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Conserved domains on  [gi|1958659532|ref|XP_038942246|]
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thialysine N-epsilon-acetyltransferase isoform X3 [Rattus norvegicus]

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-118 2.93e-19

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 78.50  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   3 STRIREAKESDCGDIMRMIRE-----LAEFEKLSHQVK-----------------ISEEGSLVVGYgLYYFIYSTWTG-R 59
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEEereawfaailapgrpvlVAEEDGEVVGF-ASLGPFRPRPAyR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659532  60 NIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQ 118
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-118 2.93e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 78.50  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   3 STRIREAKESDCGDIMRMIRE-----LAEFEKLSHQVK-----------------ISEEGSLVVGYgLYYFIYSTWTG-R 59
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEEereawfaailapgrpvlVAEEDGEVVGF-ASLGPFRPRPAyR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659532  60 NIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQ 118
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
19-116 4.11e-16

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: 69.08  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  19 RMIRELAEFEKLSHQVKISEEGSLVVGYGLYYFIYSTWtgRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFR 98
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97
                          90
                  ....*....|....*...
gi 1958659532  99 LAVLNWNKKAVNLYKFLG 116
Cdd:pfam00583  98 LEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
38-99 3.51e-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: 52.66  E-value: 3.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659532  38 EEGSLVVGYGLYYFIYstWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 99
Cdd:cd04301     5 EDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PTZ00330 PTZ00330
acetyltransferase; Provisional
3-116 3.48e-07

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 46.37  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   3 STRIREAKESDCGDIMRMIRELAEFEKLSH-----------------QVKISEEGSLVVGYGlYYFIYSTWT--GRNI-Y 62
Cdd:PTZ00330    6 SLELRDLEEGDLGSVLELLSHLTSAPALSQeeleqiaarrrlagvvtRVFVHSPTQRIVGTA-SLFVEPKFTrgGKCVgH 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659532  63 LEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQfrlAVLNWNKKAVNLYKFLG 116
Cdd:PTZ00330   85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
38-122 1.79e-05

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: 41.55  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  38 EEGSLVVGYGLYYFIYSTWTgrniyLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGA 117
Cdd:TIGR01575  37 RIGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGF 111

                  ....*
gi 1958659532 118 QDLTE 122
Cdd:TIGR01575 112 NEIAI 116
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-118 2.93e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 78.50  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   3 STRIREAKESDCGDIMRMIRE-----LAEFEKLSHQVK-----------------ISEEGSLVVGYgLYYFIYSTWTG-R 59
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEEereawfaailapgrpvlVAEEDGEVVGF-ASLGPFRPRPAyR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659532  60 NIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQ 118
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
5-132 2.64e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.48  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   5 RIREAKESDCG---DIMRMIRELAEFEKLSH--QVKISEEGSLVVGYGLYyFIYSTWTGrniYLEDIYVMPKYRGQGIGT 79
Cdd:COG0454     2 SIRKATPEDINfilLIEALDAELKAMEGSLAgaEFIAVDDKGEPIGFAGL-RRLDDKVL---ELKRLYVLPEYRGKGIGK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958659532  80 KIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTESEGWLSFRFE 132
Cdd:COG0454    78 ALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFE 130
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
19-116 4.11e-16

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: 69.08  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  19 RMIRELAEFEKLSHQVKISEEGSLVVGYGLYYFIYSTWtgRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFR 98
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97
                          90
                  ....*....|....*...
gi 1958659532  99 LAVLNWNKKAVNLYKFLG 116
Cdd:pfam00583  98 LEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
45-126 2.46e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.60  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  45 GYGLYYFIYstwTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTESE 124
Cdd:COG0456     1 GFALLGLVD---GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                  ..
gi 1958659532 125 GW 126
Cdd:COG0456    78 NY 79
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
5-116 7.49e-13

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: 61.16  E-value: 7.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   5 RIREAKESDCGDIMRMIRELAeFEKLSHQVKISEEGSLVVGYGLYYFIystwTGRNIYLEDIYVMPKYRGQGIGTKIIKK 84
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYA-LEEEIGEFWVAEEDGEIVGCAALHPL----DEDLAELRSLAVHPDYRGRGIGRRLLEA 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958659532  85 VAEVALRKGCSQFRLAVlnwNKKAVNLYKFLG 116
Cdd:COG1246    77 LLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-122 8.39e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 8.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   6 IREAKESDCGDIMRMIRE---LAEFEKLSHQVKIS---------EEGSLVVGYGLYYFIYSTWTGRNIYLEDIYVMPKYR 73
Cdd:COG3153     1 IRPATPEDAEAIAALLRAafgPGREAELVDRLREDpaaglslvaEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958659532  74 GQGIGTKIIKKVAEVALRKGCsqfRLAVLNWNKKAVNLYKFLGAQDLTE 122
Cdd:COG3153    81 GQGIGRALMRAALEAARERGA---RAVVLLGDPSLLPFYERFGFRPAGE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
38-99 3.51e-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: 52.66  E-value: 3.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659532  38 EEGSLVVGYGLYYFIYstWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 99
Cdd:cd04301     5 EDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
53-132 1.06e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.83  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  53 YSTWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTEsegWLSFRFE 132
Cdd:COG3393     8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE---YATVLFR 84
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
38-113 3.03e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 3.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659532  38 EEGSLVVGYGLYYFIYSTWTGRNIyleDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNwnkKAVNLYK 113
Cdd:pfam13508   9 EDDGKIVGFAALLPLDDEGALAEL---RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFYE 78
PTZ00330 PTZ00330
acetyltransferase; Provisional
3-116 3.48e-07

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 46.37  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   3 STRIREAKESDCGDIMRMIRELAEFEKLSH-----------------QVKISEEGSLVVGYGlYYFIYSTWT--GRNI-Y 62
Cdd:PTZ00330    6 SLELRDLEEGDLGSVLELLSHLTSAPALSQeeleqiaarrrlagvvtRVFVHSPTQRIVGTA-SLFVEPKFTrgGKCVgH 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958659532  63 LEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQfrlAVLNWNKKAVNLYKFLG 116
Cdd:PTZ00330   85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
38-122 1.79e-05

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: 41.55  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  38 EEGSLVVGYGLYYFIYSTWTgrniyLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGA 117
Cdd:TIGR01575  37 RIGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGF 111

                  ....*
gi 1958659532 118 QDLTE 122
Cdd:TIGR01575 112 NEIAI 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
38-129 2.02e-05

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: 41.49  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  38 EEGSLVVGYGLyyfiystwTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVlNWNKKAVNLYKFLG- 116
Cdd:pfam13673  37 FEGGQIVGVIA--------LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV-NASPYAVPFYEKLGf 107
                          90
                  ....*....|....
gi 1958659532 117 -AQDLTESEGWLSF 129
Cdd:pfam13673 108 rATGPEQEFNGIRF 121
PRK03624 PRK03624
putative acetyltransferase; Provisional
40-116 4.64e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.99  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  40 GSLVVGYG-----LYYFIystwtgrniylediyVMPKYRGQGIGTKIIKKvAEVALR-KGCSQFRLAVLNWNKKAVNLYK 113
Cdd:PRK03624   58 GTVMGGYDghrgwAYYLA---------------VHPDFRGRGIGRALVAR-LEKKLIaRGCPKINLQVREDNDAVLGFYE 121

                  ...
gi 1958659532 114 FLG 116
Cdd:PRK03624  122 ALG 124
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
62-94 8.40e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 37.38  E-value: 8.40e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958659532  62 YLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGC 94
Cdd:PLN02706   87 HIEDVVVDSAARGKGLGKKIIEALTEHARSAGC 119
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
43-139 9.76e-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: 37.29  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  43 VVGYGLYYFIysTWTGRNIYLeDIYVMPKYRGQGIGTKIIKKVAEVALRK-GCSQFRLAVLNWNKKAVNLYKFLGaqdlt 121
Cdd:COG1670    73 LIGVVGLYDI--DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG----- 144
                          90
                  ....*....|....*...
gi 1958659532 122 esegwlsFRFEGEAMREL 139
Cdd:COG1670   145 -------FRLEGTLRDAL 155
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
63-99 1.23e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 36.70  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958659532  63 LEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 99
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL 97
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
51-93 7.84e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 33.59  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958659532  51 FIYSTWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKG 93
Cdd:COG2388    23 ELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
2-136 9.54e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 34.52  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532   2 ASTRIREAKESDCGDIMRM----IRELAEFeklsHQVKISEEGSlvvgYGLYYFiYSTWTGRNIY--------------- 62
Cdd:COG5628     1 MKVSIERVTAEDKPILENLyqlyLHDLSEF----TGILPDADGL----FEYEYL-DTYWTDDDRHpyliyvdgepagfal 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659532  63 ------------LEDIYVMPKYRGQGIGTKIIKKVaeVALRKGcsQFRLAVLNWNKKAV----NLYKFLGAQDLTESEG- 125
Cdd:COG5628    72 vrrlpflesdyeIAEFFVLRKYRRKGIGKRAAHEL--FKRFPG--RWEVKQLEANVPAVafwrKVIGEYTGGAYTEEERy 147
                         170
                  ....*....|....*.
gi 1958659532 126 -----WLSFRFEGEAM 136
Cdd:COG5628   148 idgrpGLVQRFEVAGP 163
 
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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