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Conserved domains on  [gi|507085830|ref|WP_016156571|]
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MULTISPECIES: L-methionine sulfoximine/L-methionine sulfone acetyltransferase [Citrobacter]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-162 1.63e-67

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 202.53  E-value: 1.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAAIWNDQTVDAENRISWYQARQLMGYPVLVSEENGVITGYASFGDWRNFDGFRHT 80
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  81 VEHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQVGTKFGRWLDLTFMQL 160
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 507085830 161 QL 162
Cdd:COG1247  162 RL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-162 1.63e-67

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 202.53  E-value: 1.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAAIWNDQTVDAENRISWYQARQLMGYPVLVSEENGVITGYASFGDWRNFDGFRHT 80
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  81 VEHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQVGTKFGRWLDLTFMQL 160
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 507085830 161 QL 162
Cdd:COG1247  162 RL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-136 1.25e-19

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: 79.10  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   14 IAEIYNHAVLHTAAIWNDQTVDAenrisWYQARQLMGYPVLVSEENGVITGYASFgdWRNFDGFRHTVEHSVYVHPAHQG 93
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDL-----LEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507085830   94 KGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGF 136
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-117 1.74e-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: 54.20  E-value: 1.74e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085830  53 VLVSEENGVITGYASFGDWRNFDgfrHTVE-HSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMV 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG---DTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-154 3.43e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 52.62  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAaiWNDQTVDAEnriswyqaRQLMGYP--VLVSEENGVITGYASFGdwrnFDGFR 78
Cdd:PRK03624   3 MEIRVFRQADFEAVIALWERCDLTRP--WNDPEMDIE--------RKLNHDPslFLVAEVGGEVVGTVMGG----YDGHR 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507085830  79 HTVeHSVYVHPAHQGKGLGRALLSRLIEE--ARACGK-HVMVagiESQNQASLHLHSTLGFKTtaqmpQVGTKFGRWLD 154
Cdd:PRK03624  69 GWA-YYLAVHPDFRGRGIGRALVARLEKKliARGCPKiNLQV---REDNDAVLGFYEALGYEE-----QDRISLGKRLI 138
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-137 1.51e-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: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   54 LVSEENGVITGYASFgdwrNFDGFRHTVeHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHST 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGV----QIVLDEAHI-LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKK 108


                  ....
gi 507085830  134 LGFK 137
Cdd:TIGR01575 109 LGFN 112
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-162 1.63e-67

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 202.53  E-value: 1.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAAIWNDQTVDAENRISWYQARQLMGYPVLVSEENGVITGYASFGDWRNFDGFRHT 80
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  81 VEHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQVGTKFGRWLDLTFMQL 160
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 507085830 161 QL 162
Cdd:COG1247  162 RL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-136 1.25e-19

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: 79.10  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   14 IAEIYNHAVLHTAAIWNDQTVDAenrisWYQARQLMGYPVLVSEENGVITGYASFgdWRNFDGFRHTVEHSVYVHPAHQG 93
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDL-----LEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507085830   94 KGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGF 136
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-164 7.94e-17

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: 73.49  E-value: 7.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAAIWNDQTV-DAENRISWYQARQLMGYP---VLVSEENGVITGYASFgdwRNFDG 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLeEARAWLERLLADWADGGAlpfAIEDKEDGELIGVVGL---YDIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  77 FRHTVEHSVYVHPAHQGKGLGRALLSRLIEEA-RACGKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQVGTKFGRWLDL 155
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ....*....
gi 507085830 156 TFMQLQLDD 164
Cdd:COG1670  165 VLYSLLREE 173
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-149 8.84e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 64.69  E-value: 8.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDcaaiaeiynhavlhTAAIWNDQTVDAE--NRISwyqarQLMGYPVLVSEENGVITGYASFgdwRNFDGFR 78
Cdd:COG0454    1 MSIRKATPED--------------INFILLIEALDAElkAMEG-----SLAGAEFIAVDDKGEPIGFAGL---RRLDDKV 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507085830  79 HTVEHsVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQ-VGTKF 149
Cdd:COG0454   59 LELKR-LYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAyVGGEF 129
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-163 1.61e-13

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: 63.86  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLhtaaiwndqtvdAENRISWYqarqlmgypvlVSEENGVITGYASfgdWRNFDGfrHT 80
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYAL------------EEEIGEFW-----------VAEEDGEIVGCAA---LHPLDE--DL 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  81 VE-HSVYVHPAHQGKGLGRALLSRLIEEARACG-KHVMVagiESqNQASLHLHSTLGFKTTAQMPQVGTKFGRWlDLTFM 158
Cdd:COG1246   53 AElRSLAVHPDYRGRGIGRRLLEALLAEARELGlKRLFL---LT-TSAAIHFYEKLGFEEIDKEDLPYAKVWQR-DSVVM 127


                 ....*
gi 507085830 159 QLQLD 163
Cdd:COG1246  128 EKDLE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-143 1.68e-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: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  64 GYASFGdwrnFDGFRHTVE-HSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQM 142
Cdd:COG0456    1 GFALLG----LVDGGDEAEiEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76


                 .
gi 507085830 143 P 143
Cdd:COG0456   77 P 77
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-157 6.09e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.41  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   3 IRFASKEDCAAIAEiynhavLHTAAIWNDQTVDAENRISWYQARQLmgypVLVSEENGVITGYASFGDWRNFDGFRHTVE 82
Cdd:COG3153    1 IRPATPEDAEAIAA------LLRAAFGPGREAELVDRLREDPAAGL----SLVAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085830  83 HSVYVHPAHQGKGLGRALLSRLIEEARACG-KHVMVAGiesqNQASLHLHSTLGFKTTAQMPQVGTKFGRWLDLTF 157
Cdd:COG3153   71 GPLAVDPEYRGQGIGRALMRAALEAARERGaRAVVLLG----DPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 53-137 5.30e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   53 VLVSEENGVITGYASFgdwRNFDGFRHTVEHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAgiESQNQAsLHLHS 132
Cdd:pfam13508   5 FFVAEDDGKIVGFAAL---LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL--ETTNRA-AAFYE 78


                  ....*
gi 507085830  133 TLGFK 137
Cdd:pfam13508  79 KLGFE 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-117 1.74e-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: 54.20  E-value: 1.74e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085830  53 VLVSEENGVITGYASFGDWRNFDgfrHTVE-HSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMV 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG---DTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
85-142 2.48e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.14  E-value: 2.48e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 507085830  85 VYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKTTAQM 142
Cdd:COG3393   21 VYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEY 78
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-154 3.43e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 52.62  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTAaiWNDQTVDAEnriswyqaRQLMGYP--VLVSEENGVITGYASFGdwrnFDGFR 78
Cdd:PRK03624   3 MEIRVFRQADFEAVIALWERCDLTRP--WNDPEMDIE--------RKLNHDPslFLVAEVGGEVVGTVMGG----YDGHR 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507085830  79 HTVeHSVYVHPAHQGKGLGRALLSRLIEE--ARACGK-HVMVagiESQNQASLHLHSTLGFKTtaqmpQVGTKFGRWLD 154
Cdd:PRK03624  69 GWA-YYLAVHPDFRGRGIGRALVARLEKKliARGCPKiNLQV---REDNDAVLGFYEALGYEE-----QDRISLGKRLI 138
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 50-139 6.12e-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: 51.50  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   50 GYPVLVSEENGVITGYASFGDwrnfdgfrHTVEHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQAsLH 129
Cdd:pfam13673  30 EYFFFVAFEGGQIVGVIALRD--------RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPYA-VP 100

                          90
                  ....*....|
gi 507085830  130 LHSTLGFKTT 139
Cdd:pfam13673 101 FYEKLGFRAT 110
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-137 1.51e-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: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   54 LVSEENGVITGYASFgdwrNFDGFRHTVeHSVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHST 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGV----QIVLDEAHI-LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKK 108


                  ....
gi 507085830  134 LGFK 137
Cdd:TIGR01575 109 LGFN 112
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 87-136 1.95e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 48.00  E-value: 1.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 507085830  87 VHPAHQGKGLGRALLSRLIEEARAcgKHVMVAGIE--SQNQASLHLHSTLGF 136
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEK--RGVATLWLEvrASNAAAIALYESLGF 120
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-137 2.83e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 47.34  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830    3 IRFASKEDCAAIAEIYNHAVLHTAAIWNDQTVD-AENRIS--WYQARQLMGYPVLVSEENGVITGYASFgdwRNFDGFRH 79
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEeAREWLAriWAADEAERGYGWAIELKDTGFIGSIGL---YDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 507085830   80 TVEHSVYVHPAHQGKGLGRALLSRLIEEA-RACGKHVMVAGIESQNQASLHLHSTLGFK 137
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
3-156 3.42e-07

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 47.36  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830    3 IRFASKEDCAAIAEIYNHAVLHTAAIWNDqtvdAENRISWYQAR-----QLMGYPVLVsEENGVITGYASFG--DWRnfd 75
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEY----AHSSIEEFETFlaaylSPGEIVFGV-AESDRLIGYATLRqfDYV--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   76 gFRHTVEHSVYVHpAHQGKGLGRALLSRLIEEARAC-GKHVMVAGIESQNQASLHLHSTLGFKTTAQMPQVGTKFGRWLD 154
Cdd:pfam13420  73 -KTHKAELSFYVV-KNNDEGINRELINAIIQYARKNqNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150


                  ..
gi 507085830  155 LT 156
Cdd:pfam13420 151 MM 152
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
44-139 8.42e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.95  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  44 QARQLMGYpvlvseENGVITGYASF-----GDWRnfdgFRHtvehsVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVa 118
Cdd:COG2153   33 DARHLLAY------DDGELVATARLlppgdGEAK----IGR-----VAVLPEYRGQGLGRALMEAAIEEARERGARRIV- 96

                         90       100
                 ....*....|....*....|.
gi 507085830 119 gIESQNQAsLHLHSTLGFKTT 139
Cdd:COG2153   97 -LSAQAHA-VGFYEKLGFVPV 115
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
57-115 6.82e-06

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 42.45  E-value: 6.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507085830  57 EENGVITGYASF---GDWRNFDgfrHTvehsvYVHPAHQGKGLGRALLSRLIEEARACGKHV 115
Cdd:COG2388   15 EVDGELAGELTYrleGGVIIIT---HT-----EVPPALRGQGIASALVEAALDDARERGLKV 68
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 84-136 1.13e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 41.93  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 507085830   84 SVYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESqNQASLHLHSTLGF 136
Cdd:pfam08445  26 ALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAG-NTPSRRLYEKLGF 77
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 87-112 1.62e-05

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 44.05  E-value: 1.62e-05
                         10        20
                 ....*....|....*....|....*.
gi 507085830  87 VHPAHQGKGLGRALLSRLIEEARACG 112
Cdd:COG1444  493 VHPALQRRGLGSRLLAEIREEAKEEG 518
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 77-136 8.20e-05

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 41.49  E-value: 8.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   77 FRHTVEHSVYVHPAHQGKGLGRALLSRLIEEARACGKhvmVAGIESQNQASLHLHSTLGF 136
Cdd:pfam12746 174 YEGGIEIEIDTHPDYRGKGLATICAAALILECLKRGL---YPSWDAHNEASVALAEKLGY 230
PRK07922 PRK07922
amino-acid N-acetyltransferase;
84-112 9.42e-05

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 40.67  E-value: 9.42e-05
                         10        20
                 ....*....|....*....|....*....
gi 507085830  84 SVYVHPAHQGKGLGRALLSRLIEEARACG 112
Cdd:PRK07922  75 TVAVDPAARGRGVGHAIVERLLDVARELG 103
PTZ00330 PTZ00330
acetyltransferase; Provisional
 53-137 1.15e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 40.21  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830  53 VLVSEENGVITGYASFGDWRNFDGFRHTVEH--SVYVHPAHQGKGLGRALLSRLIEEARACGKHVMvagIESQNQASLHL 130
Cdd:PTZ00330  54 VFVHSPTQRIVGTASLFVEPKFTRGGKCVGHieDVVVDPSYRGQGLGRALISDLCEIARSSGCYKV---ILDCTEDMVAF 130


                 ....*..
gi 507085830 131 HSTLGFK 137
Cdd:PTZ00330 131 YKKLGFR 137
PRK07757 PRK07757
N-acetyltransferase;
84-112 1.16e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.18  E-value: 1.16e-04
                         10        20
                 ....*....|....*....|....*....
gi 507085830  84 SVYVHPAHQGKGLGRALLSRLIEEARACG 112
Cdd:PRK07757  70 SLAVSEDYRGQGIGRMLVEACLEEARELG 98
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 57-115 2.48e-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: 37.88  E-value: 2.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507085830   57 EENGVITGYASF---GDWRNFDgfrHTvehsvYVHPAHQGKGLGRALLSRLIEEARACGKHV 115
Cdd:pfam14542   6 VDGGAEVAFLTYrrgDGVLIIT---HT-----EVPPALRGQGIASKLVKAALDDAREEGLKI 59
ectoine_EctA TIGR02406
diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. ...
 85-145 1.05e-03

diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analagous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 131459  Cd Length: 157  Bit Score: 37.78  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507085830   85 VYVHPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLhstlgFKTTAQMPQV 145
Cdd:TIGR02406  72 VAVDPRARGKGLARRLLEALLERVACERVRHLETTITPDNQASRAL-----FKALARRRGV 127
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 76-138 1.12e-03

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 38.15  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507085830   76 GFRHTVEHS-------VYV---HPAHQGKGLGRALLSRLIEEARACGKHVMVAGIESQNQASLHLHSTLGFKT 138
Cdd:TIGR03448 213 GFHWTKVHPdepalgeVYVvgvDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGFTV 285
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-115 1.85e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.96  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085830   1 MSIRFASKEDCAAIAEIYNHAVLHTaaiwndqtVDAEnRISWYQARQLMGYPVLVSEENGVITGYASFGDWRNFDGFRHT 80
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPE--------PDDE-ELEAYRPLLEPGRVLGVFDDGELVGTLALYPFTLNVGGARVP 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 507085830  81 VEH--SVYVHPAHQGKGLGRALLSRLIEEARACGKHV 115
Cdd:COG4552   72 MAGitGVAVAPEHRRRGVARALLREALAELRERGQPL 108
 
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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