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N-acetyltransferase family 8 member 4 isoform X1 [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];
104-211 1.11e-16

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.58  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 104 AHGSFWVAESGDQVVGIVGARPVKDPPlGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETSCvqySA 183
Cdd:COG3153   37 AAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP---SL 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 568943103 184 VALYQAMGFRKTDQYFVSI--ATRLMGLSI 211
Cdd:COG3153  113 LPFYERFGFRPAGELGLTLgpDEVFLAKEL 142
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
104-211 1.11e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.58  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 104 AHGSFWVAESGDQVVGIVGARPVKDPPlGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETSCvqySA 183
Cdd:COG3153   37 AAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP---SL 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 568943103 184 VALYQAMGFRKTDQYFVSI--ATRLMGLSI 211
Cdd:COG3153  113 LPFYERFGFRPAGELGLTLgpDEVFLAKEL 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 82-192 1.89e-15

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: 69.85  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103   82 WRNYVATSLQADLADITKSYLNAHGSFWVAESGDQVVGIVGARPVKDPPlgkKQMQLFRLSVSSQHRGQGIAKALVRTVL 161
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568943103  162 WFARDQDYSDVVLETSCVQYSAVALYQAMGF 192
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 108-175 5.72e-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: 5.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568943103 108 FWVAESGDQVVGIVGARPvkdPPLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLE 175
Cdd:cd04301    1 FLVAEDDGEIVGFASLSP---DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 95-196 4.03e-08

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: 50.41  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103   95 ADITKSYLNAHGSFWVAESGDQVVGIVGARPVKDpplgkkQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVL 174
Cdd:TIGR01575  20 AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|..
gi 568943103  175 ETSCVQYSAVALYQAMGFRKTD 196
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIA 115
PRK07757 PRK07757
N-acetyltransferase;
107-196 3.84e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.71  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 107 SFWVAESGDQVVGiVGARPVKDPPLGKkqmqlFR-LSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVletsCVQYSaVA 185
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAE-----IRsLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF----ALTYQ-PE 110

                         90
                 ....*....|.
gi 568943103 186 LYQAMGFRKTD 196
Cdd:PRK07757 111 FFEKLGFREVD 121
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
104-211 1.11e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.58  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 104 AHGSFWVAESGDQVVGIVGARPVKDPPlGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETSCvqySA 183
Cdd:COG3153   37 AAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP---SL 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 568943103 184 VALYQAMGFRKTDQYFVSI--ATRLMGLSI 211
Cdd:COG3153  113 LPFYERFGFRPAGELGLTLgpDEVFLAKEL 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 90-198 5.84e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 71.62  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103  90 LQADLADITKSYlnaHGSFWVAES-GDQVVGIVGARPvkdppLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQD 168
Cdd:COG0454   20 LDAELKAMEGSL---AGAEFIAVDdKGEPIGFAGLRR-----LDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 568943103 169 YSDVVLETSCVQYSAVALYQAMGFRKTDQY 198
Cdd:COG0454   92 CTALELDTLDGNPAAIRFYERLGFKEIERY 121
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 101-197 1.12e-15

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: 70.79  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 101 YLNAHGSFWVAESGDQVVGIVGARPvkdppLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETScvq 180
Cdd:COG1246   23 LEEEIGEFWVAEEDGEIVGCAALHP-----LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT--- 94

                         90
                 ....*....|....*..
gi 568943103 181 YSAVALYQAMGFRKTDQ 197
Cdd:COG1246   95 SAAIHFYEKLGFEEIDK 111
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 82-192 1.89e-15

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: 69.85  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103   82 WRNYVATSLQADLADITKSYLNAHGSFWVAESGDQVVGIVGARPVKDPPlgkKQMQLFRLSVSSQHRGQGIAKALVRTVL 161
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568943103  162 WFARDQDYSDVVLETSCVQYSAVALYQAMGF 192
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 105-194 3.52e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 68.25  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103  105 HGSFWVAESGDQVVGIVGARPVKDPPLGKKQmqlfRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETscvQYSAV 184
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGALAEL----RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAA 74

                          90
                  ....*....|
gi 568943103  185 ALYQAMGFRK 194
Cdd:pfam13508  75 AFYEKLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 119-197 4.32e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.75  E-value: 4.32e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568943103 119 GIVGARPVKDPPLGkkqmQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETSCVQYSAVALYQAMGFRKTDQ 197
Cdd:COG0456    1 GFALLGLVDGGDEA----EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
92-198 9.11e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.86  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103  92 ADLADITKSYLNAHGSFWVAESGDQVVGIVGARPVKDPPlGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSD 171
Cdd:COG1247   38 EEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRP-AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRR 116

                         90       100
                 ....*....|....*....|....*..
gi 568943103 172 VVLETSCVQYSAVALYQAMGFRKTDQY 198
Cdd:COG1247  117 LVAVVLADNEASIALYEKLGFEEVGTL 143
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 108-196 4.85e-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: 55.74  E-value: 4.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103  108 FWVAESGDQVVGIVGARpvkdpplgkKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETScVQYSAVALY 187
Cdd:pfam13673  33 FFVAFEGGQIVGVIALR---------DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN-ASPYAVPFY 102


                  ....*....
gi 568943103  188 QAMGFRKTD 196
Cdd:pfam13673 103 EKLGFRATG 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 108-175 5.72e-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: 5.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568943103 108 FWVAESGDQVVGIVGARPvkdPPLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLE 175
Cdd:cd04301    1 FLVAEDDGEIVGFASLSP---DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
110-195 8.16e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.19  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 110 VAESGDQVVGIvgARPVkdpPLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLEtscVQYSAVALYQA 189
Cdd:COG2153   38 LAYDDGELVAT--ARLL---PPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLS---AQAHAVGFYEK 109


                 ....*.
gi 568943103 190 MGFRKT 195
Cdd:COG2153  110 LGFVPV 115
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
116-198 3.46e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.52  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 116 QVVGIVGARPVkdpplGKKQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVLETSCVQYSAVALYQAMGFRKT 195
Cdd:COG3393    1 ELVAMAGVRAE-----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75


                 ...
gi 568943103 196 DQY 198
Cdd:COG3393   76 GEY 78
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 95-196 4.03e-08

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: 50.41  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103   95 ADITKSYLNAHGSFWVAESGDQVVGIVGARPVKDpplgkkQMQLFRLSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVL 174
Cdd:TIGR01575  20 AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|..
gi 568943103  175 ETSCVQYSAVALYQAMGFRKTD 196
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIA 115
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 91-195 4.03e-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: 42.68  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103  91 QADLADITKSYLNAHGSFWVAE--SGDQVVGIVGARPVKDPP----LGkkqmqlfrLSVSSQHRGQGIAKALVRTVL-WF 163
Cdd:COG1670   45 RAWLERLLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANrsaeIG--------YWLAPAYWGKGYATEALRALLdYA 116

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568943103 164 ARDQDYSDVVLETSCVQYSAVALYQAMGFRKT 195
Cdd:COG1670  117 FEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
143-169 5.68e-05

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 40.52  E-value: 5.68e-05
                         10        20
                 ....*....|....*....|....*..
gi 568943103 143 VSSQHRGQGIAKALVRTVLWFARDQDY 169
Cdd:COG2388   40 VPPALRGQGIASALVEAALDDARERGL 66
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 143-198 1.13e-04

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: 39.43  E-value: 1.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568943103  143 VSSQHRGQGIAKALVRTVLWFARDQDYSdVVLetSCvqySAVALYqamgFRKTDQY 198
Cdd:pfam14542  31 VPPALRGQGIASKLVKAALDDAREEGLK-IVP--LC---SYVAAY----LEKHPEY 76
PRK07757 PRK07757
N-acetyltransferase;
107-196 3.84e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.71  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943103 107 SFWVAESGDQVVGiVGARPVKDPPLGKkqmqlFR-LSVSSQHRGQGIAKALVRTVLWFARDQDYSDVVletsCVQYSaVA 185
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAE-----IRsLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF----ALTYQ-PE 110

                         90
                 ....*....|.
gi 568943103 186 LYQAMGFRKTD 196
Cdd:PRK07757 111 FFEKLGFREVD 121
 
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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