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Conserved domains on  [gi|15224449|ref|NP_181348|]
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Acyl-CoA N-acyltransferases (NAT) superfamily protein [Arabidopsis thaliana]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 27-140 2.05e-21

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: 84.49  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    27 LPLIMSLVDQELSEPYSIFTYRYF---VYLWPQLCFLAFHKGKCVGTIVCKMGDHRqTFRGYIAMLVVIKPYRGRGIASE 103
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwDEDASEGFFVAEEDGELVGFASLSIIDDE-PPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15224449   104 LVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGF 140
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 27-140 2.05e-21

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: 84.49  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    27 LPLIMSLVDQELSEPYSIFTYRYF---VYLWPQLCFLAFHKGKCVGTIVCKMGDHRqTFRGYIAMLVVIKPYRGRGIASE 103
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwDEDASEGFFVAEEDGELVGFASLSIIDDE-PPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15224449   104 LVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGF 140
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-161 1.31e-18

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  69 GTIVCKMGDHRQTfrGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYH 148
Cdd:COG0456   1 GFALLGLVDGGDE--AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                        90
                ....*....|...
gi 15224449 149 YYLNGMDAFRLKL 161
Cdd:COG0456  79 YYGDDALVMEKEL 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 26-157 1.56e-14

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: 66.97  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    26 HLPLIMSLVDQELSEPYSIFTYRYfVYLWPQLCFL-AFHKGKCVGTIVCKMgdhrQTFRGYIAMLVVIKPYRGRGIASEL 104
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAE-ELANYHLCYLlARIGGKVVGYAGVQI----VLDEAHILNIAVKPEYQGQGIGRAL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15224449   105 VTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHYYLNGM-DAF 157
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-123 4.59e-11

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: 56.13  E-value: 4.59e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224449  58 CFLAFHKGKCVGTIVCKMGDHRQTfRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLE 123
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-140 1.94e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449   55 PQLCFLAFHKGKCVGTIvckMGDHrQTFRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALAL 134
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTV---MGGY-DGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGF 119


                 ....*.
gi 15224449  135 YGRLGF 140
Cdd:PRK03624 120 YEALGY 125
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 27-140 2.05e-21

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: 84.49  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    27 LPLIMSLVDQELSEPYSIFTYRYF---VYLWPQLCFLAFHKGKCVGTIVCKMGDHRqTFRGYIAMLVVIKPYRGRGIASE 103
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwDEDASEGFFVAEEDGELVGFASLSIIDDE-PPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15224449   104 LVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGF 140
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-161 1.31e-18

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  69 GTIVCKMGDHRQTfrGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYH 148
Cdd:COG0456   1 GFALLGLVDGGDE--AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                        90
                ....*....|...
gi 15224449 149 YYLNGMDAFRLKL 161
Cdd:COG0456  79 YYGDDALVMEKEL 91
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
22-161 9.28e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.20  E-value: 9.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  22 AGEHHLPLIMSLVDQELSEPYSIFT-YRYFVYLWPQLCFLAFHKGKCVGTI-VCKMGDHRQTFRGYIAMLVVIKPYRGRG 99
Cdd:COG3153   4 ATPEDAEAIAALLRAAFGPGREAELvDRLREDPAAGLSLVAEDDGEIVGHVaLSPVDIDGEGPALLLGPLAVDPEYRGQG 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224449 100 IASELVTRAIKAMMESGCEEVTLeaeVSNKGALALYGRLGFIRAKRLYHYYLNGMDAFRLKL 161
Cdd:COG3153  84 IGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 26-157 1.56e-14

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: 66.97  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    26 HLPLIMSLVDQELSEPYSIFTYRYfVYLWPQLCFL-AFHKGKCVGTIVCKMgdhrQTFRGYIAMLVVIKPYRGRGIASEL 104
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAE-ELANYHLCYLlARIGGKVVGYAGVQI----VLDEAHILNIAVKPEYQGQGIGRAL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15224449   105 VTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHYYLNGM-DAF 157
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 35-154 5.64e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 60.45  E-value: 5.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  35 DQELSEPYSIFTYRYFVylwpqlcfLAFHKGKCVGTIVCKMGDHRqtfRGYIAMLVVIKPYRGRGIASELVTRAIKAMME 114
Cdd:COG0454  21 DAELKAMEGSLAGAEFI--------AVDDKGEPIGFAGLRRLDDK---VLELKRLYVLPEYRGKGIGKALLEALLEWARE 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15224449 115 SGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHYYLNGM 154
Cdd:COG0454  90 RGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEF 129
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-151 2.27e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 57.23  E-value: 2.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  71 IVCKMGDHRQTFR-GYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHY 149
Cdd:COG3393   2 LVAMAGVRAESPGvAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                ..
gi 15224449 150 YL 151
Cdd:COG3393  82 LF 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-123 4.59e-11

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: 56.13  E-value: 4.59e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224449  58 CFLAFHKGKCVGTIVCKMGDHRQTfRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLE 123
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 58-142 1.01e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.54  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    58 CFLAFHKGKCVGTIVCKMGDHrqTFRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEaevSNKGALALYGR 137
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDD--EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE---TTNRAAAFYEK 79


                  ....*
gi 15224449   138 LGFIR 142
Cdd:pfam13508  80 LGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 58-145 2.09e-10

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: 56.15  E-value: 2.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  58 CFLAFHKGKCVGTIVCKMGDHRQtfrGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEaevSNKGALALYGR 137
Cdd:COG1246  30 FWVAEEDGEIVGCAALHPLDEDL---AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEK 103


                ....*...
gi 15224449 138 LGFIRAKR 145
Cdd:COG1246 104 LGFEEIDK 111
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
59-142 4.08e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.19  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  59 FLAFHKGKCVGTI-VCKMGDHRqtfrGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSnkgALALYGR 137
Cdd:COG2153  37 LLAYDDGELVATArLLPPGDGE----AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEK 109


                ....*
gi 15224449 138 LGFIR 142
Cdd:COG2153 110 LGFVP 114
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
58-146 1.18e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.92  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  58 CFLAFHKGKCVGTIVCKMGDHRQTFRG-YIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYG 136
Cdd:COG1247  54 VLVAEEDGEVVGFASLGPFRPRPAYRGtAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133

                        90
                ....*....|
gi 15224449 137 RLGFIRAKRL 146
Cdd:COG1247 134 KLGFEEVGTL 143
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-163 3.81e-08

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: 49.96  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    57 LCFLAFHKGKCVGtiVCKMGDhrqtfRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNkGALALYG 136
Cdd:pfam13673  32 FFFVAFEGGQIVG--VIALRD-----RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFYE 103

                          90       100
                  ....*....|....*....|....*..
gi 15224449   137 RLGFIRAKRLyhYYLNGMDAFRLKLLF 163
Cdd:pfam13673 104 KLGFRATGPE--QEFNGIRFVPMEKEL 128
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-140 1.94e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449   55 PQLCFLAFHKGKCVGTIvckMGDHrQTFRGYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALAL 134
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTV---MGGY-DGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGF 119


                 ....*.
gi 15224449  135 YGRLGF 140
Cdd:PRK03624 120 YEALGY 125
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 57-151 2.01e-07

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 48.84  E-value: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  57 LCFLAFHK--GKCVGTIVCkMGDHRQTFRGYIAMlVVIKPYRGRGIASELVTRAIK-AMMESGCEEVTLEAEVSNKGALA 133
Cdd:COG1670  61 LPFAIEDKedGELIGVVGL-YDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIR 138

                        90
                ....*....|....*...
gi 15224449 134 LYGRLGFIRAKRLYHYYL 151
Cdd:COG1670 139 VLEKLGFRLEGTLRDALV 156
Eis COG4552
Predicted acetyltransferase [General function prediction only];
48-149 3.66e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 43.35  E-value: 3.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449  48 RYFVYLWPQLCFLAFHKGKCVGTivCKMGDHRQTFRG------YIAMlVVIKP-YRGRGIASELVTRAIKAMMESGCEEV 120
Cdd:COG4552  33 AYRPLLEPGRVLGVFDDGELVGT--LALYPFTLNVGGarvpmaGITG-VAVAPeHRRRGVARALLREALAELRERGQPLS 109

                        90       100       110
                ....*....|....*....|....*....|..
gi 15224449 121 TL---EAevsnkgalALYGRLGFIRAKRLYHY 149
Cdd:COG4552 110 ALypfEP--------GFYRRFGYELAGDRRRY 133
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 95-150 1.13e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 1.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15224449   95 YRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKGALALYGRLGFIRAKRLYHYY 150
Cdd:PRK09491  75 YQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 93-140 1.58e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 37.33  E-value: 1.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15224449    93 KPYRGRGIASELVTRAIKAMMES-GCEEVTLEAEVSNKGALALYGRLGF 140
Cdd:pfam13302  90 PDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGF 138
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 84-141 3.67e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 35.00  E-value: 3.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15224449    84 GYIAMLVVIKPYRGRGIASELVTRAIKAMMESGcEEVTLEAEVSNKGALALYGRLGFI 141
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFR 78
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 77-122 6.04e-03

3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163676  Cd Length: 274  Bit Score: 36.22  E-value: 6.04e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15224449  77 DHRQTFRGYIAMlVVIKPYRGRgIASELVTRAIKAMMESGCEEVTL 122
Cdd:cd07938 125 AAGLRVRGYVST-AFGCPYEGE-VPPERVAEVAERLLDLGCDEISL 168
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 58-140 9.43e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 34.85  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224449    58 CFLAFHKGKCVGTIVC---KMGDHRQTFR-GYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEA-EVsnkgal 132
Cdd:pfam13527  41 VLGAFDDGELVSTLALypfELNVPGKTLPaAGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYPsSY------ 114


                  ....*...
gi 15224449   133 ALYGRLGF 140
Cdd:pfam13527 115 PIYRRFGY 122
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 84-142 9.81e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 35.07  E-value: 9.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15224449   84 GYIAMLVVIKPYRGRGIASELVTRAIKAMMESGCEEVTLEAEVSNKgalALYGRLGFIR 142
Cdd:PLN02706  86 GHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENK---AFYEKCGYVR 141
 
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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