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Conserved domains on  [gi|6677849|ref|NP_033147|]
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diamine acetyltransferase 1 isoform 1 [Mus musculus]

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];
4-145 1.63e-21

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.43  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    4 FKIRPATASDCSDILRLIKE-----LAKYEYMEDQViltekDLQEDGFGEH--PFYHCLVAEvpkehwtpEGHSIVGFAm 76
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAE--------EDGEVVGFA- 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849   77 YYFTYDPWIG-KLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGA 145
Cdd:COG1247  68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-145 1.63e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.43  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    4 FKIRPATASDCSDILRLIKE-----LAKYEYMEDQViltekDLQEDGFGEH--PFYHCLVAEvpkehwtpEGHSIVGFAm 76
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAE--------EDGEVVGFA- 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849   77 YYFTYDPWIG-KLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGA 145
Cdd:COG1247  68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 48-144 2.18e-14

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: 65.62  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849     48 EHPFYHCLVAEvpkehwtpEGHSIVGFAMYYFTYDPWigKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHF 127
Cdd:pfam00583  29 EDASEGFFVAE--------EDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98

                          90
                  ....*....|....*..
gi 6677849    128 LVAEWNEPSINFYKRRG 144
Cdd:pfam00583  99 EVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-126 5.41e-07

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: 44.96  E-value: 5.41e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677849   54 CLVAEvpkehwtpEGHSIVGFAMYYFtyDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMH 126
Cdd:cd04301   1 FLVAE--------DDGEIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-144 4.85e-04

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: 38.08  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849     57 AEVPKEHWTPEghSIV-GFAMYYFTY------DPWIGKLLYLEDFF--------VMSDYRGFGIGSEILKNLSQVAMKCR 121
Cdd:TIGR01575  10 AAAFAFPWTEA--QFAeELANYHLCYllarigGKVVGYAGVQIVLDeahilniaVKPEYQGQGIGRALLRELIDEAKGRG 87

                          90       100
                  ....*....|....*....|...
gi 6677849    122 CSSMHFLVAEWNEPSINFYKRRG 144
Cdd:TIGR01575  88 VNEIFLEVRVSNIAAQALYKKLG 110
PTZ00330 PTZ00330
acetyltransferase; Provisional
 90-144 2.50e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 36.36  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6677849    90 YLEDFFVMSDYRGFGIGSEILKNLSQVAmkcRCSSMHFLVAEWNEPSINFYKRRG 144
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIA---RSSGCYKVILDCTEDMVAFYKKLG 135
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-145 1.63e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.43  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    4 FKIRPATASDCSDILRLIKE-----LAKYEYMEDQViltekDLQEDGFGEH--PFYHCLVAEvpkehwtpEGHSIVGFAm 76
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAIlaPGRPVLVAE--------EDGEVVGFA- 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849   77 YYFTYDPWIG-KLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGA 145
Cdd:COG1247  68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 48-144 2.18e-14

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: 65.62  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849     48 EHPFYHCLVAEvpkehwtpEGHSIVGFAMYYFTYDPWigKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHF 127
Cdd:pfam00583  29 EDASEGFFVAE--------EDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98

                          90
                  ....*....|....*..
gi 6677849    128 LVAEWNEPSINFYKRRG 144
Cdd:pfam00583  99 EVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 73-144 3.32e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.98  E-value: 3.32e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6677849   73 GFAMYYFTYDPWIGkllYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRG 144
Cdd:COG0456   1 GFALLGLVDGGDEA---EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-144 1.75e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    6 IRPATASDCSDILRLIKELAKYEYMEDQVilteKDLQEDGfgehPFYHCLVAEvpkehwtpEGHSIVGFAMYYFTYDPWI 85
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELV----DRLREDP----AAGLSLVAE--------DDGEIVGHVALSPVDIDGE 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6677849   86 GKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSsmhFLVAEWNEPSINFYKRRG 144
Cdd:COG3153  65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGAR---AVVLLGDPSLLPFYERFG 120
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-144 3.02e-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: 57.69  E-value: 3.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    4 FKIRPATASDCSDILRLIKELAKYEymedqviltekdlqedgfgehPFYHCLVAEvpkehwtpEGHSIVGFAMYYftydP 83
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEE---------------------EIGEFWVAE--------EDGEIVGCAALH----P 47

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677849   84 WIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVaewNEPSINFYKRRG 144
Cdd:COG1246  48 LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 4-162 4.82e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 54.67  E-value: 4.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    4 FKIRPATASDcsdilrlIKELAKYEYMEDQVILTEKDLQEdgfgehpfYHCLVAEVPKEhwtpeghsIVGFAMYyFTYDP 83
Cdd:COG0454   1 MSIRKATPED-------INFILLIEALDAELKAMEGSLAG--------AEFIAVDDKGE--------PIGFAGL-RRLDD 56

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6677849   84 WIGkllYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKE 162
Cdd:COG0454  57 KVL---ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-144 4.30e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.22  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849     50 PFYHCLVAEvpkehwtpEGHSIVGFAMYYFTYDPWIGKLLYLedfFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLV 129
Cdd:pfam13508   1 PGGRFFVAE--------DDGKIVGFAALLPLDDEGALAELRL---AVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET 69

                          90
                  ....*....|....*
gi 6677849    130 aewNEPSINFYKRRG 144
Cdd:pfam13508  70 ---TNRAAAFYEKLG 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-126 5.41e-07

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: 44.96  E-value: 5.41e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677849   54 CLVAEvpkehwtpEGHSIVGFAMYYFtyDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMH 126
Cdd:cd04301   1 FLVAE--------DDGEIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
2-112 1.97e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 42.61  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849    2 AKFKIRPATASDcsdiLRLIKELAKYeYMEDQVILTEKDLQEDGFGEHPFYHclvAEVPKEHWTP----EGHSIVGFAMy 77
Cdd:COG5628   1 MKVSIERVTAED----KPILENLYQL-YLHDLSEFTGILPDADGLFEYEYLD---TYWTDDDRHPyliyVDGEPAGFAL- 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6677849   78 yftydpwIGKLLYLE------DFFVMSDYRGFGIG----SEILKN 112
Cdd:COG5628  72 -------VRRLPFLEsdyeiaEFFVLRKYRRKGIGkraaHELFKR 109
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-144 4.85e-04

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: 38.08  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677849     57 AEVPKEHWTPEghSIV-GFAMYYFTY------DPWIGKLLYLEDFF--------VMSDYRGFGIGSEILKNLSQVAMKCR 121
Cdd:TIGR01575  10 AAAFAFPWTEA--QFAeELANYHLCYllarigGKVVGYAGVQIVLDeahilniaVKPEYQGQGIGRALLRELIDEAKGRG 87

                          90       100
                  ....*....|....*....|...
gi 6677849    122 CSSMHFLVAEWNEPSINFYKRRG 144
Cdd:TIGR01575  88 VNEIFLEVRVSNIAAQALYKKLG 110
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-144 8.24e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 36.81  E-value: 8.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6677849   71 IVGFAMYYftydPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRG 144
Cdd:COG3393   2 LVAMAGVR----AESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
PTZ00330 PTZ00330
acetyltransferase; Provisional
 90-144 2.50e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 36.36  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6677849    90 YLEDFFVMSDYRGFGIGSEILKNLSQVAmkcRCSSMHFLVAEWNEPSINFYKRRG 144
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIA---RSSGCYKVILDCTEDMVAFYKKLG 135
 
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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