NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|817478488|ref|NP_001295374|]
View 

N-alpha-acetyltransferase 50 isoform 2 [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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

 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 ...
 56-154 2.86e-20

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.08  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  56 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 135
Cdd:COG0456    1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*....
gi 817478488 136 NYYkriePADAHVLQKNLK 154
Cdd:COG0456   78 NYY----GDDALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 56-154 2.86e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.08  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  56 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 135
Cdd:COG0456    1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*....
gi 817478488 136 NYYkriePADAHVLQKNLK 154
Cdd:COG0456   78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-128 3.28e-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: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488   15 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 90
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 817478488   91 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 128
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 82-139 8.22e-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: 8.22e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 817478488   82 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 139
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PRK10140 PRK10140
N-acetyltransferase;
47-151 1.16e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  47 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 124
Cdd:PRK10140  55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                         90       100
                 ....*....|....*....|....*...
gi 817478488 125 KFGFEIIETKKNYYKRI-EPADAHVLQK 151
Cdd:PRK10140 133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-111 5.97e-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: 44.57  E-value: 5.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817478488  47 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 111
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 ...
 56-154 2.86e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 80.08  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  56 GAVCCRVDHsqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIETKK 135
Cdd:COG0456    1 GFALLGLVD--GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*....
gi 817478488 136 NYYkriePADAHVLQKNLK 154
Cdd:COG0456   78 NYY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-128 3.28e-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: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488   15 IKQLKRLNQVIFPVSYNDK----FYKDVLEVGELAKLAYFNDIAVGAVCCRVDHsQNQKRLYIMTLGCLAPYRRLGIGTK 90
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 817478488   91 MLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGF 128
Cdd:pfam00583  80 LLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
11-133 2.85e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.88  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  11 TPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKL--AYFNDIAVGAVCC-RVDHSQNQKRLYIMTLGCLAPYRRLGI 87
Cdd:COG3153    5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSlvAEDDGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQGI 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 817478488  88 GTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEIIET 133
Cdd:COG3153   85 GRALMRAALEAARERG-ARAVVLL---GDPSLLPFYERFGFRPAGE 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
82-153 1.92e-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: 1.92e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817478488  82 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET-KKNYYKRIEPADAHVLQKNL 153
Cdd:COG1247   92 ARGRGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTlPEVGFKFGRWLDLVLMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 51-154 3.09e-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: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  51 NDIAVGavCCRVdHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHvqiSNESAIDFYRKFGFEI 130
Cdd:COG1246   36 DGEIVG--CAAL-HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG-LKRLFLL---TTSAAIHFYEKLGFEE 108

                         90       100
                 ....*....|....*....|....
gi 817478488 131 IETKKNYYKRIEPADAHVLQKNLK 154
Cdd:COG1246  109 IDKEDLPYAKVWQRDSVVMEKDLE 132
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 82-139 8.22e-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: 8.22e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 817478488   82 YRRLGIGTKMLNHVLNICEKDGTfDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 139
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGV-NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-156 1.15e-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: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  39 LEVGELAKLAYFNDIAVGAVC-CRVDHsqnqKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNE 117
Cdd:COG0454   30 SLAGAEFIAVDDKGEPIGFAGlRRLDD----KVLELKRLYVLPEYRGKGIGKALLEALLEWARERG-CTALELDTLDGNP 104

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 817478488 118 SAIDFYRKFGFEIIEtkknyykRIEPADAHVLQKNLKVP 156
Cdd:COG0454  105 AAIRFYERLGFKEIE-------RYVAYVGGEFEKELSLS 136
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
79-131 1.79e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.58  E-value: 1.79e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 817478488  79 LAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQisnESAIDFYRKFGFEII 131
Cdd:COG2153   67 LPEYRGQGLGRALMEAAIEEARERG-ARRIVLSAQ---AHAVGFYEKLGFVPV 115
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-130 1.35e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488   47 LAYFNDIAVGavCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHvLNICEKDGTFDNIYLHVqisNESAIDFYRKF 126
Cdd:pfam13508   7 VAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAFYEKL 80


                  ....
gi 817478488  127 GFEI 130
Cdd:pfam13508  81 GFEE 84
PRK10140 PRK10140
N-acetyltransferase;
47-151 1.16e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  47 LAYFNDIAVGAVCcrVDHSQNQKRLYIMTLG-CL-APYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYR 124
Cdd:PRK10140  55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132

                         90       100
                 ....*....|....*....|....*...
gi 817478488 125 KFGFEIIETKKNYYKRI-EPADAHVLQK 151
Cdd:PRK10140 133 KYGFEIEGTGKKYALRNgEYVDAYYMAR 160
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
82-133 3.53e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.67  E-value: 3.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 817478488  82 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNESAIDFYRKFGFEIIET 133
Cdd:COG3393   27 YRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYERLGFRPVGE 77
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 82-138 5.33e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.46  E-value: 5.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 817478488  82 YRRLGIGTKMLNHVLNICEKDGTFdNIYLHVQISNESAIDFYRKFGFEIIETKKNYY 138
Cdd:PRK09491  75 YQRQGLGRALLEHLIDELEKRGVA-TLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-111 5.97e-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: 44.57  E-value: 5.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817478488  47 LAYFNDIAVGAVCCRVDHSqNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGtFDNIYLH 111
Cdd:cd04301    3 VAEDDGEIVGFASLSPDGS-GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 51-140 9.48e-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: 9.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817478488  51 NDIAVGAVCCRVDHSQNQKrlyiMTLG-CLAP-YRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGF 128
Cdd:COG1670   70 DGELIGVVGLYDIDRANRS----AEIGyWLAPaYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGF 145

                         90
                 ....*....|..
gi 817478488 129 EIIETKKNYYKR 140
Cdd:COG1670  146 RLEGTLRDALVI 157
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 82-129 3.96e-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: 3.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 817478488   82 YRRLGIGTKMLNHVLNICEKDGtFDNIYLHVQISNEsAIDFYRKFGFE 129
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPY-AVPFYEKLGFR 108
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 82-130 1.84e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 39.09  E-value: 1.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 817478488   82 YRRLGIGTKMLNHVLNICEKDG-TFdnIYLHVqisneSAIDFYRKFGFEI 130
Cdd:pfam13527  82 YRGRGVMSRLLRRSLEEMRERGvPL--SFLYP-----SSYPIYRRFGYEI 124
PRK10562 PRK10562
putative acetyltransferase; Provisional
 81-132 2.93e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 2.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 817478488  81 PYRRLGIGTKMLNHVlnicekDGTFDNIYLHVQISNESAIDFYRKFGFEIIE 132
Cdd:PRK10562  79 KAVRRGIGKALMQHV------QQRYPHLSLEVYQKNQRAVNFYHAQGFRIVD 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
82-146 5.03e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.42  E-value: 5.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817478488  82 YRRLGIGTKMLNHVLNICEKDGtfdnI---YLHVqisneSAIDFYRKFGFEIIETKKNYykRIEPADA 146
Cdd:COG4552   84 HRRRGVARALLREALAELRERG----QplsALYP-----FEPGFYRRFGYELAGDRRRY--TIPPESL 140
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
86-139 9.54e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 34.65  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 817478488   86 GIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYK 139
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