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Conserved domains on  [gi|655374630|ref|WP_028780159|]
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MULTISPECIES: GNAT family N-acetyltransferase [Shewanella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-152 8.16e-23

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: 87.35  E-value: 8.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWD-IRNLAIQAGcqgfytkaelriwtqgempsvfitmvERDFYLIEHQGKILATGML-----DNDR 74
Cdd:COG1246    1 MTIRPATPDDVPAILElIRPYALEEE--------------------------IGEFWVAEEDGEIVGCAALhpldeDLAE 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGFCGEGISQYHSPRGIVLDCVVMHKALK 152
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-152 8.16e-23

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: 87.35  E-value: 8.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWD-IRNLAIQAGcqgfytkaelriwtqgempsvfitmvERDFYLIEHQGKILATGML-----DNDR 74
Cdd:COG1246    1 MTIRPATPDDVPAILElIRPYALEEE--------------------------IGEFWVAEEDGEIVGCAALhpldeDLAE 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGFCGEGISQYHSPRGIVLDCVVMHKALK 152
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-126 1.87e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 64.40  E-value: 1.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630   55 FYLIEHQGKILATGMLDNDRIEA------LFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGF 82
PRK07757 PRK07757
N-acetyltransferase;
1-126 2.66e-11

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 57.90  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQtawDIRNLaiqagcqgfytkaeLRIW-TQGEM-PSVFITMVE--RDFYLIEHQGKILATGML-----D 71
Cdd:PRK07757   2 MEIRKARLSDVK---AIHAL--------------INVYaKKGLMlPRSLDELYEniRDFYVAEEEGEIVGCCALhilweD 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630  72 NDRIEALFVHPQAMGQGLGRDLLAHLESLARERGVT---ALTLEstlnaADFYRSCGF 126
Cdd:PRK07757  65 LAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQ-----PEFFEKLGF 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-112 1.51e-10

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: 53.82  E-value: 1.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655374630  55 FYLIEHQGKILATGMLDNDR-------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-147 3.28e-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: 54.64  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   54 DFYLIEHQGKILATGM----LDNDRIEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLE---STLNAADFYRSCGF 126
Cdd:TIGR01575  32 CYLLARIGGKVVGYAGvqivLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEvrvSNIAAQALYKKLGF 111

                          90       100
                  ....*....|....*....|...
gi 655374630  127 CGEGISQ--YHSPrgiVLDCVVM 147
Cdd:TIGR01575 112 NEIAIRRnyYPDP---GEDAIVM 131
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-152 8.16e-23

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: 87.35  E-value: 8.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWD-IRNLAIQAGcqgfytkaelriwtqgempsvfitmvERDFYLIEHQGKILATGML-----DNDR 74
Cdd:COG1246    1 MTIRPATPDDVPAILElIRPYALEEE--------------------------IGEFWVAEEDGEIVGCAALhpldeDLAE 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGFCGEGISQYHSPRGIVLDCVVMHKALK 152
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-126 2.35e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.86  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWDIRNLAiqagcqgfytkAELRIWTQGEMPSVFItmverdfyLIEHQGKILATG---MLDNDRIE- 76
Cdd:COG0454    1 MSIRKATPEDINFILLIEALD-----------AELKAMEGSLAGAEFI--------AVDDKGEPIGFAglrRLDDKVLEl 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 655374630  77 -ALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLEsTLN----AADFYRSCGF 126
Cdd:COG0454   62 kRLYVLPEYRGKGIGKALLEALLEWARERGCTALELD-TLDgnpaAIRFYERLGF 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-151 5.45e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.11  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWDIRNLAIQAGCQGFYTK----AELRIWTQGEMPSVFITMVerdfylIEHQGKILATGMLDNDR-- 74
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEppseEEREAWFAAILAPGRPVLV------AEEDGEVVGFASLGPFRpr 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  75 -------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTL-NAA--DFYRSCGF--CGEGISQYHSPrGIVL 142
Cdd:COG1247   76 payrgtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAdNEAsiALYEKLGFeeVGTLPEVGFKF-GRWL 154


                 ....*....
gi 655374630 143 DCVVMHKAL 151
Cdd:COG1247  155 DLVLMQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-126 1.87e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 64.40  E-value: 1.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630   55 FYLIEHQGKILATGMLDNDRIEA------LFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGalaelrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGF 82
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-126 2.34e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.49  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   3 LRKARKEDAqtaWDIRNLAIQAGCQGFYTKAELRIWTQGEMPSVFItmverdfylIEHQGKILATGMLDNDR-------- 74
Cdd:COG3153    1 IRPATPEDA---EAIAALLRAAFGPGREAELVDRLREDPAAGLSLV---------AEDDGEIVGHVALSPVDidgegpal 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 655374630  75 -IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:COG3153   69 lLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGF 121
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
56-129 2.38e-13

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.89  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  56 YLIEHQGKILATG-MLDND----RIEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF--CG 128
Cdd:COG2153   37 LLAYDDGELVATArLLPPGdgeaKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFvpVG 116


                 .
gi 655374630 129 E 129
Cdd:COG2153  117 E 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 75-152 3.62e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.21  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLE---STLNAADFYRSCGFCGEGISQYHSPRgivlDCVVMHKAL 151
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEvreDNEAAIALYEKLGFEEVGERPNYYGD----DALVMEKEL 91


                 .
gi 655374630 152 K 152
Cdd:COG0456   92 A 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 55-126 2.37e-11

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: 57.14  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   55 FYLIEHQGKILATGMLDNDR-------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLN---AADFYRSC 124
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDdeppvgeIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADnlaAIALYEKL 114


                  ..
gi 655374630  125 GF 126
Cdd:pfam00583 115 GF 116
PRK07757 PRK07757
N-acetyltransferase;
1-126 2.66e-11

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 57.90  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQtawDIRNLaiqagcqgfytkaeLRIW-TQGEM-PSVFITMVE--RDFYLIEHQGKILATGML-----D 71
Cdd:PRK07757   2 MEIRKARLSDVK---AIHAL--------------INVYaKKGLMlPRSLDELYEniRDFYVAEEEGEIVGCCALhilweD 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 655374630  72 NDRIEALFVHPQAMGQGLGRDLLAHLESLARERGVT---ALTLEstlnaADFYRSCGF 126
Cdd:PRK07757  65 LAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQ-----PEFFEKLGF 117
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 55-126 3.17e-11

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: 57.28  E-value: 3.17e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655374630   55 FYLIEHQGKIL-ATGMLDNDRIEALFVHPQAMGQGLGRDLLAHLESLARERG--VTALTLESTLNAADFYRSCGF 126
Cdd:pfam13673  33 FFVAFEGGQIVgVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGikLSELTVNASPYAVPFYEKLGF 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-112 1.51e-10

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: 53.82  E-value: 1.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655374630  55 FYLIEHQGKILATGMLDNDR-------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-147 3.28e-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: 54.64  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   54 DFYLIEHQGKILATGM----LDNDRIEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLE---STLNAADFYRSCGF 126
Cdd:TIGR01575  32 CYLLARIGGKVVGYAGvqivLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEvrvSNIAAQALYKKLGF 111

                          90       100
                  ....*....|....*....|...
gi 655374630  127 CGEGISQ--YHSPrgiVLDCVVM 147
Cdd:TIGR01575 112 NEIAIRRnyYPDP---GEDAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
74-126 3.42e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.98  E-value: 3.42e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 655374630  74 RIEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTL---ESTLNAADFYRSCGF 126
Cdd:COG3393   17 EISGVYTHPEYRGRGLASALVAALAREALARGARTPFLyvdADNPAARRLYERLGF 72
PRK10562 PRK10562
putative acetyltransferase; Provisional
 53-126 4.62e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 46.21  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  53 RDFYL-------IEHQGKILA-TGMLDNDRIEALFVHPQAMGQGLGRDLLAHLESLarergVTALTLE---STLNAADFY 121
Cdd:PRK10562  41 RDVYLpaaqtwvWEEDGKLLGfVSVLEGRFVGALFVAPKAVRRGIGKALMQHVQQR-----YPHLSLEvyqKNQRAVNFY 115


                 ....*
gi 655374630 122 RSCGF 126
Cdd:PRK10562 116 HAQGF 120
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 52-126 4.90e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.46  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  52 ERdfYL---IEHQGKILATGM----LDndriEA-LF---VHPQAMGQGLGRDLLAHLESLARERGVTALTLE---STLNA 117
Cdd:PRK09491  38 ER--YLnlkLTVNGQMAAFAItqvvLD----EAtLFniaVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEvraSNAAA 111


                 ....*....
gi 655374630 118 ADFYRSCGF 126
Cdd:PRK09491 112 IALYESLGF 120
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 52-109 1.50e-06

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 46.30  E-value: 1.50e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655374630  52 ERD---FYLIEHQGKILATGML---DNDRI-E--ALFVHPQAMGQGLGRDLLAHLESLARERGVTAL 109
Cdd:PRK05279 330 EREidkFTVIERDGLIIGCAALypfPEEKMgEmaCLAVHPDYRGSGRGERLLKRIEQRARQLGLKRL 396
PTZ00330 PTZ00330
acetyltransferase; Provisional
 75-126 8.32e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 42.91  E-value: 8.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGF 136
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 51-126 2.39e-05

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 42.64  E-value: 2.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655374630  51 VERDFYLIEHQGKILATGMLDNDRIEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:cd02169    4 LDYTVGIFDDAGELIATGSIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGLGF 79
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-126 3.52e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 41.14  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   2 KLRKARKEDAQTAWDIRNLAIQAgCQGFYTKAELRiwTQGEMPSVFITMVERDFyLIEHQGKILATGMLDNDRIEALFVH 81
Cdd:PRK10514   3 SIRRSRHEEGERLVAIWRRSVDA-THDFLSAEDRA--EIEELVRSFLPEAPLWV-AVDERDQPVGFMLLSGGHMEALFVD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 655374630  82 PQAMGQGLGRDLLAHleSLARERGVTALTLESTLNAADFYRSCGF 126
Cdd:PRK10514  79 PDVRGCGVGRMLVEH--ALSLHPELTTDVNEQNEQAVGFYKKMGF 121
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-126 3.96e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 42.19  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630   1 MKLRKARKEDAQTAWDIRNLAIQAGcqgfytkaelriWTQGEMPSVFITMVERDFYLIEHQGKILATGMLdNDR------ 74
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPE------------PDDEELEAYRPLLEPGRVLGVFDDGELVGTLAL-YPFtlnvgg 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655374630  75 -------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTAltleSTLNA--ADFYRSCGF 126
Cdd:COG4552   68 arvpmagITGVAVAPEHRRRGVARALLREALAELRERGQPL----SALYPfePGFYRRFGY 124
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 62-131 4.53e-05

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 41.23  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  62 GKILATGMLDNDR-----------IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRSCGFCGEG 130
Cdd:PLN02706  64 GRIIATGSVFVERkfirncgkvghIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYVRKE 143


                 .
gi 655374630 131 I 131
Cdd:PLN02706 144 I 144
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-129 9.54e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.91  E-value: 9.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655374630  55 FYLIEHQGKILATGM--LDNDR--IEALFVHPQAMGQGLGRDLLAHLESLARERG---VTALTLESTLNAADFYRSCGFC 127
Cdd:PRK03624  47 FLVAEVGGEVVGTVMggYDGHRgwAYYLAVHPDFRGRGIGRALVARLEKKLIARGcpkINLQVREDNDAVLGFYEALGYE 126


                 ..
gi 655374630 128 GE 129
Cdd:PRK03624 127 EQ 128
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 80-126 3.57e-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: 3.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 655374630  80 VHPQAMGQGLGRDLLAHLESLARERGVTALT----LESTLNAadFYRSCGF 126
Cdd:COG1444  493 VHPALQRRGLGSRLLAEIREEAKEEGLDWLGvsfgATPELLR--FWQRNGF 541
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
75-135 6.00e-03

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 34.89  E-value: 6.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVTALTLESTLNAADFYRScgFCGEGISQYH 135
Cdd:PRK10146  79 IQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRF--YLREGYEQSH 137
PRK07922 PRK07922
amino-acid N-acetyltransferase;
75-126 8.44e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 34.90  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 655374630  75 IEALFVHPQAMGQGLGRDLLAHLESLARERGVT---ALTLEstlnaADFYRSCGF 126
Cdd:PRK07922  73 IRTVAVDPAARGRGVGHAIVERLLDVARELGLSrvfVLTFE-----VEFFARHGF 122
 
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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