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Conserved domains on  [gi|446491967|ref|WP_000569821|]
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ribosomal protein S18-alanine N-acetyltransferase [Streptococcus pneumoniae]

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 4.88e-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: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967   14 AKAIYAVMIAVYPVsPWTLEQIQADLFQDQTWYALAYDGAEVIGFLAVQETLFEAEVLQIAVKGAYQGKGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446491967   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 4.88e-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: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967   14 AKAIYAVMIAVYPVsPWTLEQIQADLFQDQTWYALAYDGAEVIGFLAVQETLFEAEVLQIAVKGAYQGKGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446491967   94 TD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDPVEDAIIM 138
Cdd:TIGR01575  81 DEakgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-143 6.48e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 6.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  67 EAEVLQIAVKGAYQGKGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDpveDAIIMKR 140
Cdd:COG0456   13 EAEIEDLAVDPEYRGRGIGRALLEAALERarergaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALVMEK 89


                 ...
gi 446491967 141 EID 143
Cdd:COG0456   90 ELA 92
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 46-138 1.24e-12

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 61.10  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  46 YALAYDGaEVIGFLAVQETLFEAEVLQIAVKGAYQGKGIASALFAQLPTDKE------IFLEVRQSNQRAQAFYKKEKMA 119
Cdd:PRK09491  43 LKLTVNG-QMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEkrgvatLWLEVRASNAAAIALYESLGFN 121

                         90       100
                 ....*....|....*....|.
gi 446491967 120 VIAERKAYYHDPV--EDAIIM 138
Cdd:PRK09491 122 EVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-115 6.90e-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: 53.29  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967   33 EQIQADLFQDQTWYALAYDGaEVIGFLA---VQETLFEAEVLQIAVKGAYQGKGIASALFAQL------PTDKEIFLEVR 103
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDG-ELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALlewareRGCERIFLEVA 101

                          90
                  ....*....|..
gi 446491967  104 QSNQRAQAFYKK 115
Cdd:pfam00583 102 ADNLAAIALYEK 113
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 46-92 1.39e-04

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: 38.03  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446491967  46 YALAYDGAEVIGFLAV---QETLFEAEVLQIAVKGAYQGKGIASALFAQL 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 4.88e-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: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967   14 AKAIYAVMIAVYPVsPWTLEQIQADLFQDQTWYALAYDGAEVIGFLAVQETLFEAEVLQIAVKGAYQGKGIASALFAQLP 93
Cdd:TIGR01575   2 LKAVLEIEAAAFAF-PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446491967   94 TD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDPVEDAIIM 138
Cdd:TIGR01575  81 DEakgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-143 6.48e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 6.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  67 EAEVLQIAVKGAYQGKGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYHDpveDAIIMKR 140
Cdd:COG0456   13 EAEIEDLAVDPEYRGRGIGRALLEAALERarergaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALVMEK 89


                 ...
gi 446491967 141 EID 143
Cdd:COG0456   90 ELA 92
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 46-138 1.24e-12

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 61.10  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  46 YALAYDGaEVIGFLAVQETLFEAEVLQIAVKGAYQGKGIASALFAQLPTDKE------IFLEVRQSNQRAQAFYKKEKMA 119
Cdd:PRK09491  43 LKLTVNG-QMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEkrgvatLWLEVRASNAAAIALYESLGFN 121

                         90       100
                 ....*....|....*....|.
gi 446491967 120 VIAERKAYYHDPV--EDAIIM 138
Cdd:PRK09491 122 EVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 33-115 6.90e-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: 53.29  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967   33 EQIQADLFQDQTWYALAYDGaEVIGFLA---VQETLFEAEVLQIAVKGAYQGKGIASALFAQL------PTDKEIFLEVR 103
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDG-ELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALlewareRGCERIFLEVA 101

                          90
                  ....*....|..
gi 446491967  104 QSNQRAQAFYKK 115
Cdd:pfam00583 102 ADNLAAIALYEK 113
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-115 1.24e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491967   48 LAYDGAEVIGFLAVQETLFEAEV--LQIAVKGAYQGKGIASALFAQL---PTDKEIFLEVRQSNQRAQAFYKK 115
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAeaaAKEGGIKLLELETTNRAAAFYEK 79
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 28-127 1.65e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 47.36  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  28 SPWTLEQIQADLFQ-----DQTWYALAYDGAEVIGFLAVQETLFE-AEVLQIAVKGAYQGKGIASALFAQLPTD------ 95
Cdd:COG0454   13 FILLIEALDAELKAmegslAGAEFIAVDDKGEPIGFAGLRRLDDKvLELKRLYVLPEYRGKGIGKALLEALLEWarergc 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446491967  96 KEIFLEVRQSNQRAQAFYKKEKMAVIAERKAY 127
Cdd:COG0454   93 TALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
16-142 1.10e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 45.37  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  16 AIYAVMI----AVYPVSPWTLEQIQA---DLFQDQTWYALAYDGAEVIGFLAVQETL------FEAEVlQIAVKGAYQGK 82
Cdd:COG1247   17 AIYNEAIaegtATFETEPPSEEEREAwfaAILAPGRPVLVAEEDGEVVGFASLGPFRprpayrGTAEE-SIYVDPDARGR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491967  83 GIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKK---EKMAVIaERKAYYHDPVEDAIIMKREI 142
Cdd:COG1247   96 GIGRALLEALIERarargyRRLVAVVLADNEASIALYEKlgfEEVGTL-PEVGFKFGRWLDLVLMQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 25-144 2.29e-05

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: 41.91  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  25 YPVSPWTLEQIQADL------FQDQTWYALA---YDGAEVIGFLAVQETLFEAEVLQIA--VKGAYQGKGIASAL----- 88
Cdd:COG1670   34 LPGPPYSLEEARAWLerlladWADGGALPFAiedKEDGELIGVVGLYDIDRANRSAEIGywLAPAYWGKGYATEAlrall 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491967  89 ---FAQLPTDKeIFLEVRQSNQRAQAFYKKEKMAVIAERKAYYH--DPVEDAIIMKREIDE 144
Cdd:COG1670  114 dyaFEELGLHR-VEAEVDPDNTASIRVLEKLGFRLEGTLRDALVidGRYRDHVLYSLLREE 173
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-92 2.57e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 41.61  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  10 QPDLAKAIYAVMIAVYPVSPW--TLEQIQADLFQDQTWyaLAYDGAEVIGFLAVQETLFE-----AEVLQIAVKGAYQGK 82
Cdd:COG3153    5 TPEDAEAIAALLRAAFGPGREaeLVDRLREDPAAGLSL--VAEDDGEIVGHVALSPVDIDgegpaLLLGPLAVDPEYRGQ 82

                         90
                 ....*....|
gi 446491967  83 GIASALFAQL 92
Cdd:COG3153   83 GIGRALMRAA 92
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 46-92 1.39e-04

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: 38.03  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446491967  46 YALAYDGAEVIGFLAV---QETLFEAEVLQIAVKGAYQGKGIASALFAQL 92
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAA 50
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-143 2.21e-04

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: 38.82  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  46 YALAYDGAEVIGFLAVqETLFE--AEVLQIAVKGAYQGKGIASALFAQLPTD------KEIFLEvrqSNQRAQAFYKKEK 117
Cdd:COG1246   30 FWVAEEDGEIVGCAAL-HPLDEdlAELRSLAVHPDYRGRGIGRRLLEALLAEarelglKRLFLL---TTSAAIHFYEKLG 105

                         90       100
                 ....*....|....*....|....*..
gi 446491967 118 MAVIAERKAYYHDPVE-DAIIMKREID 143
Cdd:COG1246  106 FEEIDKEDLPYAKVWQrDSVVMEKDLE 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-115 3.67e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.20  E-value: 3.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446491967  68 AEVLQIAVKGAYQGKGIASALFAQLPTD------KEIFLEVRQSNQRAQAFYKK 115
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREalargaRTPFLYVDADNPAARRLYER 69
PRK10562 PRK10562
putative acetyltransferase; Provisional
 39-138 4.34e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.12  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491967  39 LFQDQTWyaLAYDGAEVIGFLAVQETLFEAEVLqiaVKGAYQGKGIASALF----AQLPTdkeIFLEVRQSNQRAQAFYK 114
Cdd:PRK10562  45 LPAAQTW--VWEEDGKLLGFVSVLEGRFVGALF---VAPKAVRRGIGKALMqhvqQRYPH---LSLEVYQKNQRAVNFYH 116

                         90       100
                 ....*....|....*....|....
gi 446491967 115 KEKMAViaERKAYYHDPVEDAIIM 138
Cdd:PRK10562 117 AQGFRI--VDSAWQEETQHPTWIM 138
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 48-115 5.39e-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: 34.94  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491967   48 LAYDGAEVIGFLAVQET-----LFeaevlqiaVKGAYQGKGIASALFAQLPT------DKEIFLEVRQSNQrAQAFYKK 115
Cdd:pfam13673  35 VAFEGGQIVGVIALRDRghislLF--------VDPDYQGQGIGKALLEAVEDyaekdgIKLSELTVNASPY-AVPFYEK 104
 
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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