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Conserved domains on  [gi|847055961|ref|WP_047959095|]
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MULTISPECIES: GNAT family N-acetyltransferase [Enterobacter]

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];
11-175 2.21e-63

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.90  E-value: 2.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  11 ELEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRHRMKSVAENGLPWLIALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  91 TLEESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 847055961 171 MQRPL 175
Cdd:COG1247  159 MQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
11-175 2.21e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.90  E-value: 2.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  11 ELEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRHRMKSVAENGLPWLIALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  91 TLEESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 847055961 171 MQRPL 175
Cdd:COG1247  159 MQKRL 163
PRK10140 PRK10140
N-acetyltransferase;
10-173 2.73e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 64.23  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  10 TELEVRDALPDDVHAIAAIYAW-HVLHGRAsfeEVPPTIDEM-RHRMksVAENGLPWLIALYRGIVVGY-CYATPYRPRH 86
Cdd:PRK10140   2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMwQERL--ADRPGIKQLVACIDGDVVGHlTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  87 AYryTLEESIYVDASITGRGFGSALMSALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKHGFEIVGQLRSVGYKK 162
Cdd:PRK10140  77 SH--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRN 149

                        170
                 ....*....|.
gi 847055961 163 GDWRDTVIMQR 173
Cdd:PRK10140 150 GEYVDAYYMAR 160
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-149 2.12e-10

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: 55.60  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   25 IAAIYAWHVLHGRASFEEVPPTIDEMRHRmksvaENGLPWLIALYRGIVVGYCYATPYRPRHAYRYtlEESIYVDASITG 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDE-----DASEGFFVAEEDGELVGFASLSIIDDEPPVGE--IEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 847055961  105 RGFGSALMSALIARC-EQGPWRQMIAVVgdgNNNAGSLRLHKKHGF 149
Cdd:pfam00583  74 KGIGTALLQALLEWArERGCERIFLEVA---ADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 3.50e-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: 3.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 847055961  64 WLIALYRGIVVGYCYATPYRPRHAYRYTleESIYVDASITGRGFGSALMSALIARCEQ 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYI--GDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
11-175 2.21e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.90  E-value: 2.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  11 ELEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRHRMKSVAENGLPWLIALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  91 TLEESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 847055961 171 MQRPL 175
Cdd:COG1247  159 MQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 9-177 1.68e-14

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: 67.72  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   9 ETE-LEVRDALPDDVHAIAAIYA-WHVlhgRASFEEVPPTIDEMRHRMKSVAE-----NGLPWLIALYR-GIVVGYCYAT 80
Cdd:COG1670    4 ETErLRLRPLRPEDAEALAELLNdPEV---ARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEdGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  81 PYRPRHAyryTLEESIYVDASITGRGFGSALMSALIARC-EQGPWRQMIAVVGDGNnnAGSLRLHKKHGFEIVGQLRSVG 159
Cdd:COG1670   81 DIDRANR---SAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDN--TASIRVLEKLGFRLEGTLRDAL 155

                        170
                 ....*....|....*...
gi 847055961 160 YKKGDWRDTVIMQRPLND 177
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
PRK10140 PRK10140
N-acetyltransferase;
10-173 2.73e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 64.23  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  10 TELEVRDALPDDVHAIAAIYAW-HVLHGRAsfeEVPPTIDEM-RHRMksVAENGLPWLIALYRGIVVGY-CYATPYRPRH 86
Cdd:PRK10140   2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMwQERL--ADRPGIKQLVACIDGDVVGHlTIDVQQRPRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  87 AYryTLEESIYVDASITGRGFGSALMSALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKHGFEIVGQLRSVGYKK 162
Cdd:PRK10140  77 SH--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRN 149

                        170
                 ....*....|.
gi 847055961 163 GDWRDTVIMQR 173
Cdd:PRK10140 150 GEYVDAYYMAR 160
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-149 2.12e-10

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: 55.60  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   25 IAAIYAWHVLHGRASFEEVPPTIDEMRHRmksvaENGLPWLIALYRGIVVGYCYATPYRPRHAYRYtlEESIYVDASITG 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDE-----DASEGFFVAEEDGELVGFASLSIIDDEPPVGE--IEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 847055961  105 RGFGSALMSALIARC-EQGPWRQMIAVVgdgNNNAGSLRLHKKHGF 149
Cdd:pfam00583  74 KGIGTALLQALLEWArERGCERIFLEVA---ADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
14-175 3.39e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  14 VRDALPDDVHAIAAIYawhvlhgRASFEevPPTIDEMRHRMKSVAENGLPWlIALYRGIVVGYCYATPYRPRHAYRYTLE 93
Cdd:COG3153    1 IRPATPEDAEAIAALL-------RAAFG--PGREAELVDRLREDPAAGLSL-VAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  94 ESIYVDASITGRGFGSALMSALIARCEQGPWRqMIAVVGDgnnnAGSLRLHKKHGFEIVGQLRSVGYKkgdwrDTVIMQR 173
Cdd:COG3153   71 GPLAVDPEYRGQGIGRALMRAALEAARERGAR-AVVLLGD----PSLLPFYERFGFRPAGELGLTLGP-----DEVFLAK 140


                 ..
gi 847055961 174 PL 175
Cdd:COG3153  141 EL 142
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 5.93e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 55.07  E-value: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   14 VRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRHRMKSV-AENGLPWLIAlYRGIVVGYCYATPYRPRhaYRYTL 92
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlSPGEIVFGVA-ESDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   93 EESIYVDASITgRGFGSALMSALI--ARCEQGPWRQMIAVVgdgNNNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 12-176 6.02e-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: 54.61  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  12 LEVRDALPDDVHAIAAIyawhvlhgrasfeevpptidemrHRMKSVAENGLPWLIALYRGIVVGYCYATPYRPRHAYryt 91
Cdd:COG1246    1 MTIRPATPDDVPAILEL-----------------------IRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAE--- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  92 LEeSIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDgnnnaGSLRLHKKHGFEIVGQlRSVGYKKGDWRDTVIM 171
Cdd:COG1246   55 LR-SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS-----AAIHFYEKLGFEEIDK-EDLPYAKVWQRDSVVM 127


                 ....*
gi 847055961 172 QRPLN 176
Cdd:COG1246  128 EKDLE 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 12-156 8.24e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 54.29  E-value: 8.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  12 LEVRDALPDDVHAIAAIYAWHvlhgrasfeevpptiDEMRHRMKSVAENGlpWLIALYRGIVVGYCYATPYRPRHAYryt 91
Cdd:COG0454    1 MSIRKATPEDINFILLIEALD---------------AELKAMEGSLAGAE--FIAVDDKGEPIGFAGLRRLDDKVLE--- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847055961  92 LEEsIYVDASITGRGFGSALMSALI--ARcEQGpWRQMIAVVGDGNNNAgsLRLHKKHGFEIVGQLR 156
Cdd:COG0454   61 LKR-LYVLPEYRGKGIGKALLEALLewAR-ERG-CTALELDTLDGNPAA--IRFYERLGFKEIERYV 122
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 94-176 4.90e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 51.19  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  94 ESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGNNNAgsLRLHKKHGFEIVGQLRSVGykkgdWRDTVIMQR 173
Cdd:COG0456   17 EDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAA--IALYEKLGFEEVGERPNYY-----GDDALVMEK 89


                 ...
gi 847055961 174 PLN 176
Cdd:COG0456   90 ELA 92
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
12-177 3.07e-08

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 50.70  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  12 LEVRDALPDDVHAIAAIYAWHVlhgrasfeevpPTIDEM-RHRMKSVAENGLPWLIALYRGIVVGYCYATPYRPRHA--- 87
Cdd:COG3818    5 IVIRDAREHDLDAVLALNNAAV-----------PAVSPLdAARLARLHEQAAYARVAEVDGEVAGFLLAFGPGADYDspn 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  88 YRY---TLEESIYVD-----ASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGNNNAGSLRLHKKHGFEIVGQLRSVG 159
Cdd:COG3818   74 YRWfaeRYDNFLYIDrivvaPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEPPNPGSLAFHARLGFREVGQQRVAG 153

                        170
                 ....*....|....*....
gi 847055961 160 YKKgdwrdTVIMQ-RPLND 177
Cdd:COG3818  154 GKK-----RVSLLaKELCS 167
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
73-162 3.99e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 43.36  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961  73 VVGYCYATPYRPRHAYrytlEESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIV 152
Cdd:COG3393    2 LVAMAGVRAESPGVAE----ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDAD--NPAARRLYERLGFRPV 75

                         90
                 ....*....|
gi 847055961 153 GQLRSVGYKK 162
Cdd:COG3393   76 GEYATVLFRK 85
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 65-151 6.23e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.83  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   65 LIALYRGIVVGYCYATPYrprHAYRYTLEESIYVDASITGRGFGSALMSALIARCEQGPWRQMIAvvgdgNNNAGSLRLH 144
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPL---DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL-----ETTNRAAAFY 77


                  ....*..
gi 847055961  145 KKHGFEI 151
Cdd:pfam13508  78 EKLGFEE 84
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-150 7.39e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 40.79  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847055961   12 LEVRDALPDDVHAIAAIYA-WHVLHGRASFeevPPTIDEMRHRMKSV-----AENGLPWLIALYRGIVVGYCyatPYRPR 85
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSdPEVMRYGVPW---PLTLEEAREWLARIwaadeAERGYGWAIELKDTGFIGSI---GLYDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 847055961   86 HAYRYTLEESIYVDASITGRGFGSALMSALIARC-EQGPWRQMIAVVGdgNNNAGSLRLHKKHGFE 150
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARID--PENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 3.50e-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: 3.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 847055961  64 WLIALYRGIVVGYCYATPYRPRHAYRYTleESIYVDASITGRGFGSALMSALIARCEQ 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYI--GDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
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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