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Conserved domains on  [gi|491522494|ref|WP_005380122|]
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MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Vibrio]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 12-145 7.09e-47

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 148.25  E-value: 7.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   12 HLDQVWQIEQQAHSHPWAE-SLVRDLSSRGACHHVMLEGSQVVGYFYGQNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFI 90
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEaQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491522494   91 EYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPaksgNGKEDAIIM 145
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 12-145 7.09e-47

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: 148.25  E-value: 7.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   12 HLDQVWQIEQQAHSHPWAE-SLVRDLSSRGACHHVMLEGSQVVGYFYGQNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFI 90
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEaQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491522494   91 EYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPaksgNGKEDAIIM 145
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 3-145 1.37e-45

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 145.84  E-value: 1.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   3 IEITPMRAEHLDQVWQIEQQAHSHPWAESLVrdLSSRGA--CHHVMLEGSQVVGYFYGQNIVGEVTLLNIAVAPSQQGRG 80
Cdd:PRK09491   2 NTISSLTPADLPAAYHIEQRAHAFPWSEKTF--ASNQGEryLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491522494  81 LGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPakSGNGKEDAIIM 145
Cdd:PRK09491  80 LGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYP--TADGREDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-146 5.11e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.94  E-value: 5.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  63 GEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPaksgngkEDA 142
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-------DDA 84


                 ....
gi 491522494 143 IIMS 146
Cdd:COG0456   85 LVME 88
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-121 4.42e-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: 72.17  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   13 LDQVWQIEQQAHSHPWAESLVRDL----SSRGACHHVMLEGSQVVGY---FYGQNIVGEVTLLNIAVAPSQQGRGLGQKL 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwdEDASEGFFVAEEDGELVGFaslSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491522494   86 LDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGF 121
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-104 7.61e-08

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: 46.50  E-value: 7.61e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491522494  45 VMLEGSQVVGYFYG---QNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLE 104
Cdd:cd04301    3 VAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 12-145 7.09e-47

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: 148.25  E-value: 7.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   12 HLDQVWQIEQQAHSHPWAE-SLVRDLSSRGACHHVMLEGSQVVGYFYGQNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFI 90
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEaQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491522494   91 EYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPaksgNGKEDAIIM 145
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 3-145 1.37e-45

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 145.84  E-value: 1.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   3 IEITPMRAEHLDQVWQIEQQAHSHPWAESLVrdLSSRGA--CHHVMLEGSQVVGYFYGQNIVGEVTLLNIAVAPSQQGRG 80
Cdd:PRK09491   2 NTISSLTPADLPAAYHIEQRAHAFPWSEKTF--ASNQGEryLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491522494  81 LGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPakSGNGKEDAIIM 145
Cdd:PRK09491  80 LGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYP--TADGREDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-146 5.11e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.94  E-value: 5.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  63 GEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPaksgngkEDA 142
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-------DDA 84


                 ....
gi 491522494 143 IIMS 146
Cdd:COG0456   85 LVME 88
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-148 1.04e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.73  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   2 TIEITPMRAEHLDQVWQIEQQAHSHPWA------------ESLVRDLSSRGACHHVMLEGSQVVGYFY--------GQNI 61
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTAtfeteppseeerEAWFAAILAPGRPVLVAEEDGEVVGFASlgpfrprpAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  62 VGEVTllnIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYpaKSGNGKED 141
Cdd:COG1247   81 TAEES---IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVG--FKFGRWLD 155


                 ....*..
gi 491522494 142 AIIMSYL 148
Cdd:COG1247  156 LVLMQKR 162
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-127 2.20e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.58  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   5 ITPMRAEHLDQVWQIEQQAHSHPWAESLVRDLSSRGACHH--VMLEGSQVVGY--FYGQNIVGE---VTLLNIAVAPSQQ 77
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLslVAEDDGEIVGHvaLSPVDIDGEgpaLLLGPLAVDPEYR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491522494  78 GRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPaihIYEQAGFNEVDRR 127
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVLLGDPSLLP---FYERFGFRPAGEL 127
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-121 4.42e-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: 72.17  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   13 LDQVWQIEQQAHSHPWAESLVRDL----SSRGACHHVMLEGSQVVGY---FYGQNIVGEVTLLNIAVAPSQQGRGLGQKL 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLedwdEDASEGFFVAEEDGELVGFaslSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491522494   86 LDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGF 121
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-148 8.51e-14

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: 65.02  E-value: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   1 MTIEITPMRAEHLDQVWQIEQQAH--------------SHPWAESLVRDLSSRGACHHVMLEGS--QVVGY--FYGQNIV 62
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEvarylpgppysleeARAWLERLLADWADGGALPFAIEDKEdgELIGVvgLYDIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  63 GEVTLLNIAVAPSQQGRGLGQKLLDAFIEYC-EQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNYYPAksgNGK-E 140
Cdd:COG1670   86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI---DGRyR 162


                 ....*...
gi 491522494 141 DAIIMSYL 148
Cdd:COG1670  163 DHVLYSLL 170
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-130 5.38e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 61.99  E-value: 5.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   1 MTIEITPmrAEHLDQVWQIEQQAhshpwAESLVRDLSSRGACHHVMLEGSQVVGyFYGQNIVGEVTLL--NIAVAPSQQG 78
Cdd:COG0454    1 MSIRKAT--PEDINFILLIEALD-----AELKAMEGSLAGAEFIAVDDKGEPIG-FAGLRRLDDKVLElkRLYVLPEYRG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491522494  79 RGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYNY 130
Cdd:COG0454   73 KGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-132 1.78e-12

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: 60.39  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   3 IEITPMRAEHLDQVWQIEQQAhshpwaeslvrDLSSRGACHHVMLEGSQVVG----YFYGQNiVGEVTLLniAVAPSQQG 78
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPY-----------ALEEEIGEFWVAEEDGEIVGcaalHPLDED-LAELRSL--AVHPDYRG 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491522494  79 RGLGQKLLDAFIEYCEQAKAESAWLevrESNHPAIHIYEQAGFNEVDRRYNYYP 132
Cdd:COG1246   67 RGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEEIDKEDLPYA 117
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-126 7.58e-12

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: 58.82  E-value: 7.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   43 HHVMLEGSQVVGYFYGQNIVGEVTLLN------IAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHpAIHIY 116
Cdd:pfam13673  24 ERIDQGEYFFFVAFEGGQIVGVIALRDrghislLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFY 102

                          90
                  ....*....|
gi 491522494  117 EQAGFNEVDR 126
Cdd:pfam13673 103 EKLGFRATGP 112
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 39-123 1.10e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.08  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   39 RGACHHVMLEGSQVVGY--FYGQNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVREsnhPAIHIY 116
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFaaLLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFY 77


                  ....*..
gi 491522494  117 EQAGFNE 123
Cdd:pfam13508  78 EKLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-131 8.79e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.91  E-value: 8.79e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491522494  69 NIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVdRRYNYY 131
Cdd:COG3393   20 GVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV-GEYATV 81
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
42-128 3.22e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 51.72  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  42 CHHVML-EGSQVVGY----FYGqniVGEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESnhpAIHIY 116
Cdd:COG2153   34 ARHLLAyDDGELVATarllPPG---DGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFY 107

                         90
                 ....*....|..
gi 491522494 117 EQAGFNEVDRRY 128
Cdd:COG2153  108 EKLGFVPVGEEF 119
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-104 7.61e-08

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: 46.50  E-value: 7.61e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491522494  45 VMLEGSQVVGYFYG---QNIVGEVTLLNIAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLE 104
Cdd:cd04301    3 VAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10562 PRK10562
putative acetyltransferase; Provisional
 5-129 8.53e-06

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 42.75  E-value: 8.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   5 ITPMRAEHLD---QVWqIEQQAHSHP------WAES--LVRDLSSRGACHHVMLEGSQVVGYFygqNIVGEVTLLNIAVA 73
Cdd:PRK10562   2 IREYQPSDLPailQLW-LESTIWAHPfikeqyWRESapLVRDVYLPAAQTWVWEEDGKLLGFV---SVLEGRFVGALFVA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522494  74 PSQQGRGLGQKLLDAFieyceQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRRYN 129
Cdd:PRK10562  78 PKAVRRGIGKALMQHV-----QQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQ 128
Eis COG4552
Predicted acetyltransferase [General function prediction only];
3-121 2.07e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 40.27  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   3 IEITPMRAEHLDQVWQIEQQAHSHPWAESLVRDLSSR--GACHHVMLEGSQVVG----YFYGQNI------VGEVTLlnI 70
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLlePGRVLGVFDDGELVGtlalYPFTLNVggarvpMAGITG--V 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491522494  71 AVAPSQQGRGLGQKLLDAFIEyceqakaesawlEVRESNHP-------AIHIYEQAGF 121
Cdd:COG4552   79 AVAPEHRRRGVARALLREALA------------ELRERGQPlsalypfEPGFYRRFGY 124
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-121 2.34e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.87  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494    3 IEITPMRAEHLDQVWQIEQQAHSHPWAESLVRDLS-SRGACHHVMLEGSQVVGYFY-----GQNIVGEVTL--------- 67
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEeAREWLARIWAADEAERGYGWaielkDTGFIGSIGLydidgeper 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491522494   68 --LNIAVAPSQQGRGLGQKLLDAFIEYC-EQAKAESAWLEVRESNHPAIHIYEQAGF 121
Cdd:pfam13302  82 aeLGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGF 138
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 70-128 2.88e-04

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: 37.69  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491522494   70 IAVAPSQQGRGLGQKLLDAFIEYCEQaKAESAWLEVRESNHPAIHIYEQAGFNEVDRRY 128
Cdd:pfam08445  27 LQTLPEHRRRGLGSRLVAALARGIAE-RGITPFAVVVAGNTPSRRLYEKLGFRKIDETY 84
PRK03624 PRK03624
putative acetyltransferase; Provisional
 71-126 3.78e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 3.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491522494  71 AVAPSQQGRGLGQKLLDAfieyceqakAESAW---------LEVRESNHPAIHIYEQAGFNEVDR 126
Cdd:PRK03624  75 AVHPDFRGRGIGRALVAR---------LEKKLiargcpkinLQVREDNDAVLGFYEALGYEEQDR 130
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 70-95 4.19e-04

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 39.43  E-value: 4.19e-04
                         10        20
                 ....*....|....*....|....*.
gi 491522494  70 IAVAPSQQGRGLGQKLLDAFIEYCEQ 95
Cdd:COG1444  491 IAVHPALQRRGLGSRLLAEIREEAKE 516
PRK07757 PRK07757
N-acetyltransferase;
27-91 5.17e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.25  E-value: 5.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491522494  27 PWAES---LVRDLSS-----RgaCHHVMLEGSQVVGY----FYGQNIvGEVTLLniAVAPSQQGRGLGQKLLDAFIE 91
Cdd:PRK07757  21 VYAKKglmLPRSLDElyeniR--DFYVAEEEGEIVGCcalhILWEDL-AEIRSL--AVSEDYRGQGIGRMLVEACLE 92
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
70-122 7.45e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 37.99  E-value: 7.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491522494  70 IAVAPSQQGRGLGQKLLDAFIEYCEQAKAESAWLEVRESNHPAIHIYEQAGFN 122
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 3-121 1.42e-03

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: 36.95  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494    3 IEITPMRAEHLDQVWQ----------------IEQQAHSHpWAESLVRDLSSRgaCHHVMLEGSQV-VGYFYGQNIVGEV 65
Cdd:TIGR03585   1 KNFTPLNSEELELVLEwrnhpdvranmysdhlIDWEEHLH-FIEALKQDPNRR--YWIVCQESRPIgVISFTDINLVHKS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491522494   66 TLLNIAVAPSQQGrGLGQKLLDAFIEYC-EQAKAESAWLEVRESNHPAIHIYEQAGF 121
Cdd:TIGR03585  78 AFWGIYANPFCKP-GVGSVLEEAALEYAfEHLGLHKLSLEVLESNNKALKLYEKFGF 133
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 21-131 1.67e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 37.25  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494   21 QQAHSHPWAESLVRDLSS--------RGAChhvMLEGSQVVG----YFYGQNIVgEVtllNIAVAPSQQGRGLGQKLLDA 88
Cdd:pfam12746 128 EACLEEEWSRDFVSQFSSyedflkngLGFV---ILKDGEIVSgassYSVYEGGI-EI---EIDTHPDYRGKGLATICAAA 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 491522494   89 FIEYC-EQAKAESaWlevRESNHPAIHIYEQAGFnEVDRRYNYY 131
Cdd:pfam12746 201 LILEClKRGLYPS-W---DAHNEASVALAEKLGY-EFVKEYTAY 239
PTZ00330 PTZ00330
acetyltransferase; Provisional
 58-127 3.69e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.59  E-value: 3.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  58 GQNIVGEVTllNIAVAPSQQGRGLGQKLLDafiEYCEQAKAESAWLEVRESNHPAIHIYEQAGFNEVDRR 127
Cdd:PTZ00330  78 GGKCVGHIE--DVVVDPSYRGQGLGRALIS---DLCEIARSSGCYKVILDCTEDMVAFYKKLGFRACERQ 142
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 30-123 9.23e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 34.68  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522494  30 ESLVRDLSSRGACHHVML----EGSQVVG---------YFYGQNIVGEVTllNIAVAPSQQGRGLGQKLLDAFIEYCEQA 96
Cdd:PLN02706  40 EARFQELASLGDDHLICViedaASGRIIAtgsvfverkFIRNCGKVGHIE--DVVVDSAARGKGLGKKIIEALTEHARSA 117

                         90       100
                 ....*....|....*....|....*..
gi 491522494  97 KAESAWLEVRESNHPaihIYEQAGFNE 123
Cdd:PLN02706 118 GCYKVILDCSEENKA---FYEKCGYVR 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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