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Conserved domains on  [gi|1915230129|dbj|BBV87618|]
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acetyltransferase GCN5 [Enterobacter kobei]

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 4.47e-64

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 194.44  E-value: 4.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  11 ELEVRDALPDDVHAITAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLIALYRGIVVGYCYASPYRPRHAYRY 90
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  91 TLEESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247    81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                  ....*
gi 1915230129 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 4.47e-64

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 194.44  E-value: 4.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  11 ELEVRDALPDDVHAITAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLIALYRGIVVGYCYASPYRPRHAYRY 90
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  91 TLEESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247    81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                  ....*
gi 1915230129 171 MQRPL 175
Cdd:COG1247   159 MQKRL 163
PRK10140 PRK10140
N-acetyltransferase;
10-173 3.73e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 63.85  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  10 TELEVRDALPDDVHAITAIYAW-HVLHGRAsfeEVPPTIDEMRQRmKSVAENGLPWLIALYRGIVVGY-CYASPYRPRHA 87
Cdd:PRK10140    2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMWQE-RLADRPGIKQLVACIDGDVVGHlTIDVQQRPRRS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  88 YryTLEESIYVDASTTGRGFGTALMDALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKHGFEIVGQLRSVGYKKG 163
Cdd:PRK10140   78 H--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNG 150

                         170
                  ....*....|
gi 1915230129 164 DWRDTVIMQR 173
Cdd:PRK10140  151 EYVDAYYMAR 160
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 5.37e-11

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 57.76  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  14 VRDALPDDVHAITAIYAWHVLHGRASFEEVPPTIDEMRQRMKSV-AENGLPWLIAlYRGIVVGYCYASPYRPRhaYRYTL 92
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlSPGEIVFGVA-ESDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  93 EESIYVDASTTgRGFGTALMDALI--ARCEQGPWRQMIAVVgdgNNNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 4.37e-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: 4.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1915230129  64 WLIALYRGIVVGYCYASPYRPRHAYRYTleESIYVDASTTGRGFGTALMDALIARCEQ 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 4.47e-64

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 194.44  E-value: 4.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  11 ELEVRDALPDDVHAITAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLIALYRGIVVGYCYASPYRPRHAYRY 90
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  91 TLEESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247    81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                  ....*
gi 1915230129 171 MQRPL 175
Cdd:COG1247   159 MQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 9-177 6.91e-15

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: 68.87  E-value: 6.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129   9 ETE-LEVRDALPDDVHAITAIYA-WHVlhgRASFEEVPPTIDEMRQRMKSVAE-----NGLPWLIALYR-GIVVGYCYAS 80
Cdd:COG1670     4 ETErLRLRPLRPEDAEALAELLNdPEV---ARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEdGELIGVVGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  81 PYRPRHAyryTLEESIYVDASTTGRGFGTALMDALIARC-EQGPWRQMIAVVGDGNnnAGSLRLHKKHGFEIVGQLRSVG 159
Cdd:COG1670    81 DIDRANR---SAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDN--TASIRVLEKLGFRLEGTLRDAL 155

                         170
                  ....*....|....*...
gi 1915230129 160 YKKGDWRDTVIMQRPLND 177
Cdd:COG1670   156 VIDGRYRDHVLYSLLREE 173
PRK10140 PRK10140
N-acetyltransferase;
10-173 3.73e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 63.85  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  10 TELEVRDALPDDVHAITAIYAW-HVLHGRAsfeEVPPTIDEMRQRmKSVAENGLPWLIALYRGIVVGY-CYASPYRPRHA 87
Cdd:PRK10140    2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMWQE-RLADRPGIKQLVACIDGDVVGHlTIDVQQRPRRS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  88 YryTLEESIYVDASTTGRGFGTALMDALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKHGFEIVGQLRSVGYKKG 163
Cdd:PRK10140   78 H--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNG 150

                         170
                  ....*....|
gi 1915230129 164 DWRDTVIMQR 173
Cdd:PRK10140  151 EYVDAYYMAR 160
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 5.37e-11

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 57.76  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  14 VRDALPDDVHAITAIYAWHVLHGRASFEEVPPTIDEMRQRMKSV-AENGLPWLIAlYRGIVVGYCYASPYRPRhaYRYTL 92
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlSPGEIVFGVA-ESDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  93 EESIYVDASTTgRGFGTALMDALI--ARCEQGPWRQMIAVVgdgNNNAGSLRLHKKHGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 12-156 8.28e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.99  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  12 LEVRDALPDDVHAITAIYAWHvlhgrasfeevpptiDEMRQRMKSVAENGlpWLIALYRGIVVGYCYASPYRPRHAYryt 91
Cdd:COG0454     1 MSIRKATPEDINFILLIEALD---------------AELKAMEGSLAGAE--FIAVDDKGEPIGFAGLRRLDDKVLE--- 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915230129  92 LEEsIYVDASTTGRGFGTALMDALI--ARcEQGpWRQMIAVVGDGNNNAgsLRLHKKHGFEIVGQLR 156
Cdd:COG0454    61 LKR-LYVLPEYRGKGIGKALLEALLewAR-ERG-CTALELDTLDGNPAA--IRFYERLGFKEIERYV 122
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-149 1.45e-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: 55.99  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  25 ITAIYAWHVLHGRASFEEVPPTIDEMRQRmksvaENGLPWLIALYRGIVVGYCYASPYRPRHAYRYtlEESIYVDASTTG 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDE-----DASEGFFVAEEDGELVGFASLSIIDDEPPVGE--IEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1915230129 105 RGFGTALMDALIARC-EQGPWRQMIAVVgdgNNNAGSLRLHKKHGF 149
Cdd:pfam00583  74 KGIGTALLQALLEWArERGCERIFLEVA---ADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
14-175 3.03e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 3.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  14 VRDALPDDVHAITAIYawhvlhgRASFEevPPTIDEMRQRMKSVAENGLPWlIALYRGIVVGYCYASPYRPRHAYRYTLE 93
Cdd:COG3153     1 IRPATPEDAEAIAALL-------RAAFG--PGREAELVDRLREDPAAGLSL-VAEDDGEIVGHVALSPVDIDGEGPALLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  94 ESIYVDASTTGRGFGTALMDALIARCEQGPWRqMIAVVGDgnnnAGSLRLHKKHGFEIVGQLRSVGYKkgdwrDTVIMQR 173
Cdd:COG3153    71 GPLAVDPEYRGQGIGRALMRAALEAARERGAR-AVVLLGD----PSLLPFYERFGFRPAGELGLTLGP-----DEVFLAK 140


                  ..
gi 1915230129 174 PL 175
Cdd:COG3153   141 EL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 12-176 4.10e-10

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 55.00  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  12 LEVRDALPDDVHAITAIYawhvlhgrasfeevpptidemrqRMKSVAENGLPWLIALYRGIVVGYCYASPYRPRHAYryt 91
Cdd:COG1246     1 MTIRPATPDDVPAILELI-----------------------RPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAE--- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  92 LEeSIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDgnnnaGSLRLHKKHGFEIVGQlRSVGYKKGDWRDTVIM 171
Cdd:COG1246    55 LR-SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS-----AAIHFYEKLGFEEIDK-EDLPYAKVWQRDSVVM 127


                  ....*
gi 1915230129 172 QRPLN 176
Cdd:COG1246   128 EKDLE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 75-176 1.19e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 52.74  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  75 GYCYASPYRPRHayryTLE-ESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGNNNAgsLRLHKKHGFEIVG 153
Cdd:COG0456     1 GFALLGLVDGGD----EAEiEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAA--IALYEKLGFEEVG 74

                          90       100
                  ....*....|....*....|...
gi 1915230129 154 QLRSVGykkgdWRDTVIMQRPLN 176
Cdd:COG0456    75 ERPNYY-----GDDALVMEKELA 92
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
12-177 1.26e-08

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 51.86  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  12 LEVRDALPDDVHAITAIYAWHVLHgrasfeeVPP-TIDEMRQRMKS-----VAENG---LPWLIALYRGIVvgycYASP- 81
Cdd:COG3818     5 IVIRDAREHDLDAVLALNNAAVPA-------VSPlDAARLARLHEQaayarVAEVDgevAGFLLAFGPGAD----YDSPn 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  82 YR------PRHAY--RytleesIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGNNNAGSLRLHKKHGFEIVG 153
Cdd:COG3818    74 YRwfaeryDNFLYidR------IVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEPPNPGSLAFHARLGFREVG 147

                         170       180
                  ....*....|....*....|....*
gi 1915230129 154 QLRSVGYKKgdwrdTVIMQ-RPLND 177
Cdd:COG3818   148 QQRVAGGKK-----RVSLLaKELCS 167
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 65-151 1.77e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  65 LIALYRGIVVGYCYAspyRPRHAYRYTLEESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAvvgdgNNNAGSLRLH 144
Cdd:pfam13508   6 FVAEDDGKIVGFAAL---LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL-----ETTNRAAAFY 77


                  ....*..
gi 1915230129 145 KKHGFEI 151
Cdd:pfam13508  78 EKLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
73-162 4.56e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 4.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  73 VVGYCYASPYRPRHAYrytlEESIYVDASTTGRGFGTALMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKHGFEIV 152
Cdd:COG3393     2 LVAMAGVRAESPGVAE----ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDAD--NPAARRLYERLGFRPV 75

                          90
                  ....*....|
gi 1915230129 153 GQLRSVGYKK 162
Cdd:COG3393    76 GEYATVLFRK 85
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-150 4.78e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.56  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  12 LEVRDALPDDVHAITAIYA-WHVLHGRASFeevPPTIDEMRQRMKSV-----AENGLPWLIALYRGIVVGYCyasPYRPR 85
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSdPEVMRYGVPW---PLTLEEAREWLARIwaadeAERGYGWAIELKDTGFIGSI---GLYDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915230129  86 HAYRYTLEESIYVDASTTGRGFGTALMDALIARC-EQGPWRQMIAVVGdgNNNAGSLRLHKKHGFE 150
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARID--PENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 4.37e-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: 4.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1915230129  64 WLIALYRGIVVGYCYASPYRPRHAYRYTleESIYVDASTTGRGFGTALMDALIARCEQ 121
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYI--GDLAVLPEYRGKGIGSALLEAAEEEARE 56
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 48-163 4.47e-04

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: 38.41  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915230129  48 DEMRQRMksvAENGLPWLIALYRGIVVGYcyASPYRPRHAYRytleesIYVDASTTGRGFGTALMDALIARCEQGPWRQM 127
Cdd:pfam13673  20 EALRERI---DQGEYFFFVAFEGGQIVGV--IALRDRGHISL------LFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1915230129 128 IAVVgdgNNNAGSLRLHKKHGFEIVGQLRsvgYKKG 163
Cdd:pfam13673  89 ELTV---NASPYAVPFYEKLGFRATGPEQ---EFNG 118
 
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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