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Conserved domains on  [gi|15228439|ref|NP_186948|]
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MEIOTIC CONTROL OF CROSSOVERS1 [Arabidopsis thaliana]

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
109-188 1.75e-12

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.60  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 109 GEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRLMFRCVRRLHGFYLINRHHF 188
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
27-196 5.63e-12

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.64  E-value: 5.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  27 YRPINPNDLDRLEQIHRDIFPIKYESEFFQSVVNGVDI-VSWAAVDrsrpddhSDELIGFVTAKFVLAKdseiddlihyd 105
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAED-------DGEIVGHVALSPVDID----------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 106 sskGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAaicLYKRLmfrcvrrlhGFYLINR 185
Cdd:COG3153  63 ---GEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG-ARAVVLLGDPSLLP---FYERF---------GFRPAGE 126
                       170
                ....*....|.
gi 15228439 186 HHFDAFLFVYF 196
Cdd:COG3153 127 LGLTLGPDEVF 137
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
109-188 1.75e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.60  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 109 GEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRLMFRCVRRLHGFYLINRHHF 188
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
27-196 5.63e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.64  E-value: 5.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  27 YRPINPNDLDRLEQIHRDIFPIKYESEFFQSVVNGVDI-VSWAAVDrsrpddhSDELIGFVTAKFVLAKdseiddlihyd 105
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAED-------DGEIVGHVALSPVDID----------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 106 sskGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAaicLYKRLmfrcvrrlhGFYLINR 185
Cdd:COG3153  63 ---GEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG-ARAVVLLGDPSLLP---FYERF---------GFRPAGE 126
                       170
                ....*....|.
gi 15228439 186 HHFDAFLFVYF 196
Cdd:COG3153 127 LGLTLGPDEVF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
35-169 5.78e-08

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: 49.82  E-value: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439    35 LDRLEQIHRDIFPIKYESEFFQsvvngvDIVSWAAVDRSRP--DDHSDELIGFVTAKFVLakdseiddlihydsskGEET 112
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLD------LLEDWDEDASEGFfvAEEDGELVGFASLSIID----------------DEPP 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228439   113 LIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRL 169
Cdd:pfam00583  59 VGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKL 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
90-154 1.45e-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: 38.80  E-value: 1.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228439  90 FVLAKDSEIDDLIHYDSSKGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLH 154
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
109-169 9.61e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 9.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228439   109 GEETLIYILTLGVVETYRNRGIAMSLISEvIKYASGLSVCRGVYLHViahNNAAICLYKRL 169
Cdd:pfam13508  24 DDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAFYEKL 80
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
109-188 1.75e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.60  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 109 GEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRLMFRCVRRLHGFYLINRHHF 188
Cdd:COG0456   9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
27-196 5.63e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.64  E-value: 5.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  27 YRPINPNDLDRLEQIHRDIFPIKYESEFFQSVVNGVDI-VSWAAVDrsrpddhSDELIGFVTAKFVLAKdseiddlihyd 105
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAED-------DGEIVGHVALSPVDID----------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439 106 sskGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAaicLYKRLmfrcvrrlhGFYLINR 185
Cdd:COG3153  63 ---GEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG-ARAVVLLGDPSLLP---FYERF---------GFRPAGE 126
                       170
                ....*....|.
gi 15228439 186 HHFDAFLFVYF 196
Cdd:COG3153 127 LGLTLGPDEVF 137
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-193 4.87e-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: 54.23  E-value: 4.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  28 RPINPNDLDRLEQIHRD------IFPIKYESEFFQSVVNGV-------DIVSWAAVDRSrpddhSDELIGFVTAKFVLAK 94
Cdd:COG1670  11 RPLRPEDAEALAELLNDpevaryLPGPPYSLEEARAWLERLladwadgGALPFAIEDKE-----DGELIGVVGLYDIDRA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  95 DSEIDdlIHYdsskgeetliyiltlGVVETYRNRGIAMSLISEVIKYA-SGLSVCRgVYLHVIAHNNAAICLYKRLMFRC 173
Cdd:COG1670  86 NRSAE--IGY---------------WLAPAYWGKGYATEALRALLDYAfEELGLHR-VEAEVDPDNTASIRVLEKLGFRL 147
                       170       180
                ....*....|....*....|
gi 15228439 174 VRRLHGFYLINRHHFDAFLF 193
Cdd:COG1670 148 EGTLRDALVIDGRYRDHVLY 167
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
24-197 1.66e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 52.30  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  24 SIHYRPINPNDLDRLEQIHRDIFP---IKYESEffqsvvnGVDIVSWAAVDRSRPDDH--------SDELIGFVTAKFVL 92
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAIAegtATFETE-------PPSEEEREAWFAAILAPGrpvlvaeeDGEVVGFASLGPFR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  93 AKDseiddliHYDSskgeetlIYILTLGVVETYRNRGIAMSLISEVIKYA--SGlsvCRGVYLHVIAHNNAAICLYKRLM 170
Cdd:COG1247  74 PRP-------AYRG-------TAEESIYVDPDARGRGIGRALLEALIERAraRG---YRRLVAVVLADNEASIALYEKLG 136
                       170       180
                ....*....|....*....|....*..
gi 15228439 171 FRCVRRLHGFYLINRHHFDAFLFVYFI 197
Cdd:COG1247 137 FEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
35-169 5.78e-08

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: 49.82  E-value: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439    35 LDRLEQIHRDIFPIKYESEFFQsvvngvDIVSWAAVDRSRP--DDHSDELIGFVTAKFVLakdseiddlihydsskGEET 112
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLD------LLEDWDEDASEGFfvAEEDGELVGFASLSIID----------------DEPP 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228439   113 LIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRL 169
Cdd:pfam00583  59 VGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKL 114
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
114-178 4.75e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.44  E-value: 4.75e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228439 114 IYILTLGVVETYRNRGIAMSLISEVIKYASGlSVCRGVYLHVIAHNNAAICLYKRLMFRCVRRLH 178
Cdd:COG3393  16 AEISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVGEYA 79
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
28-177 1.19e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 43.89  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439  28 RPINPNDLDRL---EQIHRDIFPIkyeseffqsvVNGVDIVSWAAVDrsrpddHSDELIGFVTAKFVlakdseiddlihy 104
Cdd:COG0454   4 RKATPEDINFIlliEALDAELKAM----------EGSLAGAEFIAVD------DKGEPIGFAGLRRL------------- 54
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228439 105 dsskGEETLiYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLHVIAHNNAAICLYKRLMFRCVRRL 177
Cdd:COG0454  55 ----DDKVL-ELKRLYVLPEYRGKGIGKALLEALLEWARERG-CTALELDTLDGNPAAIRFYERLGFKEIERY 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
90-154 1.45e-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: 38.80  E-value: 1.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228439  90 FVLAKDSEIDDLIHYDSSKGEETLIYILTLGVVETYRNRGIAMSLISEVIKYASGLSvCRGVYLH 154
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
109-169 9.61e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 9.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228439   109 GEETLIYILTLGVVETYRNRGIAMSLISEvIKYASGLSVCRGVYLHViahNNAAICLYKRL 169
Cdd:pfam13508  24 DDEGALAELRLAVHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAFYEKL 80
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
115-172 1.25e-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: 36.92  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439   115 YILTLGVVETYRNRGIAMSLISEVIKyasGLSVcRG--VYLHVIAHNNAAICLYKRLMFR 172
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALAR---GIAE-RGitPFAVVVAGNTPSRRLYEKLGFR 78
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
111-189 2.31e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 37.35  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228439   111 ETLIYILTLGVVETYR--------------NRGIAMSLISEVIKYASGLSVCRGVYLHVIAHNNAAICLYKRLMFRCVRR 176
Cdd:pfam13420  58 DRLIGYATLRQFDYVKthkaelsfyvvknnDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGI 137
                          90
                  ....*....|...
gi 15228439   177 LHGFYLINRHHFD 189
Cdd:pfam13420 138 ERNAIKKNGRWID 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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