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Conserved domains on  [gi|510836548|ref|WP_016208167|]
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GNAT family N-acetyltransferase [Clostridium sartagoforme]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-168 2.24e-33

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: 116.25  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   1 MEFLIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRnEDFIMNM-----DGNQHQFVAVVKnknGEEEIIGTAGLTi 75
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEA-RAWLERLladwaDGGALPFAIEDK---EDGELIGVVGLY- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  76 nSNPRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNG 155
Cdd:COG1670   81 -DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159

                        170
                 ....*....|...
gi 510836548 156 KYENEYLMARINP 168
Cdd:COG1670  160 RYRDHVLYSLLRE 172
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-168 2.24e-33

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: 116.25  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   1 MEFLIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRnEDFIMNM-----DGNQHQFVAVVKnknGEEEIIGTAGLTi 75
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEA-RAWLERLladwaDGGALPFAIEDK---EDGELIGVVGLY- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  76 nSNPRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNG 155
Cdd:COG1670   81 -DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159

                        170
                 ....*....|...
gi 510836548 156 KYENEYLMARINP 168
Cdd:COG1670  160 RYRDHVLYSLLRE 172
PRK10140 PRK10140
N-acetyltransferase;
2-166 4.05e-29

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 105.06  E-value: 4.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   2 EFLIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRNEDFIMNMDGNQhQFVAVVknkngEEEIIGTAGLTINSNPRL 81
Cdd:PRK10140   3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIK-QLVACI-----DGDVVGHLTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  82 RHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNGKYENEY 161
Cdd:PRK10140  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAY 156


                 ....*
gi 510836548 162 LMARI 166
Cdd:PRK10140 157 YMARV 161
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 64-141 6.53e-18

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: 74.86  E-value: 6.53e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510836548   64 EEEIIGTAGLTINsNPRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLmLIRVELGVFEDNKRAIHLYEKLGF 141
Cdd:pfam00583  41 DGELVGFASLSII-DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 87-163 1.90e-10

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: 55.80  E-value: 1.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510836548   87 IGIMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRlAAIRNGKyENEYLM 163
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRR-NYYPDPG-EDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-115 1.03e-05

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: 41.49  E-value: 1.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 510836548  64 EEEIIGTAGLTINsnPRLRHSGGIG-IMIHKDYQNMGVGTALMEALLDVADNW 115
Cdd:cd04301    7 DGEIVGFASLSPD--GSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-168 2.24e-33

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: 116.25  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   1 MEFLIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRnEDFIMNM-----DGNQHQFVAVVKnknGEEEIIGTAGLTi 75
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEA-RAWLERLladwaDGGALPFAIEDK---EDGELIGVVGLY- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  76 nSNPRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNG 155
Cdd:COG1670   81 -DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159

                        170
                 ....*....|...
gi 510836548 156 KYENEYLMARINP 168
Cdd:COG1670  160 RYRDHVLYSLLRE 172
PRK10140 PRK10140
N-acetyltransferase;
2-166 4.05e-29

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 105.06  E-value: 4.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   2 EFLIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRNEDFIMNMDGNQhQFVAVVknkngEEEIIGTAGLTINSNPRL 81
Cdd:PRK10140   3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIK-QLVACI-----DGDVVGHLTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  82 RHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNGKYENEY 161
Cdd:PRK10140  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAY 156


                 ....*
gi 510836548 162 LMARI 166
Cdd:PRK10140 157 YMARV 161
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-166 1.37e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.82  E-value: 1.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   2 EFLIRPIEIGDGKGVNALRR-----MPGVFENILGIPSERVKRNEDFImnmDGNQHQFVAVVknkngEEEIIGTAGLTIN 76
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNeaiaeGTATFETEPPSEEEREAWFAAIL---APGRPVLVAEE-----DGEVVGFASLGPF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  77 SN-PRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADN---WlmliRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAI 152
Cdd:COG1247   73 RPrPAYRGTAEESIYVDPDARGRGIGRALLEALIERARArgyR----RLVAVVLADNEASIALYEKLGFEEVGTLPEVGF 148

                        170
                 ....*....|....
gi 510836548 153 RNGKYENEYLMARI 166
Cdd:COG1247  149 KFGRWLDLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 64-141 6.53e-18

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: 74.86  E-value: 6.53e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510836548   64 EEEIIGTAGLTINsNPRLRHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLmLIRVELGVFEDNKRAIHLYEKLGF 141
Cdd:pfam00583  41 DGELVGFASLSII-DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 89-165 1.51e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 1.51e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510836548  89 IMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLkrlaaIRNGKYENEYLMAR 165
Cdd:COG0456   19 LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGE-----RPNYYGDDALVMEK 89
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 64-143 1.91e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.78  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   64 EEEIIGTAGLTINSNPRlrHSGGIGIMIHKDYQNMGVGTALMEAlldvADNWLMLIRVELGVFEDNKRAIHLYEKLGFKK 143
Cdd:pfam13508  11 DGKIVGFAALLPLDDEG--ALAELRLAVHPEYRGQGIGRALLEA----AEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-165 4.58e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.10  E-value: 4.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   5 IRPIEIGDGKGVNALRRmpgvfeniLGIPSERVKRNEDFIMNMDGNQHQFVAVVknkngEEEIIGTAGLTINSNPRLRHS 84
Cdd:COG3153    1 IRPATPEDAEAIAALLR--------AAFGPGREAELVDRLREDPAAGLSLVAED-----DGEIVGHVALSPVDIDGEGPA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  85 GGIG-IMIHKDYQNMGVGTALMEALLDVADNWlmliRVELGVFEDNKRAIHLYEKLGFkkeglKRLAAIRNGKYENEYLM 163
Cdd:COG3153   68 LLLGpLAVDPEYRGQGIGRALMRAALEAARER----GARAVVLLGDPSLLPFYERFGF-----RPAGELGLTLGPDEVFL 138


                 ..
gi 510836548 164 AR 165
Cdd:COG3153  139 AK 140
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 46-158 1.34e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 58.91  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  46 NMDGNQH--QFVAVVKNkngeEEIIGTAGLTINSNPRLRhsggIGIM-IHKDYQNMGVGTALMEALLDVADNwLMLIRVE 122
Cdd:COG0454   26 AMEGSLAgaEFIAVDDK----GEPIGFAGLRRLDDKVLE----LKRLyVLPEYRGKGIGKALLEALLEWARE-RGCTALE 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 510836548 123 LGVFEDNKRAIHLYEKLGFKKEGlkRLAAIRNGKYE 158
Cdd:COG0454   97 LDTLDGNPAAIRFYERLGFKEIE--RYVAYVGGEFE 130
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
66-142 2.14e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.84  E-value: 2.14e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510836548  66 EIIGTAGLtinsNPRLRHSGGI-GIMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVFEDNKRAIHLYEKLGFK 142
Cdd:COG3393    1 ELVAMAGV----RAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFR 73
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-142 1.41e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 56.20  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548    4 LIRPIEIGDGKGVNALRRMPGVFENILGIPSERVKRnEDFIMNM-----DGNQHQFVAVVKnkngEEEIIGTAGLTINSN 78
Cdd:pfam13302   3 LLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEA-REWLARIwaadeAERGYGWAIELK----DTGFIGSIGLYDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510836548   79 PRlrHSGGIGIMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFK 142
Cdd:pfam13302  78 EP--ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 87-163 1.90e-10

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: 55.80  E-value: 1.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510836548   87 IGIMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRlAAIRNGKyENEYLM 163
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRR-NYYPDPG-EDAIVM 131
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-142 7.62e-09

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: 51.53  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   5 IRPIEIGDGKGVNALRRMPGVFENIlgipservkrnEDFimnmdgnqhqFVAVVknkngEEEIIGTAGLTINSNPR--LR 82
Cdd:COG1246    3 IRPATPDDVPAILELIRPYALEEEI-----------GEF----------WVAEE-----DGEIVGCAALHPLDEDLaeLR 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  83 HsggigIMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVFEDnkrAIHLYEKLGFK 142
Cdd:COG1246   57 S-----LAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLTTSA---AIHFYEKLGFE 107
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 64-164 1.58e-08

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 50.82  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   64 EEEIIGTAGLT-INSNprlRHSGGIGImihkdYQN----MGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEK 138
Cdd:TIGR03585  59 ESRPIGVISFTdINLV---HKSAFWGI-----YANpfckPGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEK 130

                          90       100
                  ....*....|....*....|....*.
gi 510836548  139 LGFKKEGLKRlaaiRNGKYENEYLMA 164
Cdd:TIGR03585 131 FGFEREGVFR----QGGEYYDVLLMY 152
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-145 5.56e-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: 46.50  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548   45 MNMDGNQHQFVAVVKNKngeeeIIGTAgltinsnpRLRHSGGIGIM-IHKDYQNMGVGTALMEALLDVADNWLMLIRvEL 123
Cdd:pfam13673  25 RIDQGEYFFFVAFEGGQ-----IVGVI--------ALRDRGHISLLfVDPDYQGQGIGKALLEAVEDYAEKDGIKLS-EL 90

                          90       100
                  ....*....|....*....|..
gi 510836548  124 GVFEDNKrAIHLYEKLGFKKEG 145
Cdd:pfam13673  91 TVNASPY-AVPFYEKLGFRATG 111
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
64-145 7.11e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.95  E-value: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  64 EEEIIGTAgltinsnpRLRHSGG----IG-IMIHKDYQNMGVGTALMEALLDVADNwLMLIRVELGVfedNKRAIHLYEK 138
Cdd:COG2153   42 DGELVATA--------RLLPPGDgeakIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGFYEK 109


                 ....*..
gi 510836548 139 LGFKKEG 145
Cdd:COG2153  110 LGFVPVG 116
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 89-170 7.41e-07

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 47.10  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  89 IMIHKDYQNMGVGTALMEALLDVADNWLMLIRVELGVFEDNKRAIHLYEKLGFKKEGLKRLAAIRNGKYENEYLMARINP 168
Cdd:PRK15130  88 IIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRMCIFQH 167


                 ..
gi 510836548 169 SY 170
Cdd:PRK15130 168 QY 169
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 89-164 6.13e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.76  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  89 IMIHKDYQNMGVGTALMEALLD------VADNWLMlirvelgVFEDNKRAIHLYEKLGFKKeglkrlAAIRNGKY----- 157
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDelekrgVATLWLE-------VRASNAAAIALYESLGFNE------VTIRRNYYptadg 135


                 ....*...
gi 510836548 158 -ENEYLMA 164
Cdd:PRK09491 136 rEDAIIMA 143
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-115 1.03e-05

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: 41.49  E-value: 1.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 510836548  64 EEEIIGTAGLTINsnPRLRHSGGIG-IMIHKDYQNMGVGTALMEALLDVADNW 115
Cdd:cd04301    7 DGEIVGFASLSPD--GSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER 57
PRK07757 PRK07757
N-acetyltransferase;
64-142 1.99e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.71  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510836548  64 EEEIIGTAGLTINSnPRL---RhsggiGIMIHKDYQNMGVGTALMEALLDVAdnwlmlirVELGVfednKRAI------H 134
Cdd:PRK07757  49 EGEIVGCCALHILW-EDLaeiR-----SLAVSEDYRGQGIGRMLVEACLEEA--------RELGV----KRVFaltyqpE 110


                 ....*...
gi 510836548 135 LYEKLGFK 142
Cdd:PRK07757 111 FFEKLGFR 118
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 82-143 2.09e-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: 35.77  E-value: 2.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510836548   82 RHSGGIGIM-IHKDYQNMGVGTALMEALLDvadnwlmLIRVE-----LGVFEDNKRAIHLYEKLGFKK 143
Cdd:pfam08445  19 LPGGELGALqTLPEHRRRGLGSRLVAALAR-------GIAERgitpfAVVVAGNTPSRRLYEKLGFRK 79
PRK03624 PRK03624
putative acetyltransferase; Provisional
 91-151 2.60e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.45  E-value: 2.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510836548  91 IHKDYQNMGVGTALMEAlldvADNWLM---LIRVELGVFEDNKRAIHLYEKLGFKKEGL----KRLAA 151
Cdd:PRK03624  76 VHPDFRGRGIGRALVAR----LEKKLIargCPKINLQVREDNDAVLGFYEALGYEEQDRislgKRLIE 139
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 99-145 5.24e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 35.57  E-value: 5.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 510836548   99 GVGTALMEALLD--VADNWLMLIRVELGVfeDNKRAIHLYEKLGFKKEG 145
Cdd:pfam13523  95 GFTTALLRALVHylFADPRTRRVVVEPDV--RNERAIRLLERAGFRKVK 141
 
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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