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Conserved domains on  [gi|489191967|ref|WP_003101319|]
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MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas]

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

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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];
8-136 1.27e-17

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.65  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   8 VSVRPVAHEDFEQWLEYWKAYQA-----FYEVELSAQATEATWRRFFDEGEPmhCAVASDGSRLHGIVnFLYHRSTWAAQ 82
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRP--VLVAEEDGEVVGFA-SLGPFRPRPAY 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489191967  83 DVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-136 1.27e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.65  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   8 VSVRPVAHEDFEQWLEYWKAYQA-----FYEVELSAQATEATWRRFFDEGEPmhCAVASDGSRLHGIVnFLYHRSTWAAQ 82
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRP--VLVAEEDGEVVGFA-SLGPFRPRPAY 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489191967  83 DVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-136 4.91e-14

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: 64.08  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   21 WLEYWKAYQAFYEVELSAQATEAtwRRFFDEGEPMHCAVASDGSRLHGIVNFLYHRSTWaaqDVCYLEDLYVSPDVRGQQ 100
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDL--LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKG 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489191967  101 IGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:pfam00583  76 IGTALLQALLEWARERGCERIFLEVAADNLAAIALY 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-124 2.83e-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: 50.35  E-value: 2.83e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489191967  57 CAVASDGSRLHGIVNFLYHRSTwaaQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWH 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 29-136 3.01e-07

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: 46.55  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   29 QAFYEVELSAQA---TEATWRRFFDEgEPMHCAVASDGSRL--HGIVNFLYHRSTwaaqdvcyLEDLYVSPDVRGQQIGK 103
Cdd:TIGR01575   3 KAVLEIEAAAFAfpwTEAQFAEELAN-YHLCYLLARIGGKVvgYAGVQIVLDEAH--------ILNIAVKPEYQGQGIGR 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489191967  104 QLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:TIGR01575  74 ALLRELIDEAKGRGVNEIFLEVRVSNIAAQALY 106
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 92-137 1.83e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.22  E-value: 1.83e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489191967  92 VSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLYD 137
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYE 116
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-136 1.27e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.65  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   8 VSVRPVAHEDFEQWLEYWKAYQA-----FYEVELSAQATEATWRRFFDEGEPmhCAVASDGSRLHGIVnFLYHRSTWAAQ 82
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRP--VLVAEEDGEVVGFA-SLGPFRPRPAY 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489191967  83 DVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 81-136 6.77e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.83  E-value: 6.77e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489191967  81 AQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG0456   10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALY 65
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-136 4.91e-14

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: 64.08  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   21 WLEYWKAYQAFYEVELSAQATEAtwRRFFDEGEPMHCAVASDGSRLHGIVNFLYHRSTWaaqDVCYLEDLYVSPDVRGQQ 100
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDL--LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKG 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489191967  101 IGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:pfam00583  76 IGTALLQALLEWARERGCERIFLEVAADNLAAIALY 111
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 8-136 9.30e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 63.92  E-value: 9.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   8 VSVRPVAHEDFEQWLEYwkayqafyevelsaQATEATWRRFFDEGEPMHCAVASDGSRLHGIVNFLYhrstwAAQDVCYL 87
Cdd:COG0454    1 MSIRKATPEDINFILLI--------------EALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGLRR-----LDDKVLEL 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489191967  88 EDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG0454   62 KRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFY 110
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-131 3.48e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.40  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967  10 VRPVAHEDFEQWLE-YWKAYQAFYEVELSAqateatwrRFFDEGEPMHCAVASDGSRLHGIVNFLYHRSTWAAqDVCYLE 88
Cdd:COG3153    1 IRPATPEDAEAIAAlLRAAFGPGREAELVD--------RLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEG-PALLLG 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489191967  89 DLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHR 131
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP 114
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 45-136 2.32e-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: 55.00  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967  45 WRRFFDEGEPMHCAVASDGSRLHGIVNFLYHrstwaAQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWH 124
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCAALHPL-----DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL 92

                         90
                 ....*....|..
gi 489191967 125 TqesNHRAQRLY 136
Cdd:COG1246   93 T---TSAAIHFY 101
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-124 2.83e-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: 50.35  E-value: 2.83e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489191967  57 CAVASDGSRLHGIVNFLYHRSTwaaQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWH 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-136 6.40e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.91  E-value: 6.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489191967  83 DVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLY 67
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-136 6.18e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.45  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   56 HCAVASDGSRLHGIVNFLYHrstwAAQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTqesNHRAQRL 135
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALLPL----DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAF 76


                  .
gi 489191967  136 Y 136
Cdd:pfam13508  77 Y 77
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 29-136 3.01e-07

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: 46.55  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   29 QAFYEVELSAQA---TEATWRRFFDEgEPMHCAVASDGSRL--HGIVNFLYHRSTwaaqdvcyLEDLYVSPDVRGQQIGK 103
Cdd:TIGR01575   3 KAVLEIEAAAFAfpwTEAQFAEELAN-YHLCYLLARIGGKVvgYAGVQIVLDEAH--------ILNIAVKPEYQGQGIGR 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 489191967  104 QLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:TIGR01575  74 ALLRELIDEAKGRGVNEIFLEVRVSNIAAQALY 106
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 27-116 1.29e-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: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   27 AYQAFYEvelsaQATEATWRRFFDEGEpMHCAVASDGSRLHGIVnflyhrstwAAQDVCYLEDLYVSPDVRGQQIGKQLI 106
Cdd:pfam13673   9 GIETFYE-----FISPEALRERIDQGE-YFFFVAFEGGQIVGVI---------ALRDRGHISLLFVDPDYQGQGIGKALL 73

                          90
                  ....*....|
gi 489191967  107 EYVRRQAEER 116
Cdd:pfam13673  74 EAVEDYAEKD 83
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 92-137 1.83e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.22  E-value: 1.83e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489191967  92 VSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLYD 137
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYE 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-136 2.38e-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: 39.21  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191967   8 VSVRPVAHEDFEQWLEYW---KAYQAFYEVELSAQATEATWRRF---FDEGEPMHCAVASDGSRLH-GIVNFlyHRSTWA 80
Cdd:COG1670    8 LRLRPLRPEDAEALAELLndpEVARYLPGPPYSLEEARAWLERLladWADGGALPFAIEDKEDGELiGVVGL--YDIDRA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489191967  81 AQDVCYleDLYVSPDVRGQQIGKQLIEYVRRQA-EERRCARLYWHTQESNHRAQRLY 136
Cdd:COG1670   86 NRSAEI--GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVL 140
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
90-136 2.68e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 39.14  E-value: 2.68e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489191967  90 LYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESNHRAQRLY 136
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLY 178
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
80-136 4.73e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.86  E-value: 4.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489191967  80 AAQDVCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRCARLYWHTQESnhrAQRLY 136
Cdd:COG2153   54 PGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFY 107
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 84-118 6.58e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 35.07  E-value: 6.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489191967  84 VCYLEDLYVSPDVRGQQIGKQLIEYVRRQAEERRC 118
Cdd:PLN02706  85 VGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGC 119
 
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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