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Conserved domains on  [gi|446540225|ref|WP_000617571|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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];
1-164 3.72e-28

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 102.38  E-value: 3.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKMIHRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGKGIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540225 160 MAKLL 164
Cdd:COG1247  159 MQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-164 3.72e-28

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 102.38  E-value: 3.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKMIHRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGKGIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540225 160 MAKLL 164
Cdd:COG1247  159 MQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-138 1.08e-16

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: 71.39  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   45 IHRFIENEYATIFVAVEDERIVGFILVNGNNiQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMA 124
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAA 102

                          90
                  ....*....|....
gi 446540225  125 HNTRAQALYKKAGF 138
Cdd:pfam00583 103 DNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 51-146 4.70e-16

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: 70.05  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   51 NEYATIFVAVEDERIVGFILVngnniQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRA 129
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGV-----QIVLDEAHILnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAA 102

                          90
                  ....*....|....*..
gi 446540225  130 QALYKKAGFEKEGVKKA 146
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRN 119
PRK10140 PRK10140
N-acetyltransferase;
57-163 6.51e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 62.69  E-value: 6.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  57 FVAVEDERIVGFILVNGNNIQRKRHVATIVIGILQEYNGRGIGTRLFKEV----EKWAKlhdVWRLELTVMAHNTRAQAL 132
Cdd:PRK10140  54 LVACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMiemcDNWLR---VDRIELTVFVDNAPAIKV 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446540225 133 YKKAGFEKEGVKKAALIIDGKGIDEYEMAKL 163
Cdd:PRK10140 131 YKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 4.52e-09

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: 49.97  E-value: 4.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540225  56 IFVAVEDERIVGFILVNGNNiqRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELT 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDG--SGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-164 3.72e-28

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 102.38  E-value: 3.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKMIHRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGKGIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540225 160 MAKLL 164
Cdd:COG1247  159 MQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-165 9.72e-28

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: 101.61  E-value: 9.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   2 IREIEIEDAASFLQLSKQlDEETKFMLYEPGERKTTAEQQEKMIHRFIENEYATIFVAV-EDERIVGFILVNgnNIQRKR 80
Cdd:COG1670   10 LRPLRPEDAEALAELLND-PEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDkEDGELIGVVGLY--DIDRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  81 HVATIVIGILQEYNGRGIGTRLFKEVEKWAKLH-DVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGKGIDEYE 159
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ....*.
gi 446540225 160 MAKLLK 165
Cdd:COG1670  167 YSLLRE 172
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-138 1.08e-16

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: 71.39  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   45 IHRFIENEYATIFVAVEDERIVGFILVNGNNiQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMA 124
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAA 102

                          90
                  ....*....|....
gi 446540225  125 HNTRAQALYKKAGF 138
Cdd:pfam00583 103 DNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 51-146 4.70e-16

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: 70.05  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   51 NEYATIFVAVEDERIVGFILVngnniQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRA 129
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGV-----QIVLDEAHILnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAA 102

                          90
                  ....*....|....*..
gi 446540225  130 QALYKKAGFEKEGVKKA 146
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRN 119
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-145 6.84e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.53  E-value: 6.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  67 GFILVNgnnIQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKK 145
Cdd:COG0456    1 GFALLG---LVDGGDEAEIEdLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 52-140 2.65e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 61.70  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   52 EYATIFVAVEDERIVGFILVNGnnIQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVmahNTRAQA 131
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP--LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAA 75


                  ....*....
gi 446540225  132 LYKKAGFEK 140
Cdd:pfam13508  76 FYEKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-140 4.58e-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: 4.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  39 EQQEKMIHRFIENEYATIFVAVED-ERIVGFI---LVNGNNIQRKRhvativIGILQEYNGRGIGTRLFKEVEKWAKLHD 114
Cdd:COG0454   18 EALDAELKAMEGSLAGAEFIAVDDkGEPIGFAglrRLDDKVLELKR------LYVLPEYRGKGIGKALLEALLEWARERG 91

                         90       100
                 ....*....|....*....|....*.
gi 446540225 115 VWRLELTVMAHNTRAQALYKKAGFEK 140
Cdd:COG0454   92 CTALELDTLDGNPAAIRFYERLGFKE 117
PRK10140 PRK10140
N-acetyltransferase;
57-163 6.51e-13

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 62.69  E-value: 6.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  57 FVAVEDERIVGFILVNGNNIQRKRHVATIVIGILQEYNGRGIGTRLFKEV----EKWAKlhdVWRLELTVMAHNTRAQAL 132
Cdd:PRK10140  54 LVACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMiemcDNWLR---VDRIELTVFVDNAPAIKV 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446540225 133 YKKAGFEKEGVKKAALIIDGKGIDEYEMAKL 163
Cdd:PRK10140 131 YKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-143 6.72e-13

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: 61.90  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   43 KMIHRFIENEYATIFVAVEDERIVGFIlvngnNIQRKRHVATIVIgiLQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTV 122
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVI-----ALRDRGHISLLFV--DPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV 92

                          90       100
                  ....*....|....*....|.
gi 446540225  123 MAHNTrAQALYKKAGFEKEGV 143
Cdd:pfam13673  93 NASPY-AVPFYEKLGFRATGP 112
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-142 2.08e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.87  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   2 IREIEIEDAASFLQLSKQLdeetkfmlYEPGERkttaeqqEKMIHRFIENEYAT-IFVAVEDERIVGFILVNGNNIQRKR 80
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA--------FGPGRE-------AELVDRLREDPAAGlSLVAEDDGEIVGHVALSPVDIDGEG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446540225  81 HVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVmahNTRAQALYKKAGFEKEG 142
Cdd:COG3153   66 PALLLGpLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAG 125
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-139 2.72e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.43  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225    2 IREIEIEDAASFLQLSKqlDEEtkFMLYEPGERKTTAEQQEKMIHRFIENEYATIF---VAVEDERIVGFILVNgnNIQR 78
Cdd:pfam13302   4 LRPLTEEDAEALFELLS--DPE--VMRYGVPWPLTLEEAREWLARIWAADEAERGYgwaIELKDTGFIGSIGLY--DIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446540225   79 KRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVW-RLELTVMAHNTRAQALYKKAGFE 139
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLpRLVARIDPENTASRRVLEKLGFK 139
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
64-139 1.30e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.22  E-value: 1.30e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540225  64 RIVGFILVNGNNiqrkRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFE 139
Cdd:COG3393    1 ELVAMAGVRAES----PGVAEISgVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-139 2.10e-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: 52.69  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   1 MIREIEIEDAASFLQLSKQLDeetkfmLYEPGERkttaeqqekmihrfieneyatIFVAVEDERIVGFILVngnnIQRKR 80
Cdd:COG1246    2 TIRPATPDDVPAILELIRPYA------LEEEIGE---------------------FWVAEEDGEIVGCAAL----HPLDE 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  81 HVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVmahNTRAQALYKKAGFE 139
Cdd:COG1246   51 DLAELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFE 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 4.52e-09

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: 49.97  E-value: 4.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540225  56 IFVAVEDERIVGFILVNGNNiqRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELT 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDG--SGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
52-142 3.15e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.41  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  52 EYATIFVAVEDERIVGF--ILVNGNNIQRKRHVATivigiLQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHntrA 129
Cdd:COG2153   32 EDARHLLAYDDGELVATarLLPPGDGEAKIGRVAV-----LPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---A 103

                         90
                 ....*....|...
gi 446540225 130 QALYKKAGFEKEG 142
Cdd:COG2153  104 VGFYEKLGFVPVG 116
PRK03624 PRK03624
putative acetyltransferase; Provisional
 45-157 5.22e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 43.76  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  45 IHRFIENEYATIFVAVEDERIVGFILV--NGnniqrkrHVATI-VIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELT 121
Cdd:PRK03624  36 IERKLNHDPSLFLVAEVGGEVVGTVMGgyDG-------HRGWAyYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQ 108

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446540225 122 VMAHNTRAQALYKKAGFEKEGVkkaalIIDGKGIDE 157
Cdd:PRK03624 109 VREDNDAVLGFYEALGYEEQDR-----ISLGKRLIE 139
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
123-153 6.88e-05

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 41.26  E-value: 6.88e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446540225 123 MAHNTRAQALYKKAGFEKEGVKKAALIIDGK 153
Cdd:PRK10809 146 MPHNKRSGDLLARLGFEKEGYAKDYLLIDGQ 176
PRK10514 PRK10514
putative acetyltransferase; Provisional
 42-142 3.58e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.83  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225  42 EKMIHRFIEneYATIFVAVEDE-RIVGFILVNGNniqrkrHVATIVIGilQEYNGRGIGTRLfkeVEKWAKLHDvwRLEL 120
Cdd:PRK10514  39 EELVRSFLP--EAPLWVAVDERdQPVGFMLLSGG------HMEALFVD--PDVRGCGVGRML---VEHALSLHP--ELTT 103

                         90       100
                 ....*....|....*....|..
gi 446540225 121 TVMAHNTRAQALYKKAGFEKEG 142
Cdd:PRK10514 104 DVNEQNEQAVGFYKKMGFKVTG 125
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-142 6.71e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.12  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   1 MIREIEIEDAASFLQLskQLDEetkfmlyepgerkTTAEqqekmiHRFIENEY---------------ATIFVAVEDERI 65
Cdd:PRK10562   1 MIREYQPSDLPAILQL--WLES-------------TIWA------HPFIKEQYwresaplvrdvylpaAQTWVWEEDGKL 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540225  66 VGFIlvngnNIQRKRHVATIVIGilQEYNGRGIGTRLFKEVEKWAKLhdvwrLELTVMAHNTRAQALYKKAGFEKEG 142
Cdd:PRK10562  60 LGFV-----SVLEGRFVGALFVA--PKAVRRGIGKALMQHVQQRYPH-----LSLEVYQKNQRAVNFYHAQGFRIVD 124
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 2-153 1.89e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 37.08  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   2 IREIEIEDaasfLQLSKQLDEETKFMLY---EPGERKTT-AEQQEKMIHRFIENEyatiFVAVEDERIVGFI-LVNGNNI 76
Cdd:PRK15130   9 LRPLERED----LRFVHQLDNNASVMRYwfeEPYEAFVElSDLYDKHIHDQSERR----FVVECDGEKAGLVeLVEINHV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446540225  77 QRKrhvATIVIGILQEYNGRGIGTRLFKEVEKWA-KLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGK 153
Cdd:PRK15130  81 HRR---AEFQIIISPEYQGKGLATRAAKLAMDYGfTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGE 155
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 89-140 2.72e-03

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: 35.38  E-value: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446540225   89 ILQEYNGRGIGTRLFKEVEkwaklHDVWRLELTVMAH----NTRAQALYKKAGFEK 140
Cdd:pfam08445  29 TLPEHRRRGLGSRLVAALA-----RGIAERGITPFAVvvagNTPSRRLYEKLGFRK 79
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 87-145 2.87e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.06  E-value: 2.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446540225  87 IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKK 145
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRR 127
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
2-157 4.39e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 35.81  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225    2 IREIEIEDAASFLQLSKQLDEETKFMLYEpgerkttAEQQEKMIHRFIEN---EYATIFVAVEDERIVGFILVNGNNIQR 78
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEY-------AHSSIEEFETFLAAylsPGEIVFGVAESDRLIGYATLRQFDYVK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540225   79 KRHVATIVIgiLQEYNGRGIGTRLFKEVEKWA-KLHDVWRLELTVMAHNTRAQALYKKAGFEKEGVKKAALIIDGKGIDE 157
Cdd:pfam13420  74 THKAELSFY--VVKNNDEGINRELINAIIQYArKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDM 151
 
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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