NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515937857|ref|WP_017368440|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
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
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-143 2.12e-20

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: 80.64  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   33 WNQEEAQKNAEEQFDRLLPEGLQTEDHELWNILHGEEAIGWVwLCYDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALE 112
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA-SLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 515937857  113 EQAKSLGVKKLSLHVFAHNQIARSLYEKTGF 143
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-143 2.12e-20

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: 80.64  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   33 WNQEEAQKNAEEQFDRLLPEGLQTEDHELWNILHGEEAIGWVwLCYDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALE 112
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA-SLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 515937857  113 EQAKSLGVKKLSLHVFAHNQIARSLYEKTGF 143
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 75-154 5.71e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.23  E-value: 5.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  75 WLCYDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETG------- 147
Cdd:COG0456    2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGerpnyyg 81

                         90
                 ....*....|
gi 515937857 148 ---IYMSKPL 154
Cdd:COG0456   82 ddaLVMEKEL 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 25-148 1.03e-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: 58.49  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   25 EEKVHAGTWNqeeaqknaEEQFDrllpEGLQTEDHELWNILHGEEAIGWVWLCYDPDhpqhEGFIYNFILFEAYRGKGLA 104
Cdd:TIGR01575   9 EAAAFAFPWT--------EAQFA----EELANYHLCYLLARIGGKVVGYAGVQIVLD----EAHILNIAVKPEYQGQGIG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 515937857  105 KQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETGI 148
Cdd:TIGR01575  73 RALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-126 1.14e-10

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: 54.20  E-value: 1.14e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515937857  64 ILHGEEAIGWVWLCYDPDHPqHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLH 126
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 67-154 7.03e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  67 GEEAIGWVWLCYDpdhpQHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGF-AE 145
Cdd:PRK03624  53 GGEVVGTVMGGYD----GHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYeEQ 128


                 ....*....
gi 515937857 146 TGIYMSKPL 154
Cdd:PRK03624 129 DRISLGKRL 137
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-143 2.12e-20

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: 80.64  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   33 WNQEEAQKNAEEQFDRLLPEGLQTEDHELWNILHGEEAIGWVwLCYDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALE 112
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA-SLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 515937857  113 EQAKSLGVKKLSLHVFAHNQIARSLYEKTGF 143
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 75-154 5.71e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.23  E-value: 5.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  75 WLCYDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETG------- 147
Cdd:COG0456    2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGerpnyyg 81

                         90
                 ....*....|
gi 515937857 148 ---IYMSKPL 154
Cdd:COG0456   82 ddaLVMEKEL 91
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-148 7.09e-16

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: 70.41  E-value: 7.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   1 MVTLLPMSQTDYDVLIEkaikRYAEEKVHAGTWNQEEAQKNAEEQFDRLLpEGLQTEDHELWNILHGE--EAIGWVWLcY 78
Cdd:COG1670    7 RLRLRPLRPEDAEALAE----LLNDPEVARYLPGPPYSLEEARAWLERLL-ADWADGGALPFAIEDKEdgELIGVVGL-Y 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515937857  79 DPDHPQHEGFIYnFILFEAYRGKGLAKQAMTALEEQAKS-LGVKKLSLHVFAHNQIARSLYEKTGFAETGI 148
Cdd:COG1670   81 DIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGT 150
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
96-151 1.29e-15

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 67.63  E-value: 1.29e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515937857  96 EAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETGIYMS 151
Cdd:COG3393   25 PEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-149 3.62e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 68.48  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   1 MVTLLPMSQTDYDVLIEkAIKRYAEEkvHAGTWNQEEAqknAEEQFDRLLpEGLQTEDHELWNILHGEEAIGWVWLCYDP 80
Cdd:COG1247    1 EMTIRPATPEDAPAIAA-IYNEAIAE--GTATFETEPP---SEEEREAWF-AAILAPGRPVLVAEEDGEVVGFASLGPFR 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  81 DHPQHEGFIYNFILF-EAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETGIY 149
Cdd:COG1247   74 PRPAYRGTAEESIYVdPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTL 143
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 44-149 1.39e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 60.84  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  44 EQFDRLLPEGLQTEDHELWNIL-HGEEAIGWVWLC-YDPDHpqheGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVK 121
Cdd:COG0454   18 EALDAELKAMEGSLAGAEFIAVdDKGEPIGFAGLRrLDDKV----LELKRLYVLPEYRGKGIGKALLEALLEWARERGCT 93

                         90       100
                 ....*....|....*....|....*...
gi 515937857 122 KLSLHVFAHNQIARSLYEKTGFAETGIY 149
Cdd:COG0454   94 ALELDTLDGNPAAIRFYERLGFKEIERY 121
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 25-148 1.03e-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: 58.49  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   25 EEKVHAGTWNqeeaqknaEEQFDrllpEGLQTEDHELWNILHGEEAIGWVWLCYDPDhpqhEGFIYNFILFEAYRGKGLA 104
Cdd:TIGR01575   9 EAAAFAFPWT--------EAQFA----EELANYHLCYLLARIGGKVVGYAGVQIVLD----EAHILNIAVKPEYQGQGIG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 515937857  105 KQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETGI 148
Cdd:TIGR01575  73 RALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 49-147 6.81e-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: 56.54  E-value: 6.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  49 LLPEGLQTEDHELWNILHGEEAIGWVWLCYDPDHpqhEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVf 128
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDED---LAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT- 93

                         90
                 ....*....|....*....
gi 515937857 129 ahNQIARSLYEKTGFAETG 147
Cdd:COG1246   94 --TSAAIHFYEKLGFEEID 110
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-126 1.14e-10

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: 54.20  E-value: 1.14e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515937857  64 ILHGEEAIGWVWLCYDPDHPqHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLH 126
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-143 2.90e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.04  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857    2 VTLLPMSQTDYDVLIEKaikrYAEEKVHAGTWNQEEAQKNAEEQFDRLLPEGLQTEDHeLWNILH-GEEAIGWVWLcYDP 80
Cdd:pfam13302   2 LLLRPLTEEDAEALFEL----LSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERGY-GWAIELkDTGFIGSIGL-YDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515937857   81 DHPQHEGFIYnFILFEAYRGKGLAKQAMTALEEQA-KSLGVKKLSLHVFAHNQIARSLYEKTGF 143
Cdd:pfam13302  76 DGEPERAELG-YWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-145 4.52e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857   57 EDHELWNILHGEEAIGWVWLCYDPDHpqHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHnqiARS 136
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDE--GALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAA 75


                  ....*....
gi 515937857  137 LYEKTGFAE 145
Cdd:pfam13508  76 FYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
96-154 3.16e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.41  E-value: 3.16e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515937857  96 EAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHnqiARSLYEKTGFAETG----------IYMSKPL 154
Cdd:COG2153   68 PEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPVGeefleagiphIDMRKPL 133
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
66-154 2.15e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.39  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  66 HGEEAIGWVWLC-YDPDHPQHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNqiaRSLYEKTGFA 144
Cdd:COG3153   46 DDGEIVGHVALSpVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFR 122

                         90       100
                 ....*....|....*....|
gi 515937857 145 ETG----------IYMSKPL 154
Cdd:COG3153  123 PAGelgltlgpdeVFLAKEL 142
PRK03624 PRK03624
putative acetyltransferase; Provisional
 67-154 7.03e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515937857  67 GEEAIGWVWLCYDpdhpQHEGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGF-AE 145
Cdd:PRK03624  53 GGEVVGTVMGGYD----GHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYeEQ 128


                 ....*....
gi 515937857 146 TGIYMSKPL 154
Cdd:PRK03624 129 DRISLGKRL 137
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 86-147 8.02e-07

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: 45.34  E-value: 8.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515937857   86 EGFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQiARSLYEKTGFAETG 147
Cdd:pfam13673  51 RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATG 111
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 87-152 5.33e-06

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 43.54  E-value: 5.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515937857  87 GFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNqiaRSLYEKTGFAETGIYMSK 152
Cdd:PLN02706  86 GHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEEN---KAFYEKCGYVRKEIQMVK 148
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 97-148 9.57e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.99  E-value: 9.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515937857  97 AYRGKGLAKQAMTALEEQAKSLGVKKLSLHVFAHNQIARSLYEKTGFAETGI 148
Cdd:PRK09491  74 DYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTI 125
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 87-143 4.64e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.23  E-value: 4.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515937857   87 GFIYNFILFEAYRGKGLAKQAMTALEEQAKSLGvKKLSLHVFAHNQIARSLYEKTGF 143
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGF 77
PRK07757 PRK07757
N-acetyltransferase;
96-146 8.97e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 34.78  E-value: 8.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515937857  96 EAYRGKGLAKQAMTALEEQAKSLGVKKlslhVFAHNqIARSLYEKTGFAET 146
Cdd:PRK07757  75 EDYRGQGIGRMLVEACLEEARELGVKR----VFALT-YQPEFFEKLGFREV 120
 
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