NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17553596|ref|NP_498219|]
View 

N-terminal methionine N(alpha)-acetyltransferase NatE [Caenorhabditis elegans]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-166 2.38e-17

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.38  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  80 ETGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYQRcsppDA 159
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD----DA 84


                ....*..
gi 17553596 160 FIMRKPF 166
Cdd:COG0456  85 LVMEKEL 91
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-166 2.38e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.38  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  80 ETGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYQRcsppDA 159
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD----DA 84


                ....*..
gi 17553596 160 FIMRKPF 166
Cdd:COG0456  85 LVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 30-141 1.02e-15

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: 69.08  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    30 IKTVRILVSSIFPVSYSDKFYQE-----CMNNELTGVVIRNGEAIAIVAVKPENFEtGRVLYIRSFGVHPRHREAGLGSF 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLledwdEDASEGFFVAEEDGELVGFASLSIIDDE-PPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17553596   105 LMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGF 141
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-124 2.25e-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: 48.43  E-value: 2.25e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17553596  61 VVIRNGEAIAIVAVKPENFEtGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLH 124
Cdd:cd04301   3 VAEDDGEIVGFASLSPDGSG-GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 41-162 6.24e-07

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: 46.17  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    41 FPVSYSDKFYQECMNNELTG--VVIRNGEAIAIVAVKPENFETgrvlYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKL 118
Cdd:TIGR01575  13 FAFPWTEAQFAEELANYHLCylLARIGGKVVGYAGVQIVLDEA----HILNIAVKPEYQGQGIGRALLRELIDEAKGRGV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17553596   119 PHAMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYqRCSPPDAFIM 162
Cdd:TIGR01575  89 NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYY-PDPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
 89-144 1.61e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17553596   89 SFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNVD 144
Cdd:PRK03624  73 YLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-166 2.38e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.38  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  80 ETGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYQRcsppDA 159
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD----DA 84


                ....*..
gi 17553596 160 FIMRKPF 166
Cdd:COG0456  85 LVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 30-141 1.02e-15

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: 69.08  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    30 IKTVRILVSSIFPVSYSDKFYQE-----CMNNELTGVVIRNGEAIAIVAVKPENFEtGRVLYIRSFGVHPRHREAGLGSF 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLledwdEDASEGFFVAEEDGELVGFASLSIIDDE-PPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17553596   105 LMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGF 141
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 61-167 8.16e-12

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: 59.24  E-value: 8.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  61 VVIRNGEAIAIVAVKPEnfeTGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHvqtSNKTAIEFYKNRG 140
Cdd:COG1246  32 VAEEDGEIVGCAALHPL---DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLG 105

                        90       100
                ....*....|....*....|....*..
gi 17553596 141 FNVDCLVPQYYQRCSPPDAFIMRKPFH 167
Cdd:COG1246 106 FEEIDKEDLPYAKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
24-166 1.36e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  24 RVTAENIKTVRILVSSIFPVSYSDKF---YQECMNNELTGVVIRNGEAIAIVAVKPENFE-TGRVLYIRSFGVHPRHREA 99
Cdd:COG3153   3 PATPEDAEAIAALLRAAFGPGREAELvdrLREDPAAGLSLVAEDDGEIVGHVALSPVDIDgEGPALLLGPLAVDPEYRGQ 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17553596 100 GLGSFLMDFVDEKGKLLKLPHAMLHvqtSNKTAIEFYKNRGFNVdclVPQYYQRCSPPDAFiMRKPF 166
Cdd:COG3153  83 GIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRP---AGELGLTLGPDEVF-LAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 61-141 8.33e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.84  E-value: 8.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    61 VVIRNGEAIAIVAVKPENFETgrVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVqtsNKTAIEFYKNRG 140
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEG--ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLG 81


                  .
gi 17553596   141 F 141
Cdd:pfam13508  82 F 82
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-124 2.25e-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: 48.43  E-value: 2.25e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17553596  61 VVIRNGEAIAIVAVKPENFEtGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLH 124
Cdd:cd04301   3 VAEDDGEIVGFASLSPDGSG-GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 20-143 1.02e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 48.51  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  20 LRLQRVTAENIKtvriLVSSIFPVSYS-DKFYQECMNNELTGVVIrNGEAIAIVAVKPENfetGRVLYIRSFGVHPRHRE 98
Cdd:COG0454   1 MSIRKATPEDIN----FILLIEALDAElKAMEGSLAGAEFIAVDD-KGEPIGFAGLRRLD---DKVLELKRLYVLPEYRG 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17553596  99 AGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNV 143
Cdd:COG0454  73 KGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
61-141 1.06e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  61 VVIRNGEAIAIVAVKPENFETGRvlyIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTsnkTAIEFYKNRG 140
Cdd:COG2153  38 LAYDDGELVATARLLPPGDGEAK---IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA---HAVGFYEKLG 111


                .
gi 17553596 141 F 141
Cdd:COG2153 112 F 112
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 41-162 6.24e-07

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: 46.17  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    41 FPVSYSDKFYQECMNNELTG--VVIRNGEAIAIVAVKPENFETgrvlYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKL 118
Cdd:TIGR01575  13 FAFPWTEAQFAEELANYHLCylLARIGGKVVGYAGVQIVLDEA----HILNIAVKPEYQGQGIGRALLRELIDEAKGRGV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17553596   119 PHAMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYqRCSPPDAFIM 162
Cdd:TIGR01575  89 NEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYY-PDPGEDAIVM 131
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
61-165 1.02e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.14  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596  61 VVIRNGEAIAIVAVKP-ENFETGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNR 139
Cdd:COG1247  56 VAEEDGEVVGFASLGPfRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL 135

                        90       100
                ....*....|....*....|....*..
gi 17553596 140 GFNVDCLVPQYYQRC-SPPDAFIMRKP 165
Cdd:COG1247 136 GFEEVGTLPEVGFKFgRWLDLVLMQKR 162
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-141 4.44e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 4.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17553596  67 EAIAIVAVKPEnfeTGRVLYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGF 141
Cdd:COG3393   1 ELVAMAGVRAE---SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
PRK03624 PRK03624
putative acetyltransferase; Provisional
 89-144 1.61e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17553596   89 SFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHVQTSNKTAIEFYKNRGFNVD 144
Cdd:PRK03624  73 YLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 92-144 3.66e-03

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: 35.00  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17553596    92 VHPRHREAGLGSFLMDFVD----EKGKllklpHAMLHVQTSNKTAIEFYKNRGFNVD 144
Cdd:pfam08445  29 TLPEHRRRGLGSRLVAALArgiaERGI-----TPFAVVVAGNTPSRRLYEKLGFRKI 80
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 47-141 5.64e-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: 35.32  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596    47 DKFYQECMNNELTGVVIRNGEAIA-IVAVKPENfetgrvlYIRSFGVHPRHREAGLGSFLMDFVDEKGKLLKLPHAMLHV 125
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVgVIALRDRG-------HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV 92

                          90
                  ....*....|....*.
gi 17553596   126 qTSNKTAIEFYKNRGF 141
Cdd:pfam13673  93 -NASPYAVPFYEKLGF 107
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 92-162 7.59e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553596   92 VHPRHREAGLG----SFLMDFVDEKGkLLKLphaMLHVQTSNKTAIEFYKNRGFNVDCLVPQYYqrcspP------DAFI 161
Cdd:PRK09491  71 VDPDYQRQGLGrallEHLIDELEKRG-VATL---WLEVRASNAAAIALYESLGFNEVTIRRNYY-----PtadgreDAII 141


                 .
gi 17553596  162 M 162
Cdd:PRK09491 142 M 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH