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Conserved domains on  [gi|47115157|emb|CAG28538|]
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NAT8, partial [Homo sapiens]

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
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 ...
92-193 2.35e-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: 85.26  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    92 TDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPtlrEKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYS 171
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94
                          90       100
                  ....*....|....*....|..
gi 47115157   172 EVILDTGTIQLSAMALYQSMGF 193
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
92-193 2.35e-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: 85.26  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    92 TDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPtlrEKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYS 171
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94
                          90       100
                  ....*....|....*....|..
gi 47115157   172 EVILDTGTIQLSAMALYQSMGF 193
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
97-220 1.15e-20

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: 83.89  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157  97 ITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:COG1246  18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 47115157 177 TGTiqlSAMALYQSMGFKKTGQSFFRVwARLVALHTVHFIYHLP 220
Cdd:COG1246  93 TTS---AAIHFYEKLGFEEIDKEDLPY-AKVWQRDSVVMEKDLE 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
109-176 5.05e-14

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: 64.60  E-value: 5.05e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47115157 109 FWVAESEEKVVGMVGALPVDDptlREKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
81-197 7.56e-11

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 57.72  E-value: 7.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    81 PWTEyvdmtlctdmsDITKSYLSERGSCFWVAESEEKVVGMVGAlpvdDPTLREKrlQLFHLSVDSEHRRQGIAKALVRT 160
Cdd:TIGR01575  16 PWTE-----------AQFAEELANYHLCYLLARIGGKVVGYAGV----QIVLDEA--HILNIAVKPEYQGQGIGRALLRE 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47115157   161 VLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTG 197
Cdd:TIGR01575  79 LIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
PRK07757 PRK07757
N-acetyltransferase;
108-205 5.16e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 53.27  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157  108 CFWVAESEEKVVGmVGALPVDDPTLREKRlqlfHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVIldTGTIQlsaMAL 187
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAEIR----SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF--ALTYQ---PEF 111
                         90       100
                 ....*....|....*....|
gi 47115157  188 YQSMGFKKTGQSFF--RVWA 205
Cdd:PRK07757 112 FEKLGFREVDKEALpqKVWA 131
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
92-193 2.35e-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: 85.26  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    92 TDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPtlrEKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYS 171
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94
                          90       100
                  ....*....|....*....|..
gi 47115157   172 EVILDTGTIQLSAMALYQSMGF 193
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
97-220 1.15e-20

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: 83.89  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157  97 ITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:COG1246  18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 47115157 177 TGTiqlSAMALYQSMGFKKTGQSFFRVwARLVALHTVHFIYHLP 220
Cdd:COG1246  93 TTS---AAIHFYEKLGFEEIDKEDLPY-AKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
103-210 1.56e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 83.98  E-value: 1.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 103 SERGSCFWVAESEEKVVGMVGALPVDDPTlREKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTiql 182
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP--- 110
                        90       100
                ....*....|....*....|....*...
gi 47115157 183 SAMALYQSMGFKKTGQSFFRVWARLVAL 210
Cdd:COG3153 111 SLLPFYERFGFRPAGELGLTLGPDEVFL 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
105-195 5.89e-19

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 78.27  E-value: 5.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157   105 RGSCFWVAESEEKVVGMVGALPVDDPTLREKRlqlfHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiQLSA 184
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAEL----RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRA 73
                          90
                  ....*....|.
gi 47115157   185 MALYQSMGFKK 195
Cdd:pfam13508  74 AAFYEKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
103-209 3.08e-17

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.09  E-value: 3.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 103 SERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQL 182
Cdd:COG0454  30 SLAGAEFIAVDDKGEPIGFAGLRRLDDKVL-----ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNP 104
                        90       100
                ....*....|....*....|....*..
gi 47115157 183 SAMALYQSMGFKKTGQSFFRVWARLVA 209
Cdd:COG0454 105 AAIRFYERLGFKEIERYVAYVGGEFEK 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
120-198 4.19e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 4.19e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47115157 120 GMVGALPVDDPtlreKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTGQ 198
Cdd:COG0456   1 GFALLGLVDGG----DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
102-197 1.82e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 71.18  E-value: 1.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 102 LSERGSCFWVAESEEKVVGMVGALPVDDptlREKRLQLFHLS--VDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGT 179
Cdd:COG1247  47 ILAPGRPVLVAEEDGEVVGFASLGPFRP---RPAYRGTAEESiyVDPDARGRGIGRALLEALIERARARGYRRLVAVVLA 123
                        90
                ....*....|....*...
gi 47115157 180 IQLSAMALYQSMGFKKTG 197
Cdd:COG1247 124 DNEASIALYEKLGFEEVG 141
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
109-176 5.05e-14

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: 64.60  E-value: 5.05e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47115157 109 FWVAESEEKVVGMVGALPVDDptlREKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
99-208 6.29e-13

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: 63.44  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    99 KSYLSERGSCFWVAESEEKVVGMVGalpvddptLREKRlQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGY--SEVILD 176
Cdd:pfam13673  23 RERIDQGEYFFFVAFEGGQIVGVIA--------LRDRG-HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIklSELTVN 93
                          90       100       110
                  ....*....|....*....|....*....|..
gi 47115157   177 TgtiQLSAMALYQSMGFKKTGQSFFRVWARLV 208
Cdd:pfam13673  94 A---SPYAVPFYEKLGFRATGPEQEFNGIRFV 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
117-206 2.83e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 60.31  E-value: 2.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 117 KVVGMVGALPVDDptlreKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKT 196
Cdd:COG3393   1 ELVAMAGVRAESP-----GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75
                        90
                ....*....|
gi 47115157 197 GQSFFRVWAR 206
Cdd:COG3393  76 GEYATVLFRK 85
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
111-200 5.87e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 60.97  E-value: 5.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 111 VAESEEKVVGMVGALPVDDPTLRekrlqLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiQLSAMALYQS 190
Cdd:COG2153  38 LAYDDGELVATARLLPPGDGEAK-----IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEK 109
                        90
                ....*....|
gi 47115157 191 MGFKKTGQSF 200
Cdd:COG2153 110 LGFVPVGEEF 119
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
81-197 7.56e-11

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 57.72  E-value: 7.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    81 PWTEyvdmtlctdmsDITKSYLSERGSCFWVAESEEKVVGMVGAlpvdDPTLREKrlQLFHLSVDSEHRRQGIAKALVRT 160
Cdd:TIGR01575  16 PWTE-----------AQFAEELANYHLCYLLARIGGKVVGYAGV----QIVLDEA--HILNIAVKPEYQGQGIGRALLRE 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47115157   161 VLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTG 197
Cdd:TIGR01575  79 LIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
PRK07757 PRK07757
N-acetyltransferase;
108-205 5.16e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 53.27  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157  108 CFWVAESEEKVVGmVGALPVDDPTLREKRlqlfHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVIldTGTIQlsaMAL 187
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAEIR----SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF--ALTYQ---PEF 111
                         90       100
                 ....*....|....*....|
gi 47115157  188 YQSMGFKKTGQSFF--RVWA 205
Cdd:PRK07757 112 FEKLGFREVDKEALpqKVWA 131
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
103-197 8.31e-09

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: 53.08  E-value: 8.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 103 SERGSCFWVAE--SEEKVVGMVGALPVDDPTLR-EkrlqlFHLSVDSEHRRQGIAKALVRTVLQFARDQ-GYSEVILDTG 178
Cdd:COG1670  56 ADGGALPFAIEdkEDGELIGVVGLYDIDRANRSaE-----IGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVD 130
                        90
                ....*....|....*....
gi 47115157 179 TIQLSAMALYQSMGFKKTG 197
Cdd:COG1670 131 PDNTASIRVLEKLGFRLEG 149
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
109-193 3.00e-08

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 50.65  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157   109 FWVAESEEKVVGMVGALPVDdPTLREKRLQLFHL---SVDSEHRRQGIAKALVRTVLQFARDQGYSEVILdtgtiQLSAM 185
Cdd:pfam13527  41 VLGAFDDGELVSTLALYPFE-LNVPGKTLPAAGItgvATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFL-----YPSSY 114

                  ....*...
gi 47115157   186 ALYQSMGF 193
Cdd:pfam13527 115 PIYRRFGY 122
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
131-170 1.47e-07

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 47.84  E-value: 1.47e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47115157 131 TLREKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGY 170
Cdd:COG2388  27 RLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGL 66
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
132-170 3.42e-07

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: 46.36  E-value: 3.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 47115157   132 LREKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGY 170
Cdd:pfam14542  19 RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGL 57
Eis COG4552
Predicted acetyltransferase [General function prediction only];
109-207 3.59e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 43.73  E-value: 3.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157 109 FWVAESEEKVVGMVGALPvDDPTLREKRLQLFHLS---VDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiqlSAM 185
Cdd:COG4552  43 VLGVFDDGELVGTLALYP-FTLNVGGARVPMAGITgvaVAPEHRRRGVARALLREALAELRERGQPLSALYP-----FEP 116
                        90       100
                ....*....|....*....|..
gi 47115157 186 ALYQSMGFkktGQSFFRVWARL 207
Cdd:COG4552 117 GFYRRFGY---ELAGDRRRYTI 135
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
105-175 5.17e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 42.21  E-value: 5.17e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47115157 105 RGSCFWVAESEEKVVGMVGALPVDDPTLREkrlQLFHL--SVDSEHRRQGIAKALVRTVLQFARDQGYSEVIL 175
Cdd:COG3981  61 PATTYWLVDEDGRIVGAINLRHELNEFLLR---VGGHIgyGVRPSERGKGYATEMLRLALEEARELGLDRVLI 130
PRK07922 PRK07922
amino-acid N-acetyltransferase;
109-173 3.86e-04

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 39.90  E-value: 3.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47115157  109 FWVAESEE-KVVGmVGALPVDDPTLREKRLqlfhLSVDSEHRRQGIAKALVRTVLQFARDQGYSEV 173
Cdd:PRK07922  47 FWVAEHLDgEVVG-CGALHVMWEDLAEIRT----VAVDPAARGRGVGHAIVERLLDVARELGLSRV 107
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
94-194 6.61e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.48  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157    94 MSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLRekrlqlFHL--SVDSEHRRQGIAKALVRTVLQFA-RDQGY 170
Cdd:pfam13302  42 LARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPER------AELgyWLGPDYWGKGYATEAVRALLEYAfEELGL 115
                          90       100
                  ....*....|....*....|....
gi 47115157   171 SEVILDTGTIQLSAMALYQSMGFK 194
Cdd:pfam13302 116 PRLVARIDPENTASRRVLEKLGFK 139
PRK03624 PRK03624
putative acetyltransferase; Provisional
109-193 9.75e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 9.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115157  109 FWVAESEEKVVG--MVGalpVDDptlreKRLQLFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMA 186
Cdd:PRK03624  47 FLVAEVGGEVVGtvMGG---YDG-----HRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118

                 ....*..
gi 47115157  187 LYQSMGF 193
Cdd:PRK03624 119 FYEALGY 125
PRK10514 PRK10514
putative acetyltransferase; Provisional
142-199 1.08e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.06  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 47115157  142 LSVDSEHRRQGIAKALVRTVLQFArdqgySEVILDTGTIQLSAMALYQSMGFKKTGQS 199
Cdd:PRK10514  75 LFVDPDVRGCGVGRMLVEHALSLH-----PELTTDVNEQNEQAVGFYKKMGFKVTGRS 127
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
139-193 1.85e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47115157  139 LFHLSVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGF 193
Cdd:PRK09491  66 LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
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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