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Conserved domains on  [gi|12963681|ref|NP_075944|]
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N-acetyltransferase 8 [Mus musculus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
103-198 3.28e-18

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 77.82  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 103 SVRGSGFWVAESGGQVVGTVAARPVKDPPlGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGllqQ 182
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---P 110

                        90
                ....*....|....*.
gi 12963681 183 GAVTLYYSMGFQKTGE 198
Cdd:COG3153 111 SLLPFYERFGFRPAGE 126
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
103-198 3.28e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 77.82  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 103 SVRGSGFWVAESGGQVVGTVAARPVKDPPlGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGllqQ 182
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---P 110

                        90
                ....*....|....*.
gi 12963681 183 GAVTLYYSMGFQKTGE 198
Cdd:COG3153 111 SLLPFYERFGFRPAGE 126
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 91-193 2.98e-16

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: 71.78  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681    91 HTDMADITKSYLSVRGSGFWVAESGGQVVGTVAARPVKDPPlgrKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGY 170
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93

                          90       100
                  ....*....|....*....|...
gi 12963681   171 SDVVLVTGLLQQGAVTLYYSMGF 193
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 109-175 5.82e-12

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 59.21  E-value: 5.82e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12963681 109 FWVAESGGQVVGTVAARPvkdPPLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVL 175
Cdd:cd04301   1 FLVAEDDGEIVGFASLSP---DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 102-198 1.27e-07

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: 48.86  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681   102 LSVRGSGFWVAESGGQVVGTVAARPVKDpplgrkQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQ 181
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSN 99

                          90
                  ....*....|....*..
gi 12963681   182 QGAVTLYYSMGFQKTGE 198
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAI 116
PRK07757 PRK07757
N-acetyltransferase;
109-202 1.94e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.48  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681  109 FWVAESGGQVVGTVAarpvkdpplgrkqLQLF-------R-LSVSSQHRGQGIAKALTRTVLQFARDQGYSDVvlvtgll 180
Cdd:PRK07757  43 FYVAEEEGEIVGCCA-------------LHILwedlaeiRsLAVSEDYRGQGIGRMLVEACLEEARELGVKRV------- 102

                         90       100
                 ....*....|....*....|...
gi 12963681  181 qqgaVTLYYSMG-FQKTGESFVD 202
Cdd:PRK07757 103 ----FALTYQPEfFEKLGFREVD 121
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
103-198 3.28e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 77.82  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 103 SVRGSGFWVAESGGQVVGTVAARPVKDPPlGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGllqQ 182
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---P 110

                        90
                ....*....|....*.
gi 12963681 183 GAVTLYYSMGFQKTGE 198
Cdd:COG3153 111 SLLPFYERFGFRPAGE 126
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-202 3.83e-18

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: 77.34  E-value: 3.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681  97 ITKSYLSVRGSGFWVAESGGQVVGTVAARPvkdppLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLV 176
Cdd:COG1246  18 IRPYALEEEIGEFWVAEEDGEIVGCAALHP-----LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92

                        90       100
                ....*....|....*....|....*.
gi 12963681 177 TGllqQGAVTLYYSMGFQKTGESFVD 202
Cdd:COG1246  93 TT---SAAIHFYEKLGFEEIDKEDLP 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
105-198 3.02e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.80  E-value: 3.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 105 RGSGFWVAESGGQVVGTVAARPVKDPPlGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQQGA 184
Cdd:COG1247  50 PGRPVLVAEEDGEVVGFASLGPFRPRP-AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEAS 128

                        90
                ....*....|....
gi 12963681 185 VTLYYSMGFQKTGE 198
Cdd:COG1247 129 IALYEKLGFEEVGT 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 91-193 2.98e-16

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: 71.78  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681    91 HTDMADITKSYLSVRGSGFWVAESGGQVVGTVAARPVKDPPlgrKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGY 170
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93

                          90       100
                  ....*....|....*....|...
gi 12963681   171 SDVVLVTGLLQQGAVTLYYSMGF 193
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 95-205 7.49e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 71.24  E-value: 7.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681  95 ADITKSYLSVRGSGFWVAESGGQVVGTVAARPvkdppLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVV 174
Cdd:COG0454  22 AELKAMEGSLAGAEFIAVDDKGEPIGFAGLRR-----LDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALE 96

                        90       100       110
                ....*....|....*....|....*....|.
gi 12963681 175 LVTGLLQQGAVTLYYSMGFQKTGESFVDILT 205
Cdd:COG0454  97 LDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 105-195 2.83e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 63.24  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681   105 RGSGFWVAESGGQVVGTVAARPVKDpplgRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTgllQQGA 184
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDD----EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRA 73

                          90
                  ....*....|.
gi 12963681   185 VTLYYSMGFQK 195
Cdd:pfam13508  74 AAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
111-202 5.67e-13

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 63.66  E-value: 5.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 111 VAESGGQVVGTVAARPvkdppLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTgllQQGAVTLYYS 190
Cdd:COG2153  38 LAYDDGELVATARLLP-----PGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEK 109

                        90
                ....*....|..
gi 12963681 191 MGFQKTGESFVD 202
Cdd:COG2153 110 LGFVPVGEEFLE 121
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 120-198 1.35e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.60  E-value: 1.35e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12963681 120 GTVAARPVKDPPLGRkqlqLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQQGAVTLYYSMGFQKTGE 198
Cdd:COG0456   1 GFALLGLVDGGDEAE----IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 109-175 5.82e-12

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 59.21  E-value: 5.82e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12963681 109 FWVAESGGQVVGTVAARPvkdPPLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVL 175
Cdd:cd04301   1 FLVAEDDGEIVGFASLSP---DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 109-202 1.45e-09

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 54.20  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681   109 FWVAESGGQVVGTVAARpvkdpplgRKQlQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSdVVLVTGLLQQGAVTLY 188
Cdd:pfam13673  33 FFVAFEGGQIVGVIALR--------DRG-HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIK-LSELTVNASPYAVPFY 102

                          90
                  ....*....|....
gi 12963681   189 YSMGFQKTGESFVD 202
Cdd:pfam13673 103 EKLGFRATGPEQEF 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
117-198 1.65e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.99  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 117 QVVGTVAARPVkdpplGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQQGAVTLYYSMGFQKT 196
Cdd:COG3393   1 ELVAMAGVRAE-----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75


                ..
gi 12963681 197 GE 198
Cdd:COG3393  76 GE 77
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 102-198 1.27e-07

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: 48.86  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681   102 LSVRGSGFWVAESGGQVVGTVAARPVKDpplgrkQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQ 181
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSN 99

                          90
                  ....*....|....*..
gi 12963681   182 QGAVTLYYSMGFQKTGE 198
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAI 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 105-198 1.13e-05

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: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 105 RGSGFWVAE--SGGQVVGTVAARPVkDPPLGRKQLqlfRLSVSSQHRGQGIAKALTRTVLQFARDQ-GYSDVVLVTGLLQ 181
Cdd:COG1670  58 GGALPFAIEdkEDGELIGVVGLYDI-DRANRSAEI---GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDN 133

                        90
                ....*....|....*..
gi 12963681 182 QGAVTLYYSMGFQKTGE 198
Cdd:COG1670 134 TASIRVLEKLGFRLEGT 150
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
144-170 2.53e-05

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 41.68  E-value: 2.53e-05
                        10        20
                ....*....|....*....|....*..
gi 12963681 144 VSSQHRGQGIAKALTRTVLQFARDQGY 170
Cdd:COG2388  40 VPPALRGQGIASALVEAALDDARERGL 66
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 144-170 3.16e-05

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 40.97  E-value: 3.16e-05
                          10        20
                  ....*....|....*....|....*..
gi 12963681   144 VSSQHRGQGIAKALTRTVLQFARDQGY 170
Cdd:pfam14542  31 VPPALRGQGIASKLVKAALDDAREEGL 57
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
104-177 4.16e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 39.51  E-value: 4.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681 104 VRGSGFWVAESGGQVVGTVAARPVKDPPL-------GrkqlqlfrLSVSSQHRGQGIAKALTRTVLQFARDQGYsDVVLV 176
Cdd:COG3981  60 VPATTYWLVDEDGRIVGAINLRHELNEFLlrvgghiG--------YGVRPSERGKGYATEMLRLALEEARELGL-DRVLI 130


                .
gi 12963681 177 T 177
Cdd:COG3981 131 T 131
PRK07757 PRK07757
N-acetyltransferase;
109-202 1.94e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.48  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963681  109 FWVAESGGQVVGTVAarpvkdpplgrkqLQLF-------R-LSVSSQHRGQGIAKALTRTVLQFARDQGYSDVvlvtgll 180
Cdd:PRK07757  43 FYVAEEEGEIVGCCA-------------LHILwedlaeiRsLAVSEDYRGQGIGRMLVEACLEEARELGVKRV------- 102

                         90       100
                 ....*....|....*....|...
gi 12963681  181 qqgaVTLYYSMG-FQKTGESFVD 202
Cdd:PRK07757 103 ----FALTYQPEfFEKLGFREVD 121
PRK03624 PRK03624
putative acetyltransferase; Provisional
 95-157 3.90e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.45  E-value: 3.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12963681   95 ADITKSyLSVRGSGFWVAESGGQVVGTVAA-----RpvkdpplGrkqlQLFRLSVSSQHRGQGIAKAL 157
Cdd:PRK03624  34 MDIERK-LNHDPSLFLVAEVGGEVVGTVMGgydghR-------G----WAYYLAVHPDFRGRGIGRAL 89
PRK10514 PRK10514
putative acetyltransferase; Provisional
 142-202 4.63e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 36.13  E-value: 4.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12963681  142 LSVSSQHRGQGIAKALTRTVLQFARDqgysdvvLVTGLLQQG--AVTLYYSMGFQKTGESFVD 202
Cdd:PRK10514  75 LFVDPDVRGCGVGRMLVEHALSLHPE-------LTTDVNEQNeqAVGFYKKMGFKVTGRSEVD 130
 
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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