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Conserved domains on  [gi|488249930|ref|WP_002321138|]
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MULTISPECIES: N-acetyltransferase [Enterococcus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 18514852)

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:0008080
PubMed:  15581578|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 ...
 80-164 1.61e-21

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.17  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  80 ADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGFIKYSEHVFYMGDDpqtDYL 159
Cdd:COG0456   10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALV 86


                 ....*
gi 488249930 160 FIKQL 164
Cdd:COG0456   87 MEKEL 91
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-140 2.96e-16

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 71.56  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQI---SIETFTDTFGKDN-SPEHLADYLtqayalekltEELKDKETDFFLVSIDQEPAGYLKLntGTSQS 76
Cdd:COG1247    7 ATPEDAPAIAAIyneAIAEGTATFETEPpSEEEREAWF----------AAILAPGRPVLVAEEDGEVVGFASL--GPFRP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488249930  77 EEMADHFLEiERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGF 140
Cdd:COG1247   75 RPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-164 1.61e-21

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.17  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  80 ADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGFIKYSEHVFYMGDDpqtDYL 159
Cdd:COG0456   10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALV 86


                 ....*
gi 488249930 160 FIKQL 164
Cdd:COG0456   87 MEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-140 1.79e-17

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: 73.32  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   54 FFLVSIDQEPAGYLKLNTGTSQseemaDHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALA 133
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDE-----PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIA 109


                  ....*..
gi 488249930  134 FYRKKGF 140
Cdd:pfam00583 110 LYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-140 2.96e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 71.56  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQI---SIETFTDTFGKDN-SPEHLADYLtqayalekltEELKDKETDFFLVSIDQEPAGYLKLntGTSQS 76
Cdd:COG1247    7 ATPEDAPAIAAIyneAIAEGTATFETEPpSEEEREAWF----------AAILAPGRPVLVAEEDGEVVGFASL--GPFRP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488249930  77 EEMADHFLEiERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGF 140
Cdd:COG1247   75 RPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-140 8.43e-13

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: 61.58  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   45 EELKDKETDFFLVSIDQEPAGYLklntGTSQSEEMAdhflEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGV 124
Cdd:TIGR01575  24 EELANYHLCYLLARIGGKVVGYA----GVQIVLDEA----HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEV 95

                          90
                  ....*....|....*.
gi 488249930  125 WEHNDVALAFYRKKGF 140
Cdd:TIGR01575  96 RVSNIAAQALYKKLGF 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-122 1.41e-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: 54.20  E-value: 1.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488249930  54 FFLVSIDQEPAGYLKLNTgtsqsEEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWL 122
Cdd:cd04301    1 FLVAEDDGEIVGFASLSP-----DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
1-113 4.00e-05

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 41.07  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQISIETFTDTFGKDNSPEHLADYLTQAYALEKLTEELKDKETDFFLVSI----DQEPAGYLKLNTGTSQS 76
Cdd:NF041158   7 LSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNLDIIFLgafvNSALIGFIELKIIADKA 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488249930  77 EEMadhfleieRIYVRKKFKHQGIGTFLLDTAIEKAK 113
Cdd:NF041158  87 ELL--------RLYLKPEYTHRGIGKLLLSEAEKIMK 115
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 89-140 3.59e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.06  E-value: 3.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488249930  89 IYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGF 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-164 1.61e-21

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.17  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  80 ADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGFIKYSEHVFYMGDDpqtDYL 159
Cdd:COG0456   10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALV 86


                 ....*
gi 488249930 160 FIKQL 164
Cdd:COG0456   87 MEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-140 1.79e-17

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: 73.32  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   54 FFLVSIDQEPAGYLKLNTGTSQseemaDHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALA 133
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDE-----PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIA 109


                  ....*..
gi 488249930  134 FYRKKGF 140
Cdd:pfam00583 110 LYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-140 2.96e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 71.56  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQI---SIETFTDTFGKDN-SPEHLADYLtqayalekltEELKDKETDFFLVSIDQEPAGYLKLntGTSQS 76
Cdd:COG1247    7 ATPEDAPAIAAIyneAIAEGTATFETEPpSEEEREAWF----------AAILAPGRPVLVAEEDGEVVGFASL--GPFRP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488249930  77 EEMADHFLEiERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGF 140
Cdd:COG1247   75 RPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 41-152 1.15e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.31  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  41 EKLTEELKDKETD-----FFLVSIDQEPAGYLKLNtgtsqseEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEK 115
Cdd:COG0454   18 EALDAELKAMEGSlagaeFIAVDDKGEPIGFAGLR-------RLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARER 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488249930 116 QKTAIWLGVWEHNDVALAFYRKKGFIKYSEHVFYMGD 152
Cdd:COG0454   91 GCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-145 2.50e-13

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 63.28  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  48 KDKETDFFLVSIDQEPAGYLKLNtgtsqseEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEH 127
Cdd:COG2153   30 KDEDARHLLAYDDGELVATARLL-------PPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH 102

                         90
                 ....*....|....*...
gi 488249930 128 ndvALAFYRKKGFIKYSE 145
Cdd:COG2153  103 ---AVGFYEKLGFVPVGE 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-140 8.43e-13

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: 61.58  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   45 EELKDKETDFFLVSIDQEPAGYLklntGTSQSEEMAdhflEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGV 124
Cdd:TIGR01575  24 EELANYHLCYLLARIGGKVVGYA----GVQIVLDEA----HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEV 95

                          90
                  ....*....|....*.
gi 488249930  125 WEHNDVALAFYRKKGF 140
Cdd:TIGR01575  96 RVSNIAAQALYKKLGF 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
1-164 1.46e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQISIETFTDTfgkdnspehladylTQAYALEKLTEELKDKEtdFFLVSIDQEPAGYLKLNTGTSQSEema 80
Cdd:COG3153    4 ATPEDAEAIAALLRAAFGPG--------------REAELVDRLREDPAAGL--SLVAEDDGEIVGHVALSPVDIDGE--- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  81 DHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVwehNDVALAFYRKKGFIKYSEHVFYMGDDpqtDYLF 160
Cdd:COG3153   65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELGLTLGPD---EVFL 138


                 ....
gi 488249930 161 IKQL 164
Cdd:COG3153  139 AKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-140 3.85e-12

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: 60.01  E-value: 3.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930  34 LTQAYALEklteelkDKETDFFLVSIDQEPAGYLKLntgtsqsEEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAK 113
Cdd:COG1246   17 LIRPYALE-------EEIGEFWVAEEDGEIVGCAAL-------HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEAR 82

                         90       100
                 ....*....|....*....|....*..
gi 488249930 114 EKQKTAIWLGVwehNDVALAFYRKKGF 140
Cdd:COG1246   83 ELGLKRLFLLT---TSAAIHFYEKLGF 106
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-142 4.71e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   54 FFLVSIDQEPAGYLKLntgtsqSEEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHndvALA 133
Cdd:pfam13508   5 FFVAEDDGKIVGFAAL------LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAA 75


                  ....*....
gi 488249930  134 FYRKKGFIK 142
Cdd:pfam13508  76 FYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-122 1.41e-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: 54.20  E-value: 1.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488249930  54 FFLVSIDQEPAGYLKLNTgtsqsEEMADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWL 122
Cdd:cd04301    1 FLVAEDDGEIVGFASLSP-----DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 24-141 6.16e-09

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: 51.50  E-value: 6.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   24 DNSPEHLADYLTQAYAlEKLTEELKDKETDFFLVSIDQEPAGYLKLNTGtsqseemaDHfleIERIYVRKKFKHQGIGTF 103
Cdd:pfam13673   4 DYSEEGIETFYEFISP-EALRERIDQGEYFFFVAFEGGQIVGVIALRDR--------GH---ISLLFVDPDYQGQGIGKA 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488249930  104 LLDTAIEKAKEKQKTAIWLGVWEHNdVALAFYRKKGFI 141
Cdd:pfam13673  72 LLEAVEDYAEKDGIKLSELTVNASP-YAVPFYEKLGFR 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
79-150 1.60e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.44  E-value: 1.60e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488249930  79 MADHFLEIERIYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGFIKYSEHVFYM 150
Cdd:COG3393   11 ESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVL 82
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-142 2.34e-07

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: 48.07  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQI--SIETFTDTFGKDNSPEHLADYLtqayalEKLTEELKDKETDFFLV--SIDQEPAGYLKLNtgtsqS 76
Cdd:COG1670   13 LRPEDAEALAELlnDPEVARYLPGPPYSLEEARAWL------ERLLADWADGGALPFAIedKEDGELIGVVGLY-----D 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488249930  77 EEMADHFLEIeRIYVRKKFKHQGIGTFLLDTAIEKAKEKQK-TAIWLGVWEHNDVALAFYRKKGFIK 142
Cdd:COG1670   82 IDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGlHRVEAEVDPDNTASIRVLEKLGFRL 147
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
1-113 4.00e-05

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 41.07  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488249930   1 MTPSDVDLLQQISIETFTDTFGKDNSPEHLADYLTQAYALEKLTEELKDKETDFFLVSI----DQEPAGYLKLNTGTSQS 76
Cdd:NF041158   7 LSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNLDIIFLgafvNSALIGFIELKIIADKA 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488249930  77 EEMadhfleieRIYVRKKFKHQGIGTFLLDTAIEKAK 113
Cdd:NF041158  87 ELL--------RLYLKPEYTHRGIGKLLLSEAEKIMK 115
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 89-140 3.59e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.06  E-value: 3.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488249930  89 IYVRKKFKHQGIGTFLLDTAIEKAKEKQKTAIWLGVWEHNDVALAFYRKKGF 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Acetyltransf_13 pfam13880
ESCO1/2 acetyl-transferase;
86-111 4.07e-03

ESCO1/2 acetyl-transferase;


Pssm-ID: 464015  Cd Length: 69  Bit Score: 34.38  E-value: 4.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 488249930   86 IERIYVRKKFKHQGIGTFLLDTAIEK 111
Cdd:pfam13880   7 ISRIWVSPSHRRKGIATRLLDAARSN 32
 
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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