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Conserved domains on  [gi|612906071|gb|EZV17743|]
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hypothetical protein U926_02020 [Staphylococcus aureus 12S00881]

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];
1-157 6.28e-16

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.41  E-value: 6.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   1 MFKVRQATEKDVVQIRDVAtKAWFNTYLNIYAATTVNHLLEASYNEHHLKKRLqeqLFLVVEEGNDIVGFANFI------ 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIY-NEAIAEGTATFETEPPSEEEREAWFAAILAPGR---PVLVAEEDGEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  75 -YGEELYLSAhYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDNKNEEAVAYYKEQGFTILRSYEPEMY--GEKLD 150
Cdd:COG1247   77 aYRGTAEESI-YVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFkfGRWLD 155


                 ....*..
gi 612906071 151 LALMYKA 157
Cdd:COG1247  156 LVLMQKR 162
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-157 6.28e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.41  E-value: 6.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   1 MFKVRQATEKDVVQIRDVAtKAWFNTYLNIYAATTVNHLLEASYNEHHLKKRLqeqLFLVVEEGNDIVGFANFI------ 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIY-NEAIAEGTATFETEPPSEEEREAWFAAILAPGR---PVLVAEEDGEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  75 -YGEELYLSAhYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDNKNEEAVAYYKEQGFTILRSYEPEMY--GEKLD 150
Cdd:COG1247   77 aYRGTAEESI-YVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFkfGRWLD 155


                 ....*..
gi 612906071 151 LALMYKA 157
Cdd:COG1247  156 LVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-134 4.50e-11

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: 56.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   24 FNTYLNIYAATTVNHLLEASYNEHHLKKRLQEQLFLVVEEGNDIVGFANFI----YGEELYLSAHYVKPESQHTGYGTAL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSiiddEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 612906071  100 LNEGLSR-FEDKFEGVYLEVDNKNEEAVAYYKEQGF 134
Cdd:pfam00583  81 LQALLEWaRERGCERIFLEVAADNLAAIALYEKLGF 116
PRK10562 PRK10562
putative acetyltransferase; Provisional
 60-139 1.03e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 48.14  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  60 VVEEGNDIVGFANFIygEELYLSAHYVKPESQHTGYGTALLNEGLSRFEdkfeGVYLEVDNKNEEAVAYYKEQGFTILRS 139
Cdd:PRK10562  52 VWEEDGKLLGFVSVL--EGRFVGALFVAPKAVRRGIGKALMQHVQQRYP----HLSLEVYQKNQRAVNFYHAQGFRIVDS 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-117 2.68e-06

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: 42.65  E-value: 2.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612906071  58 FLVVEEGNDIVGFANFI----YGEELYLSAHYVKPESQHTGYGTALLNEGLSR-FEDKFEGVYLE 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEaRERGAKRLRLE 65
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
1-102 1.02e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.83  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   1 MFKVRQATEKDVVQIRDVATKAWFNTYLNIYAattvNHLLEASYNEHHLKKRLQEQ----------LFLVVEEGNDIVGF 70
Cdd:NF041158   1 MITIRKLSAEDVDALIEVARESWKWTYRDIYS----NEFIESWISEKYSKEKLLNEiirsqsnldiIFLGAFVNSALIGF 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 612906071  71 ANF-IYGEELYLSAHYVKPESQHTGYGTALLNE 102
Cdd:NF041158  77 IELkIIADKAELLRLYLKPEYTHRGIGKLLLSE 109
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-157 6.28e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.41  E-value: 6.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   1 MFKVRQATEKDVVQIRDVAtKAWFNTYLNIYAATTVNHLLEASYNEHHLKKRLqeqLFLVVEEGNDIVGFANFI------ 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIY-NEAIAEGTATFETEPPSEEEREAWFAAILAPGR---PVLVAEEDGEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  75 -YGEELYLSAhYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDNKNEEAVAYYKEQGFTILRSYEPEMY--GEKLD 150
Cdd:COG1247   77 aYRGTAEESI-YVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFkfGRWLD 155


                 ....*..
gi 612906071 151 LALMYKA 157
Cdd:COG1247  156 LVLMQKR 162
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-153 4.08e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.80  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   4 VRQATEKDVVQIRDVATKAWFNTYlniyAATTVnhlleasyneHHLKKRLQEQLFLVVEEGNDIVGFANF----IYGEE- 78
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR----EAELV----------DRLREDPAAGLSLVAEDDGEIVGHVALspvdIDGEGp 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612906071  79 -LYLSAHYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDnknEEAVAYYKEQGFTILRSYEPEMYGEKLDLAL 153
Cdd:COG3153   67 aLLLGPLAVDPEYRGQGIGRALMRAALEAARERgARAVVLLGD---PSLLPFYERFGFRPAGELGLTLGPDEVFLAK 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-134 4.50e-11

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: 56.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   24 FNTYLNIYAATTVNHLLEASYNEHHLKKRLQEQLFLVVEEGNDIVGFANFI----YGEELYLSAHYVKPESQHTGYGTAL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSiiddEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 612906071  100 LNEGLSR-FEDKFEGVYLEVDNKNEEAVAYYKEQGF 134
Cdd:pfam00583  81 LQALLEWaRERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 49-147 8.55e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  49 LKKRLQEQ---LFLVVEEGNDIVGFANF-IYGEE-LYLSAHYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDNKN 122
Cdd:COG0454   24 LKAMEGSLagaEFIAVDDKGEPIGFAGLrRLDDKvLELKRLYVLPEYRGKGIGKALLEALLEWARERgCTALELDTLDGN 103

                         90       100
                 ....*....|....*....|....*
gi 612906071 123 EEAVAYYKEQGFTILRSYEPEMYGE 147
Cdd:COG0454  104 PAAIRFYERLGFKEIERYVAYVGGE 128
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-138 4.00e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 53.51  E-value: 4.00e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612906071  69 GFANFIY---GEELYLSAHYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVDNKNEEAVAYYKEQGFTILR 138
Cdd:COG0456    1 GFALLGLvdgGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERgARRLRLEVREDNEAAIALYEKLGFEEVG 74
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 2-158 4.29e-09

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: 51.92  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   2 FKVRQATEKDVVQIRDvatkawfntylniyaattvnhLLEASYNEHHLkkrlqeQLFLVVEEGNDIVGFA--NFIYGEEL 79
Cdd:COG1246    1 MTIRPATPDDVPAILE---------------------LIRPYALEEEI------GEFWVAEEDGEIVGCAalHPLDEDLA 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  80 YLSAHYVKPESQHTGYGTALLNEGLSRFEDK-FEGVYLEVdnkNEEAVAYYKEQGFTIL-RSYEPEMYGEKLDLALMYKA 157
Cdd:COG1246   54 ELRSLAVHPDYRGRGIGRRLLEALLAEARELgLKRLFLLT---TSAAIHFYEKLGFEEIdKEDLPYAKVWQRDSVVMEKD 130


                 .
gi 612906071 158 F 158
Cdd:COG1246  131 L 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-136 4.76e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   54 QEQLFLVVEEGNDIVGFANFIYGEELYLSAH---YVKPESQHTGYGTALLNEglSRFEDKFEGVYLEVDNKNEEAVAYYK 130
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAElrlAVHPEYRGQGIGRALLEA--AEAAAKEGGIKLLELETTNRAAAFYE 78


                  ....*.
gi 612906071  131 EQGFTI 136
Cdd:pfam13508  79 KLGFEE 84
PRK10562 PRK10562
putative acetyltransferase; Provisional
 60-139 1.03e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 48.14  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071  60 VVEEGNDIVGFANFIygEELYLSAHYVKPESQHTGYGTALLNEGLSRFEdkfeGVYLEVDNKNEEAVAYYKEQGFTILRS 139
Cdd:PRK10562  52 VWEEDGKLLGFVSVL--EGRFVGALFVAPKAVRRGIGKALMQHVQQRYP----HLSLEVYQKNQRAVNFYHAQGFRIVDS 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-117 2.68e-06

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: 42.65  E-value: 2.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612906071  58 FLVVEEGNDIVGFANFI----YGEELYLSAHYVKPESQHTGYGTALLNEGLSR-FEDKFEGVYLE 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEaRERGAKRLRLE 65
PRK10514 PRK10514
putative acetyltransferase; Provisional
 57-134 1.29e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.99  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612906071  57 LFLVVEEGNDIVGFAnFIYGEelYLSAHYVKPESQHTGYGTALLNEGLSRFEDkfegVYLEVDNKNEEAVAYYKEQGF 134
Cdd:PRK10514  51 LWVAVDERDQPVGFM-LLSGG--HMEALFVDPDVRGCGVGRMLVEHALSLHPE----LTTDVNEQNEQAVGFYKKMGF 121
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
1-102 1.02e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.83  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906071   1 MFKVRQATEKDVVQIRDVATKAWFNTYLNIYAattvNHLLEASYNEHHLKKRLQEQ----------LFLVVEEGNDIVGF 70
Cdd:NF041158   1 MITIRKLSAEDVDALIEVARESWKWTYRDIYS----NEFIESWISEKYSKEKLLNEiirsqsnldiIFLGAFVNSALIGF 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 612906071  71 ANF-IYGEELYLSAHYVKPESQHTGYGTALLNE 102
Cdd:NF041158  77 IELkIIADKAELLRLYLKPEYTHRGIGKLLLSE 109
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 86-142 2.76e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.06  E-value: 2.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612906071  86 VKPESQHTGYGTALLNEGLSRFEDKfeGV---YLEVDNKNEEAVAYYKEQGF---TILRSYEP 142
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKR--GVatlWLEVRASNAAAIALYESLGFnevTIRRNYYP 131
 
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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