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Conserved domains on  [gi|550542400|ref|WP_022624394|]
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MULTISPECIES: GNAT family N-acetyltransferase [Pantoea]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 12153134)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  10940244|9175471|15581578
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-142 3.03e-26

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: 95.80  E-value: 3.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   37 FIDSTKPDVLQPLIVSDDYLWLIAVERGEVTGVLTLFEGNLVKYLFVHPKFQRKGVARALWQRAIPELR------SEISV 110
Cdd:pfam13673  13 FYEFISPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEkdgiklSELTV 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 550542400  111 RSSLLAVPFYEKRGFKKVGEVKFFNGVSFQTM 142
Cdd:pfam13673  93 NASPYAVPFYEKLGFRATGPEQEFNGIRFVPM 124
 
Name Accession Description Interval E-value
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-142 3.03e-26

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: 95.80  E-value: 3.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   37 FIDSTKPDVLQPLIVSDDYLWLIAVERGEVTGVLTLFEGNLVKYLFVHPKFQRKGVARALWQRAIPELR------SEISV 110
Cdd:pfam13673  13 FYEFISPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEkdgiklSELTV 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 550542400  111 RSSLLAVPFYEKRGFKKVGEVKFFNGVSFQTM 142
Cdd:pfam13673  93 NASPYAVPFYEKLGFRATGPEQEFNGIRFVPM 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-146 1.19e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.96  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   3 IRTALESDAAGISELIQlvsvqcnfsetepcpQWFIDSTKPDVLQPLIVS-DDYLWLIAVERGEVTGVLTLFEGNLVK-- 79
Cdd:COG3153    1 IRPATPEDAEAIAALLR---------------AAFGPGREAELVDRLREDpAAGLSLVAEDDGEIVGHVALSPVDIDGeg 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550542400  80 ------YLFVHPKFQRKGVARALWQRAIPELR----SEISVRSSLLAVPFYEKRGFKKVGEVKFFNGVSFQTMIAQL 146
Cdd:COG3153   66 palllgPLAVDPEYRGQGIGRALMRAALEAARergaRAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
PRK10562 PRK10562
putative acetyltransferase; Provisional
 50-130 3.76e-08

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 49.30  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400  50 IVSDDYL-----WlIAVERGEVTGVLTLFEGNLVKYLFVHPKFQRKGVARALW---QRAIPELRSEIsVRSSLLAVPFYE 121
Cdd:PRK10562  39 LVRDVYLpaaqtW-VWEEDGKLLGFVSVLEGRFVGALFVAPKAVRRGIGKALMqhvQQRYPHLSLEV-YQKNQRAVNFYH 116


                 ....*....
gi 550542400 122 KRGFKKVGE 130
Cdd:PRK10562 117 AQGFRIVDS 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-132 6.28e-08

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: 48.48  E-value: 6.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   57 WLIAVERGEVTGV----LTLFEGNLVKyLFVHPKFQRKGVARALWQRAIPELRSE------ISVR-SSLLAVPFYEKRGF 125
Cdd:TIGR01575  33 YLLARIGGKVVGYagvqIVLDEAHILN-IAVKPEYQGQGIGRALLRELIDEAKGRgvneifLEVRvSNIAAQALYKKLGF 111


                  ....*..
gi 550542400  126 KKVGEVK 132
Cdd:TIGR01575 112 NEIAIRR 118
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-106 1.16e-05

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: 40.72  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550542400  57 WLIAVERGEVTGVLTLFEGNL------VKYLFVHPKFQRKGVARALWQRAIPELRS 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-142 3.03e-26

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: 95.80  E-value: 3.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   37 FIDSTKPDVLQPLIVSDDYLWLIAVERGEVTGVLTLFEGNLVKYLFVHPKFQRKGVARALWQRAIPELR------SEISV 110
Cdd:pfam13673  13 FYEFISPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEkdgiklSELTV 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 550542400  111 RSSLLAVPFYEKRGFKKVGEVKFFNGVSFQTM 142
Cdd:pfam13673  93 NASPYAVPFYEKLGFRATGPEQEFNGIRFVPM 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-146 1.19e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.96  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   3 IRTALESDAAGISELIQlvsvqcnfsetepcpQWFIDSTKPDVLQPLIVS-DDYLWLIAVERGEVTGVLTLFEGNLVK-- 79
Cdd:COG3153    1 IRPATPEDAEAIAALLR---------------AAFGPGREAELVDRLREDpAAGLSLVAEDDGEIVGHVALSPVDIDGeg 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550542400  80 ------YLFVHPKFQRKGVARALWQRAIPELR----SEISVRSSLLAVPFYEKRGFKKVGEVKFFNGVSFQTMIAQL 146
Cdd:COG3153   66 palllgPLAVDPEYRGQGIGRALMRAALEAARergaRAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-132 6.46e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 67.33  E-value: 6.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   1 MEIRTALESDAAGISELIQLVSVQCNFS-ETEP-----CPQWFIDstkpdvlqplIVSDDYLWLIAVERGEVTGVLTLFE 74
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATfETEPpseeeREAWFAA----------ILAPGRPVLVAEEDGEVVGFASLGP 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550542400  75 GNLVK-Y-------LFVHPKFQRKGVARALWQRAIPELRSE--ISVRSSLL-----AVPFYEKRGFKKVGEVK 132
Cdd:COG1247   72 FRPRPaYrgtaeesIYVDPDARGRGIGRALLEALIERARARgyRRLVAVVLadneaSIALYEKLGFEEVGTLP 144
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-130 2.57e-13

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: 62.32  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   1 MEIRTALESDAAGISELIQlvsvqcnfsetepcpQWFIDSTKPDvlqplivsddylWLIAVERGEVTGV--LTLFEGNL- 77
Cdd:COG1246    1 MTIRPATPDDVPAILELIR---------------PYALEEEIGE------------FWVAEEDGEIVGCaaLHPLDEDLa 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 550542400  78 -VKYLFVHPKFQRKGVARALWQRAIPELR----SEISVRSSLLAVPFYEKRGFKKVGE 130
Cdd:COG1246   54 eLRSLAVHPDYRGRGIGRRLLEALLAEARelglKRLFLLTTSAAIHFYEKLGFEEIDK 111
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-140 2.74e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 62.38  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   1 MEIRTALESDAAGIseliqlvsvqcnfsetepcpqWFIDSTKPDVLQPLIVSDDYLWLIAVERGEVTGVLTLFEGN---- 76
Cdd:COG0454    1 MSIRKATPEDINFI---------------------LLIEALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGLRRLDdkvl 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550542400  77 LVKYLFVHPKFQRKGVARALWQRAIPELRsEISVRSSLL--------AVPFYEKRGFKKVGEVKFFNGVSFQ 140
Cdd:COG0454   60 ELKRLYVLPEYRGKGIGKALLEALLEWAR-ERGCTALELdtldgnpaAIRFYERLGFKEIERYVAYVGGEFE 130
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 81-146 9.38e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 9.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550542400  81 LFVHPKFQRKGVARALWQRAIPELRS------EISVRSS-LLAVPFYEKRGFKKVGEVKFFNGVSFQTMIAQL 146
Cdd:COG0456   19 LAVDPEYRGRGIGRALLEAALERARErgarrlRLEVREDnEAAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 53-127 2.59e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   53 DDYLWLIAVERGEVTGVLTLF-----EGNLVKYLFVHPKFQRKGVARALWQRAIPELRSE----ISVRSSLLAVPFYEKR 123
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLplddeGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGgiklLELETTNRAAAFYEKL 80


                  ....
gi 550542400  124 GFKK 127
Cdd:pfam13508  81 GFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
58-146 4.09e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 56.73  E-value: 4.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400  58 LIAVERGEVTGVLTLFEGNLVKY----LFVHPKFQRKGVARALWQRAIPELRS------EISVRSSllAVPFYEKRGFKK 127
Cdd:COG2153   37 LLAYDDGELVATARLLPPGDGEAkigrVAVLPEYRGQGLGRALMEAAIEEARErgarriVLSAQAH--AVGFYEKLGFVP 114

                         90
                 ....*....|....*....
gi 550542400 128 VGEVKFFNGVSFQTMIAQL 146
Cdd:COG2153  115 VGEEFLEAGIPHIDMRKPL 133
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 27-125 1.06e-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: 52.52  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   27 FSETEPCPQWFIDSTKPDVLQPLIVSDDYLWLIAVERGEVTGVLTLFEGNL------VKYLFVHPKFQRKGVARALWQRA 100
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDeppvgeIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 550542400  101 IPELRSEISVRSSLL-------AVPFYEKRGF 125
Cdd:pfam00583  85 LEWARERGCERIFLEvaadnlaAIALYEKLGF 116
PRK10562 PRK10562
putative acetyltransferase; Provisional
 50-130 3.76e-08

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 49.30  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400  50 IVSDDYL-----WlIAVERGEVTGVLTLFEGNLVKYLFVHPKFQRKGVARALW---QRAIPELRSEIsVRSSLLAVPFYE 121
Cdd:PRK10562  39 LVRDVYLpaaqtW-VWEEDGKLLGFVSVLEGRFVGALFVAPKAVRRGIGKALMqhvQQRYPHLSLEV-YQKNQRAVNFYH 116


                 ....*....
gi 550542400 122 KRGFKKVGE 130
Cdd:PRK10562 117 AQGFRIVDS 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 57-132 6.28e-08

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: 48.48  E-value: 6.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   57 WLIAVERGEVTGV----LTLFEGNLVKyLFVHPKFQRKGVARALWQRAIPELRSE------ISVR-SSLLAVPFYEKRGF 125
Cdd:TIGR01575  33 YLLARIGGKVVGYagvqIVLDEAHILN-IAVKPEYQGQGIGRALLRELIDEAKGRgvneifLEVRvSNIAAQALYKKLGF 111


                  ....*..
gi 550542400  126 KKVGEVK 132
Cdd:TIGR01575 112 NEIAIRR 118
PRK03624 PRK03624
putative acetyltransferase; Provisional
 53-125 2.22e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400  53 DDYLWLIAVERGEVTG-VLTLFEGN--LVKYLFVHPKFQRKGVARALWQRAIPELRSE------ISVRSSLLAV-PFYEK 122
Cdd:PRK03624  43 DPSLFLVAEVGGEVVGtVMGGYDGHrgWAYYLAVHPDFRGRGIGRALVARLEKKLIARgcpkinLQVREDNDAVlGFYEA 122


                 ...
gi 550542400 123 RGF 125
Cdd:PRK03624 123 LGY 125
PRK09831 PRK09831
GNAT family N-acetyltransferase;
59-130 3.06e-07

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 46.88  E-value: 3.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550542400  59 IAVERGEVTGVLTLFeGNLVKYLFVHPKFQRKGVARALWQRAIPElRSEISVRSSLLAVPFYEKRGFKKVGE 130
Cdd:PRK09831  57 VAVINAQPVGFITCI-EHYIDMLFVDPEYTRRGVASALLKPLIKS-ESELTVDASITAKPFFERYGFQTVKQ 126
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-134 8.21e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.82  E-value: 8.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550542400  78 VKYLFVHPKFQRKGVARALWQRAIPELRSEISVRSSLL-------AVPFYEKRGFKKVGEVKFF 134
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYvdadnpaARRLYERLGFRPVGEYATV 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-106 1.16e-05

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: 40.72  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550542400  57 WLIAVERGEVTGVLTLFEGNL------VKYLFVHPKFQRKGVARALWQRAIPELRS 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
PRK10514 PRK10514
putative acetyltransferase; Provisional
 56-129 1.07e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.99  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550542400  56 LWLIAVERGEVTGVLTLFEGNLvKYLFVHPKFQRKGVARALWQRAI---PELRSEISVRSSLlAVPFYEKRGFKKVG 129
Cdd:PRK10514  51 LWVAVDERDQPVGFMLLSGGHM-EALFVDPDVRGCGVGRMLVEHALslhPELTTDVNEQNEQ-AVGFYKKMGFKVTG 125
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 71-128 3.71e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.37  E-value: 3.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550542400  71 TLFegNLVkylfVHPKFQRKGVARALWQRAIPELRSE------ISVRSS-LLAVPFYEKRGFKKV 128
Cdd:PRK09491  65 TLF--NIA----VDPDYQRQGLGRALLEHLIDELEKRgvatlwLEVRASnAAAIALYESLGFNEV 123
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-125 1.35e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 36.40  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400    3 IRTALESDAAGISELIQLVsvqcnFSETEPCPQWFIdstkpdvLQPLIVSDDYLwlIAVERGEVTGVLTLFE------GN 76
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYA-----FQDEDSPELREY-------FRPLLEEGRVL--GAFDDGELVSTLALYPfelnvpGK 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 550542400   77 LVKYLF-----VHPKFQRKGVARALWQRAIPELRSEiSVRSSLL---AVPFYEKRGF 125
Cdd:pfam13527  67 TLPAAGitgvaTYPEYRGRGVMSRLLRRSLEEMRER-GVPLSFLypsSYPIYRRFGY 122
PRK07757 PRK07757
N-acetyltransferase;
59-128 4.28e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 4.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550542400  59 IAVERGEVTGV--LTLFEGNL--VKYLFVHPKFQRKGVARALWQRAIPELRsEISVRSSL---LAVPFYEKRGFKKV 128
Cdd:PRK07757  45 VAEEEGEIVGCcaLHILWEDLaeIRSLAVSEDYRGQGIGRMLVEACLEEAR-ELGVKRVFaltYQPEFFEKLGFREV 120
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-125 5.64e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 35.64  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550542400   1 MEIRTALESDAAGISELIQLVsvqcnFsetepcpQWFIDSTKPDVLQPLIVSDDYLwlIAVERGEVTGVLTLFE------ 74
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYA-----F-------GPEPDDEELEAYRPLLEPGRVL--GVFDDGELVGTLALYPftlnvg 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 550542400  75 GNLVK-----YLFVHPKFQRKGVARALWQRAIPELRSE-ISVrSSLLA--VPFYEKRGF 125
Cdd:COG4552   67 GARVPmagitGVAVAPEHRRRGVARALLREALAELRERgQPL-SALYPfePGFYRRFGY 124
 
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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