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Conserved domains on  [gi|484873958|gb|EOB20470|]
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ribosomal-protein-alanine acetyltransferase [Streptococcus pneumoniae 801]

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 ...
 14-138 4.93e-52

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: 161.34  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   14 AQAIYAVMIAVYPInPWTLEQIQADLSQDQTWYALAYDGAEVIGFLAVQENLFEAEVLQIAVKGAYQGQGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 484873958   94 TD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDPVEDAIIM 138
Cdd:TIGR01575  81 DEakgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 14-138 4.93e-52

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: 161.34  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   14 AQAIYAVMIAVYPInPWTLEQIQADLSQDQTWYALAYDGAEVIGFLAVQENLFEAEVLQIAVKGAYQGQGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 484873958   94 TD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDPVEDAIIM 138
Cdd:TIGR01575  81 DEakgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 57-143 3.83e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  57 GFLAVQENLF--EAEVLQIAVKGAYQGQGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYY 128
Cdd:COG0456    1 GFALLGLVDGgdEAEIEDLAVDPEYRGRGIGRALLEAALERarergaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*
gi 484873958 129 HDpveDAIIMKREID 143
Cdd:COG0456   81 GD---DALVMEKELA 92
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 29-138 2.56e-12

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 60.33  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  29 PWTLEQIQADLSQDQTWYALAYDGaEVIGFLAVQENLFEAEVLQIAVKGAYQGQGIASALFAQLPTDKE------IFLEV 102
Cdd:PRK09491  26 PWSEKTFASNQGERYLNLKLTVNG-QMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEkrgvatLWLEV 104

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 484873958 103 RQSNQRAQAFYKKEKMAVIAERKAYYHDPV--EDAIIM 138
Cdd:PRK09491 105 RASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-115 9.48e-10

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: 52.91  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   33 EQIQADLSQDQTWYALAYDGaEVIGFLA---VQENLFEAEVLQIAVKGAYQGQGIASALFAQL------PTDKEIFLEVR 103
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDG-ELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALlewareRGCERIFLEVA 101

                          90
                  ....*....|..
gi 484873958  104 QSNQRAQAFYKK 115
Cdd:pfam00583 102 ADNLAAIALYEK 113
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 46-92 9.98e-05

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: 38.41  E-value: 9.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 484873958  46 YALAYDGAEVIGFLAV---QENLFEAEVLQIAVKGAYQGQGIASALFAQL 92
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAA 50
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 14-138 4.93e-52

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: 161.34  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   14 AQAIYAVMIAVYPInPWTLEQIQADLSQDQTWYALAYDGAEVIGFLAVQENLFEAEVLQIAVKGAYQGQGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 484873958   94 TD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDPVEDAIIM 138
Cdd:TIGR01575  81 DEakgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 57-143 3.83e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  57 GFLAVQENLF--EAEVLQIAVKGAYQGQGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYY 128
Cdd:COG0456    1 GFALLGLVDGgdEAEIEDLAVDPEYRGRGIGRALLEAALERarergaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*
gi 484873958 129 HDpveDAIIMKREID 143
Cdd:COG0456   81 GD---DALVMEKELA 92
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 29-138 2.56e-12

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 60.33  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  29 PWTLEQIQADLSQDQTWYALAYDGaEVIGFLAVQENLFEAEVLQIAVKGAYQGQGIASALFAQLPTDKE------IFLEV 102
Cdd:PRK09491  26 PWSEKTFASNQGERYLNLKLTVNG-QMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEkrgvatLWLEV 104

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 484873958 103 RQSNQRAQAFYKKEKMAVIAERKAYYHDPV--EDAIIM 138
Cdd:PRK09491 105 RASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-115 9.48e-10

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: 52.91  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   33 EQIQADLSQDQTWYALAYDGaEVIGFLA---VQENLFEAEVLQIAVKGAYQGQGIASALFAQL------PTDKEIFLEVR 103
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDG-ELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALlewareRGCERIFLEVA 101

                          90
                  ....*....|..
gi 484873958  104 QSNQRAQAFYKK 115
Cdd:pfam00583 102 ADNLAAIALYEK 113
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-115 1.13e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.68  E-value: 1.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 484873958   48 LAYDGAEVIGFLAVQENLFEAEV--LQIAVKGAYQGQGIASALFAQL---PTDKEIFLEVRQSNQRAQAFYKK 115
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAeaaAKEGGIKLLELETTNRAAAFYEK 79
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-142 1.89e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 47.68  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   1 MIEIKRIQQRpDLAQ--AIYAVMI----AVYPINPWTLEQIQA---DLSQDQTWYALAYDGAEVIGFLAVQENL------ 65
Cdd:COG1247    1 EMTIRPATPE-DAPAiaAIYNEAIaegtATFETEPPSEEEREAwfaAILAPGRPVLVAEEDGEVVGFASLGPFRprpayr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  66 FEAEVlQIAVKGAYQGQGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKK---EKMAVIaERKAYYHDPVEDAI 136
Cdd:COG1247   80 GTAEE-SIYVDPDARGRGIGRALLEALIERarargyRRLVAVVLADNEASIALYEKlgfEEVGTL-PEVGFKFGRWLDLV 157


                 ....*.
gi 484873958 137 IMKREI 142
Cdd:COG1247  158 LMQKRL 163
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 30-127 9.73e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 45.04  E-value: 9.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  30 WTLEQIQADL-----SQDQTWYALAYDGAEVIGFLAVQE-NLFEAEVLQIAVKGAYQGQGIASALFAQLPTD------KE 97
Cdd:COG0454   15 LLIEALDAELkamegSLAGAEFIAVDDKGEPIGFAGLRRlDDKVLELKRLYVLPEYRGKGIGKALLEALLEWarergcTA 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 484873958  98 IFLEVRQSNQRAQAFYKKEKMAVIAERKAY 127
Cdd:COG0454   95 LELDTLDGNPAAIRFYERLGFKEIERYVAY 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-92 3.37e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 41.22  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  10 RPDLAQAIYAVMIAVYPINPW--TLEQIQADLSQDQTWyaLAYDGAEVIGFLAVQENLFE-----AEVLQIAVKGAYQGQ 82
Cdd:COG3153    5 TPEDAEAIAALLRAAFGPGREaeLVDRLREDPAAGLSL--VAEDDGEIVGHVALSPVDIDgegpaLLLGPLAVDPEYRGQ 82

                         90
                 ....*....|
gi 484873958  83 GIASALFAQL 92
Cdd:COG3153   83 GIGRALMRAA 92
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 10-143 7.17e-05

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: 39.98  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  10 RPDLAQAIYAVmiavypINPWTLEQiqadlsQDQTWYALAYDGaEVIGFLAVQ---ENLfeAEVLQIAVKGAYQGQGIAS 86
Cdd:COG1246    7 TPDDVPAILEL------IRPYALEE------EIGEFWVAEEDG-EIVGCAALHpldEDL--AELRSLAVHPDYRGRGIGR 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 484873958  87 ALFAQLPTD------KEIFLEvrqSNQRAQAFYKKEKMAVIAERKAYYHDPVE-DAIIMKREID 143
Cdd:COG1246   72 RLLEALLAEarelglKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYAKVWQrDSVVMEKDLE 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 46-92 9.98e-05

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: 38.41  E-value: 9.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 484873958  46 YALAYDGAEVIGFLAV---QENLFEAEVLQIAVKGAYQGQGIASALFAQL 92
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAA 50
PRK10562 PRK10562
putative acetyltransferase; Provisional
 39-138 1.17e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 39.67  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  39 LSQDQTWyaLAYDGAEVIGFLAVQENLFEAEVLqiaVKGAYQGQGIASALF----AQLPTdkeIFLEVRQSNQRAQAFYK 114
Cdd:PRK10562  45 LPAAQTW--VWEEDGKLLGFVSVLEGRFVGALF---VAPKAVRRGIGKALMqhvqQRYPH---LSLEVYQKNQRAVNFYH 116

                         90       100
                 ....*....|....*....|....
gi 484873958 115 KEKMAViaERKAYYHDPVEDAIIM 138
Cdd:PRK10562 117 AQGFRI--VDSAWQEETQHPTWIM 138
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-144 1.35e-04

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: 39.98  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  10 RPDLAQAIYAVM----IAVY-PINPWTLEQIQADLS------QDQTWYALA---YDGAEVIGFLAVQENLFEAEVLQIA- 74
Cdd:COG1670   14 RPEDAEALAELLndpeVARYlPGPPYSLEEARAWLErlladwADGGALPFAiedKEDGELIGVVGLYDIDRANRSAEIGy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958  75 -VKGAYQGQGIASAL--------FAQLPTDKeIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYH--DPVEDAIIMKREID 143
Cdd:COG1670   94 wLAPAYWGKGYATEAlralldyaFEELGLHR-VEAEVDPDNTASIRVLEKLGFRLEGTLRDALVidGRYRDHVLYSLLRE 172


                 .
gi 484873958 144 E 144
Cdd:COG1670  173 E 173
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-115 4.11e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.20  E-value: 4.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 484873958  68 AEVLQIAVKGAYQGQGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKK 115
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREalargaRTPFLYVDADNPAARRLYER 69
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 33-115 1.15e-03

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: 36.87  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 484873958   33 EQIQADLSQDQTWYALAYDGAEVIGFLAVQEN-----LFeaevlqiaVKGAYQGQGIASALFAQLPT------DKEIFLE 101
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIALRDRghislLF--------VDPDYQGQGIGKALLEAVEDyaekdgIKLSELT 91

                          90
                  ....*....|....
gi 484873958  102 VRQSNQrAQAFYKK 115
Cdd:pfam13673  92 VNASPY-AVPFYEK 104
PRK07757 PRK07757
N-acetyltransferase;
46-88 3.93e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 3.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 484873958  46 YALAYDGAEVIGFLAVQ---ENLfeAEVLQIAVKGAYQGQGIASAL 88
Cdd:PRK07757  43 FYVAEEEGEIVGCCALHilwEDL--AEIRSLAVSEDYRGQGIGRML 86
 
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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