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Conserved domains on  [gi|82178405|sp|Q58ED9|]
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RecName: Full=N-alpha-acetyltransferase 20; AltName: Full=Methionine N-acetyltransferase; AltName: Full=N-acetyltransferase 5; AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20; AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5; Short=NatB complex subunit NAT5; AltName: Full=NatB catalytic subunit

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-128 1.84e-17

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: 73.71  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    12 LFKFNNINLDPLTETYGIPFY---LQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGL 88
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdllEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 82178405    89 AAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGY 128
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-128 1.84e-17

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: 73.71  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    12 LFKFNNINLDPLTETYGIPFY---LQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGL 88
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdllEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 82178405    89 AAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGY 128
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-157 6.04e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 6.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  55 GYIMGkaegSVAREEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTV 134
Cdd:COG0456   1 GFALL----GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76

                        90       100
                ....*....|....*....|...
gi 82178405 135 IEYYsasngepDEDAYDMRKALS 157
Cdd:COG0456  77 PNYY-------GDDALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 22-152 1.13e-14

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: 66.97  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    22 PLTETYGIPFYLQYLAHWpeyfIVAEApGGELMGYIMGkaegSVAREEwhGHVTALSVAPEFRRLGLAAKLMEMLEEISE 101
Cdd:TIGR01575  16 PWTEAQFAEELANYHLCY----LLARI-GGKVVGYAGV----QIVLDE--AHILNIAVKPEYQGQGIGRALLRELIDEAK 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 82178405   102 RKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSasngEPDEDAYDM 152
Cdd:TIGR01575  85 GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
 36-130 1.76e-12

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 61.48  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405   36 LAHWPEYFIVAEApGGELMGYIMGKAEGsvareewH-GHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRV 114
Cdd:PRK03624  40 LNHDPSLFLVAEV-GGEVVGTVMGGYDG-------HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVRE 111

                         90
                 ....*....|....*.
gi 82178405  115 SNQVAVNMYKQLGYSV 130
Cdd:PRK03624 112 DNDAVLGFYEALGYEE 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-110 4.40e-08

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: 47.66  E-value: 4.40e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82178405  43 FIVAEApGGELMGYIMGKAEGSVAReewHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDL 110
Cdd:cd04301   1 FLVAED-DGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-128 1.84e-17

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: 73.71  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    12 LFKFNNINLDPLTETYGIPFY---LQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGL 88
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdllEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 82178405    89 AAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGY 128
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-157 6.04e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 6.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  55 GYIMGkaegSVAREEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTV 134
Cdd:COG0456   1 GFALL----GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76

                        90       100
                ....*....|....*....|...
gi 82178405 135 IEYYsasngepDEDAYDMRKALS 157
Cdd:COG0456  77 PNYY-------GDDALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 22-152 1.13e-14

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: 66.97  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    22 PLTETYGIPFYLQYLAHWpeyfIVAEApGGELMGYIMGkaegSVAREEwhGHVTALSVAPEFRRLGLAAKLMEMLEEISE 101
Cdd:TIGR01575  16 PWTEAQFAEELANYHLCY----LLARI-GGKVVGYAGV----QIVLDE--AHILNIAVKPEYQGQGIGRALLRELIDEAK 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 82178405   102 RKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSasngEPDEDAYDM 152
Cdd:TIGR01575  85 GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
 36-130 1.76e-12

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 61.48  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405   36 LAHWPEYFIVAEApGGELMGYIMGKAEGsvareewH-GHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRV 114
Cdd:PRK03624  40 LNHDPSLFLVAEV-GGEVVGTVMGGYDG-------HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVRE 111

                         90
                 ....*....|....*.
gi 82178405  115 SNQVAVNMYKQLGYSV 130
Cdd:PRK03624 112 DNDAVLGFYEALGYEE 127
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
63-137 6.13e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 53.37  E-value: 6.13e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82178405  63 GSVAREEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEY 137
Cdd:COG3393   7 GVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-130 1.93e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    41 EYFIVAEApGGELMGYIMGKAEGSVAREEWHGhvtaLSVAPEFRRLGLAAKLMEMLEEISERKGgffVDLFVRVSNQVAV 120
Cdd:pfam13508   3 GRFFVAED-DGKIVGFAALLPLDDEGALAELR----LAVHPEYRGQGIGRALLEAAEAAAKEGG---IKLLELETTNRAA 74

                          90
                  ....*....|
gi 82178405   121 NMYKQLGYSV 130
Cdd:pfam13508  75 AFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
40-156 1.89e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.85  E-value: 1.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  40 PEYFIVAEApGGELMGYIMGkAEGSVAREEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGgffVDLFVRVSNQVA 119
Cdd:COG3153  38 AGLSLVAED-DGEIVGHVAL-SPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG---ARAVVLLGDPSL 112

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 82178405 120 VNMYKQLGYSVYRTVieyysasNGEPDEDAYDMRKAL 156
Cdd:COG3153 113 LPFYERFGFRPAGEL-------GLTLGPDEVFLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-110 4.40e-08

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: 47.66  E-value: 4.40e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82178405  43 FIVAEApGGELMGYIMGKAEGSVAReewHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDL 110
Cdd:cd04301   1 FLVAED-DGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
42-156 6.92e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.61  E-value: 6.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  42 YFIVAEApGGELMGYimgkAEGSVAREEWHGHVTA---LSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQV 118
Cdd:COG1247  53 PVLVAEE-DGEVVGF----ASLGPFRPRPAYRGTAeesIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEA 127

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 82178405 119 AVNMYKQLGYSVYRTVIEYYSASNGEPDEdaYDMRKAL 156
Cdd:COG1247 128 SIALYEKLGFEEVGTLPEVGFKFGRWLDL--VLMQKRL 163
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
79-157 1.07e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  79 VAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSnqvAVNMYKQLGYSVYrtvieyysasnGEPDEDA----YDMRK 154
Cdd:COG2153  66 VLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPV-----------GEEFLEAgiphIDMRK 131


                ...
gi 82178405 155 ALS 157
Cdd:COG2153 132 PLS 134
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 42-128 1.44e-07

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: 48.04  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405    42 YFIVAEApGGELMGYImgkaegSVAReewHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQvAVN 121
Cdd:pfam13673  32 FFFVAFE-GGQIVGVI------ALRD---RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVP 100


                  ....*..
gi 82178405   122 MYKQLGY 128
Cdd:pfam13673 101 FYEKLGF 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 41-137 2.92e-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: 2.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  41 EYFIVAEApGGELMGYIMGKAEGsvareEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQVAV 120
Cdd:COG0454  34 AEFIAVDD-KGEPIGFAGLRRLD-----DKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAI 107

                        90
                ....*....|....*..
gi 82178405 121 NMYKQLGYSVYRTVIEY 137
Cdd:COG0454 108 RFYERLGFKEIERYVAY 124
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 43-130 3.71e-07

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: 46.91  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  43 FIVAEApGGELMGYImgkaeGSVAREEWHGHVTALSVAPEFRRLGLAAKLMEMLEEISERKGgfFVDLFVrVSNQVAVNM 122
Cdd:COG1246  30 FWVAEE-DGEIVGCA-----ALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG--LKRLFL-LTTSAAIHF 100


                ....*...
gi 82178405 123 YKQLGYSV 130
Cdd:COG1246 101 YEKLGFEE 108
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 77-152 1.31e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.69  E-value: 1.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82178405   77 LSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGY---SVYRtviEYYSASNGEpdEDAYDM 152
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFnevTIRR---NYYPTADGR--EDAIIM 142
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-155 3.05e-06

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: 44.99  E-value: 3.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405   3 TLRAFTCDDLFKFNNINLDPLTETYGIP----------FYLQYLAHWPE----YFIVAEAPGGELMGYImgkaegSVARE 68
Cdd:COG1670   9 RLRPLRPEDAEALAELLNDPEVARYLPGppysleearaWLERLLADWADggalPFAIEDKEDGELIGVV------GLYDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82178405  69 EWHGHVT--ALSVAPEFRRLGLAAKLMEMLEEISERKGGF-FVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEP 145
Cdd:COG1670  83 DRANRSAeiGYWLAPAYWGKGYATEALRALLDYAFEELGLhRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162

                       170
                ....*....|
gi 82178405 146 DEDAYDMRKA 155
Cdd:COG1670 163 DHVLYSLLRE 172
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 72-133 2.63e-05

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: 40.78  E-value: 2.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82178405    72 GHVTALSVAPEFRRLGLAAKLM-EMLEEISERkgGFFVDLFVRVSNQVAVNMYKQLGYSVYRT 133
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVaALARGIAER--GITPFAVVVAGNTPSRRLYEKLGFRKIDE 82
Eis COG4552
Predicted acetyltransferase [General function prediction only];
72-102 1.33e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 38.34  E-value: 1.33e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 82178405  72 GHVTALSVAPEFRRLGLAAKLM-EMLEEISER 102
Cdd:COG4552  73 AGITGVAVAPEHRRRGVARALLrEALAELRER 104
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 72-130 7.46e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 34.85  E-value: 7.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 82178405    72 GHVTALSVAPEFRRLGLAAKLMEMLEEISERKGGFFVDLFVRvsnqvAVNMYKQLGYSV 130
Cdd:pfam13527  71 AGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYPS-----SYPIYRRFGYEI 124
 
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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