NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446294903|ref|WP_000372758|]
View 

MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Staphylococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 18-148 2.46e-32

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: 111.65  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   18 DVPQVFDLERRSFNdSSWTIDAFYHEIeQNNFAKYFVLEFEQQIIGYLGLWIVIDQAQITTVAIDDNYRGYGLGQMLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446294903   98 GINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYYGEG-EDAMVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPgEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 18-148 2.46e-32

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: 111.65  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   18 DVPQVFDLERRSFNdSSWTIDAFYHEIeQNNFAKYFVLEFEQQIIGYLGLWIVIDQAQITTVAIDDNYRGYGLGQMLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446294903   98 GINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYYGEG-EDAMVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPgEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-153 8.24e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.85  E-value: 8.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  63 GYLGLWIVIDQ--AQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYY 139
Cdd:COG0456    1 GFALLGLVDGGdeAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 446294903 140 geGEDAMVMWVNLN 153
Cdd:COG0456   81 --GDDALVMEKELA 92
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-148 8.54e-17

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 72.27  E-value: 8.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  10 NIREMTKEDVPQVFDLERRS--FndsSWTIDAFYheieQNNFAKY--FVLEFEQQIIGYLGLWIVIDQAQITTVAIDDNY 85
Cdd:PRK09491   3 TISSLTPADLPAAYHIEQRAhaF---PWSEKTFA----SNQGERYlnLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446294903  86 RGYGLGQMLLKYGINYASHTcDVMSL--EVRVNNKVAQHVYENLGFQYGGKRKNYY--GEG-EDAMVM 148
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEKR-GVATLwlEVRASNAAAIALYESLGFNEVTIRRNYYptADGrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 19-129 1.20e-16

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: 71.01  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   19 VPQVFDLERRSFNDSSWTIDAFYH-EIEQNNFAKYFVLEFEQQIIGYLGLWIV---IDQAQITTVAIDDNYRGYGLGQML 94
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLeDWDEDASEGFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446294903   95 LKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGF 129
Cdd:pfam00583  81 LQALLEWArERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 1.23e-07

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: 46.11  E-value: 1.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446294903  52 YFVLEFEQQIIGYLGLWI---VIDQAQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEArERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 18-148 2.46e-32

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: 111.65  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   18 DVPQVFDLERRSFNdSSWTIDAFYHEIeQNNFAKYFVLEFEQQIIGYLGLWIVIDQAQITTVAIDDNYRGYGLGQMLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446294903   98 GINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYYGEG-EDAMVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPgEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-153 8.24e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.85  E-value: 8.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  63 GYLGLWIVIDQ--AQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYY 139
Cdd:COG0456    1 GFALLGLVDGGdeAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 446294903 140 geGEDAMVMWVNLN 153
Cdd:COG0456   81 --GDDALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
11-148 8.47e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 72.04  E-value: 8.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  11 IREMTKEDVPQVFDLERRSFNDSsWTIDAFYHEIEQNNFAKYFVLEFEQQIIGYLGLWIV-----IDQAQITTVAIDDNY 85
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPG-REAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446294903  86 RGYGLGQMLLKYGINYA-SHTCDVMSLEVrvnNKVAQHVYENLGFQYGGKRKNYYGEGEDAMVM 148
Cdd:COG3153   80 RGQGIGRALMRAALEAArERGARAVVLLG---DPSLLPFYERFGFRPAGELGLTLGPDEVFLAK 140
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-148 8.54e-17

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 72.27  E-value: 8.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  10 NIREMTKEDVPQVFDLERRS--FndsSWTIDAFYheieQNNFAKY--FVLEFEQQIIGYLGLWIVIDQAQITTVAIDDNY 85
Cdd:PRK09491   3 TISSLTPADLPAAYHIEQRAhaF---PWSEKTFA----SNQGERYlnLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446294903  86 RGYGLGQMLLKYGINYASHTcDVMSL--EVRVNNKVAQHVYENLGFQYGGKRKNYY--GEG-EDAMVM 148
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEKR-GVATLwlEVRASNAAAIALYESLGFNEVTIRRNYYptADGrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 19-129 1.20e-16

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: 71.01  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   19 VPQVFDLERRSFNDSSWTIDAFYH-EIEQNNFAKYFVLEFEQQIIGYLGLWIV---IDQAQITTVAIDDNYRGYGLGQML 94
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLeDWDEDASEGFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446294903   95 LKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGF 129
Cdd:pfam00583  81 LQALLEWArERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
9-152 9.84e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 69.64  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   9 LNIREMTKEDVPQVFDLERRSFNDSSWT----------IDAFYHEIEQNNFAkYFVLEFEQQIIGY--LGLWIVIDQAQI 76
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATfeteppseeeREAWFAAILAPGRP-VLVAEEDGEVVGFasLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  77 T---TVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGGKRKNYY---GEGEDAMVMW 149
Cdd:COG1247   81 TaeeSIYVDPDARGRGIGRALLEALIERArARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGfkfGRWLDLVLMQ 160


                 ...
gi 446294903 150 VNL 152
Cdd:COG1247  161 KRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-148 1.13e-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: 67.33  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   7 EQLNIREMTKEDVPQVFDLERR------------SFNDSSWTIDAFYHEIEQNNFAKYFVLEFE-QQIIGYLGLWIVIDQ 73
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDpevarylpgppySLEEARAWLERLLADWADGGALPFAIEDKEdGELIGVVGLYDIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  74 AQITTVA--IDDNYRGYGLGQMLLKYGINYASHTCDV--MSLEVRVNNKVAQHVYENLGFQYGGKRKNYY---GEGEDAM 146
Cdd:COG1670   86 NRSAEIGywLAPAYWGKGYATEALRALLDYAFEELGLhrVEAEVDPDNTASIRVLEKLGFRLEGTLRDALvidGRYRDHV 165


                 ..
gi 446294903 147 VM 148
Cdd:COG1670  166 LY 167
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 11-153 1.02e-13

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: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  11 IREMTKEDVPQVFDLERRSfndsswtidAFYHEIEQnnfakYFVLEFEQQIIGYLGLWIVI-DQAQITTVAIDDNYRGYG 89
Cdd:COG1246    3 IRPATPDDVPAILELIRPY---------ALEEEIGE-----FWVAEEDGEIVGCAALHPLDeDLAELRSLAVHPDYRGRG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446294903  90 LGQMLLKYGINYA-SHTCDVMSLEVRVNnkvAQHVYENLGFQYGGKRKNYYGEGE--DAMVMWVNLN 153
Cdd:COG1246   69 IGRRLLEALLAEArELGLKRLFLLTTSA---AIHFYEKLGFEEIDKEDLPYAKVWqrDSVVMEKDLE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-130 1.03e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.46  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   50 AKYFVLEFEQQIIGYLGLWIVIDQAQIT--TVAIDDNYRGYGLGQMLLKYgINYASHTCDVMSLEVRVNNKvAQHVYENL 127
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELETTNR-AAAFYEKL 80


                  ...
gi 446294903  128 GFQ 130
Cdd:pfam13508  81 GFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 11-130 6.89e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.21  E-value: 6.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  11 IREMTKEDVPqvFDLERRSFNDsswTIDAFYheiEQNNFAKYFVLEFEQQIIGYLGLWIVIDQ-AQITTVAIDDNYRGYG 89
Cdd:COG0454    3 IRKATPEDIN--FILLIEALDA---ELKAME---GSLAGAEFIAVDDKGEPIGFAGLRRLDDKvLELKRLYVLPEYRGKG 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446294903  90 LGQMLLKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQ 130
Cdd:COG0454   75 IGKALLEALLEWArERGCTALELDTLDGNPAAIRFYERLGFK 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 38-130 1.19e-08

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: 50.35  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   38 DAFYHEIEQNNFaKYFVLEFEQQIIGYLGLwivIDQAQITTVAIDDNYRGYGLGQMLLKYGINYAsHTCDVMSLEVRVN- 116
Cdd:pfam13673  20 EALRERIDQGEY-FFFVAFEGGQIVGVIAL---RDRGHISLLFVDPDYQGQGIGKALLEAVEDYA-EKDGIKLSELTVNa 94

                          90
                  ....*....|....
gi 446294903  117 NKVAQHVYENLGFQ 130
Cdd:pfam13673  95 SPYAVPFYEKLGFR 108
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 1.23e-07

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: 46.11  E-value: 1.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446294903  52 YFVLEFEQQIIGYLGLWI---VIDQAQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEArERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
74-133 1.38e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.44  E-value: 1.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446294903  74 AQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLEVRVNNKVAQHVYENLGFQYGG 133
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDADNPAARRLYERLGFRPVG 76
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
53-130 5.15e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.25  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903  53 FVLEFEQQIIGYLGL-WIVIDQAQITTVAIDDNYRGYGLGQMLLKYGINYA-SHTCDVMSLEVRVNnkvAQHVYENLGFQ 130
Cdd:COG2153   37 LLAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEArERGARRIVLSAQAH---AVGFYEKLGFV 113
PRK07757 PRK07757
N-acetyltransferase;
52-94 2.98e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 41.72  E-value: 2.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446294903  52 YFVLEFEQQIIGYLGLWIV-IDQAQITTVAIDDNYRGYGLGQML 94
Cdd:PRK07757  43 FYVAEEEGEIVGCCALHILwEDLAEIRSLAVSEDYRGQGIGRML 86
PRK10514 PRK10514
putative acetyltransferase; Provisional
 9-134 1.73e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.22  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   9 LNIREMTKEDVPQVFDLERRSfndsswtIDAFYHEIEQNNFAkyfvlEFEQQIIGYLG---LWIVIDQA----------- 74
Cdd:PRK10514   2 ISIRRSRHEEGERLVAIWRRS-------VDATHDFLSAEDRA-----EIEELVRSFLPeapLWVAVDERdqpvgfmllsg 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446294903  75 -QITTVAIDDNYRGYGLGQMLLKYGINYASHtcdvMSLEVRVNNKVAQHVYENLGFQYGGK 134
Cdd:PRK10514  70 gHMEALFVDPDVRGCGVGRMLVEHALSLHPE----LTTDVNEQNEQAVGFYKKMGFKVTGR 126
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-102 6.97e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.55  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   11 IREMTKEDVPQVFDLERRSFNDS-SWTIDAFYHEIEQNNfaKYFVLEFEQQIIGYLGLWI--------VIDQAQITTVAI 81
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAFQDEdSPELREYFRPLLEEG--RVLGAFDDGELVSTLALYPfelnvpgkTLPAAGITGVAT 78

                          90       100
                  ....*....|....*....|.
gi 446294903   82 DDNYRGYGLGQMLLKYGINYA 102
Cdd:pfam13527  79 YPEYRGRGVMSRLLRRSLEEM 99
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 38-148 8.82e-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: 37.34  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   38 DAFYHEIEQNNFAKYFVLEFEQQIIGYLGLWIVIDQAQITTVAIDDN-YRGYGLGQMLLKYGINYASHT--CDVMSLEVR 114
Cdd:TIGR03585  39 LHFIEALKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYANpFCKPGVGSVLEEAALEYAFEHlgLHKLSLEVL 118

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446294903  115 VNNKVAQHVYENLGFQYGGKRKNyYGEGEDAMVM 148
Cdd:TIGR03585 119 ESNNKALKLYEKFGFEREGVFRQ-GGEYYDVLLM 151
Eis COG4552
Predicted acetyltransferase [General function prediction only];
9-96 3.49e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.42  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446294903   9 LNIREMTKEDVPQVFDLERRSFNDsSWTIDAFYHEIEQNNFAKYFVLEFEQQIIGYLGLW--------IVIDQAQITTVA 80
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGP-EPDDEELEAYRPLLEPGRVLGVFDDGELVGTLALYpftlnvggARVPMAGITGVA 79

                         90
                 ....*....|....*.
gi 446294903  81 IDDNYRGYGLGQMLLK 96
Cdd:COG4552   80 VAPEHRRRGVARALLR 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH