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Conserved domains on  [gi|1267630299|ref|WP_098399771|]
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MULTISPECIES: GNAT family N-acetyltransferase [Priestia]

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];
1-156 2.36e-19

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDYYVISPLINEW-------WNGRQMSDMLPKLFFDHFQN---TSFIAEEKGEIIGFLigFLSQSRMNEAY- 69
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSEEEREAWFAAILApgrPVLVAEEDGEVVGFA--SLGPFRPRPAYr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  70 ---IHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFKiEQGHknLDNVSLHtnyDGVN 146
Cdd:COG1247    80 gtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE-EVGT--LPEVGFK---FGRW 153

                         170
                  ....*....|
gi 1267630299 147 QDRVLFVKHL 156
Cdd:COG1247   154 LDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-156 2.36e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDYYVISPLINEW-------WNGRQMSDMLPKLFFDHFQN---TSFIAEEKGEIIGFLigFLSQSRMNEAY- 69
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSEEEREAWFAAILApgrPVLVAEEDGEVVGFA--SLGPFRPRPAYr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  70 ---IHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFKiEQGHknLDNVSLHtnyDGVN 146
Cdd:COG1247    80 gtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE-EVGT--LPEVGFK---FGRW 153

                         170
                  ....*....|
gi 1267630299 147 QDRVLFVKHL 156
Cdd:COG1247   154 LDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 35-124 7.05e-19

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: 76.79  E-value: 7.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  35 FFDHFQNTSFIAEEKGEIIGFLIGFLSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKI 114
Cdd:pfam00583  27 WDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 1267630299 115 SIAYHTKMGF 124
Cdd:pfam00583 107 AIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-106 3.08e-15

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: 66.15  E-value: 3.08e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267630299  43 SFIAEEKGEIIGFLIGFLSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRC 106
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-132 5.75e-11

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: 56.57  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  46 AEEKGEIIGFLIGflsQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFK 125
Cdd:TIGR01575  36 ARIGGKVVGYAGV---QIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....*..
gi 1267630299 126 IEQGHKN 132
Cdd:TIGR01575 113 EIAIRRN 119
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 47-142 7.46e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.38  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  47 EEKGEIIGFLIgflSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFki 126
Cdd:PRK09491   46 TVNGQMAAFAI---TQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF-- 120

                          90
                  ....*....|....*.
gi 1267630299 127 eqghknlDNVSLHTNY 142
Cdd:PRK09491  121 -------NEVTIRRNY 129
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-156 2.36e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDYYVISPLINEW-------WNGRQMSDMLPKLFFDHFQN---TSFIAEEKGEIIGFLigFLSQSRMNEAY- 69
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSEEEREAWFAAILApgrPVLVAEEDGEVVGFA--SLGPFRPRPAYr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  70 ---IHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFKiEQGHknLDNVSLHtnyDGVN 146
Cdd:COG1247    80 gtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE-EVGT--LPEVGFK---FGRW 153

                         170
                  ....*....|
gi 1267630299 147 QDRVLFVKHL 156
Cdd:COG1247   154 LDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 35-124 7.05e-19

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: 76.79  E-value: 7.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  35 FFDHFQNTSFIAEEKGEIIGFLIGFLSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKI 114
Cdd:pfam00583  27 WDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 1267630299 115 SIAYHTKMGF 124
Cdd:pfam00583 107 AIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-125 3.49e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.20  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   3 IRSVEGTDYYVISPLINEWWNGRQMSDMLPKLFFDHFQNTSFIAEEKGEIIGF--LIGFLSQSRMNEAYIHFVGVHPKYR 80
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHvaLSPVDIDGEGPALLLGPLAVDPEYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1267630299  81 GKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNkisIAYHTKMGFK 125
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFR 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-106 3.08e-15

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: 66.15  E-value: 3.08e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267630299  43 SFIAEEKGEIIGFLIGFLSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRC 106
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-156 6.74e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.83  E-value: 6.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  54 GFLIGFLSQSRmNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFKIeqghknl 133
Cdd:COG0456     1 GFALLGLVDGG-DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE------- 72

                          90       100
                  ....*....|....*....|...
gi 1267630299 134 dnVSLHTNYdgVNQDRVLFVKHL 156
Cdd:COG0456    73 --VGERPNY--YGDDALVMEKEL 91
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-128 5.16e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 64.69  E-value: 5.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDyyvisplINEWWNGRQMSDMLPKLFFDHFQNTSFIAEEKGEIIGFLIGflsqSRMNE--AYIHFVGVHPK 78
Cdd:COG0454     1 MSIRKATPED-------INFILLIEALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGL----RRLDDkvLELKRLYVLPE 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267630299  79 YRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFKIEQ 128
Cdd:COG0454    70 YRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIE 119
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-125 1.08e-12

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: 61.16  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDYYVISPLINEWwngrqmsDMLPKLffDHFqntsFIAEEKGEIIGFliGFLSQSRMNEAYIHFVGVHPKYR 80
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPY-------ALEEEI--GEF----WVAEEDGEIVGC--AALHPLDEDLAELRSLAVHPDYR 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1267630299  81 GKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVnkiSIAYHTKMGFK 125
Cdd:COG1246    66 GRGIGRRLLEALLAEARELGLKRLFLLTTSA---AIHFYEKLGFE 107
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 44-126 6.36e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 6.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  44 FIAEEKGEIIGFLIGFLSQSRMNEAYIHFVgVHPKYRGKKIGKQLYSHFFDVIKQNGrntIRCVTSPVNKISIAYHTKMG 123
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLA-VHPEYRGQGIGRALLEAAEAAAKEGG---IKLLELETTNRAAAFYEKLG 81


                  ...
gi 1267630299 124 FKI 126
Cdd:pfam13508  82 FEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-132 5.75e-11

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: 56.57  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  46 AEEKGEIIGFLIGflsQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFK 125
Cdd:TIGR01575  36 ARIGGKVVGYAGV---QIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....*..
gi 1267630299 126 IEQGHKN 132
Cdd:TIGR01575 113 EIAIRRN 119
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
1-125 2.06e-10

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 56.10  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDYYVISPLINEwwNGRQMSDM-LPKLffDHFQNTSF---IAEEKGEIIGFLIGFLSQSRM----------- 65
Cdd:COG3818     5 IVIRDAREHDLDAVLALNNA--AVPAVSPLdAARL--ARLHEQAAyarVAEVDGEVAGFLLAFGPGADYdspnyrwfaer 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267630299  66 --NEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRC-V-TSPVNKISIAYHTKMGFK 125
Cdd:COG3818    81 ydNFLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCeVnLEPPNPGSLAFHARLGFR 144
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-152 3.25e-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: 47.30  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299   1 MKIRSVEGTDY-----YVISPLINEWWNGRQMSDMLPKLFFDHFQNT-------SFIAEEK--GEIIGFlIGFLSQSRMN 66
Cdd:COG1670     8 LRLRPLRPEDAealaeLLNDPEVARYLPGPPYSLEEARAWLERLLADwadggalPFAIEDKedGELIGV-VGLYDIDRAN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  67 -EAYIHFVgVHPKYRGKKIGKQLYSHFFDVIKQN-GRNTIRCVTSPVNKISIAYHTKMGFKIEQGHKNldnvslHTNYDG 144
Cdd:COG1670    87 rSAEIGYW-LAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD------ALVIDG 159


                  ....*...
gi 1267630299 145 VNQDRVLF 152
Cdd:COG1670   160 RYRDHVLY 167
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 47-142 7.46e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.38  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  47 EEKGEIIGFLIgflSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFki 126
Cdd:PRK09491   46 TVNGQMAAFAI---TQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF-- 120

                          90
                  ....*....|....*.
gi 1267630299 127 eqghknlDNVSLHTNY 142
Cdd:PRK09491  121 -------NEVTIRRNY 129
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 44-125 3.57e-05

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: 41.10  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  44 FIAEEKGEIIGFLigflsqSRMNEAYIHFVGVHPKYRGKKIGKQLyshFFDVIKqngrntiRCVTSPVNKISI------- 116
Cdd:pfam13673  34 FVAFEGGQIVGVI------ALRDRGHISLLFVDPDYQGQGIGKAL---LEAVED-------YAEKDGIKLSELtvnaspy 97

                          90
                  ....*....|..
gi 1267630299 117 ---AYHtKMGFK 125
Cdd:pfam13673  98 avpFYE-KLGFR 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-125 4.85e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.89  E-value: 4.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267630299  68 AYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMGFK 125
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
COG3375 COG3375
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
46-88 7.40e-04

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


Pssm-ID: 442602 [Multi-domain]  Cd Length: 271  Bit Score: 38.39  E-value: 7.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1267630299  46 AEEKGEIIGFLIGFLsqSRMNEA---YIHFVGVHPKYRGKKIGKQL 88
Cdd:COG3375    53 AFDGGELVGFSFGFP--GFRPGGlylHSHMAGVLPEYRGRGVGYAL 96
PRK07757 PRK07757
N-acetyltransferase;
44-126 8.63e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.48  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  44 FIAEEKGEIIGFligflsqsrmneAYIHFVG----------VHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTspvnk 113
Cdd:PRK07757   44 YVAEEEGEIVGC------------CALHILWedlaeirslaVSEDYRGQGIGRMLVEACLEEARELGVKRVFALT----- 106

                          90
                  ....*....|...
gi 1267630299 114 ISIAYHTKMGFKI 126
Cdd:PRK07757  107 YQPEFFEKLGFRE 119
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
44-106 9.79e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 9.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267630299  44 FIAEEKGEIIGFLigflsqsRM-----NEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRC 106
Cdd:COG2153    37 LLAYDDGELVATA-------RLlppgdGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL 97
PRK10562 PRK10562
putative acetyltransferase; Provisional
 47-128 3.10e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.81  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  47 EEKGEIIGFLigflsqSRMNEAYIHFVGVHPKYRGKKIGKQLYSHF--------FDVIKQNgrntircvTSPVNkisiAY 118
Cdd:PRK10562   54 EEDGKLLGFV------SVLEGRFVGALFVAPKAVRRGIGKALMQHVqqryphlsLEVYQKN--------QRAVN----FY 115

                          90
                  ....*....|
gi 1267630299 119 HtKMGFKIEQ 128
Cdd:PRK10562  116 H-AQGFRIVD 124
PTZ00330 PTZ00330
acetyltransferase; Provisional
 69-134 4.32e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.59  E-value: 4.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267630299  69 YIHFVGVHPKYRGKKIGKQLYSHFFDVIKqnGRNTIRCVTSPVNKiSIAYHTKMGFKIEQGHKNLD 134
Cdd:PTZ00330   84 HIEDVVVDPSYRGQGLGRALISDLCEIAR--SSGCYKVILDCTED-MVAFYKKLGFRACERQMRLD 146
PRK03624 PRK03624
putative acetyltransferase; Provisional
 44-128 5.36e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 35.29  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267630299  44 FIAEEKGEIIGFLIGFLSQSRmneAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNGRNTIRCVTSPVNKISIAYHTKMG 123
Cdd:PRK03624   48 LVAEVGGEVVGTVMGGYDGHR---GWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALG 124


                  ....*
gi 1267630299 124 FKIEQ 128
Cdd:PRK03624  125 YEEQD 129
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 44-100 6.11e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 34.85  E-value: 6.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267630299  44 FIAEEKGEIIGFLIGF-----LSQSRMNEAYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNG 100
Cdd:pfam13527  42 LGAFDDGELVSTLALYpfelnVPGKTLPAAGITGVATYPEYRGRGVMSRLLRRSLEEMRERG 103
Eis COG4552
Predicted acetyltransferase [General function prediction only];
68-100 8.36e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 35.64  E-value: 8.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1267630299  68 AYIHFVGVHPKYRGKKIGKQLYSHFFDVIKQNG 100
Cdd:COG4552    73 AGITGVAVAPEHRRRGVARALLREALAELRERG 105
 
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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