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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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];
14-178 4.50e-22

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 87.74  E-value: 4.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  14 TYTIRSAAEKDAEQLSKI------RVQIDGETENMDRDAGEGFIDDLgfqkiiktdsEETKNLFLVVEVHNRIVGFSRCE 87
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneaiaEGTATFETEPPSEEEREAWFAAI----------LAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  88 -GSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNDKRLs 166
Cdd:COG1247   71 pFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFK- 149

                        170
                 ....*....|..
gi 446558330 167 DGKYYNTVVMGR 178
Cdd:COG1247  150 FGRWLDLVLMQK 161
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
14-178 4.50e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 87.74  E-value: 4.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  14 TYTIRSAAEKDAEQLSKI------RVQIDGETENMDRDAGEGFIDDLgfqkiiktdsEETKNLFLVVEVHNRIVGFSRCE 87
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneaiaEGTATFETEPPSEEEREAWFAAI----------LAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  88 -GSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNDKRLs 166
Cdd:COG1247   71 pFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFK- 149

                        170
                 ....*....|..
gi 446558330 167 DGKYYNTVVMGR 178
Cdd:COG1247  150 FGRWLDLVLMQK 161
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 65-153 3.26e-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: 63.31  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   65 EETKNLFLVVEVHNRIVGFSRCeGSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKA 144
Cdd:pfam00583  29 EDASEGFFVAEEDGELVGFASL-SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAA 107


                  ....*....
gi 446558330  145 IHLYKKLGF 153
Cdd:pfam00583 108 IALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 100-175 2.11e-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: 2.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446558330  100 FGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNdkrlsdgkYYNTVV 175
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRN--------YYPDPG 125
PRK10140 PRK10140
N-acetyltransferase;
17-178 1.31e-09

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  17 IRSAAEKDAEQLSKIRVQ--IDGETENMDRDAGEGFIDDLGFQKIIKTdseetknlfLVVEVHNRIVGFSRCEGSNFKRL 94
Cdd:PRK10140   6 IRHAETRDYEAIRQIHAQpeVYHNTLQVPHPSDHMWQERLADRPGIKQ---------LVACIDGDVVGHLTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  95 SHKVEFGVCILKEFWGYRMGKSLLQQSIKWADE-NAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNdKRLSDGKYYNT 173
Cdd:PRK10140  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKK-YALRNGEYVDA 155


                 ....*
gi 446558330 174 VVMGR 178
Cdd:PRK10140 156 YYMAR 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-135 5.10e-04

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: 37.26  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446558330  71 FLVVEVHNRIVGFSRCEGSNFKRLSHKVEFgVCILKEFWGYRMGKSLLQQSIKWADENAVNKISL 135
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
14-178 4.50e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 87.74  E-value: 4.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  14 TYTIRSAAEKDAEQLSKI------RVQIDGETENMDRDAGEGFIDDLgfqkiiktdsEETKNLFLVVEVHNRIVGFSRCE 87
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneaiaEGTATFETEPPSEEEREAWFAAI----------LAPGRPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  88 -GSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNDKRLs 166
Cdd:COG1247   71 pFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFK- 149

                        170
                 ....*....|..
gi 446558330 167 DGKYYNTVVMGR 178
Cdd:COG1247  150 FGRWLDLVLMQK 161
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-178 3.54e-20

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: 83.12  E-value: 3.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  10 INGLTYTIRSAAEKDAEQLSKI----RVQIDGETENMDRDAGEGFIDDlgfqkiIKTDSEETKNLFLVVE--VHNRIVGF 83
Cdd:COG1670    3 LETERLRLRPLRPEDAEALAELlndpEVARYLPGPPYSLEEARAWLER------LLADWADGGALPFAIEdkEDGELIGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  84 SRCegSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWA-DENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKND 162
Cdd:COG1670   77 VGL--YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154

                        170
                 ....*....|....*.
gi 446558330 163 KRLsDGKYYNTVVMGR 178
Cdd:COG1670  155 LVI-DGRYRDHVLYSL 169
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 15-155 1.58e-14

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: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  15 YTIRSAAEKDAEQLSKIRvQIDGETENMDrdagegfiddlgfqkiiktdSEETKNLFLVVEVHNRIVGFSrcegsNFKRL 94
Cdd:COG0454    1 MSIRKATPEDINFILLIE-ALDAELKAME--------------------GSLAGAEFIAVDDKGEPIGFA-----GLRRL 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446558330  95 SHKVEF--GVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEV 155
Cdd:COG0454   55 DDKVLElkRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 102-161 1.40e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.52  E-value: 1.40e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330 102 VCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKN 161
Cdd:COG0456   19 LAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 65-153 3.26e-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: 63.31  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   65 EETKNLFLVVEVHNRIVGFSRCeGSNFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKA 144
Cdd:pfam00583  29 EDASEGFFVAEEDGELVGFASL-SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAA 107


                  ....*....
gi 446558330  145 IHLYKKLGF 153
Cdd:pfam00583 108 IALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 71-155 1.42e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.54  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   71 FLVVEVHNRIVGFSRCEGsnFKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKIslqVLETNEKAIHLYKK 150
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLP--LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLL---ELETTNRAAAFYEK 79


                  ....*
gi 446558330  151 LGFEV 155
Cdd:pfam13508  80 LGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 100-175 2.11e-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: 2.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446558330  100 FGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNdkrlsdgkYYNTVV 175
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRN--------YYPDPG 125
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
17-157 7.08e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.09  E-value: 7.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  17 IRSAAEKDAEQLSKIRVQIDGETENMDrdagegFIDDLgfqkiiktDSEETKNLFLVVEVHNRIVGFSRCEGSNFKRLSH 96
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAE------LVDRL--------REDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGP 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446558330  97 KVEFG-VCILKEFWGYRMGKSLLQQSIKWADENAVNKIslqVLETNEKAIHLYKKLGFEVEG 157
Cdd:COG3153   67 ALLLGpLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAG 125
PRK10140 PRK10140
N-acetyltransferase;
17-178 1.31e-09

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  17 IRSAAEKDAEQLSKIRVQ--IDGETENMDRDAGEGFIDDLGFQKIIKTdseetknlfLVVEVHNRIVGFSRCEGSNFKRL 94
Cdd:PRK10140   6 IRHAETRDYEAIRQIHAQpeVYHNTLQVPHPSDHMWQERLADRPGIKQ---------LVACIDGDVVGHLTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  95 SHKVEFGVCILKEFWGYRMGKSLLQQSIKWADE-NAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNdKRLSDGKYYNT 173
Cdd:PRK10140  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKK-YALRNGEYVDA 155


                 ....*
gi 446558330 174 VVMGR 178
Cdd:PRK10140 156 YYMAR 160
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 40-167 3.51e-09

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 53.13  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   40 ENMDRDAGEGFIDDLGFQKIIKTDSEetKNLFLVVEvHNRIVGFSrcegsNFKR--LSHKVEFGVCILKEFWGYRMGKSL 117
Cdd:TIGR03585  25 ANMYSDHLIDWEEHLHFIEALKQDPN--RRYWIVCQ-ESRPIGVI-----SFTDinLVHKSAFWGIYANPFCKPGVGSVL 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446558330  118 LQQSIKWADEN-AVNKISLQVLETNEKAIHLYKKLGFEVEGILKNDKRLSD 167
Cdd:TIGR03585  97 EEAALEYAFEHlGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQGGEYYD 147
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 65-155 2.03e-07

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: 48.06  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  65 EETKNLFLVVEVHNRIVGFSRcegsnFKRLSHKV-EFG-VCILKEFWGYRMGKSLLQQSIKWADENAVNKIslqVLETNE 142
Cdd:COG1246   24 EEEIGEFWVAEEDGEIVGCAA-----LHPLDEDLaELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRL---FLLTTS 95

                         90
                 ....*....|...
gi 446558330 143 KAIHLYKKLGFEV 155
Cdd:COG1246   96 AAIHFYEKLGFEE 108
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 97-179 2.81e-07

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 48.64  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  97 KVEFGVCILKEFwgyrMGKSLLQQSIKWADENAVN-----KISLQVLETNEKAIHLYKKLGFEVEGILKNDKRLsDGKYY 171
Cdd:PRK15130  83 RAEFQIIISPEY----QGKGLATRAAKLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFI-NGEYR 157


                 ....*...
gi 446558330 172 NTVVMGRF 179
Cdd:PRK15130 158 NTIRMCIF 165
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
63-157 1.07e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.95  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  63 DSEETKNLFLVVEVHNRIVGFSRC--EGSNFKRLSHkvefgVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLET 140
Cdd:COG2153   28 DGKDEDARHLLAYDDGELVATARLlpPGDGEAKIGR-----VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH 102

                         90
                 ....*....|....*..
gi 446558330 141 nekAIHLYKKLGFEVEG 157
Cdd:COG2153  103 ---AVGFYEKLGFVPVG 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 16-154 2.25e-06

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 45.41  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   16 TIRSAAEKDAEQLSKIR----VQIDGETENMDRDAGEGFIDDlgfqkIIKTDSEETKNLFLVVEVHNRIVGFSRCegSNF 91
Cdd:pfam13302   3 LLRPLTEEDAEALFELLsdpeVMRYGVPWPLTLEEAREWLAR-----IWAADEAERGYGWAIELKDTGFIGSIGL--YDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446558330   92 KRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWA-DENAVNKISLQVLETNEKAIHLYKKLGFE 154
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 70-176 4.48e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 44.53  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330  70 LFLVVEVHNRIVGFSRCEgsnfKRLSHKVEFGVCILKEFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYK 149
Cdd:PRK09491  41 LNLKLTVNGQMAAFAITQ----VVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYE 116

                         90       100
                 ....*....|....*....|....*..
gi 446558330 150 KLGFEVEGILKNDKRLSDGKyYNTVVM 176
Cdd:PRK09491 117 SLGFNEVTIRRNYYPTADGR-EDAIIM 142
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
101-157 5.73e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 5.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446558330 101 GVCILKEFW--GYrmGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEG 157
Cdd:COG3393   20 GVYTHPEYRgrGL--ASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
17-161 3.54e-05

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 42.35  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   17 IRSAAEKDAEQLSKIRVQIDGETEnMDRDAGEGFIDDlgFQKIIKTDSEETKNLFLVVEvHNRIVGFSRCEGSNFKRlSH 96
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPA-FTQEYAHSSIEE--FETFLAAYLSPGEIVFGVAE-SDRLIGYATLRQFDYVK-TH 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446558330   97 KVEFGVCILKEF-WGYrmGKSLLQQSIKWAD-ENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKN 161
Cdd:pfam13420  76 KAELSFYVVKNNdEGI--NRELINAIIQYARkNQNIENLEACIASNNINAIVFLKAIGFEWLGIERN 140
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 56-157 7.43e-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: 40.72  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446558330   56 FQKIIKTDSEETK-----NLFLVVEVHNRIVGFsrCEGSNFKRLSHkvefgVCILKEFWGYRMGKSLLQQSIKWADENAV 130
Cdd:pfam13673  13 FYEFISPEALRERidqgeYFFFVAFEGGQIVGV--IALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYAEKDGI 85

                          90       100
                  ....*....|....*....|....*..
gi 446558330  131 NKISLQVLETNEkAIHLYKKLGFEVEG 157
Cdd:pfam13673  86 KLSELTVNASPY-AVPFYEKLGFRATG 111
PRK03624 PRK03624
putative acetyltransferase; Provisional
 107-165 8.38e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.07  E-value: 8.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446558330 107 EFWGYRMGKSLLQQSIKWADENAVNKISLQVLETNEKAIHLYKKLGFEVEGILKNDKRL 165
Cdd:PRK03624  79 DFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISLGKRL 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-135 5.10e-04

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: 37.26  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446558330  71 FLVVEVHNRIVGFSRCEGSNFKRLSHKVEFgVCILKEFWGYRMGKSLLQQSIKWADENAVNKISL 135
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
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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