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Conserved domains on  [gi|489110117|ref|WP_003019973|]
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N-acetyltransferase [Francisella tularensis]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-136 1.14e-19

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 77.77  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  53 GYILCFEY--KKTIRVYSLAVSKNYQGQGIGKKLLEYILNNTDKN----ISLEVNTNNLIAISLYQKLGFEINKQINNYY 126
Cdd:COG0456    1 GFALLGLVdgGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERgarrLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|
gi 489110117 127 enGDAAYKMT 136
Cdd:COG0456   81 --GDDALVME 88
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-136 1.14e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 77.77  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  53 GYILCFEY--KKTIRVYSLAVSKNYQGQGIGKKLLEYILNNTDKN----ISLEVNTNNLIAISLYQKLGFEINKQINNYY 126
Cdd:COG0456    1 GFALLGLVdgGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERgarrLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|
gi 489110117 127 enGDAAYKMT 136
Cdd:COG0456   81 --GDDALVME 88
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-135 1.24e-19

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: 78.52  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   10 DLQALIDLENSTFlSDKISKKQFAYN-INKQKYFFVAKRQDSLAGYILCFEYKKTIRVYSLAVSKNYQGQGIGKKLLE-- 86
Cdd:TIGR01575   1 DLKAVLEIEAAAF-AFPWTEAQFAEElANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRel 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489110117   87 --YILNNTDKNISLEVNTNNLIAISLYQKLGFEINKQINNYYENGDA-AYKM 135
Cdd:TIGR01575  80 idEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEdAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-116 1.10e-18

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: 76.02  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   11 LQALIDLENSTFL---SDKISKKQFAYNINKQKYFFVAKRQDSLAGYILCF---EYKKTIRVYSLAVSKNYQGQGIGKKL 84
Cdd:pfam00583   1 LEALYELLSEEFPepwPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSiidDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489110117   85 LEYIL----NNTDKNISLEVNTNNLIAISLYQKLGF 116
Cdd:pfam00583  81 LQALLewarERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-90 5.85e-10

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: 51.89  E-value: 5.85e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489110117  42 FFVAKRQDSLAGYILCFEY---KKTIRVYSLAVSKNYQGQGIGKKLLEYILN 90
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 67-126 3.46e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 51.85  E-value: 3.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489110117  67 YSLAVSKNYQGQGIGKKLLEYILNN-TDKNIS---LEVNTNNLIAISLYQKLGF---EINKqinNYY 126
Cdd:PRK09491  67 FNIAVDPDYQRQGLGRALLEHLIDElEKRGVAtlwLEVRASNAAAIALYESLGFnevTIRR---NYY 130
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-136 1.14e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 77.77  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  53 GYILCFEY--KKTIRVYSLAVSKNYQGQGIGKKLLEYILNNTDKN----ISLEVNTNNLIAISLYQKLGFEINKQINNYY 126
Cdd:COG0456    1 GFALLGLVdgGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERgarrLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|
gi 489110117 127 enGDAAYKMT 136
Cdd:COG0456   81 --GDDALVME 88
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-135 1.24e-19

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: 78.52  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   10 DLQALIDLENSTFlSDKISKKQFAYN-INKQKYFFVAKRQDSLAGYILCFEYKKTIRVYSLAVSKNYQGQGIGKKLLE-- 86
Cdd:TIGR01575   1 DLKAVLEIEAAAF-AFPWTEAQFAEElANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRel 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489110117   87 --YILNNTDKNISLEVNTNNLIAISLYQKLGFEINKQINNYYENGDA-AYKM 135
Cdd:TIGR01575  80 idEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEdAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-116 1.10e-18

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: 76.02  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   11 LQALIDLENSTFL---SDKISKKQFAYNINKQKYFFVAKRQDSLAGYILCF---EYKKTIRVYSLAVSKNYQGQGIGKKL 84
Cdd:pfam00583   1 LEALYELLSEEFPepwPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSiidDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489110117   85 LEYIL----NNTDKNISLEVNTNNLIAISLYQKLGF 116
Cdd:pfam00583  81 LQALLewarERGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-141 1.68e-17

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: 73.10  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   1 MQISKAQLTDLQALIDLENSTFLSDKISKkqfayninkqkyFFVAKRQDSLAGYI-LCFEYKKTIRVYSLAVSKNYQGQG 79
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE------------FWVAEEDGEIVGCAaLHPLDEDLAELRSLAVHPDYRGRG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489110117  80 IGKKLLEYILNN-TDKNIS-LEVNTNNlIAISLYQKLGFEINKQINNYYENGDAAYKMTIIRKI 141
Cdd:COG1246   69 IGRRLLEALLAEaRELGLKrLFLLTTS-AAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-118 2.13e-16

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 69.02  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   41 YFFVAKRQDSLAGYI--LCFEYKKTIRVYSLAVSKNYQGQGIGKKLLEYILN-NTDKNISLEVNTNNLIAISLYQKLGFE 117
Cdd:pfam13508   4 RFFVAEDDGKIVGFAalLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAaAKEGGIKLLELETTNRAAAFYEKLGFE 83


                  .
gi 489110117  118 I 118
Cdd:pfam13508  84 E 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-141 3.18e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 68.10  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   1 MQISKAQLTDLQALIDLEN-------STFLSDKIS----KKQFAYNINKQKYFFVAKRQDSLAGYILCFEYK-----KTI 64
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNeaiaegtATFETEPPSeeerEAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRprpayRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  65 RVYSLAVSKNYQGQGIGKKLLEYIL----NNTDKNISLEVNTNNLIAISLYQKLGFEINKQINNYYENGDAAYKMTIIRK 140
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIerarARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 .
gi 489110117 141 I 141
Cdd:COG1247  162 R 162
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 16-117 1.03e-14

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: 65.76  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   16 DLENSTFLSDkISKKQFAYNINKQ-KYFFVAKRQDSLAGYIlcfEYKKTIRVYSLAVSKNYQGQGIGKKLLEYILNNTDK 94
Cdd:pfam13673   7 EEGIETFYEF-ISPEALRERIDQGeYFFFVAFEGGQIVGVI---ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100
                  ....*....|....*....|....*..
gi 489110117   95 ----NISLEVNTNNlIAISLYQKLGFE 117
Cdd:pfam13673  83 dgikLSELTVNASP-YAVPFYEKLGFR 108
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-117 4.74e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.33  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   3 ISKAQLTDLQALIDLENSTFLSDKISKKQFAYNINKQK-YFFVAKRQDSLAGYILCFEYK-----KTIRVYSLAVSKNYQ 76
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAEDDGEIVGHVALSPVDidgegPALLLGPLAVDPEYR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489110117  77 GQGIGKKLLEYILNNTDKN----ISLEVNTNNliaISLYQKLGFE 117
Cdd:COG3153   81 GQGIGRALMRAALEAARERgaraVVLLGDPSL---LPFYERFGFR 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-90 5.85e-10

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: 51.89  E-value: 5.85e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489110117  42 FFVAKRQDSLAGYILCFEY---KKTIRVYSLAVSKNYQGQGIGKKLLEYILN 90
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 67-126 3.46e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 51.85  E-value: 3.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489110117  67 YSLAVSKNYQGQGIGKKLLEYILNN-TDKNIS---LEVNTNNLIAISLYQKLGF---EINKqinNYY 126
Cdd:PRK09491  67 FNIAVDPDYQRQGLGRALLEHLIDElEKRGVAtlwLEVRASNAAAIALYESLGFnevTIRR---NYY 130
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-125 9.74e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.44  E-value: 9.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   1 MQISKAQLTDLQALIDLEnstFLSDKISKkqfAYNINKQKYFFVAKRQDSLAGYILCFEY-KKTIRVYSLAVSKNYQGQG 79
Cdd:COG0454    1 MSIRKATPEDINFILLIE---ALDAELKA---MEGSLAGAEFIAVDDKGEPIGFAGLRRLdDKVLELKRLYVLPEYRGKG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489110117  80 IGKKLLEYILNNTDKN----ISLEVNTNNLIAISLYQKLGFEINKQINNY 125
Cdd:COG0454   75 IGKALLEALLEWARERgctaLELDTLDGNPAAIRFYERLGFKEIERYVAY 124
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
64-117 1.54e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.06  E-value: 1.54e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489110117  64 IRVYSLAVSKNYQGQGIGKKLL----EYILNNTDKNISLEVNTNNLIAISLYQKLGFE 117
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVaalaREALARGARTPFLYVDADNPAARRLYERLGFR 73
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
43-118 1.58e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.10  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  43 FVAKRQDSLAGYILCFEYKKTI----RVyslAVSKNYQGQGIGKKLLEYIL----NNTDKNISLEVNTNnliAISLYQKL 114
Cdd:COG2153   37 LLAYDDGELVATARLLPPGDGEakigRV---AVLPEYRGQGLGRALMEAAIeearERGARRIVLSAQAH---AVGFYEKL 110


                 ....
gi 489110117 115 GFEI 118
Cdd:COG2153  111 GFVP 114
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 41-140 3.53e-06

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: 44.22  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  41 YFFVAKRQDSLAGYILCFEYKKTIRVYSLA--VSKNYQGQGIG----KKLLEYILNNTD-KNISLEVNTNNLIAISLYQK 113
Cdd:COG1670   63 FAIEDKEDGELIGVVGLYDIDRANRSAEIGywLAPAYWGKGYAtealRALLDYAFEELGlHRVEAEVDPDNTASIRVLEK 142

                         90       100       110
                 ....*....|....*....|....*....|
gi 489110117 114 LGFEINKQINNYYENGDAAYK---MTIIRK 140
Cdd:COG1670  143 LGFRLEGTLRDALVIDGRYRDhvlYSLLRE 172
PRK10562 PRK10562
putative acetyltransferase; Provisional
 44-118 6.06e-06

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 43.13  E-value: 6.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489110117  44 VAKRQDSLAGYILCFEYKktiRVYSLAVSKNYQGQGIGKKLLEYILNNTDKnISLEVNTNNLIAISLYQKLGFEI 118
Cdd:PRK10562  52 VWEEDGKLLGFVSVLEGR---FVGALFVAPKAVRRGIGKALMQHVQQRYPH-LSLEVYQKNQRAVNFYHAQGFRI 122
PRK03624 PRK03624
putative acetyltransferase; Provisional
 42-117 7.65e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.61  E-value: 7.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117  42 FFVAKRQDSLAGyilcfeykkTI-------R--VYSLAVSKNYQGQGIGKKLleyiLNNTDK--------NISLEVNTNN 104
Cdd:PRK03624  47 FLVAEVGGEVVG---------TVmggydghRgwAYYLAVHPDFRGRGIGRAL----VARLEKkliargcpKINLQVREDN 113

                         90
                 ....*....|...
gi 489110117 105 LIAISLYQKLGFE 117
Cdd:PRK03624 114 DAVLGFYEALGYE 126
PRK07757 PRK07757
N-acetyltransferase;
1-120 2.84e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 41.33  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117   1 MQISKAQLTD---LQALIDLENSTFLSDKISKKQFAYNInkqKYFFVAKRQDSLAGYI-LCFEYKKTIRVYSLAVSKNYQ 76
Cdd:PRK07757   2 MEIRKARLSDvkaIHALINVYAKKGLMLPRSLDELYENI---RDFYVAEEEGEIVGCCaLHILWEDLAEIRSLAVSEDYR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489110117  77 GQGIGKKLLEYILNNTdknISLEVNTnnLIAISL----YQKLGF-EINK 120
Cdd:PRK07757  79 GQGIGRMLVEACLEEA---RELGVKR--VFALTYqpefFEKLGFrEVDK 122
PRK10514 PRK10514
putative acetyltransferase; Provisional
 69-118 1.43e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.22  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489110117  69 LAVSKNYQGQGIGKKLLEYILNNTdKNISLEVNTNNLIAISLYQKLGFEI 118
Cdd:PRK10514  75 LFVDPDVRGCGVGRMLVEHALSLH-PELTTDVNEQNEQAVGFYKKMGFKV 123
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
37-90 1.05e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 35.90  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489110117  37 NKQKYFFVAKRQDSLAGYIlcfEYKK---TIRVYSLAVSKNYQGQGIGKKLLEYILN 90
Cdd:COG2388    6 NEEKGRFELEVDGELAGEL---TYRLeggVIIITHTEVPPALRGQGIASALVEAALD 59
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
69-118 2.58e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.06  E-value: 2.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489110117  69 LAVSKNYQGQGIGKKLLEYILN-NTDKNIS-LEVNT--NNLIAISLYQKLGFEI 118
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNwCQARGLTrLRVATqmGNLAALRLYIRSGANI 185
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-118 5.17e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 34.85  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489110117    3 ISKAQLTDLQALIDLENSTFL-SDKISKKQFAYNINKQKYFFVAKRQDSLAGYILCFEYKKTIR--------VYSLAVSK 73
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAFQdEDSPELREYFRPLLEEGRVLGAFDDGELVSTLALYPFELNVPgktlpaagITGVATYP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489110117   74 NYQGQGIGKKLLEYILNNT-DKNISLEVNTNnlIAISLYQKLGFEI 118
Cdd:pfam13527  81 EYRGRGVMSRLLRRSLEEMrERGVPLSFLYP--SSYPIYRRFGYEI 124
 
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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