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Conserved domains on  [gi|24655202|ref|NP_728606|]
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N(alpha)-acetyltransferase 30 B [Drosophila melanogaster]

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 ...
 105-198 2.25e-19

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 78.93  E-value: 2.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202 105 GVIVCKLEAKRDGylqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGFIRERRFL 184
Cdd:COG0456   1 GFALLGLVDGGDE---AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....
gi 24655202 185 RYYLNGMDAFHLKL 198
Cdd:COG0456  78 NYYGDDALVMEKEL 91
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-198 2.25e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 78.93  E-value: 2.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202 105 GVIVCKLEAKRDGylqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGFIRERRFL 184
Cdd:COG0456   1 GFALLGLVDGGDE---AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....
gi 24655202 185 RYYLNGMDAFHLKL 198
Cdd:COG0456  78 NYYGDDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-177 9.04e-17

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: 72.94  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    63 LKVLMGLIDKELSEPYSIYTYRYF---VYNWPDLCFFALDGDRYVGVIVCKLEAKRDGYlqGYIAMLAVDAEYRKRGIGR 139
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwDEDASEGFFVAEEDGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 24655202   140 ALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGF 177
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 70-194 2.93e-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: 66.58  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    70 IDKE-LSEPYSIYTYRYFVYNWPDLCFFALDGDRYVGVIVCKLEAKrdgylQGYIAMLAVDAEYRKRGIGRALSEMAIDA 148
Cdd:TIGR01575   8 IEAAaFAFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 24655202   149 MAIRDAAMIVLETELSNKPALALYQSLGFIRERRFLRYYLNGM-DAF 194
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 94-160 4.78e-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: 53.82  E-value: 4.78e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655202  94 CFFALDGDRYVGVIVCKLEAKRDGYlqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLE 160
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGDT--AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 91-182 2.13e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 53.78  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202   91 PDLCFFALDGDRYVGVIVckleAKRDGYlQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALA 170
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVM----GGYDGH-RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118

                         90
                 ....*....|..
gi 24655202  171 LYQSLGFIRERR 182
Cdd:PRK03624 119 FYEALGYEEQDR 130
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-198 2.25e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 78.93  E-value: 2.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202 105 GVIVCKLEAKRDGylqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGFIRERRFL 184
Cdd:COG0456   1 GFALLGLVDGGDE---AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....
gi 24655202 185 RYYLNGMDAFHLKL 198
Cdd:COG0456  78 NYYGDDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-177 9.04e-17

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: 72.94  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    63 LKVLMGLIDKELSEPYSIYTYRYF---VYNWPDLCFFALDGDRYVGVIVCKLEAKRDGYlqGYIAMLAVDAEYRKRGIGR 139
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwDEDASEGFFVAEEDGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 24655202   140 ALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGF 177
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
91-183 6.09e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.96  E-value: 6.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  91 PDLCFFALDGDRYVGVIVCKLEAKRDGYLQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETelsNKPALA 170
Cdd:COG3153  38 AGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLP 114

                        90
                ....*....|...
gi 24655202 171 LYQSLGFIRERRF 183
Cdd:COG3153 115 FYERFGFRPAGEL 127
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 70-194 2.93e-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: 66.58  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    70 IDKE-LSEPYSIYTYRYFVYNWPDLCFFALDGDRYVGVIVCKLEAKrdgylQGYIAMLAVDAEYRKRGIGRALSEMAIDA 148
Cdd:TIGR01575   8 IEAAaFAFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 24655202   149 MAIRDAAMIVLETELSNKPALALYQSLGFIRERRFLRYYLNGM-DAF 194
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 58-191 1.17e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  58 HDESQLKVLMGLIDKELSEPYSIYTYRYFVynwpdlcfFALDGDRYVGVIVCKLEAKRDGYlqgyIAMLAVDAEYRKRGI 137
Cdd:COG0454   8 PEDINFILLIEALDAELKAMEGSLAGAEFI--------AVDDKGEPIGFAGLRRLDDKVLE----LKRLYVLPEYRGKGI 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24655202 138 GRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGFIRERRFLRYYLNGM 191
Cdd:COG0454  76 GKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEF 129
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
107-188 4.17e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 62.23  E-value: 4.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202 107 IVCKLEAKRDGYLQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGFIRERRFLRY 186
Cdd:COG3393   2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                ..
gi 24655202 187 YL 188
Cdd:COG3393  82 LF 83
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
94-199 1.33e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.09  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  94 CFFALDGDRYVGVIVCKLEAKRDGYLQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQ 173
Cdd:COG1247  54 VLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133

                        90       100
                ....*....|....*....|....*.
gi 24655202 174 SLGFIRERRFLRYYLNGMDAFHLKLM 199
Cdd:COG1247 134 KLGFEEVGTLPEVGFKFGRWLDLVLM 159
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 92-179 1.40e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 58.23  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    92 DLCFFALDGDRYVGVIVCkleAKRDGYLQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETelsNKPALAL 171
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAAL---LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAF 76


                  ....*...
gi 24655202   172 YQSLGFIR 179
Cdd:pfam13508  77 YEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 94-160 4.78e-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: 53.82  E-value: 4.78e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655202  94 CFFALDGDRYVGVIVCKLEAKRDGYlqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLE 160
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGGDT--AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 93-200 4.99e-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: 55.35  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    93 LCFFALDGDRYVGVIvcklEAKRDGYlqgyIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETElSNKPALALY 172
Cdd:pfam13673  32 FFFVAFEGGQIVGVI----ALRDRGH----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN-ASPYAVPFY 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 24655202   173 QSLGFI---RERRFlryylNGMDAFHLKLML 200
Cdd:pfam13673 103 EKLGFRatgPEQEF-----NGIRFVPMEKEL 128
PRK03624 PRK03624
putative acetyltransferase; Provisional
 91-182 2.13e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 53.78  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202   91 PDLCFFALDGDRYVGVIVckleAKRDGYlQGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALA 170
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVM----GGYDGH-RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118

                         90
                 ....*....|..
gi 24655202  171 LYQSLGFIRERR 182
Cdd:PRK03624 119 FYEALGYEEQDR 130
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 94-179 7.41e-09

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: 52.30  E-value: 7.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  94 CFFALDGDRYVGVIVckLEAKRDGYlqGYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETelsNKPALALYQ 173
Cdd:COG1246  30 FWVAEEDGEIVGCAA--LHPLDEDL--AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYE 102


                ....*.
gi 24655202 174 SLGFIR 179
Cdd:COG1246 103 KLGFEE 108
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 126-177 9.15e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 52.24  E-value: 9.15e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24655202  126 LAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSLGF 177
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
95-180 2.13e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 2.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  95 FFALDGDRYVGVIVCKLEAKRDGYlqgyIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSnkpALALYQS 174
Cdd:COG2153  37 LLAYDDGELVATARLLPPGDGEAK----IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEK 109


                ....*.
gi 24655202 175 LGFIRE 180
Cdd:COG2153 110 LGFVPV 115
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 88-188 6.12e-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: 47.69  E-value: 6.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  88 YNWPDLCFFAL---DGDRYVGVIVCKLEAKRDGylQGYIAMlAVDAEYRKRGIGRALSEMAID-AMAIRDAAMIVLETEL 163
Cdd:COG1670  55 WADGGALPFAIedkEDGELIGVVGLYDIDRANR--SAEIGY-WLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDP 131

                        90       100
                ....*....|....*....|....*
gi 24655202 164 SNKPALALYQSLGFIRERRFLRYYL 188
Cdd:COG1670 132 DNTASIRVLEKLGFRLEGTLRDALV 156
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
108-181 4.38e-06

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 45.31  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202  108 VCKLEAKRDGYLQGY------------IAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLETELSNKPALALYQSL 175
Cdd:PRK10975 102 QCLLLRDASGQIQGFvtlrelndtdarIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRS 181


                 ....*.
gi 24655202  176 GFIRER 181
Cdd:PRK10975 182 GANIES 187
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 97-177 1.10e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.55  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655202    97 ALDGDRYVGVIVCkleAKRDGYLQG------YIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVLEtelsnkPAL- 169
Cdd:pfam13527  44 AFDDGELVSTLAL---YPFELNVPGktlpaaGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLY------PSSy 114


                  ....*...
gi 24655202   170 ALYQSLGF 177
Cdd:pfam13527 115 PIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
121-159 4.55e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.19  E-value: 4.55e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24655202 121 GYIAMLAVDAEYRKRGIGRALSEMAIDAMAIRDAAMIVL 159
Cdd:COG4552  73 AGITGVAVAPEHRRRGVARALLREALAELRERGQPLSAL 111
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 129-183 7.00e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 35.57  E-value: 7.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24655202   129 DAEYRKRGIGRALSEMAIDAMAIRDAAM-IVLETELSNKPALALYQSLGFIRERRF 183
Cdd:pfam13523  88 EPAFRGRGFTTALLRALVHYLFADPRTRrVVVEPDVRNERAIRLLERAGFRKVKEI 143
 
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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