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MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas]

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, ...
 10-177 7.71e-29

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: 105.08  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  10 PELQLVPFQLGHFPILQRWFATEkELVQWAGPalrHPLSLEQMHEDLAESRR--RPPLRLLWSACR--DDQVIGHCQLL- 84
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDP-EVARYLPG---PPYSLEEARAWLERLLAdwADGGALPFAIEDkeDGELIGVVGLYd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  85 FDRRNGVVRLArIVLAPSARGQGLGLPMLEALLAEAFADADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRE 164
Cdd:COG1670   82 IDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|...
gi 489206320 165 RWNVVLMGLLRQE 177
Cdd:COG1670  161 YRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-177 7.71e-29

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: 105.08  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  10 PELQLVPFQLGHFPILQRWFATEkELVQWAGPalrHPLSLEQMHEDLAESRR--RPPLRLLWSACR--DDQVIGHCQLL- 84
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDP-EVARYLPG---PPYSLEEARAWLERLLAdwADGGALPFAIEDkeDGELIGVVGLYd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  85 FDRRNGVVRLArIVLAPSARGQGLGLPMLEALLAEAFADADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRE 164
Cdd:COG1670   82 IDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|...
gi 489206320 165 RWNVVLMGLLRQE 177
Cdd:COG1670  161 YRDHVLYSLLREE 173
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-149 7.15e-14

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: 64.85  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   33 KELVQWAGPALRHPLSLEQMHEDLAESRRRPPLrlLWSACRDDQVIGHCQL-LFDRRNGVVRLARIVLAPSARGQGLGLP 111
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEG--FFVAEEDGELVGFASLsIIDDEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489206320  112 MLEALLAEAFaDADIERVELNVYDWNAAARHLYRRAGF 149
Cdd:pfam00583  80 LLQALLEWAR-ERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 42-171 5.36e-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: 57.34  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   42 ALRHPLSLEQMHEDLAEsrrrPPLRLLWsACRDDQVIGHCQLLFDRRNGvvRLARIVLAPSARGQGLGLPMLEALLAEAF 121
Cdd:TIGR01575  12 AFAFPWTEAQFAEELAN----YHLCYLL-ARIGGKVVGYAGVQIVLDEA--HILNIAVKPEYQGQGIGRALLRELIDEAK 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489206320  122 aDADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRErwNVVLM 171
Cdd:TIGR01575  85 -GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 72-173 4.16e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 47.23  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  72 CRDDQVIGH--CQLLFDRrngvVRLARIVLAPSARGQGLGLPMLEALLAEaFADADIERVELNVYDWNAAARHLYRRAGF 149
Cdd:PRK09491  46 TVNGQMAAFaiTQVVLDE----ATLFNIAVDPDYQRQGLGRALLEHLIDE-LEKRGVATLWLEVRASNAAAIALYESLGF 120

                         90       100
                 ....*....|....*....|....*.
gi 489206320 150 REEGLRRS--ATRVGRErwNVVLMGL 173
Cdd:PRK09491 121 NEVTIRRNyyPTADGRE--DAIIMAL 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 68-132 7.67e-06

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: 41.88  E-value: 7.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489206320  68 LWSACRDDQVIGHCQLLFDR-RNGVVRLARIVLAPSARGQGLGLPMLEALLAEAFAdADIERVELN 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-177 7.71e-29

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: 105.08  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  10 PELQLVPFQLGHFPILQRWFATEkELVQWAGPalrHPLSLEQMHEDLAESRR--RPPLRLLWSACR--DDQVIGHCQLL- 84
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDP-EVARYLPG---PPYSLEEARAWLERLLAdwADGGALPFAIEDkeDGELIGVVGLYd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  85 FDRRNGVVRLArIVLAPSARGQGLGLPMLEALLAEAFADADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRE 164
Cdd:COG1670   82 IDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|...
gi 489206320 165 RWNVVLMGLLRQE 177
Cdd:COG1670  161 YRDHVLYSLLREE 173
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-174 2.18e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.03  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  46 PLSLEQMHEDLAEsrRRPPLRLLWSACRDDQVIGHCQL----LFDRRNGVVRLArIVLAPSARGQGLGLPMLEALLAEAf 121
Cdd:COG1247   34 PPSEEEREAWFAA--ILAPGRPVLVAEEDGEVVGFASLgpfrPRPAYRGTAEES-IYVDPDARGRGIGRALLEALIERA- 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489206320 122 ADADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRERWNVVLMGLL 174
Cdd:COG1247  110 RARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 79-156 1.14e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 1.14e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489206320  79 GHCQLLFDRRNGVVRLARIVLAPSARGQGLGLPMLEALLAEAfADADIERVELNVYDWNAAARHLYRRAGFREEGLRR 156
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERA-RERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-149 7.15e-14

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: 64.85  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   33 KELVQWAGPALRHPLSLEQMHEDLAESRRRPPLrlLWSACRDDQVIGHCQL-LFDRRNGVVRLARIVLAPSARGQGLGLP 111
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEG--FFVAEEDGELVGFASLsIIDDEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489206320  112 MLEALLAEAFaDADIERVELNVYDWNAAARHLYRRAGF 149
Cdd:pfam00583  80 LLQALLEWAR-ERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-150 3.65e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 63.52  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   12 LQLVPFQLGHFPILQRWFAtEKELVQWAGPalrHPLSLEQMHEDLAESRRRPPLR--LLWSAC-RDDQVIGHCQL-LFDR 87
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLS-DPEVMRYGVP---WPLTLEEAREWLARIWAADEAErgYGWAIElKDTGFIGSIGLyDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489206320   88 RNGVVRLArIVLAPSARGQGLGLPMLEALLAEAFADADIERVELNVYDWNAAARHLYRRAGFR 150
Cdd:pfam13302  78 EPERAELG-YWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 64-151 1.54e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   64 PLRLLWSACRDDQVIGHCQLLFDRRNGVVRLARIVLAPSARGQGLGlpmlEALLAEAFADADIERVELNVYDWNAAARHL 143
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIG----RALLEAAEAAAKEGGIKLLELETTNRAAAF 76


                  ....*...
gi 489206320  144 YRRAGFRE 151
Cdd:pfam13508  77 YEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 49-171 1.67e-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: 58.85  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  49 LEQMHEDLAESRRRPPLRLLWSACRDDQVIGHCQLLFdRRNGVVRLARIVLAPSARGQGLGLPMLEALLAEAfADADIER 128
Cdd:COG1246   11 VPAILELIRPYALEEEIGEFWVAEEDGEIVGCAALHP-LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEA-RELGLKR 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489206320 129 VELNVYDwnaAARHLYRRAGFREEGLRRSATRVGRERWNVVLM 171
Cdd:COG1246   89 LFLLTTS---AAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVME 128
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-151 1.93e-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: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  50 EQMHEDLAESRRRPPLRLLWSACRDDQVIGHCQL-LFDrrNGVVRLARIVLAPSARGQGLGLPMLEALLAEAfADADIER 128
Cdd:COG0454   18 EALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGLrRLD--DKVLELKRLYVLPEYRGKGIGKALLEALLEWA-RERGCTA 94

                         90       100
                 ....*....|....*....|...
gi 489206320 129 VELNVYDWNAAARHLYRRAGFRE 151
Cdd:COG0454   95 LELDTLDGNPAAIRFYERLGFKE 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 42-171 5.36e-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: 57.34  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   42 ALRHPLSLEQMHEDLAEsrrrPPLRLLWsACRDDQVIGHCQLLFDRRNGvvRLARIVLAPSARGQGLGLPMLEALLAEAF 121
Cdd:TIGR01575  12 AFAFPWTEAQFAEELAN----YHLCYLL-ARIGGKVVGYAGVQIVLDEA--HILNIAVKPEYQGQGIGRALLRELIDEAK 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489206320  122 aDADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRErwNVVLM 171
Cdd:TIGR01575  85 -GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
87-153 7.40e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.07  E-value: 7.40e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489206320  87 RRNGVVRLARIVLAPSARGQGLGLPMLEALLAEAFAdADIERVELNVYDWNAAARHLYRRAGFREEG 153
Cdd:COG3393   11 ESPGVAEISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVG 76
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
53-153 2.31e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.86  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  53 HEDLAESRRRPPLRLLWSACRDDQVIGHCQLLFDRRNG---VVRLARIVLAPSARGQGLGLPMLEALLAEAfADADIERV 129
Cdd:COG3153   26 AELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGegpALLLGPLAVDPEYRGQGIGRALMRAALEAA-RERGARAV 104

                         90       100
                 ....*....|....*....|....
gi 489206320 130 ELnvyDWNAAARHLYRRAGFREEG 153
Cdd:COG3153  105 VL---LGDPSLLPFYERFGFRPAG 125
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
71-153 6.07e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.41  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  71 ACRDDQVIGhCQLLFDRRNGVVRLARIVLAPSARGQGLGLPMLEALLAEAfADADIERVELNVydwNAAARHLYRRAGFR 150
Cdd:COG2153   39 AYDDGELVA-TARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEA-RERGARRIVLSA---QAHAVGFYEKLGFV 113


                 ...
gi 489206320 151 EEG 153
Cdd:COG2153  114 PVG 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 72-173 4.16e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 47.23  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  72 CRDDQVIGH--CQLLFDRrngvVRLARIVLAPSARGQGLGLPMLEALLAEaFADADIERVELNVYDWNAAARHLYRRAGF 149
Cdd:PRK09491  46 TVNGQMAAFaiTQVVLDE----ATLFNIAVDPDYQRQGLGRALLEHLIDE-LEKRGVATLWLEVRASNAAAIALYESLGF 120

                         90       100
                 ....*....|....*....|....*.
gi 489206320 150 REEGLRRS--ATRVGRErwNVVLMGL 173
Cdd:PRK09491 121 NEVTIRRNyyPTADGRE--DAIIMAL 144
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 44-153 7.35e-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: 46.11  E-value: 7.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320   44 RHPLSLEQMHEDLAESRRrpplrLLWSACRDDQVIGHCQLlfdRRNGvvRLARIVLAPSARGQGLGLPMLEALLAEAFAD 123
Cdd:pfam13673  14 YEFISPEALRERIDQGEY-----FFFVAFEGGQIVGVIAL---RDRG--HISLLFVDPDYQGQGIGKALLEAVEDYAEKD 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 489206320  124 aDIERVELNVydwNAA--ARHLYRRAGFREEG 153
Cdd:pfam13673  84 -GIKLSELTV---NASpyAVPFYEKLGFRATG 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 68-132 7.67e-06

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: 41.88  E-value: 7.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489206320  68 LWSACRDDQVIGHCQLLFDR-RNGVVRLARIVLAPSARGQGLGLPMLEALLAEAFAdADIERVELN 132
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
PRK10140 PRK10140
N-acetyltransferase;
45-162 9.76e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 43.82  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  45 HPlSLEQMHEDLAEsrrRPPLRLLwSACRDDQVIGHCQLLFDRRNGVVRLARIVLAPSARGQGLGLPmlEALLAEAFADA 124
Cdd:PRK10140  35 HP-SDHMWQERLAD---RPGIKQL-VACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVA--SALMREMIEMC 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489206320 125 D----IERVELNVYDWNAAARHLYRRAGFREEGL-RRSATRVG 162
Cdd:PRK10140 108 DnwlrVDRIELTVFVDNAPAIKVYKKYGFEIEGTgKKYALRNG 150
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 101-153 1.42e-04

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 40.20  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489206320  101 PSARGQGLGLPMLEALLAEAFADADIERVelnVYD---WNAAARHLYRRAGFREEG 153
Cdd:pfam13523  89 PAFRGRGFTTALLRALVHYLFADPRTRRV---VVEpdvRNERAIRLLERAGFRKVK 141
PRK07757 PRK07757
N-acetyltransferase;
49-151 5.51e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489206320  49 LEQMHEDLAESrrrppLRLLWSACRDDQVIGHCQLLFDRRNgvvrLARI---VLAPSARGQGLGLPMLEALLAEAfADAD 125
Cdd:PRK07757  29 LPRSLDELYEN-----IRDFYVAEEEGEIVGCCALHILWED----LAEIrslAVSEDYRGQGIGRMLVEACLEEA-RELG 98

                         90       100
                 ....*....|....*....|....*.
gi 489206320 126 IERVELNVYDwnaaaRHLYRRAGFRE 151
Cdd:PRK07757  99 VKRVFALTYQ-----PEFFEKLGFRE 119
 
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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