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Conserved domains on  [gi|446540222|ref|WP_000617568|]
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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 2.89e-27

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 100.07  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKIIDRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQTLYKKAGFEKEGVKKAALIIDGKCIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540222 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 2.89e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 100.07  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKIIDRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQTLYKKAGFEKEGVKKAALIIDGKCIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540222 160 MAKLL 164
Cdd:COG1247  159 MQKRL 163
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 42-146 1.14e-15

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: 69.28  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   42 EKIIDRFIENEYATIFVAVEDERIVGFILVngnniQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLEL 120
Cdd:TIGR01575  19 EAQFAEELANYHLCYLLARIGGKVVGYAGV-----QIVLDEAHILnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|....*.
gi 446540222  121 TVMAHNTRAQTLYKKAGFEKEGVKKA 146
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIAIRRN 119
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-138 1.57e-15

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: 68.31  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   44 IIDRFIENEYATIFVAVEDERIVGFILVNGNNiQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVM 123
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVA 101

                          90
                  ....*....|....*
gi 446540222  124 AHNTRAQTLYKKAGF 138
Cdd:pfam00583 102 ADNLAAIALYEKLGF 116
PRK10140 PRK10140
N-acetyltransferase;
57-163 1.83e-12

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 61.54  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  57 FVAVEDERIVGFILVNGNNIQRKRHVATIVIGILQEYNGRGIGTRLFKEV----EKWAKlhdVWRLELTVMAHNTRAQTL 132
Cdd:PRK10140  54 LVACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMiemcDNWLR---VDRIELTVFVDNAPAIKV 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446540222 133 YKKAGFEKEGVKKAALIIDGKCIDEYEMAKL 163
Cdd:PRK10140 131 YKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 2.56e-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: 50.74  E-value: 2.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540222  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 2.89e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 100.07  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   1 MIREIEIEDAASFLQLSKQLDEETKfMLYEPGERktTAEQQEKIIDRFIENEYAtIFVAVEDERIVGFI-LVNGNNIQRK 79
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGT-ATFETEPP--SEEEREAWFAAILAPGRP-VLVAEEDGEVVGFAsLGPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  80 RHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQTLYKKAGFEKEGVKKAALIIDGKCIDEYE 159
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158


                 ....*
gi 446540222 160 MAKLL 164
Cdd:COG1247  159 MQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-165 1.41e-26

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: 98.53  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   2 IREIEIEDAASFLQLSKQlDEETKFMLYEPGERKTTAEQQEKIIDRFIENEYATIFVAV-EDERIVGFILVNgnNIQRKR 80
Cdd:COG1670   10 LRPLRPEDAEALAELLND-PEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDkEDGELIGVVGLY--DIDRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  81 HVATIVIGILQEYNGRGIGTRLFKEVEKWAKLH-DVWRLELTVMAHNTRAQTLYKKAGFEKEGVKKAALIIDGKCIDEYE 159
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ....*.
gi 446540222 160 MAKLLK 165
Cdd:COG1670  167 YSLLRE 172
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 42-146 1.14e-15

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: 69.28  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   42 EKIIDRFIENEYATIFVAVEDERIVGFILVngnniQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLEL 120
Cdd:TIGR01575  19 EAQFAEELANYHLCYLLARIGGKVVGYAGV-----QIVLDEAHILnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|....*.
gi 446540222  121 TVMAHNTRAQTLYKKAGFEKEGVKKA 146
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIAIRRN 119
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-145 1.43e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 67.76  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  67 GFILVNgnnIQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQTLYKKAGFEKEGVKK 145
Cdd:COG0456    1 GFALLG---LVDGGDEAEIEdLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-138 1.57e-15

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: 68.31  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   44 IIDRFIENEYATIFVAVEDERIVGFILVNGNNiQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVM 123
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVA 101

                          90
                  ....*....|....*
gi 446540222  124 AHNTRAQTLYKKAGF 138
Cdd:pfam00583 102 ADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-140 4.98e-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: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  39 EQQEKIIDRFIENEYATIFVAVED-ERIVGFI---LVNGNNIQRKRhvativIGILQEYNGRGIGTRLFKEVEKWAKLHD 114
Cdd:COG0454   18 EALDAELKAMEGSLAGAEFIAVDDkGEPIGFAglrRLDDKVLELKR------LYVLPEYRGKGIGKALLEALLEWARERG 91

                         90       100
                 ....*....|....*....|....*.
gi 446540222 115 VWRLELTVMAHNTRAQTLYKKAGFEK 140
Cdd:COG0454   92 CTALELDTLDGNPAAIRFYERLGFKE 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 52-140 5.30e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.93  E-value: 5.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   52 EYATIFVAVEDERIVGFILVNGnnIQRKRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVmahNTRAQT 131
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP--LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAA 75


                  ....*....
gi 446540222  132 LYKKAGFEK 140
Cdd:pfam13508  76 FYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-142 9.47e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.03  E-value: 9.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   2 IREIEIEDAASFLQLSKQLdeetkfmlYEPGERkttaeqqEKIIDRFIENEYAT-IFVAVEDERIVGFILVNGNNIQRKR 80
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA--------FGPGRE-------AELVDRLREDPAAGlSLVAEDDGEIVGHVALSPVDIDGEG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446540222  81 HVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVmahNTRAQTLYKKAGFEKEG 142
Cdd:COG3153   66 PALLLGpLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAG 125
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-143 1.69e-12

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: 60.75  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   45 IDRFIENEYATIFVAVEDERIVGFIlvngnNIQRKRHVATIVIgiLQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMA 124
Cdd:pfam13673  22 LRERIDQGEYFFFVAFEGGQIVGVI-----ALRDRGHISLLFV--DPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNA 94

                          90
                  ....*....|....*....
gi 446540222  125 HNTrAQTLYKKAGFEKEGV 143
Cdd:pfam13673  95 SPY-AVPFYEKLGFRATGP 112
PRK10140 PRK10140
N-acetyltransferase;
57-163 1.83e-12

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 61.54  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  57 FVAVEDERIVGFILVNGNNIQRKRHVATIVIGILQEYNGRGIGTRLFKEV----EKWAKlhdVWRLELTVMAHNTRAQTL 132
Cdd:PRK10140  54 LVACIDGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMiemcDNWLR---VDRIELTVFVDNAPAIKV 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446540222 133 YKKAGFEKEGVKKAALIIDGKCIDEYEMAKL 163
Cdd:PRK10140 131 YKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-139 2.99e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.04  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222    2 IREIEIEDAASFLQLSKqlDEEtkFMLYEPGERKTTAEQQEKIIDRFIENEYATIF---VAVEDERIVGFILVNgnNIQR 78
Cdd:pfam13302   4 LRPLTEEDAEALFELLS--DPE--VMRYGVPWPLTLEEAREWLARIWAADEAERGYgwaIELKDTGFIGSIGLY--DIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446540222   79 KRHVATIVIGILQEYNGRGIGTRLFKEVEKWAKLHDVW-RLELTVMAHNTRAQTLYKKAGFE 139
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLpRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 2.56e-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: 50.74  E-value: 2.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540222  56 IFVAVEDERIVGFILVNGNNiqRKRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELT 121
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDG--SGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-139 2.78e-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: 52.30  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  34 RKTTAEQQEKIID----RFIENEYATIFVAVEDERIVGFILVngnnIQRKRHVATIV-IGILQEYNGRGIGTRLFKEVEK 108
Cdd:COG1246    4 RPATPDDVPAILElirpYALEEEIGEFWVAEEDGEIVGCAAL----HPLDEDLAELRsLAVHPDYRGRGIGRRLLEALLA 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446540222 109 WAKLHDVWRLELTVmahNTRAQTLYKKAGFE 139
Cdd:COG1246   80 EARELGLKRLFLLT---TSAAIHFYEKLGFE 107
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
64-139 5.50e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 50.29  E-value: 5.50e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446540222  64 RIVGFILVNGNNiqrkRHVATIV-IGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHNTRAQTLYKKAGFE 139
Cdd:COG3393    1 ELVAMAGVRAES----PGVAEISgVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
52-142 7.19e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.64  E-value: 7.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  52 EYATIFVAVEDERIVGF--ILVNGNNIQRKRHVATivigiLQEYNGRGIGTRLFKEVEKWAKLHDVWRLELTVMAHntrA 129
Cdd:COG2153   32 EDARHLLAYDDGELVATarLLPPGDGEAKIGRVAV-----LPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---A 103

                         90
                 ....*....|...
gi 446540222 130 QTLYKKAGFEKEG 142
Cdd:COG2153  104 VGFYEKLGFVPVG 116
PRK03624 PRK03624
putative acetyltransferase; Provisional
 45-157 1.49e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.61  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  45 IDRFIENEYATIFVAVEDERIVGFILV--NGnniqrkrHVATI-VIGILQEYNGRGIGTRLFKEVEKWAKLHDVWRLELT 121
Cdd:PRK03624  36 IERKLNHDPSLFLVAEVGGEVVGTVMGgyDG-------HRGWAyYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQ 108

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446540222 122 VMAHNTRAQTLYKKAGFEKEGVkkaalIIDGKCIDE 157
Cdd:PRK03624 109 VREDNDAVLGFYEALGYEEQDR-----ISLGKRLIE 139
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
123-153 1.15e-04

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 40.49  E-value: 1.15e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446540222 123 MAHNTRAQTLYKKAGFEKEGVKKAALIIDGK 153
Cdd:PRK10809 146 MPHNKRSGDLLARLGFEKEGYAKDYLLIDGQ 176
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 2-153 4.12e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 39.01  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   2 IREIEIEDaasfLQLSKQLDEETKFMLYEPGERKTTAEQQEKIIDRFIENEYATIFVAVEDERIVGFI-LVNGNNIQRKr 80
Cdd:PRK15130   9 LRPLERED----LRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVeLVEINHVHRR- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446540222  81 hvATIVIGILQEYNGRGIGTRLFKEVEKWA-KLHDVWRLELTVMAHNTRAQTLYKKAGFEKEGVKKAALIIDGK 153
Cdd:PRK15130  84 --AEFQIIISPEYQGKGLATRAAKLAMDYGfTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGE 155
PRK10514 PRK10514
putative acetyltransferase; Provisional
 46-142 2.20e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 36.52  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  46 DRF-IENE------YATIFVAVEDE-RIVGFILVNGNniqrkrHVATIVIGilQEYNGRGIGTRLfkeVEKWAKLHDvwR 117
Cdd:PRK10514  34 DRAeIEELvrsflpEAPLWVAVDERdQPVGFMLLSGG------HMEALFVD--PDVRGCGVGRML---VEHALSLHP--E 100

                         90       100
                 ....*....|....*....|....*
gi 446540222 118 LELTVMAHNTRAQTLYKKAGFEKEG 142
Cdd:PRK10514 101 LTTDVNEQNEQAVGFYKKMGFKVTG 125
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-142 2.39e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 36.58  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222   1 MIREIEIEDAASFLQL-------------------SKQLDEETkfmlYEPGERKTTAEQQEKIIDrfieneyatiFVAVE 61
Cdd:PRK10562   1 MIREYQPSDLPAILQLwlestiwahpfikeqywreSAPLVRDV----YLPAAQTWVWEEDGKLLG----------FVSVL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446540222  62 DERIVGFILVNgnniqrkrhvativigilQEYNGRGIGTRLFKEVEKWAKLhdvwrLELTVMAHNTRAQTLYKKAGFEKE 141
Cdd:PRK10562  67 EGRFVGALFVA------------------PKAVRRGIGKALMQHVQQRYPH-----LSLEVYQKNQRAVNFYHAQGFRIV 123


                 .
gi 446540222 142 G 142
Cdd:PRK10562 124 D 124
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 89-140 4.74e-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: 34.61  E-value: 4.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446540222   89 ILQEYNGRGIGTRLFKEVEkwaklHDVWRLELTVMAH----NTRAQTLYKKAGFEK 140
Cdd:pfam08445  29 TLPEHRRRGLGSRLVAALA-----RGIAERGITPFAVvvagNTPSRRLYEKLGFRK 79
 
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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