NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490998983|ref|WP_004860706|]
View 

MULTISPECIES: GNAT family N-acetyltransferase [Raoultella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-150 1.26e-16

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: 72.34  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   1 MMMFRPMREEEYPAYLEYFITDYAREIAANYRLSAEDsltkaTREIAEDLPEGVNTPGQVLLSLFSQSDnrDEHVGYLWY 80
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEE-----ARAWLERLLADWADGGALPFAIEDKED--GELIGVVGL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998983  81 K-PDTAARTVFIfDFYIFNACQGQGLGTQALRAFEREMREQ-GIEQIRLRVAGDNQRARHVYESTGFWVTGI 150
Cdd:COG1670   80 YdIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGT 150
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-150 1.26e-16

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: 72.34  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   1 MMMFRPMREEEYPAYLEYFITDYAREIAANYRLSAEDsltkaTREIAEDLPEGVNTPGQVLLSLFSQSDnrDEHVGYLWY 80
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEE-----ARAWLERLLADWADGGALPFAIEDKED--GELIGVVGL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998983  81 K-PDTAARTVFIfDFYIFNACQGQGLGTQALRAFEREMREQ-GIEQIRLRVAGDNQRARHVYESTGFWVTGI 150
Cdd:COG1670   80 YdIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGT 150
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
72-145 4.83e-13

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: 61.76  E-value: 4.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998983   72 DEHVGYLWYKP-DTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:pfam00583  42 GELVGFASLSIiDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
72-150 2.53e-09

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: 52.33  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   72 DEHVGYL--WYKPDTAArtvfIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGFWVTG 149
Cdd:TIGR01575  40 GKVVGYAgvQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115

                  .
gi 490998983  150 I 150
Cdd:TIGR01575 116 I 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
72-127 6.45e-09

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: 49.58  E-value: 6.45e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490998983  72 DEHVGYLWYKPDTA-ARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRL 127
Cdd:cd04301    8 GEIVGFASLSPDGSgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
96-145 2.04e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.22  E-value: 2.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490998983  96 IFN-----ACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:PRK09491  66 LFNiavdpDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-150 1.26e-16

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: 72.34  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   1 MMMFRPMREEEYPAYLEYFITDYAREIAANYRLSAEDsltkaTREIAEDLPEGVNTPGQVLLSLFSQSDnrDEHVGYLWY 80
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEE-----ARAWLERLLADWADGGALPFAIEDKED--GELIGVVGL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998983  81 K-PDTAARTVFIfDFYIFNACQGQGLGTQALRAFEREMREQ-GIEQIRLRVAGDNQRARHVYESTGFWVTGI 150
Cdd:COG1670   80 YdIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGT 150
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
76-145 5.21e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.91  E-value: 5.21e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983  76 GYLWYKPDTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGF 70
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-149 8.18e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 8.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   1 MMMFRPMREEEYPAYLEyFITDYAREIAANYRLSAEDSLTKATReIAEDLPEGVntPGQVLlslfsqsDNRDEHVGYLW- 79
Cdd:COG1247    1 EMTIRPATPEDAPAIAA-IYNEAIAEGTATFETEPPSEEEREAW-FAAILAPGR--PVLVA-------EEDGEVVGFASl 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998983  80 --YKPDTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGFWVTG 149
Cdd:COG1247   70 gpFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVG 141
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
72-145 4.83e-13

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: 61.76  E-value: 4.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998983   72 DEHVGYLWYKP-DTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:pfam00583  42 GELVGFASLSIiDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
71-145 4.20e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 54.67  E-value: 4.20e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998983  71 RDEHVGYLWYKPdTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:COG0454   42 KGEPIGFAGLRR-LDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGF 115
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
99-145 8.08e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 8.08e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490998983  99 ACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:COG3393   26 EYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
72-150 2.53e-09

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: 52.33  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   72 DEHVGYL--WYKPDTAArtvfIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGFWVTG 149
Cdd:TIGR01575  40 GKVVGYAgvQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115

                  .
gi 490998983  150 I 150
Cdd:TIGR01575 116 I 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
72-127 6.45e-09

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: 49.58  E-value: 6.45e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490998983  72 DEHVGYLWYKPDTA-ARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRL 127
Cdd:cd04301    8 GEIVGFASLSPDGSgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
72-145 4.77e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.83  E-value: 4.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998983   72 DEHVGYLWYKPDTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVagdNQRARHVYESTGF 145
Cdd:pfam13508  12 GKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLGF 82
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
4-145 7.08e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 45.80  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983    4 FRPMREEEYPAYLEYFITDYAREIAANYRLSAEDSLTKATREIAEDLPEGVntpgqVLLSLFSQSDNrdeHVGYLWYKPD 83
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERG-----YGWAIELKDTG---FIGSIGLYDI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998983   84 TAARTVFIFDFYIFNACQGQGLGTQALRAFEREM-REQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGF 138
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
86-145 1.78e-05

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: 41.90  E-value: 1.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983  86 ARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVagdNQRARHVYESTGF 145
Cdd:COG1246   50 EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGF 106
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
96-145 2.04e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.22  E-value: 2.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490998983  96 IFN-----ACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGF 145
Cdd:PRK09491  66 LFNiavdpDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-149 5.05e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 40.84  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   4 FRPMREEEYPA----YLEYFITDYAREIAANYRLSAEDSLTkatrEIAEDlpegvntPGQVllslfsqsdnrdehVGYLW 79
Cdd:COG3153    1 IRPATPEDAEAiaalLRAAFGPGREAELVDRLREDPAAGLS----LVAED-------DGEI--------------VGHVA 55
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998983  80 YKPDTAA---RTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLrvAGDNQRARhVYESTGFWVTG 149
Cdd:COG3153   56 LSPVDIDgegPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL--LGDPSLLP-FYERFGFRPAG 125
PRK03624 PRK03624
putative acetyltransferase; Provisional
98-156 1.78e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983  98 NACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQRARHVYESTGFWV-TGINMSKTL 156
Cdd:PRK03624  78 PDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEqDRISLGKRL 137
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
101-145 3.40e-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: 37.69  E-value: 3.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 490998983  101 QGQGLGTQALRAFEREMREQGIeQIRLRVAGDNQRARHVYESTGF 145
Cdd:pfam08445  34 RRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLGF 77
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
72-156 3.51e-04

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: 38.41  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998983   72 DEHVGYLwykpdTAARTVFIFDFYIFNACQGQGLGTQALRAFEREMREQGIEQIRLRVAGDNQrARHVYESTGFWVTG-- 149
Cdd:pfam13673  40 GQIVGVI-----ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATGpe 113
                          90
                  ....*....|....*
gi 490998983  150 --------INMSKTL 156
Cdd:pfam13673 114 qefngirfVPMEKEL 128
 
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