIAaqaLYKK 108


                  ....
gi 488976685  139 LGFA 142
Cdd:TIGR01575 109 LGFN 112
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-141 4.17e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.67  E-value: 4.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976685  71 QPVGFI-LTEPLDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREVPWNAPFYTRLGF 141
Cdd:COG3393    1 ELVAMAgVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
PRK07922 PRK07922
amino-acid N-acetyltransferase;
90-151 1.53e-06

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 46.07  E-value: 1.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976685  90 VAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFrEVpwnaPFYTRLGFAMLDELTLPA 151
Cdd:PRK07922  76 VAVDPAARGRGVGHAIVERLLDVARELGLSRVFVLTF-EV----EFFARHGFVEIDGTPVTP 132
Eis COG4552
Predicted acetyltransferase [General function prediction only];
12-163 1.26e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 44.12  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDialLPAIERSAAQAFRQIPSLAwladseviSVARHHDYLETEHSLLAVAAGQPVGFILTEPLD--------D 83
Cdd:COG4552    3 IRPLTEDD---LDAFARLLAYAFGPEPDDE--------ELEAYRPLLEPGRVLGVFDDGELVGTLALYPFTlnvggarvP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  84 ALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFRevpwnAPFYTRLGFAM---LDELTLPAGLAAKREQE 160
Cdd:COG4552   72 MAGITGVAVAPEHRRRGVARALLREALAELRERGQPLSALYPFE-----PGFYRRFGYELagdRRRYTIPPESLPLRPDA 146


                 ...
gi 488976685 161 TRH 163
Cdd:COG4552  147 PGR 149
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 87-118 3.21e-05

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 43.28  E-value: 3.21e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGY 118
Cdd:COG1444  488 IVRIAVHPALQRRGLGSRLLAEIREEAKEEGL 519
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 70-141 4.81e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.45  E-value: 4.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976685  70 GQPVGFILTEP-LDDA-LFivEVAVHQAWQQQGIGRMLLERVIESARQMGypavTLTTFREV-PWNAP---FYTRLGF 141
Cdd:PRK09491  49 GQMAAFAITQVvLDEAtLF--NIAVDPDYQRQGLGRALLEHLIDELEKRG----VATLWLEVrASNAAaiaLYESLGF 120
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-141 8.87e-05

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 40.25  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685   12 LRLTQESDIallpaiersaaQAFRQIPSLAWLADSEVISVARHHDYLETEHSLLAVAAGQPVGFILTEPLD--------D 83
Cdd:pfam13527   1 IRPLTEDEF-----------DEVLRLLEYAFQDEDSPELREYFRPLLEEGRVLGAFDDGELVSTLALYPFElnvpgktlP 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488976685   84 ALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTtfrevPWNAPFYTRLGF 141
Cdd:pfam13527  70 AAGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLY-----PSSYPIYRRFGY 122
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 90-128 2.78e-04

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 40.52  E-value: 2.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488976685  90 VAVHQAWQQQGIGRMLLERVIESARQMGYPAV-TLTT-----FRE 128
Cdd:PRK05279 365 LAVHPDYRGSGRGERLLKRIEQRARQLGLKRLfVLTTrtahwFLE 409
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
70-121 5.08e-04

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 37.44  E-value: 5.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488976685  70 GQPVGFILTEPLDDALFIVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAV 121
Cdd:COG2388   18 GELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVV 69
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 87-141 1.24e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 37.38  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTFREvpwNAPFYTRLGF 141
Cdd:PLN02706  88 IEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEE---NKAFYEKCGY 139
PRK12308 PRK12308
argininosuccinate lyase;
87-150 2.04e-03

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 37.84  E-value: 2.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976685  87 IVEVAVHQAWQQQGIGRMLLERVIESARQMGYPAVTLTTfrEVPwnaPFYTRLGFAMLDELTLP 150
Cdd:PRK12308 530 IRSLGVEAGWQVQGQGSALVQYLVEKARQMAIKKVFVLT--RVP---EFFMKQGFSPTSKSLLP 588
PRK09831 PRK09831
GNAT family N-acetyltransferase;
12-146 2.38e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 36.47  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976685  12 LRLTQESDIALLPAI-ERSAAQAFRQIPSLAWLADSEVISVARHHDYLETEHSLLAVAAGQPVGFIL-TEPLDDALFive 89
Cdd:PRK09831   3 IRNYQPGDFQQLCAIfIRAVTMTASQHYSPQQIAAWAQIDESRWKEKLAKSQVRVAVINAQPVGFITcIEHYIDMLF--- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488976685  90 vaVHQAWQQQGIGRMLLERVIESarqmgYPAVTLTTFREVpwnAPFYTRLGFAMLDE 146
Cdd:PRK09831  80 --VDPEYTRRGVASALLKPLIKS-----ESELTVDASITA---KPFFERYGFQTVKQ 126
 
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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