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Conserved domains on  [gi|1095436890|gb|AOZ94015|]
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GNAT family N-acetyltransferase [Paenibacillus crassostreae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 20260227)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  9175471|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
87-171 6.82e-19

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 6.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  87 GNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDeeqTDFI 166
Cdd:COG0456    10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALV 86

                  ....*
gi 1095436890 167 MTKTL 171
Cdd:COG0456    87 MEKEL 91
Spm_actase_Thplmales super family cl46108
spermidine N(1)-acetyltransferase;
3-118 2.33e-03

spermidine N(1)-acetyltransferase;


The actual alignment was detected with superfamily member NF041158:

Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.06  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890   3 INIKKCTFEDLGLLQEISVETFNETFKIQNSPKNMKAYLEKAFN----LKQLEKELSNISSEFYFIYSNEEIAGYLKLNT 78
Cdd:NF041158    2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSkeklLNEIIRSQSNLDIIFLGAFVNSALIGFIELKI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1095436890  79 YEVQTEMMgndsleieRIYIRKKLHKQGLGKYLINKAIEI 118
Cdd:NF041158   82 IADKAELL--------RLYLKPEYTHRGIGKLLLSEAEKI 113
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
87-171 6.82e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 6.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  87 GNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDeeqTDFI 166
Cdd:COG0456    10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALV 86

                  ....*
gi 1095436890 167 MTKTL 171
Cdd:COG0456    87 MEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
50-147 2.48e-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: 62.92  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  50 LEKELSNISSEFYFIYSNEEIAGYLKLNTYEVQTEMMgndslEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWL 129
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG-----EIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98
                          90
                  ....*....|....*...
gi 1095436890 130 GVWEKNESAITFYKKIDF 147
Cdd:pfam00583  99 EVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
46-167 1.27e-10

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: 56.18  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  46 NLKQLEKELSNISSEFYFIYSNEEIAGYLKLNTYEvqtemmgnDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKE 125
Cdd:TIGR01575  18 TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVL--------DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVN 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1095436890 126 KIWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDEEQTDFIM 167
Cdd:TIGR01575  90 EIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
61-129 3.03e-08

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: 48.04  E-value: 3.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1095436890  61 FYFIYSNEEIAGYLKLNTYEvqtemMGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWL 129
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDG-----SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
3-118 2.33e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.06  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890   3 INIKKCTFEDLGLLQEISVETFNETFKIQNSPKNMKAYLEKAFN----LKQLEKELSNISSEFYFIYSNEEIAGYLKLNT 78
Cdd:NF041158    2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSkeklLNEIIRSQSNLDIIFLGAFVNSALIGFIELKI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1095436890  79 YEVQTEMMgndsleieRIYIRKKLHKQGLGKYLINKAIEI 118
Cdd:NF041158   82 IADKAELL--------RLYLKPEYTHRGIGKLLLSEAEKI 113
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
105-147 8.07e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 8.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1095436890 105 QGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDF 147
Cdd:PRK09491   78 QGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
87-171 6.82e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 6.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  87 GNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDeeqTDFI 166
Cdd:COG0456    10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD---DALV 86

                  ....*
gi 1095436890 167 MTKTL 171
Cdd:COG0456    87 MEKEL 91
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
47-165 8.54e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 67.39  E-value: 8.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  47 LKQLEKELSNisSEFYFIYSNEEIAGYLKLNtyevqteMMGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEK 126
Cdd:COG0454    24 LKAMEGSLAG--AEFIAVDDKGEPIGFAGLR-------RLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTA 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1095436890 127 IWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDEEQTDF 165
Cdd:COG0454    95 LELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKEL 133
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
50-147 2.48e-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: 62.92  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  50 LEKELSNISSEFYFIYSNEEIAGYLKLNTYEVQTEMMgndslEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWL 129
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG-----EIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98
                          90
                  ....*....|....*...
gi 1095436890 130 GVWEKNESAITFYKKIDF 147
Cdd:pfam00583  99 EVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-171 1.73e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 61.93  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890   2 TINIKKCTFEDLGLLQEIsvetFNETfkiqnSPKNMKAYLEKAFNLKQLEKELSNISSEFYFIY---SNEEIAGYLKLNT 78
Cdd:COG1247     1 EMTIRPATPEDAPAIAAI----YNEA-----IAEGTATFETEPPSEEEREAWFAAILAPGRPVLvaeEDGEVVGFASLGP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  79 YevQTEMMGNDSLEiERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDFVQTGAHS--FY 156
Cdd:COG1247    72 F--RPRPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPevGF 148
                         170
                  ....*....|....*
gi 1095436890 157 MGDEEQTDFIMTKTL 171
Cdd:COG1247   149 KFGRWLDLVLMQKRL 163
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
62-151 1.13e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 56.35  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  62 YFIYSNEEIAGYLKLNTYevqtemmGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVwekNESAITF 141
Cdd:COG2153    37 LLAYDDGELVATARLLPP-------GDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGF 106
                          90
                  ....*....|
gi 1095436890 142 YKKIDFVQTG 151
Cdd:COG2153   107 YEKLGFVPVG 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
46-167 1.27e-10

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: 56.18  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  46 NLKQLEKELSNISSEFYFIYSNEEIAGYLKLNTYEvqtemmgnDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKE 125
Cdd:TIGR01575  18 TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVL--------DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVN 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1095436890 126 KIWLGVWEKNESAITFYKKIDFVQTGAHSFYMGDEEQTDFIM 167
Cdd:TIGR01575  90 EIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
54-171 1.34e-09

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: 53.46  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  54 LSNISSEFYFIYSNEEIAGYLKLNTYevqtemmGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVwe 133
Cdd:COG1246    23 LEEEIGEFWVAEEDGEIVGCAALHPL-------DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT-- 93
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1095436890 134 kNESAITFYKKIDFVQTGAHSFYMGDEEQTDFI-MTKTL 171
Cdd:COG1246    94 -TSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVvMEKDL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
58-149 1.29e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  58 SSEFYFIYSNEEIAGYLKLNTYEvqtemmGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVwekNES 137
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLD------DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNR 72
                          90
                  ....*....|..
gi 1095436890 138 AITFYKKIDFVQ 149
Cdd:pfam13508  73 AAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
61-129 3.03e-08

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: 48.04  E-value: 3.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1095436890  61 FYFIYSNEEIAGYLKLNTYEvqtemMGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWL 129
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDG-----SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
67-171 7.31e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.23  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  67 NEEIAGYLKLNTYEVQTEMmgnDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVwekNESAITFYKKID 146
Cdd:COG3153    47 DGEIVGHVALSPVDIDGEG---PALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFG 120
                          90       100
                  ....*....|....*....|....*
gi 1095436890 147 FVQTGAHSFYMGDEEqtdFIMTKTL 171
Cdd:COG3153   121 FRPAGELGLTLGPDE---VFLAKEL 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
48-151 1.31e-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: 45.34  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890  48 KQLEKELSNISSEFYFIYSNEEIAGYLKLNTYEVqtemmgndsleIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKI 127
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIALRDRGH-----------ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS 88
                          90       100
                  ....*....|....*....|....*.
gi 1095436890 128 WLGVwekNES--AITFYKKIDFVQTG 151
Cdd:pfam13673  89 ELTV---NASpyAVPFYEKLGFRATG 111
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
85-157 1.60e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.13  E-value: 1.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1095436890  85 MMGNDSLEIERIYIRKKLHKQGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDFVQTGAHSFYM 157
Cdd:COG3393    10 AESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVL 82
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
3-118 2.33e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.06  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095436890   3 INIKKCTFEDLGLLQEISVETFNETFKIQNSPKNMKAYLEKAFN----LKQLEKELSNISSEFYFIYSNEEIAGYLKLNT 78
Cdd:NF041158    2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSkeklLNEIIRSQSNLDIIFLGAFVNSALIGFIELKI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1095436890  79 YEVQTEMMgndsleieRIYIRKKLHKQGLGKYLINKAIEI 118
Cdd:NF041158   82 IADKAELL--------RLYLKPEYTHRGIGKLLLSEAEKI 113
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
105-147 8.07e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 8.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1095436890 105 QGLGKYLINKAIEIAIVRNKEKIWLGVWEKNESAITFYKKIDF 147
Cdd:PRK09491   78 QGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
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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