NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119620133|gb|EAW99727|]
View 

N-acetyltransferase 8 (camello like) [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-220 7.90e-22

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: 86.97  E-value: 7.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133  97 ITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119620133 177 TGTiqlSAMALYQSMGFKKTGQSfFCVWARLVALHTVHFIYHLP 220
Cdd:COG1246   93 TTS---AAIHFYEKLGFEEIDKE-DLPYAKVWQRDSVVMEKDLE 132
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-220 7.90e-22

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: 86.97  E-value: 7.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133  97 ITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119620133 177 TGTiqlSAMALYQSMGFKKTGQSfFCVWARLVALHTVHFIYHLP 220
Cdd:COG1246   93 TTS---AAIHFYEKLGFEEIDKE-DLPYAKVWQRDSVVMEKDLE 132
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 92-193 8.04e-22

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: 86.42  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   92 TDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPtlrEKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYS 171
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 119620133  172 EVILDTGTIQLSAMALYQSMGF 193
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 109-176 1.15e-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: 66.15  E-value: 1.15e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119620133 109 FWVAESEEKVVGMVGALPVDDptlREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 81-197 2.07e-10

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: 56.57  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   81 PWTEyvdmtlctdmsDITKSYLSERGSCFWVAESEEKVVGMVGAlpvdDPTLREKrlQLFHLFVDSEHRRQGIAKALVRT 160
Cdd:TIGR01575  16 PWTE-----------AQFAEELANYHLCYLLARIGGKVVGYAGV----QIVLDEA--HILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119620133  161 VLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTG 197
Cdd:TIGR01575  79 LIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
PRK07757 PRK07757
N-acetyltransferase;
108-205 7.62e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 50.19  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 108 CFWVAESEEKVVGmVGALPVDDPTLREKRlqlfHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVIldTGTIQlsaMAL 187
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAEIR----SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF--ALTYQ---PEF 111

                         90       100
                 ....*....|....*....|
gi 119620133 188 YQSMGFKKTGQSFFC--VWA 205
Cdd:PRK07757 112 FEKLGFREVDKEALPqkVWA 131
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-220 7.90e-22

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: 86.97  E-value: 7.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133  97 ITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119620133 177 TGTiqlSAMALYQSMGFKKTGQSfFCVWARLVALHTVHFIYHLP 220
Cdd:COG1246   93 TTS---AAIHFYEKLGFEEIDKE-DLPYAKVWQRDSVVMEKDLE 132
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 92-193 8.04e-22

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: 86.42  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   92 TDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPtlrEKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYS 171
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 119620133  172 EVILDTGTIQLSAMALYQSMGF 193
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
103-210 2.36e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 83.60  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 103 SERGSCFWVAESEEKVVGMVGALPVDDPTlREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTiql 182
Cdd:COG3153   35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP--- 110

                         90       100
                 ....*....|....*....|....*...
gi 119620133 183 SAMALYQSMGFKKTGQSFFCVWARLVAL 210
Cdd:COG3153  111 SLLPFYERFGFRPAGELGLTLGPDEVFL 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 105-195 1.19e-19

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 79.81  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133  105 RGSCFWVAESEEKVVGMVGALPVDDPTLREKRlqlfHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiQLSA 184
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAEL----RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRA 73

                          90
                  ....*....|.
gi 119620133  185 MALYQSMGFKK 195
Cdd:pfam13508  74 AAFYEKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 103-209 5.05e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 77.02  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 103 SERGSCFWVAESEEKVVGMVGALPVDDPTLrekrlQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQL 182
Cdd:COG0454   30 SLAGAEFIAVDDKGEPIGFAGLRRLDDKVL-----ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNP 104

                         90       100
                 ....*....|....*....|....*..
gi 119620133 183 SAMALYQSMGFKKTGQSFFCVWARLVA 209
Cdd:COG0454  105 AAIRFYERLGFKEIERYVAYVGGEFEK 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 120-198 7.46e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.77  E-value: 7.46e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119620133 120 GMVGALPVDDPtlreKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTGQ 198
Cdd:COG0456    1 GFALLGLVDGG----DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
102-197 5.13e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 72.72  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 102 LSERGSCFWVAESEEKVVGMVGALPVDDPTLReKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQ 181
Cdd:COG1247   47 ILAPGRPVLVAEEDGEVVGFASLGPFRPRPAY-RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADN 125

                         90
                 ....*....|....*.
gi 119620133 182 LSAMALYQSMGFKKTG 197
Cdd:COG1247  126 EASIALYEKLGFEEVG 141
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 109-176 1.15e-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: 66.15  E-value: 1.15e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119620133 109 FWVAESEEKVVGMVGALPVDDptlREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILD 176
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 99-200 1.80e-14

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: 67.68  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   99 KSYLSERGSCFWVAESEEKVVGMVGalpvddptLREKRlQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGY--SEVILD 176
Cdd:pfam13673  23 RERIDQGEYFFFVAFEGGQIVGVIA--------LRDRG-HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIklSELTVN 93

                          90       100
                  ....*....|....*....|....
gi 119620133  177 TgtiQLSAMALYQSMGFKKTGQSF 200
Cdd:pfam13673  94 A---SPYAVPFYEKLGFRATGPEQ 114
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
117-206 2.82e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 63.00  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 117 KVVGMVGALPVDDptlreKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKT 196
Cdd:COG3393    1 ELVAMAGVRAESP-----GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75

                         90
                 ....*....|
gi 119620133 197 GQSFFCVWAR 206
Cdd:COG3393   76 GEYATVLFRK 85
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
111-200 2.06e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.12  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 111 VAESEEKVVGMVGALPVDDPTLRekrlqLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiQLSAMALYQS 190
Cdd:COG2153   38 LAYDDGELVATARLLPPGDGEAK-----IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEK 109

                         90
                 ....*....|
gi 119620133 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 2.07e-10

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: 56.57  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   81 PWTEyvdmtlctdmsDITKSYLSERGSCFWVAESEEKVVGMVGAlpvdDPTLREKrlQLFHLFVDSEHRRQGIAKALVRT 160
Cdd:TIGR01575  16 PWTE-----------AQFAEELANYHLCYLLARIGGKVVGYAGV----QIVLDEA--HILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119620133  161 VLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTG 197
Cdd:TIGR01575  79 LIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 103-197 6.29e-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: 53.46  E-value: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 103 SERGSCFWVAE--SEEKVVGMVGALPVDDPTLR-EkrlqlFHLFVDSEHRRQGIAKALVRTVLQFARDQ-GYSEVILDTG 178
Cdd:COG1670   56 ADGGALPFAIEdkEDGELIGVVGLYDIDRANRSaE-----IGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVD 130

                         90
                 ....*....|....*....
gi 119620133 179 TIQLSAMALYQSMGFKKTG 197
Cdd:COG1670  131 PDNTASIRVLEKLGFRLEG 149
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
131-170 1.04e-08

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 50.92  E-value: 1.04e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 119620133 131 TLREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGY 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 2.32e-08

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: 49.83  E-value: 2.32e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119620133  132 LREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGY 170
Cdd:pfam14542  19 RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGL 57
PRK07757 PRK07757
N-acetyltransferase;
108-205 7.62e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 50.19  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 108 CFWVAESEEKVVGmVGALPVDDPTLREKRlqlfHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVIldTGTIQlsaMAL 187
Cdd:PRK07757  42 DFYVAEEEGEIVG-CCALHILWEDLAEIR----SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF--ALTYQ---PEF 111

                         90       100
                 ....*....|....*....|
gi 119620133 188 YQSMGFKKTGQSFFC--VWA 205
Cdd:PRK07757 112 FEKLGFREVDKEALPqkVWA 131
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 109-193 3.73e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 47.57  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133  109 FWVAESEEKVVGMVGALPVDdPTLREKRLQLFHLF---VDSEHRRQGIAKALVRTVLQFARDQGYSEVILdtgtiQLSAM 185
Cdd:pfam13527  41 VLGAFDDGELVSTLALYPFE-LNVPGKTLPAAGITgvaTYPEYRGRGVMSRLLRRSLEEMRERGVPLSFL-----YPSSY 114


                  ....*...
gi 119620133  186 ALYQSMGF 193
Cdd:pfam13527 115 PIYRRFGY 122
PRK10514 PRK10514
putative acetyltransferase; Provisional
 142-199 2.23e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 43.07  E-value: 2.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119620133 142 LFVDSEHRRQGIAKALVRTVLQFArdqgySEVILDTGTIQLSAMALYQSMGFKKTGQS 199
Cdd:PRK10514  75 LFVDPDVRGCGVGRMLVEHALSLH-----PELTTDVNEQNEQAVGFYKKMGFKVTGRS 127
Eis COG4552
Predicted acetyltransferase [General function prediction only];
144-193 3.74e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 40.65  E-value: 3.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119620133 144 VDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTgtiqlSAMALYQSMGF 193
Cdd:COG4552   80 VAPEHRRRGVARALLREALAELRERGQPLSALYP-----FEPGFYRRFGY 124
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
105-175 5.03e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 39.51  E-value: 5.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119620133 105 RGSCFWVAESEEKVVGMVGALPVDDPTLREkrlQLFHL--FVDSEHRRQGIAKALVRTVLQFARDQGYSEVIL 175
Cdd:COG3981   61 PATTYWLVDEDGRIVGAINLRHELNEFLLR---VGGHIgyGVRPSERGKGYATEMLRLALEEARELGLDRVLI 130
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 94-194 8.50e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.48  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133   94 MSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLRekrlqlFHL--FVDSEHRRQGIAKALVRTVLQFA-RDQGY 170
Cdd:pfam13302  42 LARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPER------AELgyWLGPDYWGKGYATEAVRALLEYAfEELGL 115

                          90       100
                  ....*....|....*....|....
gi 119620133  171 SEVILDTGTIQLSAMALYQSMGFK 194
Cdd:pfam13302 116 PRLVARIDPENTASRRVLEKLGFK 139
PRK07922 PRK07922
amino-acid N-acetyltransferase;
109-173 1.07e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 38.36  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119620133 109 FWVAESEE-KVVGmVGALPVDDPTLREKRLqlfhLFVDSEHRRQGIAKALVRTVLQFARDQGYSEV 173
Cdd:PRK07922  47 FWVAEHLDgEVVG-CGALHVMWEDLAEIRT----VAVDPAARGRGVGHAIVERLLDVARELGLSRV 107
PRK03624 PRK03624
putative acetyltransferase; Provisional
 109-193 4.63e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.06  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 109 FWVAESEEKVVG--MVGalpVDDptlreKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMA 186
Cdd:PRK03624  47 FLVAEVGGEVVGtvMGG---YDG-----HRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118


                 ....*..
gi 119620133 187 LYQSMGF 193
Cdd:PRK03624 119 FYEALGY 125
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 139-193 5.47e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.06  E-value: 5.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119620133 139 LFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGF 193
Cdd:PRK09491  66 LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
PRK09831 PRK09831
GNAT family N-acetyltransferase;
119-198 5.69e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 36.09  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119620133 119 VGMVGALPVDDPTLREKRLQLfhLFVDSEHRRQGIAKALVRTVLqfardQGYSEVILDTgtiQLSAMALYQSMGFKKTGQ 198
Cdd:PRK09831  57 VAVINAQPVGFITCIEHYIDM--LFVDPEYTRRGVASALLKPLI-----KSESELTVDA---SITAKPFFERYGFQTVKQ 126
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH