NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1251770413|ref|NP_001343397|]
View 

thialysine N-epsilon-acetyltransferase isoform 1 [Mus musculus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 2.72e-24

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 2.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251770413  81 YSTWTG-RNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTESEG 153
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 2.72e-24

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 2.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251770413  81 YSTWTG-RNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTESEG 153
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-144 2.00e-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: 68.31  E-value: 2.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251770413  71 VVGYGLYYFIYSTWtgRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLG 144
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-127 1.20e-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: 51.89  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1251770413  71 VVGYGLYYFIYstWTGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRL 127
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-150 1.70e-08

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: 50.41  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  23 ELAEFEKLSHQVKISEEALRADgFGeNPFFHCLVAEiipapgesQGSLVVGYGLYYFIYSTWTgrnvyLEDIYVMPQYRG 102
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEE-LA-NYHLCYLLAR--------IGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1251770413 103 QGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTE 150
Cdd:TIGR01575  69 QGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
PTZ00330 PTZ00330
acetyltransferase; Provisional
 3-144 1.95e-08

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 50.61  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   3 STRIREARESDCGDIMRMIRELAEFEKLShQVKISE--EALRADGFGENPFFHCLVAEIIpapgeSQGSLVVGYGLyyfi 80
Cdd:PTZ00330    6 SLELRDLEEGDLGSVLELLSHLTSAPALS-QEELEQiaARRRLAGVVTRVFVHSPTQRIV-----GTASLFVEPKF---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770413  81 ysTWTGRNV-YLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQfrlAVLDWNKKAVNLYKFLG 144
Cdd:PTZ00330   76 --TRGGKCVgHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 2.72e-24

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 2.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251770413  81 YSTWTG-RNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTESEG 153
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 71-160 4.93e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 70.47  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  71 VVGYGLYyFIYSTWTGrnvYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTE 150
Cdd:COG0454    45 PIGFAGL-RRLDDKVL---ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIER 120

                          90
                  ....*....|
gi 1251770413 151 SEGWLSFRFE 160
Cdd:COG0454   121 YVAYVGGEFE 130
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-144 2.00e-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: 68.31  E-value: 2.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251770413  71 VVGYGLYYFIYSTWtgRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLG 144
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 73-154 2.47e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 67.37  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  73 GYGLYYFIYstwTGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTESE 152
Cdd:COG0456     1 GFALLGLVD---GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77


                  ..
gi 1251770413 153 GW 154
Cdd:COG0456    78 NY 79
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-150 1.68e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 63.95  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   6 IREARESDCGDIMRMIRELAEFEKLSHQVkiseEALRADGfgenPFFHCLVAEIipapgesqGSLVVGYGLYYFIYSTWT 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELV----DRLREDP----AAGLSLVAED--------DGEIVGHVALSPVDIDGE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770413  86 GRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCsqfRLAVLDWNKKAVNLYKFLGAQDLTE 150
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGA---RAVVLLGDPSLLPFYERFGFRPAGE 126
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-144 4.41e-10

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: 54.61  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   5 RIREARESDCGDIMRMIRELAEFEKLSHqvkiseealradgfgenpffhCLVAEiipapgesQGSLVVGYGLYYFIystw 84
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYALEEEIGE---------------------FWVAE--------EDGEIVGCAALHPL---- 48

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  85 TGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWnkkAVNLYKFLG 144
Cdd:COG1246    49 DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSA---AIHFYEKLG 105
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
81-160 5.76e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.99  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  81 YSTWTGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTEsegWLSFRFE 160
Cdd:COG3393     8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE---YATVLFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-127 1.20e-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: 51.89  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1251770413  71 VVGYGLYYFIYstWTGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRL 127
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-150 1.70e-08

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: 50.41  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  23 ELAEFEKLSHQVKISEEALRADgFGeNPFFHCLVAEiipapgesQGSLVVGYGLYYFIYSTWTgrnvyLEDIYVMPQYRG 102
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEE-LA-NYHLCYLLAR--------IGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1251770413 103 QGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTE 150
Cdd:TIGR01575  69 QGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
PTZ00330 PTZ00330
acetyltransferase; Provisional
 3-144 1.95e-08

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 50.61  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   3 STRIREARESDCGDIMRMIRELAEFEKLShQVKISE--EALRADGFGENPFFHCLVAEIIpapgeSQGSLVVGYGLyyfi 80
Cdd:PTZ00330    6 SLELRDLEEGDLGSVLELLSHLTSAPALS-QEELEQiaARRRLAGVVTRVFVHSPTQRIV-----GTASLFVEPKF---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770413  81 ysTWTGRNV-YLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQfrlAVLDWNKKAVNLYKFLG 144
Cdd:PTZ00330   76 --TRGGKCVgHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 53-141 3.65e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.22  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  53 HCLVAEiipapgesQGSLVVGYGLYYFIYSTWTgrnVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVldw 132
Cdd:pfam13508   4 RFFVAE--------DDGKIVGFAALLPLDDEGA---LAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET--- 69


                  ....*....
gi 1251770413 133 NKKAVNLYK 141
Cdd:pfam13508  70 TNRAAAFYE 78
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-167 1.88e-05

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: 42.68  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   5 RIREARESDCGDIMRMIRElAEFEKLSHQVKISEEALRA------DGFGENPFFHCLVAEiiPAPGEsqgslVVGYGLYY 78
Cdd:COG1670     9 RLRPLRPEDAEALAELLND-PEVARYLPGPPYSLEEARAwlerllADWADGGALPFAIED--KEDGE-----LIGVVGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  79 FIysTWTGRNVYLeDIYVMPQYRGQGIGTKIIKKVAEVALNK-GCSQFRLAVLDWNKKAVNLYKFLGaqdltesegwlsF 157
Cdd:COG1670    81 DI--DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG------------F 145

                         170
                  ....*....|
gi 1251770413 158 RFEGEAMREL 167
Cdd:COG1670   146 RLEGTLRDAL 155
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-144 1.09e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.30  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  55 LVAEiipAPGESQGSLVVGYG-----LYYFIystwtgrnvylediyVMPQYRGQGIGTKIIKKvAEVAL-NKGCSQFRLA 128
Cdd:PRK03624   48 LVAE---VGGEVVGTVMGGYDghrgwAYYLA---------------VHPDFRGRGIGRALVAR-LEKKLiARGCPKINLQ 108

                          90
                  ....*....|....*.
gi 1251770413 129 VLDWNKKAVNLYKFLG 144
Cdd:PRK03624  109 VREDNDAVLGFYEALG 124
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 87-157 2.85e-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: 38.79  E-value: 2.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251770413  87 RNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVlDWNKKAVNLYKFLG--AQDLTESEGWLSF 157
Cdd:pfam13673  50 DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV-NASPYAVPFYEKLGfrATGPEQEFNGIRF 121
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
89-127 1.74e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 36.70  E-value: 1.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1251770413  89 VYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRL 127
Cdd:COG2153    59 AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL 97
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 90-122 2.13e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 36.61  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1251770413  90 YLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGC 122
Cdd:PLN02706   87 HIEDVVVDSAARGKGLGKKIIEALTEHARSAGC 119
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
1-159 5.06e-03

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 35.66  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413   1 MASTRIREARESDCGDIMRMIRELAEFEkLSHQvkiseeALRAdGFGEN---PFFHCLVAEIipapgesQGSLVVGYGL- 76
Cdd:PRK10146    1 MPACELRPATQYDTDAVYALICELKQAE-FDHQ------AFRV-GFNANlrdPNMRYHLALL-------DGEVVGMIGLh 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770413  77 --YYFIYSTWTGRnvyLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCsqfRLAVLDWNKKAVNLYKFLGAQDLTESEgw 154
Cdd:PRK10146   66 lqFHLHHVNWIGE---IQELVVMPQARGLNVGSKLLAWAEEEARQAGA---EMTELSTNVKRHDAHRFYLREGYEQSH-- 137


                  ....*
gi 1251770413 155 lsFRF 159
Cdd:PRK10146  138 --FRF 140
 
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