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Conserved domains on  [gi|17557298|ref|NP_504411|]
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N-acetyltransferase domain-containing protein [Caenorhabditis elegans]

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 ...
 106-222 4.97e-23

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: 91.04  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   106 INDIMRLITKDLSEPYSIYTYRYFLHNW---PEYCFLAYDqtNNTYIGAVLCKLELDMYGRckGYLAMLAVDESCRRLGI 182
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEE--DGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 17557298   183 GTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGF 222
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 106-222 4.97e-23

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: 91.04  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   106 INDIMRLITKDLSEPYSIYTYRYFLHNW---PEYCFLAYDqtNNTYIGAVLCKLELDMYGRckGYLAMLAVDESCRRLGI 182
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEE--DGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 17557298   183 GTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGF 222
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 150-243 8.14e-21

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 84.32  E-value: 8.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298 150 GAVLCKLEldmYGRCKGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLL 229
Cdd:COG0456   1 GFALLGLV---DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....
gi 17557298 230 KYYLNGGDAFRLKL 243
Cdd:COG0456  78 NYYGDDALVMEKEL 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 108-239 5.23e-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: 67.35  E-value: 5.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   108 DIMRLITKDLSEPYSIYTYRYFLHNWPEYCFLAYDqtNNTYIGAVLCKLELDmygrcKGYLAMLAVDESCRRLGIGTRLV 187
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARI--GGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17557298   188 RRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLLKYYLNGG-DAF 239
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 137-205 3.18e-10

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: 54.97  E-value: 3.18e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 137 CFLAYDqtNNTYIGAVLCKLELDMYGRckGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLE 205
Cdd:cd04301   1 FLVAED--DGEIVGFASLSPDGSGGDT--AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 165-228 1.36e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 55.32  E-value: 1.36e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17557298  165 KGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRL 228
Cdd:PRK03624  68 RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRI 131
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 106-222 4.97e-23

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: 91.04  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   106 INDIMRLITKDLSEPYSIYTYRYFLHNW---PEYCFLAYDqtNNTYIGAVLCKLELDMYGRckGYLAMLAVDESCRRLGI 182
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEE--DGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 17557298   183 GTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGF 222
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 150-243 8.14e-21

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 84.32  E-value: 8.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298 150 GAVLCKLEldmYGRCKGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLL 229
Cdd:COG0456   1 GFALLGLV---DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....
gi 17557298 230 KYYLNGGDAFRLKL 243
Cdd:COG0456  78 NYYGDDALVMEKEL 91
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
95-243 1.29e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 80.13  E-value: 1.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298  95 IRIVAYKDESQINDIMRLITKDLSEPYSIYTYRyfLHNWPEYCFLAYDqtNNTYIGAVLCKLELDMYGRCKGYLAMLAVD 174
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLR--EDPAAGLSLVAED--DGEIVGHVALSPVDIDGEGPALLLGPLAVD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 175 ESCRRLGIGTRLVRRALDAMQSKGCDEIVLeteVSNKNAQRLYSNLGFIRQKRLLKYYLNGGDAFRLKL 243
Cdd:COG3153  77 PEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 108-239 5.23e-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: 67.35  E-value: 5.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   108 DIMRLITKDLSEPYSIYTYRYFLHNWPEYCFLAYDqtNNTYIGAVLCKLELDmygrcKGYLAMLAVDESCRRLGIGTRLV 187
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARI--GGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17557298   188 RRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLLKYYLNGG-DAF 239
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 95-243 3.74e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 3.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298  95 IRIVAYKDESQINDImRLITKDLSEPYSIYTYRYFLhnwpeycfLAYDqtNNTYIGAVLckleLDMYGRCKGYLAMLAVD 174
Cdd:COG0454   3 IRKATPEDINFILLI-EALDAELKAMEGSLAGAEFI--------AVDD--KGEPIGFAG----LRRLDDKVLELKRLYVL 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 175 ESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLLKYYLNGgdaFRLKL 243
Cdd:COG0454  68 PEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE---FEKEL 133
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 135-224 4.24e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.55  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298   135 EYCFLAYDqtNNTYIGAVLCKLELDMYGRCKGylaMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETevsNKNAQ 214
Cdd:pfam13508   3 GRFFVAED--DGKIVGFAALLPLDDEGALAEL---RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAA 74

                          90
                  ....*....|
gi 17557298   215 RLYSNLGFIR 224
Cdd:pfam13508  75 AFYEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 166-224 4.58e-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: 61.93  E-value: 4.58e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 166 GYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETevsNKNAQRLYSNLGFIR 224
Cdd:COG1246  53 AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEE 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
166-224 1.96e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.07  E-value: 1.96e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 166 GYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIR 224
Cdd:COG3393  16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRP 74
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 137-205 3.18e-10

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: 54.97  E-value: 3.18e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17557298 137 CFLAYDqtNNTYIGAVLCKLELDMYGRckGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLE 205
Cdd:cd04301   1 FLVAED--DGEIVGFASLSPDGSGGDT--AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 165-228 1.36e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 55.32  E-value: 1.36e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17557298  165 KGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRL 228
Cdd:PRK03624  68 RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRI 131
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
171-236 2.72e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.00  E-value: 2.72e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557298 171 LAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLLKYYLNGG 236
Cdd:COG1247  86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFG 151
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 108-236 8.16e-09

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: 53.85  E-value: 8.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298 108 DIMRLITkdlSEPYSIYTYRYFLHNW-------PEYCFLAYDQTNNTYIGAVLCKLELDMYGRCK-GYlamlAVDESCRR 179
Cdd:COG1670  29 EVARYLP---GPPYSLEEARAWLERLladwadgGALPFAIEDKEDGELIGVVGLYDIDRANRSAEiGY----WLAPAYWG 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17557298 180 LGIGTRLVRRALD-AMQSKGCDEIVLETEVSNKNAQRLYSNLGFIRQKRLLKYYLNGG 236
Cdd:COG1670 102 KGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
171-225 5.47e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.57  E-value: 5.47e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17557298 171 LAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSnknAQRLYSNLGFIRQ 225
Cdd:COG2153  64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPV 115
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 163-227 2.25e-06

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: 45.72  E-value: 2.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557298   163 RCKGYLAMLAVDESCRRLGIGTRLVRRALDamQSKGCDEIVLETEV-SNKNAQRLYSNLGFIRQKR 227
Cdd:pfam13673  49 RDRGHISLLFVDPDYQGQGIGKALLEAVED--YAEKDGIKLSELTVnASPYAVPFYEKLGFRATGP 112
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 107-222 1.63e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.76  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298  107 NDIMRLITKDLSEPYSI--------YTYRYFLHNWPE-YCFLAYDQtNNTYIGAVLCKLELDmygrcKGYLAMLAVDESC 177
Cdd:PRK09491   2 NTISSLTPADLPAAYHIeqrahafpWSEKTFASNQGErYLNLKLTV-NGQMAAFAITQVVLD-----EATLFNIAVDPDY 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17557298  178 RRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGF 222
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
171-222 1.10e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 42.22  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17557298  171 LAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNAQRLYSNLGF 222
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGA 183
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 166-223 4.25e-04

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


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 38.46  E-value: 4.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17557298   166 GYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGcDEIVLETEVSNKNAQRLYSNLGFI 223
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFR 78
PRK10514 PRK10514
putative acetyltransferase; Provisional
 166-227 1.12e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.44  E-value: 1.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17557298  166 GYLAMLAVDESCRRLGIGTRLVRRALdAMQSKgcdeivLETEVSNKNAQRL--YSNLGFIRQKR 227
Cdd:PRK10514  70 GHMEALFVDPDVRGCGVGRMLVEHAL-SLHPE------LTTDVNEQNEQAVgfYKKMGFKVTGR 126
PTZ00330 PTZ00330
acetyltransferase; Provisional
 162-228 2.11e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.90  E-value: 2.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557298  162 GRCKGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLEtevSNKNAQRLYSNLGFI---RQKRL 228
Cdd:PTZ00330  79 GKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILD---CTEDMVAFYKKLGFRaceRQMRL 145
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 162-232 2.21e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 37.76  E-value: 2.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17557298  162 GRCkGYLAMLAVDESCRRLGIGTRLVRRALDAMQSKGCDEIVLETEVSNKNaqrLYSNLGFIRQK-RLLKYY 232
Cdd:PLN02706  83 GKV-GHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKA---FYEKCGYVRKEiQMVKYF 150
 
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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