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Conserved domains on  [gi|1103360228|ref|NP_001334168|]
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N-alpha-acetyltransferase 50 isoform 2 [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 ...
 57-155 2.08e-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: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  57 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 136
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1103360228 137 NYYkriePADAHVLQKNLK 155
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 57-155 2.08e-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: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  57 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 136
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1103360228 137 NYYkriePADAHVLQKNLK 155
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-129 2.47e-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: 73.32  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  16 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 91
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1103360228  92 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 129
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 83-140 7.65e-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: 7.65e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 140
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PRK10140 PRK10140
N-acetyltransferase;
48-152 1.17e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  48 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 125
Cdd:PRK10140   55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                          90       100
                  ....*....|....*....|....*...
gi 1103360228 126 KFGFEIIETKKNYYKRI-EPADAHVLQK 152
Cdd:PRK10140  133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-112 4.26e-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: 4.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1103360228  48 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 112
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 ...
 57-155 2.08e-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: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  57 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 136
Cdd:COG0456     1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*....
gi 1103360228 137 NYYkriePADAHVLQKNLK 155
Cdd:COG0456    78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-129 2.47e-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: 73.32  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  16 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 91
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1103360228  92 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 129
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-134 2.93e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.88  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  12 TPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKL--AYFNDIAVGAVCC-RVDHSQNQKRLYIMTLGCLAPYRRLGI 88
Cdd:COG3153     5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSlvAEDDGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQGI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1103360228  89 GTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEIIET 134
Cdd:COG3153    85 GRALMRAALEAARERG-ARAVVLL---GDPSLLPFYERFGFRPAGE 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
83-154 1.97e-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: 1.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET-KKNYYKRIEPADAHVLQKNL 154
Cdd:COG1247    92 ARGRGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTlPEVGFKFGRWLDLVLMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 52-155 2.82e-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: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  52 NDIAVGavCCRVdHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEI 131
Cdd:COG1246    36 DGEIVG--CAAL-HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG-LKRLFLL---TTSAAIHFYEKLGFEE 108

                          90       100
                  ....*....|....*....|....
gi 1103360228 132 IETKKNYYKRIEPADAHVLQKNLK 155
Cdd:COG1246   109 IDKEDLPYAKVWQRDSVVMEKDLE 132
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 83-140 7.65e-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: 7.65e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 140
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 40-157 1.05e-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: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  40 LEVGELAKLAYFNDIAVGAVC-CRVDHsqnqKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNE 118
Cdd:COG0454    30 SLAGAEFIAVDDKGEPIGFAGlRRLDD----KVLELKRLYVLPEYRGKGIGKALLEALLEWARERG-CTALELDTLDGNP 104

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1103360228 119 SAIDFYRKFGFEIIEtkknyykRIEPADAHVLQKNLKVP 157
Cdd:COG0454   105 AAIRFYERLGFKEIE-------RYVAYVGGEFEKELSLS 136
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
80-132 1.38e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.96  E-value: 1.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1103360228  80 LAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQisnESAIDFYRKFGFEII 132
Cdd:COG2153    67 LPEYRGQGLGRALMEAAIEEARERG-ARRIVLSAQ---AHAVGFYEKLGFVPV 115
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-131 9.95e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 9.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  48 LAYFNDIAVGavCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHvLNICEKDGTFDNIYLHVqisNESAIDFYRKF 127
Cdd:pfam13508   7 VAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAFYEKL 80


                  ....
gi 1103360228 128 GFEI 131
Cdd:pfam13508  81 GFEE 84
PRK10140 PRK10140
N-acetyltransferase;
48-152 1.17e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  48 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 125
Cdd:PRK10140   55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                          90       100
                  ....*....|....*....|....*...
gi 1103360228 126 KFGFEIIETKKNYYKRI-EPADAHVLQK 152
Cdd:PRK10140  133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-134 3.59e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.67  E-value: 3.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET 134
Cdd:COG3393    27 YRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYERLGFRPVGE 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-112 4.26e-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: 4.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1103360228  48 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 112
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGS-GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 83-139 5.76e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.46  E-value: 5.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGTFdNIYLHVQISNESAIDFYRKFGFEIIETKKNYY 139
Cdd:PRK09491   75 YQRQGLGRALLEHLIDELEKRGVA-TLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 52-141 9.64e-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: 43.45  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1103360228  52 NDIAVGAVCCRVDHSQNQKrlyiMTLG-CLAP-YRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGF 129
Cdd:COG1670    70 DGELIGVVGLYDIDRANRS----AEIGyWLAPaYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGF 145

                          90
                  ....*....|..
gi 1103360228 130 EIIETKKNYYKR 141
Cdd:COG1670   146 RLEGTLRDALVI 157
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 83-130 3.98e-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: 3.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNEsAIDFYRKFGFE 130
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPY-AVPFYEKLGFR 108
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 83-131 1.77e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 39.09  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDG-TFdnIYLHVqisneSAIDFYRKFGFEI 131
Cdd:pfam13527  82 YRGRGVMSRLLRRSLEEMRERGvPL--SFLYP-----SSYPIYRRFGYEI 124
PRK10562 PRK10562
putative acetyltransferase; Provisional
 82-133 2.97e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 2.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1103360228  82 PYRRLGIGTKMLNHVlnicekDGTFDNIYLHVQISNESAIDFYRKFGFEIIE 133
Cdd:PRK10562   79 KAVRRGIGKALMQHV------QQRYPHLSLEVYQKNQRAVNFYHAQGFRIVD 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
83-147 5.12e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.42  E-value: 5.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1103360228  83 YRRLGIGTKMLNHVLNICEKDGtfdnI---YLHVqisneSAIDFYRKFGFEIIETKKNYykRIEPADA 147
Cdd:COG4552    84 HRRRGVARALLREALAELRERG----QplsALYP-----FEPGFYRRFGYELAGDRRRY--TIPPESL 140
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
87-140 9.75e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 34.65  E-value: 9.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1103360228  87 GIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 140
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.
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