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Conserved domains on  [gi|2156005851|ref|WP_230224861|]
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GNAT family N-acetyltransferase [Blastopirellula sediminis]

Protein Classification

GNAT family protein( domain architecture ID 106742)

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

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 2-149 4.29e-29

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 PRK09831:

Pssm-ID: 473072  Cd Length: 147  Bit Score: 104.27  E-value: 4.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   2 IRRYEPGDHTAIAEIFTRAIHEVASEVYTPAQCAAWSdkRPNPEHWKTRCEQKRPYVYVSEGRVAGFLELDDDgHIDCMY 81
Cdd:PRK09831    3 IRNYQPGDFQQLCAIFIRAVTMTASQHYSPQQIAAWA--QIDESRWKEKLAKSQVRVAVINAQPVGFITCIEH-YIDMLF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156005851  82 VHPEEVRKGIASALVDLAIENCVAagllrVFVEASHCARPVFEKKGFRVVEERQVALNGELLTNFAME 149
Cdd:PRK09831   80 VDPEYTRRGVASALLKPLIKSESE-----LTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFYMR 142
 
Name Accession Description Interval E-value
PRK09831 PRK09831
GNAT family N-acetyltransferase;
2-149 4.29e-29

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 104.27  E-value: 4.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   2 IRRYEPGDHTAIAEIFTRAIHEVASEVYTPAQCAAWSdkRPNPEHWKTRCEQKRPYVYVSEGRVAGFLELDDDgHIDCMY 81
Cdd:PRK09831    3 IRNYQPGDFQQLCAIFIRAVTMTASQHYSPQQIAAWA--QIDESRWKEKLAKSQVRVAVINAQPVGFITCIEH-YIDMLF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156005851  82 VHPEEVRKGIASALVDLAIENCVAagllrVFVEASHCARPVFEKKGFRVVEERQVALNGELLTNFAME 149
Cdd:PRK09831   80 VDPEYTRRGVASALLKPLIKSESE-----LTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFYMR 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 27-150 1.13e-21

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: 84.24  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  27 EVYTPAQCAAWsDKRPNPEHWKTRCEQKR--PYVYVSEGRVAGFLELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCV 104
Cdd:pfam13673   3 PDYSEEGIETF-YEFISPEALRERIDQGEyfFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2156005851 105 AAGLL--RVFVEASHCARPVFEKKGFRVVEERQVAlNGELLTNFAMEL 150
Cdd:pfam13673  82 KDGIKlsELTVNASPYAVPFYEKLGFRATGPEQEF-NGIRFVPMEKEL 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-153 5.83e-19

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: 77.72  E-value: 5.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   1 MIRRYEPGDHTAIAEIFTRAIHEVASEVYtpaqcaawsdkrpnpehwktrceqkrpYVYVSEGRVAGFLEL----DDDGH 76
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYALEEEIGEF---------------------------WVAEEDGEIVGCAALhpldEDLAE 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156005851  77 IDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRVVEERQV-ALNGELLTNFAMELPLD 153
Cdd:COG1246    55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLpYAKVWQRDSVVMEKDLE 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-114 4.36e-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: 49.97  E-value: 4.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2156005851  57 YVYVSEGRVAGFLEL------DDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVE 114
Cdd:cd04301     2 LVAEDDGEIVGFASLspdgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-134 5.01e-05

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: 40.78  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  57 YVYVSEGRVAGFLELD---DDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVE--ASH-CARPVFEKKGFRV 130
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQivlDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEvrVSNiAAQALYKKLGFNE 113


                  ....
gi 2156005851 131 VEER 134
Cdd:TIGR01575 114 IAIR 117
 
Name Accession Description Interval E-value
PRK09831 PRK09831
GNAT family N-acetyltransferase;
2-149 4.29e-29

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 104.27  E-value: 4.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   2 IRRYEPGDHTAIAEIFTRAIHEVASEVYTPAQCAAWSdkRPNPEHWKTRCEQKRPYVYVSEGRVAGFLELDDDgHIDCMY 81
Cdd:PRK09831    3 IRNYQPGDFQQLCAIFIRAVTMTASQHYSPQQIAAWA--QIDESRWKEKLAKSQVRVAVINAQPVGFITCIEH-YIDMLF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156005851  82 VHPEEVRKGIASALVDLAIENCVAagllrVFVEASHCARPVFEKKGFRVVEERQVALNGELLTNFAME 149
Cdd:PRK09831   80 VDPEYTRRGVASALLKPLIKSESE-----LTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFYMR 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 27-150 1.13e-21

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: 84.24  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  27 EVYTPAQCAAWsDKRPNPEHWKTRCEQKR--PYVYVSEGRVAGFLELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCV 104
Cdd:pfam13673   3 PDYSEEGIETF-YEFISPEALRERIDQGEyfFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2156005851 105 AAGLL--RVFVEASHCARPVFEKKGFRVVEERQVAlNGELLTNFAMEL 150
Cdd:pfam13673  82 KDGIKlsELTVNASPYAVPFYEKLGFRATGPEQEF-NGIRFVPMEKEL 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-153 5.83e-19

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: 77.72  E-value: 5.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   1 MIRRYEPGDHTAIAEIFTRAIHEVASEVYtpaqcaawsdkrpnpehwktrceqkrpYVYVSEGRVAGFLEL----DDDGH 76
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYALEEEIGEF---------------------------WVAEEDGEIVGCAALhpldEDLAE 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156005851  77 IDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRVVEERQV-ALNGELLTNFAMELPLD 153
Cdd:COG1246    55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLpYAKVWQRDSVVMEKDLE 132
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-152 3.34e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.88  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   1 MIRRYEPGDHTAIAEIFTRAIHEVAS----EVYTPAQCAAWSDKRPNPEHwktrceqkRPYVYVSEGRVAGFLEL----- 71
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAIAEGTAtfetEPPSEEEREAWFAAILAPGR--------PVLVAEEDGEVVGFASLgpfrp 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  72 -DDDGHI--DCMYVHPEEVRKGIASALVDLAIENCVAAGL--LRVFVEAS-HCARPVFEKKGFRVVEERQVA--LNGELL 143
Cdd:COG1247    75 rPAYRGTaeESIYVDPDARGRGIGRALLEALIERARARGYrrLVAVVLADnEASIALYEKLGFEEVGTLPEVgfKFGRWL 154


                  ....*....
gi 2156005851 144 TNFAMELPL 152
Cdd:COG1247   155 DLVLMQKRL 163
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-152 7.74e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 7.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   2 IRRYEPGDHTAIAEIFTRAihevasevYTPAQCAAWSDkrpnpeHWKTRCEQKRPYVYVSEGRVAGFLEL--------DD 73
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA--------FGPGREAELVD------RLREDPAAGLSLVAEDDGEIVGHVALspvdidgeGP 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2156005851  74 DGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRVVEERQVALNGElltNFAMELPL 152
Cdd:COG3153    67 ALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPD---EVFLAKEL 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 27-128 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: 57.53  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  27 EVYTPAQCAAWSDKRPNPEHWKTRCEQKRPYVYVSEGRVAGFLEL------DDDGHIDCMYVHPEEVRKGIASALVDLAI 100
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLsiiddePPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2156005851 101 ENCVAAGLLRVFVEASHC---ARPVFEKKGF 128
Cdd:pfam00583  86 EWARERGCERIFLEVAADnlaAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 57-150 4.03e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 57.37  E-value: 4.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  57 YVYVSEGRVAGFLEL----DDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEAS---HCARPVFEKKGFR 129
Cdd:COG0454    37 IAVDDKGEPIGFAGLrrldDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLdgnPAAIRFYERLGFK 116

                          90       100
                  ....*....|....*....|.
gi 2156005851 130 VVEERQVALNGElltnFAMEL 150
Cdd:COG0454   117 EIERYVAYVGGE----FEKEL 133
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-153 1.95e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  65 VAGFLELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHC---ARPVFEKKGFRVVEERQVALNGE 141
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYYGDD 83

                          90
                  ....*....|..
gi 2156005851 142 LLTnfaMELPLD 153
Cdd:COG0456    84 ALV---MEKELA 92
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-130 3.29e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.61  E-value: 3.29e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2156005851  57 YVYVSEGRVAGFLELDDDGHIDC-----MYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRV 130
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGAlaelrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-114 4.36e-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: 49.97  E-value: 4.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2156005851  57 YVYVSEGRVAGFLEL------DDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVE 114
Cdd:cd04301     2 LVAEDDGEIVGFASLspdgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
70-133 2.38e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.66  E-value: 2.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2156005851  70 ELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHC---ARPVFEKKGFRVVEE 133
Cdd:COG3393    11 ESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADnpaARRLYERLGFRPVGE 77
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
57-133 4.69e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.94  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  57 YVYVSEGRVAG----FLELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRVVE 132
Cdd:COG2153    37 LLAYDDGELVAtarlLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVG 116


                  .
gi 2156005851 133 E 133
Cdd:COG2153   117 E 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-134 5.01e-05

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: 40.78  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  57 YVYVSEGRVAGFLELD---DDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVE--ASH-CARPVFEKKGFRV 130
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQivlDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEvrVSNiAAQALYKKLGFNE 113


                  ....
gi 2156005851 131 VEER 134
Cdd:TIGR01575 114 IAIR 117
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 63-134 1.83e-04

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 38.46  E-value: 1.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2156005851  63 GRVAGFLELDDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAG--LLRVFVEASHCARPVFEKKGFRVVEER 134
Cdd:pfam08445  10 GELAAWCLRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGitPFAVVVAGNTPSRRLYEKLGFRKIDET 83
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-133 2.75e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   1 MIRRYEPGDHTAIAEIF---TRAIHEVASEVYTPAQCAAWSDKR-PNPEHWktrceqkrpyVYVSEGRVAGFLELDDDGH 76
Cdd:PRK10562    1 MIREYQPSDLPAILQLWlesTIWAHPFIKEQYWRESAPLVRDVYlPAAQTW----------VWEEDGKLLGFVSVLEGRF 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2156005851  77 IDCMYVHPEEVRKGIASALVDlAIENCVAAGLLRVFVEASHCARpVFEKKGFRVVEE 133
Cdd:PRK10562   71 VGALFVAPKAVRRGIGKALMQ-HVQQRYPHLSLEVYQKNQRAVN-FYHAQGFRIVDS 125
PRK07757 PRK07757
N-acetyltransferase;
57-132 3.28e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.64  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  57 YVYVSEGRVAGFLEL----DDDGHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFV---EashcaRPVFEKKGFR 129
Cdd:PRK07757   44 YVAEEEGEIVGCCALhilwEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFAltyQ-----PEFFEKLGFR 118


                  ...
gi 2156005851 130 VVE 132
Cdd:PRK07757  119 EVD 121
PTZ00330 PTZ00330
acetyltransferase; Provisional
 75-139 6.45e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.90  E-value: 6.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2156005851  75 GHIDCMYVHPEEVRKGIASALVDLAIENCVAAGLLRVFVEASHCARPVFEKKGFRvVEERQVALN 139
Cdd:PTZ00330   83 GHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFR-ACERQMRLD 146
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-154 5.00e-03

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: 35.75  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851   2 IRRYEPGDHTAIAEIFTRAihEVA----SEVYTPAQCAAWsdkrpnPEHWKTRCEQKRPYVYV----SEGRVAGFLEL-- 71
Cdd:COG1670    10 LRPLRPEDAEALAELLNDP--EVArylpGPPYSLEEARAW------LERLLADWADGGALPFAiedkEDGELIGVVGLyd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156005851  72 ----DDDGHIDcMYVHPEEVRKGIASALVDLAIENCVAA-GLLRVFVEASHC---ARPVFEKKGFRV--VEERQVALNGE 141
Cdd:COG1670    82 idraNRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDntaSIRVLEKLGFRLegTLRDALVIDGR 160

                         170
                  ....*....|...
gi 2156005851 142 LLTNFAMELPLDD 154
Cdd:COG1670   161 YRDHVLYSLLREE 173
 
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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