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Conserved domains on  [gi|746089929|ref|WP_039156676|]
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MULTISPECIES: GNAT family N-acetyltransferase [Lactobacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-136 3.67e-17

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.49  E-value: 3.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRARMQELKTANMEQVFIQLRDApYLGYLLKCKM--YVATKEEKLVGFVGLRPH-------- 70
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREA-WFAAILAPGRpvLVAEEDGEVVGFASLGPFrprpayrg 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746089929  71 --ELSfLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKVVKTVVE------KWSDEY 136
Cdd:COG1247   81 taEES-IYVDPDARGRGIGRALLEALIERArargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvgfkfgRWLDLV 157
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-136 3.67e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.49  E-value: 3.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRARMQELKTANMEQVFIQLRDApYLGYLLKCKM--YVATKEEKLVGFVGLRPH-------- 70
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREA-WFAAILAPGRpvLVAEEDGEVVGFASLGPFrprpayrg 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746089929  71 --ELSfLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKVVKTVVE------KWSDEY 136
Cdd:COG1247   81 taEES-IYVDPDARGRGIGRALLEALIERArargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvgfkfgRWLDLV 157
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 53-122 3.30e-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: 64.46  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   53 YVATKEEKLVGFVGLRP-------HELSFLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYG 121
Cdd:pfam00583  36 FVAEEDGELVGFASLSIiddeppvGEIEGLAVAPEYRGKGIGTALLQALLEWArergCERIFLEVAADNLAAIALYEKLG 115


                  .
gi 746089929  122 F 122
Cdd:pfam00583 116 F 116
PRK09831 PRK09831
GNAT family N-acetyltransferase;
1-126 2.92e-12

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 60.36  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRA-RMQELKTANMEQV--FIQLRDAPYLGYLLKCKMYVATKEEKLVGFVGLRPHELSFLYV 77
Cdd:PRK09831   1 IQIRNYQPGDFQQLCAIFIRAvTMTASQHYSPQQIaaWAQIDESRWKEKLAKSQVRVAVINAQPVGFITCIEHYIDMLFV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 746089929  78 DPTFQKHGVGNKLmafaLDQLVRPIKLDVFTDNFVAKALYEKYGFKVVK 126
Cdd:PRK09831  81 DPEYTRRGVASAL----LKPLIKSESELTVDASITAKPFFERYGFQTVK 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-126 2.04e-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: 55.03  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   53 YVATKEEKLVGFVGLR--PHE--LSFLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKV 124
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQivLDEahILNIAVKPEYQGQGIGRALLRELIDEAkgrgVNEIFLEVRVSNIAAQALYKKLGFNE 113


                  ..
gi 746089929  125 VK 126
Cdd:TIGR01575 114 IA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-98 6.80e-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: 49.20  E-value: 6.80e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 746089929  52 MYVATKEEKLVGFVGLRPH-------ELSFLYVDPTFQKHGVGNKLMAFALDQL 98
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-136 3.67e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.49  E-value: 3.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRARMQELKTANMEQVFIQLRDApYLGYLLKCKM--YVATKEEKLVGFVGLRPH-------- 70
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREA-WFAAILAPGRpvLVAEEDGEVVGFASLGPFrprpayrg 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746089929  71 --ELSfLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKVVKTVVE------KWSDEY 136
Cdd:COG1247   81 taEES-IYVDPDARGRGIGRALLEALIERArargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvgfkfgRWLDLV 157
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-134 3.69e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.91  E-value: 3.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  63 GFVGLRPH------ELSFLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKVVKTVVEKW 132
Cdd:COG0456    1 GFALLGLVdggdeaEIEDLAVDPEYRGRGIGRALLEAALERArergARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80


                 ..
gi 746089929 133 SD 134
Cdd:COG0456   81 GD 82
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-127 1.65e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.57  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   3 IRKYENSDFDQLCHVMDRArmqeLKTANMEQVFIQLRDAPYLGYLLkckmyVATKEEKLVGFVGLRPH---------ELS 73
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA----FGPGREAELVDRLREDPAAGLSL-----VAEDDGEIVGHVALSPVdidgegpalLLG 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 746089929  74 FLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNfvaKALYEKYGFKVVKT 127
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAArergARAVVLLGDPSL---LPFYERFGFRPAGE 126
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-143 4.75e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 67.00  E-value: 4.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLChvmDRARMQElktanmeqvfiQLRDAPYLGYLLKCkmYVATKEEKLVGFVGLRP-----HELSFL 75
Cdd:COG0454    1 MSIRKATPEDINFIL---LIEALDA-----------ELKAMEGSLAGAEF--IAVDDKGEPIGFAGLRRlddkvLELKRL 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746089929  76 YVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKVVKTVVEKWSDEYPIEFAQD 143
Cdd:COG0454   65 YVLPEYRGKGIGKALLEALLEWArergCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKELSLS 136
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 53-122 3.30e-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: 64.46  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   53 YVATKEEKLVGFVGLRP-------HELSFLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYG 121
Cdd:pfam00583  36 FVAEEDGELVGFASLSIiddeppvGEIEGLAVAPEYRGKGIGTALLQALLEWArergCERIFLEVAADNLAAIALYEKLG 115


                  .
gi 746089929  122 F 122
Cdd:pfam00583 116 F 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 52-124 4.36e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 63.24  E-value: 4.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   52 MYVATKEEKLVGFVGLRPHELSF------LYVDPTFQKHGVGNKLMAFALDQLVRPIKLDVFTDNFV-AKALYEKYGFKV 124
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNrAAAFYEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-126 7.02e-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: 7.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMdrarmqelktanmeqvfiqlrdAPYLGYLLKCKMYVATKEEKLVGFVGLRPH-----ELSFL 75
Cdd:COG1246    1 MTIRPATPDDVPAILELI----------------------RPYALEEEIGEFWVAEEDGEIVGCAALHPLdedlaELRSL 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 746089929  76 YVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDnfvAKALYEKYGFKVVK 126
Cdd:COG1246   59 AVHPDYRGRGIGRRLLEALLAEArelgLKRLFLLTTSA---AIHFYEKLGFEEID 110
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 50-131 4.64e-13

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: 61.90  E-value: 4.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   50 CKMYVATKEEKLVGFVGLR--PHeLSFLYVDPTFQKHGVGNKLMAFALDQLVR-PIKLDVFTDN--FVAKALYEKYGFKV 124
Cdd:pfam13673  31 YFFFVAFEGGQIVGVIALRdrGH-ISLLFVDPDYQGQGIGKALLEAVEDYAEKdGIKLSELTVNasPYAVPFYEKLGFRA 109


                  ....*..
gi 746089929  125 VKTVVEK 131
Cdd:pfam13673 110 TGPEQEF 116
PRK09831 PRK09831
GNAT family N-acetyltransferase;
1-126 2.92e-12

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 60.36  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRA-RMQELKTANMEQV--FIQLRDAPYLGYLLKCKMYVATKEEKLVGFVGLRPHELSFLYV 77
Cdd:PRK09831   1 IQIRNYQPGDFQQLCAIFIRAvTMTASQHYSPQQIaaWAQIDESRWKEKLAKSQVRVAVINAQPVGFITCIEHYIDMLFV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 746089929  78 DPTFQKHGVGNKLmafaLDQLVRPIKLDVFTDNFVAKALYEKYGFKVVK 126
Cdd:PRK09831  81 DPEYTRRGVASAL----LKPLIKSESELTVDASITAKPFFERYGFQTVK 125
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
60-130 6.82e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.91  E-value: 6.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  60 KLVGFVGLRPH-----ELSFLYVDPTFQKHGVGNKLMAF----ALDQLVRPIKLDVFTDNFVAKALYEKYGFKVVKTVVE 130
Cdd:COG3393    1 ELVAMAGVRAEspgvaEISGVYTHPEYRGRGLASALVAAlareALARGARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-126 2.04e-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: 55.03  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   53 YVATKEEKLVGFVGLR--PHE--LSFLYVDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGFKV 124
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQivLDEahILNIAVKPEYQGQGIGRALLRELIDEAkgrgVNEIFLEVRVSNIAAQALYKKLGFNE 113


                  ..
gi 746089929  125 VK 126
Cdd:TIGR01575 114 IA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-98 6.80e-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: 49.20  E-value: 6.80e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 746089929  52 MYVATKEEKLVGFVGLRPH-------ELSFLYVDPTFQKHGVGNKLMAFALDQL 98
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-128 6.88e-09

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: 51.54  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLC------HVMDRARMQELKTANMEQVFIQLRDAPYLGYLLkckMYVATKEE--KLVGFVGLRPHEL 72
Cdd:COG1670    8 LRLRPLRPEDAEALAellndpEVARYLPGPPYSLEEARAWLERLLADWADGGAL---PFAIEDKEdgELIGVVGLYDIDR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746089929  73 SF------LYVDPTFQKHGVG----NKLMAFALDQL-VRPIKLDVFTDNFVAKALYEKYGFKVVKTV 128
Cdd:COG1670   85 ANrsaeigYWLAPAYWGKGYAtealRALLDYAFEELgLHRVEAEVDPDNTASIRVLEKLGFRLEGTL 151
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
32-136 6.42e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  32 EQVFIQ-LRDAPYL---GYLLKCKMYVATKEEKLVGFVGLRPHE-----LSFLYVDPTFQKHGVGNKLMAFALDQL---- 98
Cdd:COG2153   12 REVFVVeQGVPPYLeldGKDEDARHLLAYDDGELVATARLLPPGdgeakIGRVAVLPEYRGQGLGRALMEAAIEEArerg 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 746089929  99 VRPIKLDVFTDnfvAKALYEKYGFKVVktvvekwSDEY 136
Cdd:COG2153   92 ARRIVLSAQAH---AVGFYEKLGFVPV-------GEEF 119
PRK03624 PRK03624
putative acetyltransferase; Provisional
 54-135 4.04e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.46  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  54 VATKEEKLVGFV--GLRPHE--LSFLYVDPTFQKHGVGNKLMAFALDQLV----RPIKLDVFTDNFVAKALYEKYGFKVV 125
Cdd:PRK03624  49 VAEVGGEVVGTVmgGYDGHRgwAYYLAVHPDFRGRGIGRALVARLEKKLIargcPKINLQVREDNDAVLGFYEALGYEEQ 128

                         90
                 ....*....|.
gi 746089929 126 KTVV-EKWSDE 135
Cdd:PRK03624 129 DRISlGKRLIE 139
PRK10140 PRK10140
N-acetyltransferase;
51-127 9.05e-05

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 40.35  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  51 KMYVATKEEKLVGFVGL-------RPHELSF-LYVDPTFQKHGVGNKLMAFALDQL-----VRPIKLDVFTDNFVAKALY 117
Cdd:PRK10140  52 KQLVACIDGDVVGHLTIdvqqrprRSHVADFgICVDSRWKNRGVASALMREMIEMCdnwlrVDRIELTVFVDNAPAIKVY 131

                         90
                 ....*....|
gi 746089929 118 EKYGFKVVKT 127
Cdd:PRK10140 132 KKYGFEIEGT 141
PRK10562 PRK10562
putative acetyltransferase; Provisional
 2-135 1.28e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 39.67  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   2 LIRKYENSDFDQLchvmdrarMQ-ELKTANMEQVFIQ----------LRDApylgYLLKCKMYVATKEEKLVGFVG-LRP 69
Cdd:PRK10562   1 MIREYQPSDLPAI--------LQlWLESTIWAHPFIKeqywresaplVRDV----YLPAAQTWVWEEDGKLLGFVSvLEG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746089929  70 HELSFLYVDPTFQKHGVGNKLMAFaLDQLVRPIKLDVFTDNFVAKALYEKYGFKVVKtvvEKWSDE 135
Cdd:PRK10562  69 RFVGALFVAPKAVRRGIGKALMQH-VQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVD---SAWQEE 130
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 77-122 1.43e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.53  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 746089929  77 VDPTFQKHGVGNKLMAFALDQL----VRPIKLDVFTDNFVAKALYEKYGF 122
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELekrgVATLWLEVRASNAAAIALYESLGF 120
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-123 4.49e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929    2 LIRKYENSDFDQLCHVM-DRARMQ---------ELKTANMEQVFIQLRDAPYLGYLlkckmyVATKEEKLVGFVGLRPH- 70
Cdd:pfam13302   3 LLRPLTEEDAEALFELLsDPEVMRygvpwpltlEEAREWLARIWAADEAERGYGWA------IELKDTGFIGSIGLYDId 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746089929   71 ------ELSFlYVDPTFQKHGVG----NKLMAFALDQL-VRPIKLDVFTDNFVAKALYEKYGFK 123
Cdd:pfam13302  77 geperaELGY-WLGPDYWGKGYAteavRALLEYAFEELgLPRLVARIDPENTASRRVLEKLGFK 139
PRK10514 PRK10514
putative acetyltransferase; Provisional
 45-124 6.26e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  45 GYLLKCKMYVATKEE-KLVGFVGLRPHELSFLYVDPTFQKHGVGNKLMAFALdQLVRPIKLDVFTDNFVAKALYEKYGFK 123
Cdd:PRK10514  44 SFLPEAPLWVAVDERdQPVGFMLLSGGHMEALFVDPDVRGCGVGRMLVEHAL-SLHPELTTDVNEQNEQAVGFYKKMGFK 122


                 .
gi 746089929 124 V 124
Cdd:PRK10514 123 V 123
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 33-136 7.10e-04

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: 37.72  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   33 QVFIQLRDAPYLGYLLKCKmyvatkEEKLVGFVGL----RPHELSFL--YVDPtFQKHGVGNKLMAFALDQLVRPIKLD- 105
Cdd:TIGR03585  40 HFIEALKQDPNRRYWIVCQ------ESRPIGVISFtdinLVHKSAFWgiYANP-FCKPGVGSVLEEAALEYAFEHLGLHk 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 746089929  106 ----VFTDNFVAKALYEKYGFKVVKtvVEKWSDEY 136
Cdd:TIGR03585 113 lsleVLESNNKALKLYEKFGFEREG--VFRQGGEY 145
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-98 1.05e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.96  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929   1 MLIRKYENSDFDQLCHVMDRARMQELKTANMEQVFIQLRDAPYLGyllkckmyvATKEEKLVGFVGLRPHELSF------ 74
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVLG---------VFDDGELVGTLALYPFTLNVggarvp 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 746089929  75 ------LYVDPTFQKHGVGNKLMAFALDQL 98
Cdd:COG4552   72 magitgVAVAPEHRRRGVARALLREALAEL 101
PRK07757 PRK07757
N-acetyltransferase;
52-134 1.93e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.33  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  52 MYVATKEEKLVGFVGLRPH-----ELSFLYVDPTFQKHGVGNKLMAFALDQLvRPIKL-DVFTDNFVaKALYEKYGFKVV 125
Cdd:PRK07757  43 FYVAEEEGEIVGCCALHILwedlaEIRSLAVSEDYRGQGIGRMLVEACLEEA-RELGVkRVFALTYQ-PEFFEKLGFREV 120

                         90
                 ....*....|..
gi 746089929 126 K--TVVEK-WSD 134
Cdd:PRK07757 121 DkeALPQKvWAD 132
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
53-96 3.02e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 34.75  E-value: 3.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 746089929  53 YVATKEEKLVGFVG--LRPHELSFL--YVDPTFQKHGVGNKLMAFALD 96
Cdd:COG2388   12 FELEVDGELAGELTyrLEGGVIIIThtEVPPALRGQGIASALVEAALD 59
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
50-127 6.27e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 35.29  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089929  50 CKMYVATKEEkLVGFVGLRphELS-------FLYVDPTFQKHGVGNKLMAFALDQLVRP--IKLDVFTD--NFVAKALYE 118
Cdd:PRK10975 103 CLLLRDASGQ-IQGFVTLR--ELNdtdarigLLAVFPGAQGRGIGARLMQAALNWCQARglTRLRVATQmgNLAALRLYI 179


                 ....*....
gi 746089929 119 KYGFKVVKT 127
Cdd:PRK10975 180 RSGANIEST 188
 
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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