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Conserved domains on  [gi|556425029|ref|WP_023309956|]
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MULTISPECIES: N-acetyltransferase [Enterobacter]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10793418)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-145 4.85e-100

putative acetyltransferase; Provisional


:

Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 283.11  E-value: 4.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   1 MIRKWQSENTAPLLSLWLESTTEAHPFIEPGYWKENEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALFVAPSC 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425029  81 IGKGIGRALLNHVQQRFPHLTLEVYQKNVRAVNFYHAQGFRIEDSAWQDDTQHPTWIMSWQADQT 145
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-145 4.85e-100

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 283.11  E-value: 4.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   1 MIRKWQSENTAPLLSLWLESTTEAHPFIEPGYWKENEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALFVAPSC 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425029  81 IGKGIGRALLNHVQQRFPHLTLEVYQKNVRAVNFYHAQGFRIEDSAWQDDTQHPTWIMSWQADQT 145
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-120 4.05e-15

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: 66.77  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   13 LLSLWLESTTEAHPFIEPGYWKENEAmvrdvyLPSAETWVWEEDGEPCGFISVMQSQ------FVGALFVAPSCIGKGIG 86
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE------DASEGFFVAEEDGELVGFASLSIIDdeppvgEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 556425029   87 RALLNHV-----QQRFPHLTLEVYQKNVRAVNFYHAQGF 120
Cdd:pfam00583  78 TALLQALlewarERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-124 8.37e-15

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: 8.37e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425029  61 GFISVMQSQ-----FVGALFVAPSCIGKGIGRALLNHVQQR-----FPHLTLEVYQKNVRAVNFYHAQGFRIED 124
Cdd:COG0456    1 GFALLGLVDggdeaEIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFEEVG 74
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 1.37e-09

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: 51.12  E-value: 1.37e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425029  51 WVWEEDGEPCGFISVMQSQ------FVGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLE 103
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGsggdtaYIGDLAVLPEYRGKGIGSALLEAAeeearERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-124 6.43e-08

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: 48.48  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   23 EAHPFIEPgyWKEnEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALF---VAPSCIGKGIGRALLNHVQQRFPH 99
Cdd:TIGR01575   9 EAAAFAFP--WTE-AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILniaVKPEYQGQGIGRALLRELIDEAKG 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 556425029  100 -----LTLEVYQKNVRAVNFYHAQGFRIED 124
Cdd:TIGR01575  86 rgvneIFLEVRVSNIAAQALYKKLGFNEIA 115
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-145 4.85e-100

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 283.11  E-value: 4.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   1 MIRKWQSENTAPLLSLWLESTTEAHPFIEPGYWKENEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALFVAPSC 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425029  81 IGKGIGRALLNHVQQRFPHLTLEVYQKNVRAVNFYHAQGFRIEDSAWQDDTQHPTWIMSWQADQT 145
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-122 2.16e-21

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 83.90  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   2 IRKWQSENTAPLLSLWLESTTEAHPFIEPGYWKENEAMVRDvYLPSAETWVW--EEDgEPCGFIsVMQSQFVGALFVAPS 79
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRS-FLPEAPLWVAvdERD-QPVGFM-LLSGGHMEALFVDPD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 556425029  80 CIGKGIGRALLNHVQQRFPHLTLEVYQKNVRAVNFYHAQGFRI 122
Cdd:PRK10514  81 VRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKV 123
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-120 4.05e-15

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: 66.77  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   13 LLSLWLESTTEAHPFIEPGYWKENEAmvrdvyLPSAETWVWEEDGEPCGFISVMQSQ------FVGALFVAPSCIGKGIG 86
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE------DASEGFFVAEEDGELVGFASLSIIDdeppvgEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 556425029   87 RALLNHV-----QQRFPHLTLEVYQKNVRAVNFYHAQGF 120
Cdd:pfam00583  78 TALLQALlewarERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-124 8.37e-15

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: 8.37e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425029  61 GFISVMQSQ-----FVGALFVAPSCIGKGIGRALLNHVQQR-----FPHLTLEVYQKNVRAVNFYHAQGFRIED 124
Cdd:COG0456    1 GFALLGLVDggdeaEIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-121 3.60e-14

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: 64.60  E-value: 3.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   35 ENEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALFVAPSCIGKGIGRALLNHVQQRFPHLTLEVYQKNVR---- 110
Cdd:pfam13673  18 SPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNaspy 97

                          90
                  ....*....|.
gi 556425029  111 AVNFYHAQGFR 121
Cdd:pfam13673  98 AVPFYEKLGFR 108
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-122 4.85e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 63.24  E-value: 4.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   46 PSAETWVWEEDGEPCGFISVMQSQFVGA-----LFVAPSCIGKGIGRALLNHVQQ--RFPHLTLEVYQKNVRAVNFYHAQ 118
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGAlaelrLAVHPEYRGQGIGRALLEAAEAaaKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 556425029  119 GFRI 122
Cdd:pfam13508  81 GFEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
37-124 7.08e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 64.63  E-value: 7.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  37 EAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQ------FVG--ALFVAPSCIGKGIGRALLNHVQQR-----FPHLTLE 103
Cdd:COG1247   41 EAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRprpayrGTAeeSIYVDPDARGRGIGRALLEALIERarargYRRLVAV 120

                         90       100
                 ....*....|....*....|.
gi 556425029 104 VYQKNVRAVNFYHAQGFRIED 124
Cdd:COG1247  121 VLADNEASIALYEKLGFEEVG 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 42-121 8.87e-14

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 63.86  E-value: 8.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  42 DVYLPSAETWVWEEDGEPCGFISVMQSQ----FVGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLEVYQknvRAV 112
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALHPLDedlaELRSLAVHPDYRGRGIGRRLLEALlaearELGLKRLFLLTTS---AAI 98


                 ....*....
gi 556425029 113 NFYHAQGFR 121
Cdd:COG1246   99 HFYEKLGFE 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 37-122 1.20e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.83  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  37 EAMVRD-VYLPSAETWVW-EEDGEPCGFISVMQ----SQFVGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLEVY 105
Cdd:COG0454   21 DAELKAmEGSLAGAEFIAvDDKGEPIGFAGLRRlddkVLELKRLYVLPEYRGKGIGKALLEALlewarERGCTALELDTL 100

                         90
                 ....*....|....*..
gi 556425029 106 QKNVRAVNFYHAQGFRI 122
Cdd:COG0454  101 DGNPAAIRFYERLGFKE 117
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
48-121 5.35e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.94  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  48 AETWVWEEDGEPCGFISVMQSQ--------FVGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLEVyqkNVRAVNF 114
Cdd:COG3153   39 GLSLVAEDDGEIVGHVALSPVDidgegpalLLGPLAVDPEYRGQGIGRALMRAAleaarERGARAVVLLG---DPSLLPF 115


                 ....*..
gi 556425029 115 YHAQGFR 121
Cdd:COG3153  116 YERFGFR 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 1.37e-09

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: 51.12  E-value: 1.37e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425029  51 WVWEEDGEPCGFISVMQSQ------FVGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLE 103
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGsggdtaYIGDLAVLPEYRGKGIGSALLEAAeeearERGAKRLRLE 65
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-144 5.66e-08

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: 49.23  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   2 IRKWQSENTAPLLSLWleSTTEAHPFIEPGYWKENEA------MVRDVYLPSAETWV--WEEDGEPCGFISVMQSQFVG- 72
Cdd:COG1670   10 LRPLRPEDAEALAELL--NDPEVARYLPGPPYSLEEArawlerLLADWADGGALPFAieDKEDGELIGVVGLYDIDRANr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  73 ----ALFVAPSCIGKGIG----RALLNHV--QQRFPHLTLEVYQKNVRAVNFYHAQGFRIE----DSAWQDDTQHPTWIM 138
Cdd:COG1670   88 saeiGYWLAPAYWGKGYAtealRALLDYAfeELGLHRVEAEVDPDNTASIRVLEKLGFRLEgtlrDALVIDGRYRDHVLY 167


                 ....*.
gi 556425029 139 SWQADQ 144
Cdd:COG1670  168 SLLREE 173
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-124 6.43e-08

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: 48.48  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   23 EAHPFIEPgyWKEnEAMVRDVYLPSAETWVWEEDGEPCGFISVMQSQFVGALF---VAPSCIGKGIGRALLNHVQQRFPH 99
Cdd:TIGR01575   9 EAAAFAFP--WTE-AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILniaVKPEYQGQGIGRALLRELIDEAKG 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 556425029  100 -----LTLEVYQKNVRAVNFYHAQGFRIED 124
Cdd:TIGR01575  86 rgvneIFLEVRVSNIAAQALYKKLGFNEIA 115
PRK03624 PRK03624
putative acetyltransferase; Provisional
 74-125 9.38e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 9.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556425029  74 LFVAPSCIGKGIGRALLNHVQQRF-----PHLTLEVYQKNVRAVNFYHAQGFRIEDS 125
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLiargcPKINLQVREDNDAVLGFYEALGYEEQDR 130
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-121 1.44e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 43.74  E-value: 1.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556425029  71 VGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLEVYQKNVRAVNFYHAQGFR 121
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALarealARGARTPFLYVDADNPAARRLYERLGFR 73
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 74-120 6.90e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.99  E-value: 6.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556425029  74 LF---VAPSCIGKGIGRALLNHVQQRFPH-----LTLEVYQKNVRAVNFYHAQGF 120
Cdd:PRK09491  66 LFniaVDPDYQRQGLGRALLEHLIDELEKrgvatLWLEVRASNAAAIALYESLGF 120
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 46-123 9.95e-06

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: 42.73  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029   46 PSAETWVWEEDGEPCGFISVMQSQFV---------GALFVAPScIGKGIGRALLNHVQQRF--PHLTLEVYQKNVRAVNF 114
Cdd:TIGR03585  49 PNRRYWIVCQESRPIGVISFTDINLVhksafwgiyANPFCKPG-VGSVLEEAALEYAFEHLglHKLSLEVLESNNKALKL 127


                  ....*....
gi 556425029  115 YHAQGFRIE 123
Cdd:TIGR03585 128 YEKFGFERE 136
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
55-127 1.16e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.30  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  55 EDGEPCGFISVM----QSQFVGALFVAPSCIGKGIGRALLNH-----VQQRFPHLTLEVYQKNVRAVNFYHAQGFRIEDS 125
Cdd:PRK10975 109 ASGQIQGFVTLRelndTDARIGLLAVFPGAQGRGIGARLMQAalnwcQARGLTRLRVATQMGNLAALRLYIRSGANIEST 188


                 ...
gi 556425029 126 A-W 127
Cdd:PRK10975 189 AyW 191
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
46-123 1.18e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  46 PSAETWVWEEDGEPCGFISVMQSQF----VGALFVAPSCIGKGIGRALLNHV-----QQRFPHLTLEVyQknVRAVNFYH 116
Cdd:COG2153   32 EDARHLLAYDDGELVATARLLPPGDgeakIGRVAVLPEYRGQGLGRALMEAAieearERGARRIVLSA-Q--AHAVGFYE 108


                 ....*..
gi 556425029 117 AQGFRIE 123
Cdd:COG2153  109 KLGFVPV 115
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
32-116 4.18e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 38.38  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  32 YWKENEamvRDVYLpsaetwvWEEDGEPCGFISVMQSQF------VGALFVAPSCIGKGIGRALLNHVQQRFP-HLTLEV 104
Cdd:COG5628   49 YWTDDD---RHPYL-------IYVDGEPAGFALVRRLPFlesdyeIAEFFVLRKYRRKGIGKRAAHELFKRFPgRWEVKQ 118

                         90
                 ....*....|..
gi 556425029 105 YQKNVRAVNFYH 116
Cdd:COG5628  119 LEANVPAVAFWR 130
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
36-121 4.39e-03

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 35.68  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425029  36 NEAMVRDVYLPSAETWVWEEDGEPCGFISVM--------------QSQFVGALF-----VAPSCIGKGIGRALLNHVQ-- 94
Cdd:COG3818   33 DAARLARLHEQAAYARVAEVDGEVAGFLLAFgpgadydspnyrwfAERYDNFLYidrivVAPSARGRGLGRALYADVFsy 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556425029  95 ---QRFPHLTLEVYQK--NVRAVNFYHAQGFR 121
Cdd:COG3818  113 araRGVPRVTCEVNLEppNPGSLAFHARLGFR 144
PRK09831 PRK09831
GNAT family N-acetyltransferase;
56-122 9.49e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 34.55  E-value: 9.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556425029  56 DGEPCGFISVMQsQFVGALFVAPSCIGKGIGRALLNHVQQRFPHLTLEVyqkNVRAVNFYHAQGFRI 122
Cdd:PRK09831  61 NAQPVGFITCIE-HYIDMLFVDPEYTRRGVASALLKPLIKSESELTVDA---SITAKPFFERYGFQT 123
 
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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