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Conserved domains on  [gi|527036467|ref|WP_020883208|]
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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 2.52e-63

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.52  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  11 EVEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLVALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  91 TLEESIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKYGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 527036467 171 MQRSL 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 2.52e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.52  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  11 EVEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLVALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  91 TLEESIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKYGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 527036467 171 MQRSL 175
Cdd:COG1247  159 MQKRL 163
PRK10140 PRK10140
N-acetyltransferase;
10-173 1.02e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 65.39  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  10 TEVEVRDALPDDVHAIAAIYAW-HVLHGRAsfeEVPPTIDEMRQRmKSVAENGLPWLVALYRGIVVGY-CYATPYRPRHA 87
Cdd:PRK10140   2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMWQE-RLADRPGIKQLVACIDGDVVGHlTIDVQQRPRRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  88 YryTLEESIYVDASTTGRGFGSVLMDALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKYGFEIVGQLRSVGYKKG 163
Cdd:PRK10140  78 H--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNG 150

                        170
                 ....*....|
gi 527036467 164 DWRDTVIMQR 173
Cdd:PRK10140 151 EYVDAYYMAR 160
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 7.43e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 54.68  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   14 VRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRQRMKSV-AENGLPWLVAlYRGIVVGYCYATPYRPRhaYRYTL 92
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlSPGEIVFGVA-ESDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   93 EESIYVDASTTgRGFGSVLMDALI--ARCEQGPWRQMIAVVgdgNNNAGSLRLHKKYGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 1.81e-03

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: 35.33  E-value: 1.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 527036467  64 WLVALYRGIVVGYCYATPYRPRHAYRYTleESIYVDASTTGRGFGSVLMDALIARCEQ 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 2.52e-63

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 192.52  E-value: 2.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  11 EVEVRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRQRMKSVAENGLPWLVALYRGIVVGYCYATPYRPRHAYRY 90
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  91 TLEESIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDGnnNAGSLRLHKKYGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 527036467 171 MQRSL 175
Cdd:COG1247  159 MQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 9-177 5.52e-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: 66.18  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   9 ETE-VEVRDALPDDVHAIAAIYA-WHVlhgRASFEEVPPTIDEMRQRMKSVAE-----NGLPWLVALYR-GIVVGYCYAT 80
Cdd:COG1670    4 ETErLRLRPLRPEDAEALAELLNdPEV---ARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEdGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  81 PYRPRHAyryTLEESIYVDASTTGRGFGSVLMDALIARC-EQGPWRQMIAVVGDGNnnAGSLRLHKKYGFEIVGQLRSVG 159
Cdd:COG1670   81 DIDRANR---SAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDN--TASIRVLEKLGFRLEGTLRDAL 155

                        170
                 ....*....|....*...
gi 527036467 160 YKKGDWRDTVIMQRSLND 177
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
PRK10140 PRK10140
N-acetyltransferase;
10-173 1.02e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 65.39  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  10 TEVEVRDALPDDVHAIAAIYAW-HVLHGRAsfeEVPPTIDEMRQRmKSVAENGLPWLVALYRGIVVGY-CYATPYRPRHA 87
Cdd:PRK10140   2 SEIVIRHAETRDYEAIRQIHAQpEVYHNTL---QVPHPSDHMWQE-RLADRPGIKQLVACIDGDVVGHlTIDVQQRPRRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  88 YryTLEESIYVDASTTGRGFGSVLMDALIARCEQgpW----RQMIAVVGDgnnNAGSLRLHKKYGFEIVGQLRSVGYKKG 163
Cdd:PRK10140  78 H--VADFGICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNG 150

                        170
                 ....*....|
gi 527036467 164 DWRDTVIMQR 173
Cdd:PRK10140 151 EYVDAYYMAR 160
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 12-176 5.26e-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: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  12 VEVRDALPDDVHAIAAIYawhvlhgrasfeevpptidemrqRMKSVAENGLPWLVALYRGIVVGYCYATPYRPRHAYryt 91
Cdd:COG1246    1 MTIRPATPDDVPAILELI-----------------------RPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAE--- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  92 LEeSIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDgnnnaGSLRLHKKYGFEIVGQlRSVGYKKGDWRDTVIM 171
Cdd:COG1246   55 LR-SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS-----AAIHFYEKLGFEEIDK-EDLPYAKVWQRDSVVM 127


                 ....*
gi 527036467 172 QRSLN 176
Cdd:COG1246  128 EKDLE 132
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
14-170 7.43e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 54.68  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   14 VRDALPDDVHAIAAIYAWHVLHGRASFEEVPPTIDEMRQRMKSV-AENGLPWLVAlYRGIVVGYCYATPYRPRhaYRYTL 92
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlSPGEIVFGVA-ESDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   93 EESIYVDASTTgRGFGSVLMDALI--ARCEQGPWRQMIAVVgdgNNNAGSLRLHKKYGFEIVGQLRSVGYKKGDWRDTVI 170
Cdd:pfam13420  78 ELSFYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-149 2.17e-09

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: 52.91  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   25 IAAIYAWHVLHGRASFEEVPPTIDEMRQRmksvaENGLPWLVALYRGIVVGYCYATPYRPRHAYRYtlEESIYVDASTTG 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDE-----DASEGFFVAEEDGELVGFASLSIIDDEPPVGE--IEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 527036467  105 RGFGSVLMDALIARC-EQGPWRQMIAVVgdgNNNAGSLRLHKKYGF 149
Cdd:pfam00583  74 KGIGTALLQALLEWArERGCERIFLEVA---ADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
14-156 3.40e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 52.78  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  14 VRDALPDDVHAIAAIYawhvlhgRASFEevPPTIDEMRQRMKSVAENGLPWlVALYRGIVVGYCYATPYRPRHAYRYTLE 93
Cdd:COG3153    1 IRPATPEDAEAIAALL-------RAAFG--PGREAELVDRLREDPAAGLSL-VAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036467  94 ESIYVDASTTGRGFGSVLMDALIARCEQGPWRqMIAVVGDgnnnAGSLRLHKKYGFEIVGQLR 156
Cdd:COG3153   71 GPLAVDPEYRGQGIGRALMRAALEAARERGAR-AVVLLGD----PSLLPFYERFGFRPAGELG 128
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 12-156 3.78e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.75  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  12 VEVRDALPDDVHAIAAIYAWHvlhgrasfeevpptiDEMRQRMKSVAENGlpWLVALYRGIVVGYCYATPYRPRHAYryt 91
Cdd:COG0454    1 MSIRKATPEDINFILLIEALD---------------AELKAMEGSLAGAE--FIAVDDKGEPIGFAGLRRLDDKVLE--- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036467  92 LEEsIYVDASTTGRGFGSVLMDALI--ARcEQGpWRQMIAVVGDGNNNAgsLRLHKKYGFEIVGQLR 156
Cdd:COG0454   61 LKR-LYVLPEYRGKGIGKALLEALLewAR-ERG-CTALELDTLDGNPAA--IRFYERLGFKEIERYV 122
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 94-176 6.20e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.11  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  94 ESIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDGNNNAgsLRLHKKYGFEIVGQLRSVGykkgdWRDTVIMQR 173
Cdd:COG0456   17 EDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAA--IALYEKLGFEEVGERPNYY-----GDDALVMEK 89


                 ...
gi 527036467 174 SLN 176
Cdd:COG0456   90 ELA 92
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
12-173 1.45e-07

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 48.78  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  12 VEVRDALPDDVHAIAAIYAWHVlhgrasfeevpPTIDEM-RQRMKSVAENGLPWLVALYRGIVVGYCYATPYRPRHA--- 87
Cdd:COG3818    5 IVIRDAREHDLDAVLALNNAAV-----------PAVSPLdAARLARLHEQAAYARVAEVDGEVAGFLLAFGPGADYDspn 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467  88 YRY---TLEESIYVD-----ASTTGRGFGSVLMDALIARCEQGPWRQMIAVVGDGNNNAGSLRLHKKYGFEIVGQLRSVG 159
Cdd:COG3818   74 YRWfaeRYDNFLYIDrivvaPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEPPNPGSLAFHARLGFREVGQQRVAG 153

                        170
                 ....*....|....
gi 527036467 160 YKKgdwrdTVIMQR 173
Cdd:COG3818  154 GKK-----RVSLLA 162
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 65-151 1.41e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 41.67  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   65 LVALYRGIVVGYCYATPYrprHAYRYTLEESIYVDASTTGRGFGSVLMDALIARCEQGPWRQMIAvvgdgNNNAGSLRLH 144
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPL---DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL-----ETTNRAAAFY 77


                  ....*..
gi 527036467  145 KKYGFEI 151
Cdd:pfam13508  78 EKLGFEE 84
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 19-150 5.92e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.48  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   19 PDDVHAIAAIYA-WHVLHGRASFeevPPTIDEMRQRMKSV-----AENGLPWLVALYRGIVVGYCyatPYRPRHAYRYTL 92
Cdd:pfam13302   9 EEDAEALFELLSdPEVMRYGVPW---PLTLEEAREWLARIwaadeAERGYGWAIELKDTGFIGSI---GLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 527036467   93 EESIYVDASTTGRGFGSVLMDALIARC-EQGPWRQMIAVVGdgNNNAGSLRLHKKYGFE 150
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARID--PENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-121 1.81e-03

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: 35.33  E-value: 1.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 527036467  64 WLVALYRGIVVGYCYATPYRPRHAYRYTleESIYVDASTTGRGFGSVLMDALIARCEQ 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYI--GDLAVLPEYRGKGIGSALLEAAEEEARE 56
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 48-156 4.05e-03

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: 35.71  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036467   48 DEMRQRMksvAENGLPWLVALYRGIVVGYCYAtpYRPRHAYRytleesIYVDASTTGRGFGSVLMDALIARCEQGPWRQM 127
Cdd:pfam13673  20 EALRERI---DQGEYFFFVAFEGGQIVGVIAL--RDRGHISL------LFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS 88

                          90       100
                  ....*....|....*....|....*....
gi 527036467  128 IAVVgdgNNNAGSLRLHKKYGFEIVGQLR 156
Cdd:pfam13673  89 ELTV---NASPYAVPFYEKLGFRATGPEQ 114
 
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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