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Conserved domains on  [gi|1002253856|ref|XP_015631173|]
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N-terminal acetyltransferase B complex catalytic subunit NAA20 [Oryza sativa Japonica Group]

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

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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 ...
 55-151 6.97e-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: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  55 GYIMGKVEGQGEswHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDkAYFVDLFVRASNMPAIRMYEKLGYVVYRRVL 134
Cdd:COG0456     1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*..
gi 1002253856 135 RYYsgEEDGLDMRKALS 151
Cdd:COG0456    78 NYY--GDDALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-151 6.97e-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: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  55 GYIMGKVEGQGEswHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDkAYFVDLFVRASNMPAIRMYEKLGYVVYRRVL 134
Cdd:COG0456     1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*..
gi 1002253856 135 RYYsgEEDGLDMRKALS 151
Cdd:COG0456    78 NYY--GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-127 2.74e-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: 67.93  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  20 LDHLTETFNMSFYMTYMARWPDYFHAAVSP------GDRVMGYIMGKVEGQgESWHGHVTAVSVATEFRRQKLAKKLMNL 93
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEDASEGffvaeeDGELVGFASLSIIDD-EPPVGEIEGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002253856  94 LEEISDKMDkAYFVDLFVRASNMPAIRMYEKLGY 127
Cdd:pfam00583  84 LLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 50-146 3.92e-12

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: 60.04  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  50 GDRVMGYIMGKVegqgeSWH-GHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVdLFVRASNMPAIRMYEKLGYV 128
Cdd:TIGR01575  39 GGKVVGYAGVQI-----VLDeAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIF-LEVRVSNIAAQALYKKLGFN 112

                          90
                  ....*....|....*....
gi 1002253856 129 VYRRVLRYYS-GEEDGLDM 146
Cdd:TIGR01575 113 EIAIRRNYYPdPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-133 1.42e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  40 PDYFHAAVSpGDRVMGYIMGKVEGqgeswH-GHVTAVSVATEFRRQKLAKKLMNLLEE--ISDKMDKayfVDLFVRASNM 116
Cdd:PRK03624   44 PSLFLVAEV-GGEVVGTVMGGYDG-----HrGWAYYLAVHPDFRGRGIGRALVARLEKklIARGCPK---INLQVREDND 114

                          90
                  ....*....|....*..
gi 1002253856 117 PAIRMYEKLGYVVYRRV 133
Cdd:PRK03624  115 AVLGFYEALGYEEQDRI 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-97 1.68e-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: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002253856  50 GDRVMGYIMGKVEGQGESwHGHVTAVSVATEFRRQKLAKKLMNLLEEI 97
Cdd:cd04301     7 DGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-151 6.97e-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: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  55 GYIMGKVEGQGEswHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDkAYFVDLFVRASNMPAIRMYEKLGYVVYRRVL 134
Cdd:COG0456     1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*..
gi 1002253856 135 RYYsgEEDGLDMRKALS 151
Cdd:COG0456    78 NYY--GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-127 2.74e-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: 67.93  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  20 LDHLTETFNMSFYMTYMARWPDYFHAAVSP------GDRVMGYIMGKVEGQgESWHGHVTAVSVATEFRRQKLAKKLMNL 93
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEDASEGffvaeeDGELVGFASLSIIDD-EPPVGEIEGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002253856  94 LEEISDKMDkAYFVDLFVRASNMPAIRMYEKLGY 127
Cdd:pfam00583  84 LLEWARERG-CERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 50-146 3.92e-12

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: 60.04  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  50 GDRVMGYIMGKVegqgeSWH-GHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVdLFVRASNMPAIRMYEKLGYV 128
Cdd:TIGR01575  39 GGKVVGYAGVQI-----VLDeAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIF-LEVRVSNIAAQALYKKLGFN 112

                          90
                  ....*....|....*....
gi 1002253856 129 VYRRVLRYYS-GEEDGLDM 146
Cdd:TIGR01575 113 EIAIRRNYYPdPGEDAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-136 1.76e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.83  E-value: 1.76e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002253856  69 HGHVTAVSVATEFRRQKLAKKLMN-LLEEISDkmDKAYFVDLFVRASNMPAIRMYEKLGYVVYRRVLRY 136
Cdd:COG3393    15 VAEISGVYTHPEYRGRGLASALVAaLAREALA--RGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-129 3.68e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.60  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  50 GDRVMGYIMGKVEGQGESWHGHvtAVSVATEFRRQKLAKKLMNLLEEISdkmdKAYFVDLFVRASNMPAIRMYEKLGYVV 129
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAEL--RLAVHPEYRGQGIGRALLEAAEAAA----KEGGIKLLELETTNRAAAFYEKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 41-153 1.24e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 48.13  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  41 DYFHAAVSPGDRVMGYIMGKVEGQgesWHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVdLFVRASNMPAIR 120
Cdd:COG0454    33 GAEFIAVDDKGEPIGFAGLRRLDD---KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALE-LDTLDGNPAAIR 108

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002253856 121 MYEKLGYVVYRRVLRYYSGEedgldMRKALSQD 153
Cdd:COG0454   109 FYERLGFKEIERYVAYVGGE-----FEKELSLS 136
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-133 1.42e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  40 PDYFHAAVSpGDRVMGYIMGKVEGqgeswH-GHVTAVSVATEFRRQKLAKKLMNLLEE--ISDKMDKayfVDLFVRASNM 116
Cdd:PRK03624   44 PSLFLVAEV-GGEVVGTVMGGYDG-----HrGWAYYLAVHPDFRGRGIGRALVARLEKklIARGCPK---INLQVREDND 114

                          90
                  ....*....|....*..
gi 1002253856 117 PAIRMYEKLGYVVYRRV 133
Cdd:PRK03624  115 AVLGFYEALGYEEQDRI 131
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
36-150 2.93e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 47.68  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  36 MARW------PDYFHAAVSPGDRVMGYI-MGKVEGQGESWHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVd 108
Cdd:COG1247    40 REAWfaailaPGRPVLVAEEDGEVVGFAsLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLV- 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002253856 109 LFVRASNMPAIRMYEKLGYVV---YRRVLRYYSGEEDGLDMRKAL 150
Cdd:COG1247   119 AVVLADNEASIALYEKLGFEEvgtLPEVGFKFGRWLDLVLMQKRL 163
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 75-146 5.91e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 46.46  E-value: 5.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002253856  75 VSVATEFRRQKLAKKLmnlLEEISDKMDKAYFVDLF--VRASNMPAIRMYEKLGY--VVYRRvlRYY---SGEEDGLDM 146
Cdd:PRK09491   69 IAVDPDYQRQGLGRAL---LEHLIDELEKRGVATLWleVRASNAAAIALYESLGFneVTIRR--NYYptaDGREDAIIM 142
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
50-150 9.16e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 45.85  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  50 GDRVMGYIMG-KVEGQGESWHGHVTAVSVATEFRRQKLAKKLMNLLEEISDKMDkAYFVDLFvraSNMPAIRMYEKLGYV 128
Cdd:COG3153    47 DGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG-ARAVVLL---GDPSLLPFYERFGFR 122

                          90       100
                  ....*....|....*....|..
gi 1002253856 129 VYRRvLRYYSGEEDGLdMRKAL 150
Cdd:COG3153   123 PAGE-LGLTLGPDEVF-LAKEL 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 69-150 1.59e-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: 44.95  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  69 HGHVTAVSVATEFRRQKLAKKLMNLLEEISDKmDKAYFVDLFVRASNmPAIRMYEKLGYVVYRRVlryysGEEDGL---D 145
Cdd:pfam13673  51 RGHISLLFVDPDYQGQGIGKALLEAVEDYAEK-DGIKLSELTVNASP-YAVPFYEKLGFRATGPE-----QEFNGIrfvP 123


                  ....*
gi 1002253856 146 MRKAL 150
Cdd:pfam13673 124 MEKEL 128
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
75-151 2.08e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.09  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856  75 VSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVdLFVRASnmpAIRMYEKLGYVVYrrvlryysGE---EDG---LDMRK 148
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIV-LSAQAH---AVGFYEKLGFVPV--------GEeflEAGiphIDMRK 131


                  ...
gi 1002253856 149 ALS 151
Cdd:COG2153   132 PLS 134
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 70-135 6.31e-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: 39.62  E-value: 6.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253856  70 GHVTAVSVATEFRRQKLAKKLMN-LLEEISDKMDKAYfvdLFVRASNMPAIRMYEKLGYVVYRRVLR 135
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAaLARGIAERGITPF---AVVVAGNTPSRRLYEKLGFRKIDETYW 85
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-97 1.68e-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: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002253856  50 GDRVMGYIMGKVEGQGESwHGHVTAVSVATEFRRQKLAKKLMNLLEEI 97
Cdd:cd04301     7 DGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-137 7.28e-04

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: 38.44  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253856   3 TIRRFCCDDLLRFSSVNLDHLTETFNMSFYMTY--MARWPDYFHAAVSPGDRVMGYIMGKVEGQ--------GESWHGHV 72
Cdd:COG1670     9 RLRPLRPEDAEALAELLNDPEVARYLPGPPYSLeeARAWLERLLADWADGGALPFAIEDKEDGEligvvglyDIDRANRS 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253856  73 T--AVSVATEFRRQKLAKKLMNLLEEISDKMDKAYFVDLFVRASNMPAIRMYEKLGYVVYRRVLRYY 137
Cdd:COG1670    89 AeiGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 69-129 8.46e-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: 37.66  E-value: 8.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002253856  69 HGHVTAVSVATEFRRQKLAKKLMNLLEEisdKMDKAYFVDLFVrASNMPAIRMYEKLGYVV 129
Cdd:COG1246    52 LAELRSLAVHPDYRGRGIGRRLLEALLA---EARELGLKRLFL-LTTSAAIHFYEKLGFEE 108
 
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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