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Conserved domains on  [gi|333441000|gb|AEF32774|]
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nourseothricin drug marker protein [Artificial vector pJL519]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 94-177 4.21e-22

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 85.48  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  94 GFVVVSYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCGLDTALY 173
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80


                 ....
gi 333441000 174 DGTA 177
Cdd:COG0456   81 GDDA 84
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 94-177 4.21e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 85.48  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  94 GFVVVSYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCGLDTALY 173
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80


                 ....
gi 333441000 174 DGTA 177
Cdd:COG0456   81 GDDA 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 75-163 1.83e-21

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: 84.49  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   75 DGDPDSRTFVAYgDDGDLAGFVVVSYSGW-NRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAP 153
Cdd:pfam00583  28 DEDASEGFFVAE-EDGELVGFASLSIIDDePPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 333441000  154 AIHAYRRMGF 163
Cdd:pfam00583 107 AIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 88-186 8.83e-14

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: 65.04  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   88 DDGDLAGFVVVSYSGWNRRLTveDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCG 167
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHIL--NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115

                          90
                  ....*....|....*....
gi 333441000  168 LDTALYDGTasdGEQALYM 186
Cdd:TIGR01575 116 IRRNYYPDP---GEDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 83-146 1.03e-12

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: 60.37  E-value: 1.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333441000  83 FVAYgDDGDLAGFVVVSYSGW-NRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLE 146
Cdd:cd04301    2 LVAE-DDGEIVGFASLSPDGSgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 108-189 5.94e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 52.24  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000 108 TVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCGLDTALYDgTASDGEQALYMS 187
Cdd:PRK09491  65 TLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYP-TADGREDAIIMA 143


                 ..
gi 333441000 188 MP 189
Cdd:PRK09491 144 LP 145
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 94-177 4.21e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 85.48  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  94 GFVVVSYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCGLDTALY 173
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80


                 ....
gi 333441000 174 DGTA 177
Cdd:COG0456   81 GDDA 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 75-163 1.83e-21

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: 84.49  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   75 DGDPDSRTFVAYgDDGDLAGFVVVSYSGW-NRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAP 153
Cdd:pfam00583  28 DEDASEGFFVAE-EDGELVGFASLSIIDDePPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 333441000  154 AIHAYRRMGF 163
Cdd:pfam00583 107 AIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 75-164 9.39e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.48  E-value: 9.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  75 DGDPDSRTFVAYGDDGDLAGFVVVSYSGwNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPA 154
Cdd:COG0454   28 EGSLAGAEFIAVDDKGEPIGFAGLRRLD-DKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAA 106

                         90
                 ....*....|
gi 333441000 155 IHAYRRMGFT 164
Cdd:COG0454  107 IRFYERLGFK 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
77-167 1.04e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 76.19  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  77 DPDSRTFVAyGDDGDLAGFVVVS-YSGWN-RRLTVED-IEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAP 153
Cdd:COG1247   49 APGRPVLVA-EEDGEVVGFASLGpFRPRPaYRGTAEEsIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEA 127

                         90
                 ....*....|....
gi 333441000 154 AIHAYRRMGFTLCG 167
Cdd:COG1247  128 SIALYEKLGFEEVG 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 78-164 6.97e-17

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 71.72  E-value: 6.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   78 PDSRTFVAYgDDGDLAGFVVVSYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNvnaPAIHA 157
Cdd:pfam13508   1 PGGRFFVAE-DDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAF 76


                  ....*..
gi 333441000  158 YRRMGFT 164
Cdd:pfam13508  77 YEKLGFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 77-189 4.04e-16

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: 71.18  E-value: 4.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  77 DPDSRTFVAYgDDGDLAGFVVVsYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTnvnAPAIH 156
Cdd:COG1246   25 EEIGEFWVAE-EDGEIVGCAAL-HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT---SAAIH 99

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333441000 157 AYRRMGFTLCGLDTALYDGTASDGEQALYMSMP 189
Cdd:COG1246  100 FYEKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
57-167 9.55e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.80  E-value: 9.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  57 LTKVFPDDESDDESDAGEDGDPDSRTFVAYgDDGDLAGFVVVSY---SGWNRRLTVEDIEVAPEHRGHGVGRALMGLATE 133
Cdd:COG3153   16 LRAAFGPGREAELVDRLREDPAAGLSLVAE-DDGEIVGHVALSPvdiDGEGPALLLGPLAVDPEYRGQGIGRALMRAALE 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 333441000 134 FARERGAGHLWLEvtnVNAPAIHAYRRMGFTLCG 167
Cdd:COG3153   95 AARERGARAVVLL---GDPSLLPFYERFGFRPAG 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 88-186 8.83e-14

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: 65.04  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   88 DDGDLAGFVVVSYSGWNRRLTveDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCG 167
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHIL--NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115

                          90
                  ....*....|....*....
gi 333441000  168 LDTALYDGTasdGEQALYM 186
Cdd:TIGR01575 116 IRRNYYPDP---GEDAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
97-167 9.73e-14

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 63.39  E-value: 9.73e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333441000  97 VVSYSGWNRRLT----VEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCG 167
Cdd:COG3393    2 LVAMAGVRAESPgvaeISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 83-146 1.03e-12

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: 60.37  E-value: 1.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333441000  83 FVAYgDDGDLAGFVVVSYSGW-NRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLE 146
Cdd:cd04301    2 LVAE-DDGEIVGFASLSPDGSgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
75-167 1.21e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 59.43  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  75 DG-DPDSRTFVAYgDDGDLAGFVvvsysgwnrRLTVEDIE--------VAPEHRGHGVGRALMGLATEFARERGAGHLWL 145
Cdd:COG2153   28 DGkDEDARHLLAY-DDGELVATA---------RLLPPGDGeakigrvaVLPEYRGQGLGRALMEAAIEEARERGARRIVL 97

                         90       100
                 ....*....|....*....|..
gi 333441000 146 evtNVNAPAIHAYRRMGFTLCG 167
Cdd:COG2153   98 ---SAQAHAVGFYEKLGFVPVG 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 84-188 2.53e-11

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: 59.24  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  84 VAYGDDGDLAGFVVVSYSGWNRRlTVE-DIEVAPEHRGHGVGRALMGLATEFA-RERGAGHLWLEVTNVNAPAIHAYRRM 161
Cdd:COG1670   65 IEDKEDGELIGVVGLYDIDRANR-SAEiGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKL 143

                         90       100
                 ....*....|....*....|....*....
gi 333441000 162 GFTLCGL--DTALYDGTASDgeqALYMSM 188
Cdd:COG1670  144 GFRLEGTlrDALVIDGRYRD---HVLYSL 169
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 77-167 1.73e-09

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: 53.43  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   77 DPDSRTFVAYgDDGDLAGFVVVSysgwnRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVtNVNAPAIH 156
Cdd:pfam13673  28 QGEYFFFVAF-EGGQIVGVIALR-----DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV-NASPYAVP 100

                          90
                  ....*....|.
gi 333441000  157 AYRRMGFTLCG 167
Cdd:pfam13673 101 FYEKLGFRATG 111
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 108-189 5.94e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 52.24  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000 108 TVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAYRRMGFTLCGLDTALYDgTASDGEQALYMS 187
Cdd:PRK09491  65 TLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYP-TADGREDAIIMA 143


                 ..
gi 333441000 188 MP 189
Cdd:PRK09491 144 LP 145
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
88-164 8.20e-08

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 49.55  E-value: 8.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  88 DDGDLAGFVV-----VSYSGWNRR---------LTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVtNV--- 150
Cdd:COG3818   52 VDGEVAGFLLafgpgADYDSPNYRwfaerydnfLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCEV-NLepp 130

                         90
                 ....*....|....
gi 333441000 151 NAPAIHAYRRMGFT 164
Cdd:COG3818  131 NPGSLAFHARLGFR 144
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 83-139 1.91e-07

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 46.74  E-value: 1.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 333441000   83 FVAYGDDGDLAGFVvvSYSGWNRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERG 139
Cdd:pfam14542   2 FEIRVDGGAEVAFL--TYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEG 56
PRK10562 PRK10562
putative acetyltransferase; Provisional
 78-164 2.68e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 47.75  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  78 PDSRTFVaYGDDGDLAGFVVVSYSgwnrRLtVEDIEVAPEHRGHGVGRALMglatEFARERGAgHLWLEVTNVNAPAIHA 157
Cdd:PRK10562  46 PAAQTWV-WEEDGKLLGFVSVLEG----RF-VGALFVAPKAVRRGIGKALM----QHVQQRYP-HLSLEVYQKNQRAVNF 114


                 ....*..
gi 333441000 158 YRRMGFT 164
Cdd:PRK10562 115 YHAQGFR 121
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
77-139 5.09e-07

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 45.92  E-value: 5.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333441000  77 DPDSRTFVAYgDDGDLAGFVVVSYSGwnRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERG 139
Cdd:COG2388    6 NEEKGRFELE-VDGELAGELTYRLEG--GVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-164 1.45e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.99  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  78 PDSRTFVAYgDDGDLAGFVVVSYSGwnRRLTVEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHA 157
Cdd:PRK03624  43 DPSLFLVAE-VGGEVVGTVMGGYDG--HRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGF 119


                 ....*..
gi 333441000 158 YRRMGFT 164
Cdd:PRK03624 120 YEALGYE 126
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
82-145 5.25e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 41.82  E-value: 5.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333441000  82 TFVAYGDDGDLAGFVVVSYsGWNRRLTVE--DI--EVAPEHRGHGVGRALMGLATEFARERGAGHLWL 145
Cdd:COG3981   64 TYWLVDEDGRIVGAINLRH-ELNEFLLRVggHIgyGVRPSERGKGYATEMLRLALEEARELGLDRVLI 130
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 77-167 2.26e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.17  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  77 DPDSRTFVAYgDDGDLAGFV-VVSYSGWNRRLTVEDIeVAPEHRGHGVGRALMGLATEFARE-RGAGHLWLEVTNVNAPA 154
Cdd:PRK15130  54 DQSERRFVVE-CDGEKAGLVeLVEINHVHRRAEFQII-ISPEYQGKGLATRAAKLAMDYGFTvLNLYKLYLIVDKENEKA 131

                         90
                 ....*....|...
gi 333441000 155 IHAYRRMGFTLCG 167
Cdd:PRK15130 132 IHIYRKLGFEVEG 144
PTZ00330 PTZ00330
acetyltransferase; Provisional
 109-166 3.12e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 39.44  E-value: 3.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333441000 109 VEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNvnaPAIHAYRRMGFTLC 166
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTE---DMVAFYKKLGFRAC 139
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 79-165 5.17e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 38.32  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000   79 DSRTFVAYgDDGDLAGfVVVSYSgwnRRLT----------VEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVT 148
Cdd:pfam13527  38 EGRVLGAF-DDGELVS-TLALYP---FELNvpgktlpaagITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYPS 112

                          90
                  ....*....|....*..
gi 333441000  149 nvnAPAIhaYRRMGFTL 165
Cdd:pfam13527 113 ---SYPI--YRRFGYEI 124
PRK10514 PRK10514
putative acetyltransferase; Provisional
 114-167 1.02e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 333441000 114 VAPEHRGHGVGRALMGLATEFARErgaghLWLEVTNVNAPAIHAYRRMGFTLCG 167
Cdd:PRK10514  77 VDPDVRGCGVGRMLVEHALSLHPE-----LTTDVNEQNEQAVGFYKKMGFKVTG 125
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 87-165 1.49e-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: 36.15  E-value: 1.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333441000   87 GDDGDLAGFVVVSYSGwnrrlTVEDIEVAPEHRGHGVGRALMGLATEFARERGAgHLWLEVTNVNAPAIHAYRRMGFTL 165
Cdd:pfam08445   7 GDTGELAAWCLRLPGG-----ELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLGFRK 79
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
84-165 1.81e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 37.60  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  84 VAYGDDGDLAGFVVVsysgwnRRLTVED-----IEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPAIHAY 158
Cdd:PRK10975 105 LLRDASGQIQGFVTL------RELNDTDariglLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLY 178


                 ....*..
gi 333441000 159 RRMGFTL 165
Cdd:PRK10975 179 IRSGANI 185
PRK10140 PRK10140
N-acetyltransferase;
89-187 3.03e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 36.88  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333441000  89 DGDLAGFVVVSYSGWNRRLTVEDIEVAPEHRGH--GVGRALMGLATEFARErgaghlWLEVTNV-------NAPAIHAYR 159
Cdd:PRK10140  59 DGDVVGHLTIDVQQRPRRSHVADFGICVDSRWKnrGVASALMREMIEMCDN------WLRVDRIeltvfvdNAPAIKVYK 132

                         90       100       110
                 ....*....|....*....|....*....|
gi 333441000 160 RMGFTL--CGLDTALYDGTASDgeqALYMS 187
Cdd:PRK10140 133 KYGFEIegTGKKYALRNGEYVD---AYYMA 159
Eis COG4552
Predicted acetyltransferase [General function prediction only];
114-167 3.56e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.19  E-value: 3.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 333441000 114 VAPEHRGHGVGRALMGLATEFARERGA--GHLWlevtnvnAPAIHAYRRMGFTLCG 167
Cdd:COG4552   80 VAPEHRRRGVARALLREALAELRERGQplSALY-------PFEPGFYRRFGYELAG 128
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 109-173 9.09e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 35.07  E-value: 9.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333441000 109 VEDIEVAPEHRGHGVGRALMGLATEFARERGAGHLWLEVTNVNAPaihAYRRMGFTLCGLDTALY 173
Cdd:PLN02706  88 IEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKA---FYEKCGYVRKEIQMVKY 149
 
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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