NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907119721|ref|XP_036016025|]
View 

N-alpha-acetyltransferase 50 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-161 2.84e-20

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.47  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  63 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 142
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1907119721 143 NYYkriePADAHVLQKNLK 161
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-161 2.84e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.47  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  63 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 142
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1907119721 143 NYYkriePADAHVLQKNLK 161
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 22-135 3.71e-17

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: 72.94  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  22 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 97
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907119721  98 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 135
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 89-146 8.08e-11

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 56.57  E-value: 8.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 146
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PRK10140 PRK10140
N-acetyltransferase;
54-158 1.33e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  54 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 131
Cdd:PRK10140   55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                          90       100
                  ....*....|....*....|....*...
gi 1907119721 132 KFGFEIIETKKNYYKRI-EPADAHVLQK 158
Cdd:PRK10140  133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-118 5.58e-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: 5.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907119721  54 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 118
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGS-GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-161 2.84e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.47  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  63 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 142
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1907119721 143 NYYkriePADAHVLQKNLK 161
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 22-135 3.71e-17

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: 72.94  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  22 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 97
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907119721  98 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 135
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
18-140 3.39e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.88  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  18 TPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKL--AYFNDIAVGAVCC-RVDHSQNQKRLYIMTLGCLAPYRRLGI 94
Cdd:COG3153     5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSlvAEDDGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQGI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907119721  95 GTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEIIET 140
Cdd:COG3153    85 GRALMRAALEAARERG-ARAVVLL---GDPSLLPFYERFGFRPAGE 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
89-160 2.28e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 64.25  E-value: 2.28e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET-KKNYYKRIEPADAHVLQKNL 160
Cdd:COG1247    92 ARGRGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTlPEVGFKFGRWLDLVLMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 58-161 3.25e-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: 63.09  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  58 NDIAVGavCCRVdHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEI 137
Cdd:COG1246    36 DGEIVG--CAAL-HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG-LKRLFLL---TTSAAIHFYEKLGFEE 108

                          90       100
                  ....*....|....*....|....
gi 1907119721 138 IETKKNYYKRIEPADAHVLQKNLK 161
Cdd:COG1246   109 IDKEDLPYAKVWQRDSVVMEKDLE 132
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 89-146 8.08e-11

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 56.57  E-value: 8.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 146
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 46-163 1.20e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  46 LEVGELAKLAYFNDIAVGAVC-CRVDHsqnqKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNE 124
Cdd:COG0454    30 SLAGAEFIAVDDKGEPIGFAGlRRLDD----KVLELKRLYVLPEYRGKGIGKALLEALLEWARERG-CTALELDTLDGNP 104

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907119721 125 SAIDFYRKFGFEIIEtkknyykRIEPADAHVLQKNLKVP 163
Cdd:COG0454   105 AAIRFYERLGFKEIE-------RYVAYVGGEFEKELSLS 136
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
86-138 2.35e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.58  E-value: 2.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907119721  86 LAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQisnESAIDFYRKFGFEII 138
Cdd:COG2153    67 LPEYRGQGLGRALMEAAIEEARERG-ARRIVLSAQ---AHAVGFYEKLGFVPV 115
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-137 1.07e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  54 LAYFNDIAVGavCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHvLNICEKDGTFDNIYLHVqisNESAIDFYRKF 133
Cdd:pfam13508   7 VAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAFYEKL 80


                  ....
gi 1907119721 134 GFEI 137
Cdd:pfam13508  81 GFEE 84
PRK10140 PRK10140
N-acetyltransferase;
54-158 1.33e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  54 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 131
Cdd:PRK10140   55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                          90       100
                  ....*....|....*....|....*...
gi 1907119721 132 KFGFEIIETKKNYYKRI-EPADAHVLQK 158
Cdd:PRK10140  133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
89-140 3.96e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.67  E-value: 3.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET 140
Cdd:COG3393    27 YRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYERLGFRPVGE 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-118 5.58e-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: 5.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907119721  54 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 118
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGS-GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 89-145 6.01e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.46  E-value: 6.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGTFdNIYLHVQISNESAIDFYRKFGFEIIETKKNYY 145
Cdd:PRK09491   75 YQRQGLGRALLEHLIDELEKRGVA-TLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 58-147 1.06e-05

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: 43.45  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907119721  58 NDIAVGAVCCRVDHSQNQKrlyiMTLG-CLAP-YRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGF 135
Cdd:COG1670    70 DGELIGVVGLYDIDRANRS----AEIGyWLAPaYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGF 145

                          90
                  ....*....|..
gi 1907119721 136 EIIETKKNYYKR 147
Cdd:COG1670   146 RLEGTLRDALVI 157
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 89-136 4.56e-05

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: 41.10  E-value: 4.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNEsAIDFYRKFGFE 136
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPY-AVPFYEKLGFR 108
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 89-137 2.02e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 39.09  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDG-TFdnIYLHVqisneSAIDFYRKFGFEI 137
Cdd:pfam13527  82 YRGRGVMSRLLRRSLEEMRERGvPL--SFLYP-----SSYPIYRRFGYEI 124
PRK10562 PRK10562
putative acetyltransferase; Provisional
 88-139 3.22e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 3.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907119721  88 PYRRLGIGTKMLNHVlnicekDGTFDNIYLHVQISNESAIDFYRKFGFEIIE 139
Cdd:PRK10562   79 KAVRRGIGKALMQHV------QQRYPHLSLEVYQKNQRAVNFYHAQGFRIVD 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
89-153 5.62e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.42  E-value: 5.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907119721  89 YRRLGIGTKMLNHVLNICEKDGtfdnI---YLHVqisneSAIDFYRKFGFEIIETKKNYykRIEPADA 153
Cdd:COG4552    84 HRRRGVARALLREALAELRERG----QplsALYP-----FEPGFYRRFGYELAGDRRRY--TIPPESL 140
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
93-146 8.06e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 35.04  E-value: 8.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907119721  93 GIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 146
Cdd:pfam13420  90 GINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIK 143
 
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