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Conserved domains on  [gi|254692917|ref|NP_075982|]
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probable N-acetyltransferase CML5 [Mus musculus]

Protein Classification

N-acetyltransferase( domain architecture ID 11418877)

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

EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  9175471

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 138-196 2.50e-14

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 2.50e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 138-196 2.50e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 2.50e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 138-192 2.43e-10

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: 55.99  E-value: 2.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGF 192
Cdd:pfam00583  62 IEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 138-196 1.38e-07

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 48.86  E-value: 1.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:TIGR01575  57 ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 126-175 1.05e-06

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: 44.57  E-value: 1.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 254692917 126 VKDPPLGRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLE 175
Cdd:cd04301   16 LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10514 PRK10514
putative acetyltransferase; Provisional
 128-197 8.35e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 41.53  E-value: 8.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254692917 128 DPPLGRKQMQLFHLS---VSSQHRGQGIAKALVRTVFQFARDqgysdvvLETSVIQQ--SAITLYEAMGFQRTGK 197
Cdd:PRK10514  59 DQPVGFMLLSGGHMEalfVDPDVRGCGVGRMLVEHALSLHPE-------LTTDVNEQneQAVGFYKKMGFKVTGR 126
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 138-196 2.50e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 2.50e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 130-198 7.21e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 63.53  E-value: 7.21e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 130 PLGRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTGKY 198
Cdd:COG0454   53 RLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERY 121
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
146-205 9.79e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 59.15  E-value: 9.79e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692917 146 QHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTGKYSEISIIK 205
Cdd:COG3393   26 EYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFRK 85
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 130-197 1.74e-11

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: 59.62  E-value: 1.74e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254692917 130 PLGRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSviqQSAITLYEAMGFQRTGK 197
Cdd:COG1246   47 PLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT---SAAIHFYEKLGFEEIDK 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
132-198 5.79e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.56  E-value: 5.79e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254692917 132 GRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSViqqSAITLYEAMGFQRTGKY 198
Cdd:COG3153   64 EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP---SLLPFYERFGFRPAGEL 127
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
143-201 6.19e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.85  E-value: 6.19e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 143 VSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTGKYSEI 201
Cdd:COG1247   88 VDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 138-192 2.43e-10

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: 55.99  E-value: 2.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGF 192
Cdd:pfam00583  62 IEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
130-196 3.75e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.96  E-value: 3.75e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254692917 130 PLGRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETsviQQSAITLYEAMGFQRTG 196
Cdd:COG2153   53 PPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEKLGFVPVG 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 140-194 8.81e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 8.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 254692917  140 HLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETsviQQSAITLYEAMGFQR 194
Cdd:pfam13508  33 RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 138-196 1.38e-07

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 48.86  E-value: 1.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:TIGR01575  57 ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 126-175 1.05e-06

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: 44.57  E-value: 1.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 254692917 126 VKDPPLGRKQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLE 175
Cdd:cd04301   16 LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 138-196 2.01e-06

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: 45.72  E-value: 2.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSdvVLETSVIQQ-SAITLYEAMGFQRTG 196
Cdd:pfam13673  54 ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIK--LSELTVNASpYAVPFYEKLGFRATG 111
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
134-169 2.88e-06

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 43.99  E-value: 2.88e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 254692917 134 KQMQLFHLSVSSQHRGQGIAKALVRTVFQFARDQGY 169
Cdd:COG2388   31 GVIIITHTEVPPALRGQGIASALVEAALDDARERGL 66
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 138-169 2.99e-06

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: 44.05  E-value: 2.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 254692917  138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGY 169
Cdd:pfam14542  26 ITHTEVPPALRGQGIASKLVKAALDDAREEGL 57
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 139-196 3.01e-06

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: 45.76  E-value: 3.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254692917 139 FHLSVSSQHRGQGIAKALVRTVFQFARDQ-GYSDVVLETSVIQQSAITLYEAMGFQRTG 196
Cdd:COG1670   91 IGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149
PRK10514 PRK10514
putative acetyltransferase; Provisional
 128-197 8.35e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 41.53  E-value: 8.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254692917 128 DPPLGRKQMQLFHLS---VSSQHRGQGIAKALVRTVFQFARDqgysdvvLETSVIQQ--SAITLYEAMGFQRTGK 197
Cdd:PRK10514  59 DQPVGFMLLSGGHMEalfVDPDVRGCGVGRMLVEHALSLHPE-------LTTDVNEQneQAVGFYKKMGFKVTGR 126
Eis COG4552
Predicted acetyltransferase [General function prediction only];
142-203 8.05e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 39.88  E-value: 8.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254692917 142 SVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETsviqqSAITLYEAMGFQRTGKYSEISI 203
Cdd:COG4552   79 AVAPEHRRRGVARALLREALAELRERGQPLSALYP-----FEPGFYRRFGYELAGDRRRYTI 135
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 138-205 1.98e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.22  E-value: 1.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254692917 138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFqrtgkySEISIIK 205
Cdd:PRK09491  66 LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF------NEVTIRR 127
PRK03624 PRK03624
putative acetyltransferase; Provisional
 138-208 2.03e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.22  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254692917 138 LFHLSVSSQHRGQGIAKALVRTVFQFARDQGYSDVVLETSVIQQSAITLYEAMGFQRTgkySEISIIKWLI 208
Cdd:PRK03624  71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ---DRISLGKRLI 138
 
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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