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Conserved domains on  [gi|446536324|ref|WP_000613670|]
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GNAT family N-acetyltransferase [Streptococcus pneumoniae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10137528)

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_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 162-275 4.35e-14

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: 67.16  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  162 DQISQLKFQAFSEEHESREVvdRYVAEALKDPESRLYILLKDGQVIGTCT---VDLSTNTNYFYGLAILEPERGKGYGSY 238
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPL--DLLEDWDEDASEGFFVAEEDGELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446536324  239 LAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-95 3.08e-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: 43.80  E-value: 3.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446536324  48 FFLYYEKGELVGLLTVYADDQDVEV----TILVHPGHRRQGIARALFTSFER 95
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTayigDLAVLPEYRGKGIGSALLEAAEE 52
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 162-275 4.35e-14

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: 67.16  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  162 DQISQLKFQAFSEEHESREVvdRYVAEALKDPESRLYILLKDGQVIGTCT---VDLSTNTNYFYGLAILEPERGKGYGSY 238
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPL--DLLEDWDEDASEGFFVAEEDGELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446536324  239 LAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
160-277 2.46e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 160 YQDQISQLKFQAFSEEHESREVVDRYvaEALKDPESRLYILLKDGQVIGTCTV-DLSTNTNY----FYGLAILEPERGKG 234
Cdd:COG1247   19 YNEAIAEGTATFETEPPSEEEREAWF--AAILAPGRPVLVAEEDGEVVGFASLgPFRPRPAYrgtaEESIYVDPDARGRG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446536324 235 YGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGFVK 277
Cdd:COG1247   97 IGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-95 3.08e-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: 43.80  E-value: 3.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446536324  48 FFLYYEKGELVGLLTVYADDQDVEV----TILVHPGHRRQGIARALFTSFER 95
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTayigDLAVLPEYRGKGIGSALLEAAEE 52
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-89 7.97e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.21  E-value: 7.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446536324   48 FFLYYEKGELVGLLTVYADDQDVEVTIL---VHPGHRRQGIARAL 89
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGALAELrlaVHPEYRGQGIGRAL 49
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 185-275 8.84e-06

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: 44.24  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  185 YVAEALKDPESRLYILLKDGQVIGTCTVDLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNV 264
Cdd:TIGR01575  21 QFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNI 100

                          90
                  ....*....|.
gi 446536324  265 GAKRLYEKIGF 275
Cdd:TIGR01575 101 AAQALYKKLGF 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 197-257 1.46e-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: 41.88  E-value: 1.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536324 197 LYILLKDGQVIGTCTV---DLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQI 257
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
42-118 1.96e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.83  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  42 DPNMPaFFLYYEKGELVGLLTVY------ADDQDVEVTILVHPGHRRQGIARALFTSFERGTASFPIRSVTFQterIFLE 115
Cdd:COG1247   49 APGRP-VLVAEEDGEVVGFASLGpfrprpAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAV---VLAD 124


                 ...
gi 446536324 116 NHP 118
Cdd:COG1247  125 NEA 127
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 198-275 2.59e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.30  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 198 YILLKDGQVIG--TCTVDLSTNTnyFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:PRK09491  43 LKLTVNGQMAAfaITQVVLDEAT--LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 162-275 4.35e-14

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: 67.16  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  162 DQISQLKFQAFSEEHESREVvdRYVAEALKDPESRLYILLKDGQVIGTCT---VDLSTNTNYFYGLAILEPERGKGYGSY 238
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPL--DLLEDWDEDASEGFFVAEEDGELVGFASlsiIDDEPPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446536324  239 LAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:pfam00583  80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
160-277 2.46e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 160 YQDQISQLKFQAFSEEHESREVVDRYvaEALKDPESRLYILLKDGQVIGTCTV-DLSTNTNY----FYGLAILEPERGKG 234
Cdd:COG1247   19 YNEAIAEGTATFETEPPSEEEREAWF--AAILAPGRPVLVAEEDGEVVGFASLgPFRPRPAYrgtaEESIYVDPDARGRG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446536324 235 YGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGFVK 277
Cdd:COG1247   97 IGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 176-277 3.11e-09

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: 55.01  E-value: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 176 HESREVVDRYVAEALKDPESRLYILL-----KDGQVIGTCT---VDLSTNTNYFyGLAILEPERGKGYGSYLAKSLVNQL 247
Cdd:COG1670   38 PYSLEEARAWLERLLADWADGGALPFaiedkEDGELIGVVGlydIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYA 116

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446536324 248 IEQND-KEFQIAVEDSNVGAKRLYEKIGFVK 277
Cdd:COG1670  117 FEELGlHRVEAEVDPDNTASIRVLEKLGFRL 147
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 193-277 1.23e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  193 PESRLYILLKDGQVIGTCTVDLSTNTNYFY--GLAILEPERGKGYGsylaKSLVNQLIE-QNDKEFQIAVEDSNVGAKRL 269
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIG----RALLEAAEAaAKEGGIKLLELETTNRAAAF 76


                  ....*...
gi 446536324  270 YEKIGFVK 277
Cdd:pfam13508  77 YEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 180-276 1.74e-08

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: 52.30  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 180 EVVDRYVAEALKDPESRLYILLKDGQVIGTCTVD-LSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIa 258
Cdd:COG1246   13 AILELIRPYALEEEIGEFWVAEEDGEIVGCAALHpLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL- 91

                         90
                 ....*....|....*...
gi 446536324 259 veDSNVGAKRLYEKIGFV 276
Cdd:COG1246   92 --LTTSAAIHFYEKLGFE 107
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 209-277 2.04e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 50.81  E-value: 2.04e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536324 209 TCTVDLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGFVK 277
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
223-276 4.77e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.52  E-value: 4.77e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446536324 223 GLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGFV 276
Cdd:COG3393   20 GVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 179-291 5.22e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.82  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 179 REVVDRYVAEALKDPESRLYILLKD-GQVIGTCTVD-LSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQ 256
Cdd:COG0454   17 IEALDAELKAMEGSLAGAEFIAVDDkGEPIGFAGLRrLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALE 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446536324 257 IAVEDSNVGAKRLYEKIGFVK-QTQVVYLNEKGARD 291
Cdd:COG0454   97 LDTLDGNPAAIRFYERLGFKEiERYVAYVGGEFEKE 132
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 164-285 9.41e-08

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: 49.96  E-value: 9.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  164 ISQLKFQAFSEEHESREVVDRyvaeaLKDPESRLYILLKDGQVIGTCTVDlstNTNYFYGLAILEPERGKGYGSYLAKSL 243
Cdd:pfam13673   5 YSEEGIETFYEFISPEALRER-----IDQGEYFFFVAFEGGQIVGVIALR---DRGHISLLFVDPDYQGQGIGKALLEAV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446536324  244 VNQLIEQNDKEFQIAVeDSNVGAKRLYEKIGFVKQTQVVYLN 285
Cdd:pfam13673  77 EDYAEKDGIKLSELTV-NASPYAVPFYEKLGFRATGPEQEFN 117
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
191-276 1.29e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.80  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 191 KDPESRLYILLKDGQVIGTCTV-DLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIaveDSNVGAKRL 269
Cdd:COG2153   30 KDEDARHLLAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL---SAQAHAVGF 106


                 ....*..
gi 446536324 270 YEKIGFV 276
Cdd:COG2153  107 YEKLGFV 113
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
162-276 1.65e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 49.70  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 162 DQISQLKFQAFSEEHESrEVVDRYVAEalkDPESRLYILLKDGQVIGTCT---VDLSTNTNYFY--GLAILEPERGKGYG 236
Cdd:COG3153   10 EAIAALLRAAFGPGREA-ELVDRLRED---PAAGLSLVAEDDGEIVGHVAlspVDIDGEGPALLlgPLAVDPEYRGQGIG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446536324 237 sylaKSLVNQLIEQ-NDKEFQIAVEDSNVGAKRLYEKIGFV 276
Cdd:COG3153   86 ----RALMRAALEAaRERGARAVVLLGDPSLLPFYERFGFR 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-95 3.08e-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: 43.80  E-value: 3.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446536324  48 FFLYYEKGELVGLLTVYADDQDVEV----TILVHPGHRRQGIARALFTSFER 95
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTayigDLAVLPEYRGKGIGSALLEAAEE 52
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 220-280 6.58e-06

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 43.47  E-value: 6.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536324  220 YFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEdSNVGAKRLYEKIGFVKQTQ 280
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVA-GNTPSRRLYEKLGFRKIDE 82
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-89 7.97e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.21  E-value: 7.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446536324   48 FFLYYEKGELVGLLTVYADDQDVEVTIL---VHPGHRRQGIARAL 89
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGALAELrlaVHPEYRGQGIGRAL 49
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 185-275 8.84e-06

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: 44.24  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  185 YVAEALKDPESRLYILLKDGQVIGTCTVDLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNV 264
Cdd:TIGR01575  21 QFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNI 100

                          90
                  ....*....|.
gi 446536324  265 GAKRLYEKIGF 275
Cdd:TIGR01575 101 AAQALYKKLGF 111
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 26-89 1.13e-05

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: 43.66  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536324   26 YDGTYRDPYLSNMLNFDPNMPA-FFLYYEKGELVGLLTVYADDQDVEVT----ILVHPGHRRQGIARAL 89
Cdd:pfam00583  12 FPEPWPDEPLDLLEDWDEDASEgFFVAEEDGELVGFASLSIIDDEPPVGeiegLAVAPEYRGKGIGTAL 80
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 197-257 1.46e-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: 41.88  E-value: 1.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536324 197 LYILLKDGQVIGTCTV---DLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQI 257
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
42-118 1.96e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.83  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  42 DPNMPaFFLYYEKGELVGLLTVY------ADDQDVEVTILVHPGHRRQGIARALFTSFERGTASFPIRSVTFQterIFLE 115
Cdd:COG1247   49 APGRP-VLVAEEDGEVVGFASLGpfrprpAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAV---VLAD 124


                 ...
gi 446536324 116 NHP 118
Cdd:COG1247  125 NEA 127
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 177-276 1.98e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 43.49  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  177 ESREVVDRYVAEALKDPESRLYILLKDGQVIGTCTVDLSTNTNYFY--GLAILEPERGKGYGSYLAKSLVNQLIEQND-K 253
Cdd:pfam13302  37 EAREWLARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPERAelGYWLGPDYWGKGYATEAVRALLEYAFEELGlP 116

                          90       100
                  ....*....|....*....|...
gi 446536324  254 EFQIAVEDSNVGAKRLYEKIGFV 276
Cdd:pfam13302 117 RLVARIDPENTASRRVLEKLGFK 139
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 32-90 1.86e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.81  E-value: 1.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536324  32 DPYLSNMLNFDPNMpAFFLYYEKGELVG--LLTVYADDqDVEVTIL-VHPGHRRQGIARALF 90
Cdd:COG0454   21 DAELKAMEGSLAGA-EFIAVDDKGEPIGfaGLRRLDDK-VLELKRLyVLPEYRGKGIGKALL 80
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 55-283 2.24e-04

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 42.00  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324   55 GELVGLL-TVYADDQDVEVT-ILVHPGHRRQGIARALftsfergtasfpIRSVTFQT---ERIFLE-NHP---DFASNWG 125
Cdd:TIGR03448  55 DPIVGYAnLVPARGTDPAMAeLVVHPAHRRRGIGRAL------------IRALLAKGggrLRVWAHgDLPaarALASRLG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  126 LIEDEEtetwLGKDRRpyPLANVSHLEVLLAD----SSY---QDQISQLKF--QAFSEEHESREVVDRYVAEALKDP--- 193
Cdd:TIGR03448 123 LVPTRE----LLQMRR--PLRDLELPEPQVPDgvtvRAYvgaPDDAEWLRVnnAAFAWHPEQGGWTRADLAERRAEPwfd 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  194 ESRLYILLKD--GQVIG---TCTVDLSTNTNYFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKR 268
Cdd:TIGR03448 197 PAGLFLAFDDapGELLGfhwTKVHPDEPALGEVYVVGVDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVR 276

                         250
                  ....*....|....*.
gi 446536324  269 LYEKIGF-VKQTQVVY 283
Cdd:TIGR03448 277 TYEKLGFtVAEVDVAY 292
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 198-275 2.59e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.30  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324 198 YILLKDGQVIG--TCTVDLSTNTnyFYGLAILEPERGKGYGSYLAKSLVNQLIEQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:PRK09491  43 LKLTVNGQMAAfaITQVVLDEAT--LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 48-90 3.61e-04

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: 39.59  E-value: 3.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446536324  48 FFLYYEKGELVGLLTVYADDQDV-EVT-ILVHPGHRRQGIARALF 90
Cdd:COG1246   30 FWVAEEDGEIVGCAALHPLDEDLaELRsLAVHPDYRGRGIGRRLL 74
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 48-90 1.28e-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: 38.02  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446536324   48 FFLYYEKGELVGLLTVYaddQDVEVTIL-VHPGHRRQGIARALF 90
Cdd:pfam13673  33 FFVAFEGGQIVGVIALR---DRGHISLLfVDPDYQGQGIGKALL 73
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-89 2.42e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 37.76  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  10 QEELSEAKKVINCCQNYDGTYRDPYLSNMLNFDPNMPAFFLYYEKGELVG--LLTVYADDQDVEVTIL----VHPGHRRQ 83
Cdd:COG3153    3 PATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGhvALSPVDIDGEGPALLLgplaVDPEYRGQ 82


                 ....*.
gi 446536324  84 GIARAL 89
Cdd:COG3153   83 GIGRAL 88
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
49-91 3.19e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 3.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446536324  49 FLYYEKGELVGLLTVYADDQDvEVTI---LVHPGHRRQGIARALFT 91
Cdd:COG2153   37 LLAYDDGELVATARLLPPGDG-EAKIgrvAVLPEYRGQGLGRALME 81
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
167-275 6.33e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 36.58  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536324  167 LKFQAFSEEHESREVVDRYVaEALKDPESRLYILLKDGQVIGTCTVdlsTNTNYFY-GLAILE----PERGKGYGSYLAK 241
Cdd:pfam13420  22 NPAFTQEYAHSSIEEFETFL-AAYLSPGEIVFGVAESDRLIGYATL---RQFDYVKtHKAELSfyvvKNNDEGINRELIN 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446536324  242 SLVNQLI-EQNDKEFQIAVEDSNVGAKRLYEKIGF 275
Cdd:pfam13420  98 AIIQYARkNQNIENLEACIASNNINAIVFLKAIGF 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 59-95 6.72e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.40  E-value: 6.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446536324  59 GLLTVYADDQDVEVTIL---VHPGHRRQGIARALFTSFER 95
Cdd:COG0456    1 GFALLGLVDGGDEAEIEdlaVDPEYRGRGIGRALLEAALE 40
 
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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