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Conserved domains on  [gi|1765042305|gb|KAB5911766|]
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ribosomal-protein-alanine N-acetyltransferase [Bifidobacterium adolescentis]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 17-151 3.48e-32

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 112.04  E-value: 3.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  17 IAALEKDLFgRGAWSEQSVRQEFHAPARTYLLDIEGDAVQtadpvvrGYAGYWYDGDDAEIMTIGVGRPYQRQGIAAALL 96
Cdd:TIGR01575   5 VLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVV-------GYAGVQIVLDEAHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1765042305  97 ETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYYQPEGIDAYTM 151
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-151 3.48e-32

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: 112.04  E-value: 3.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  17 IAALEKDLFgRGAWSEQSVRQEFHAPARTYLLDIEGDAVQtadpvvrGYAGYWYDGDDAEIMTIGVGRPYQRQGIAAALL 96
Cdd:TIGR01575   5 VLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVV-------GYAGVQIVLDEAHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1765042305  97 ETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYYQPEGIDAYTM 151
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-156 2.35e-24

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 90.87  E-value: 2.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  64 GYAGYW--YDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYY 141
Cdd:COG0456     1 GFALLGlvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|....*
gi 1765042305 142 QPegiDAYTMSLDLE 156
Cdd:COG0456    81 GD---DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-131 3.60e-17

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: 73.32  E-value: 3.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  36 RQEFHAPARTYLLDIEGDavqtadpVVRGYAGYWYDGDD---AEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRML 112
Cdd:pfam00583  25 EDWDEDASEGFFVAEEDG-------ELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97

                          90
                  ....*....|....*....
gi 1765042305 113 LEVRVDNVPALALYERFGF 131
Cdd:pfam00583  98 LEVAADNLAAIALYEKLGF 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 73-155 3.50e-14

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 66.11  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  73 DDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYY-QPEGI-DAYT 150
Cdd:PRK09491   62 DEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYpTADGReDAII 141


                  ....*
gi 1765042305 151 MSLDL 155
Cdd:PRK09491  142 MALPL 146
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-114 8.63e-07

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: 44.57  E-value: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1765042305  64 GYAGYWYDG---DDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLE 114
Cdd:cd04301    12 GFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-151 3.48e-32

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: 112.04  E-value: 3.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  17 IAALEKDLFgRGAWSEQSVRQEFHAPARTYLLDIEGDAVQtadpvvrGYAGYWYDGDDAEIMTIGVGRPYQRQGIAAALL 96
Cdd:TIGR01575   5 VLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVV-------GYAGVQIVLDEAHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1765042305  97 ETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYYQPEGIDAYTM 151
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-156 2.35e-24

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 90.87  E-value: 2.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  64 GYAGYW--YDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYY 141
Cdd:COG0456     1 GFALLGlvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|....*
gi 1765042305 142 QPegiDAYTMSLDLE 156
Cdd:COG0456    81 GD---DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-131 3.60e-17

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: 73.32  E-value: 3.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  36 RQEFHAPARTYLLDIEGDavqtadpVVRGYAGYWYDGDD---AEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRML 112
Cdd:pfam00583  25 EDWDEDASEGFFVAEEDG-------ELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97

                          90
                  ....*....|....*....
gi 1765042305 113 LEVRVDNVPALALYERFGF 131
Cdd:pfam00583  98 LEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
62-155 7.59e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 68.10  E-value: 7.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  62 VRGYAGYWYDGDDAeimtIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKR-- 139
Cdd:COG1247    72 FRPRPAYRGTAEES----IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvg 147

                          90
                  ....*....|....*.
gi 1765042305 140 YYQPEGIDAYTMSLDL 155
Cdd:COG1247   148 FKFGRWLDLVLMQKRL 163
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 73-155 3.50e-14

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 66.11  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  73 DDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYY-QPEGI-DAYT 150
Cdd:PRK09491   62 DEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYpTADGReDAII 141


                  ....*
gi 1765042305 151 MSLDL 155
Cdd:PRK09491  142 MALPL 146
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 2-144 4.70e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.46  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305   2 IVDHSQIPEDTAvgqIAALEKDLFGRgawsEQSVRQEFHapartYLLDIEGDAVqtadpvvrGYAGYW-YDGDDAEIMTI 80
Cdd:COG0454     5 KATPEDINFILL---IEALDAELKAM----EGSLAGAEF-----IAVDDKGEPI--------GFAGLRrLDDKVLELKRL 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765042305  81 GVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYYQPE 144
Cdd:COG0454    65 YVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 54-153 6.85e-13

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: 63.48  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  54 AVQTADPVVRGYAGYWYDGDDAEIMTIG--VGRPYQRQGIAAALLETLIVSARRQ-GAKRMLLEVRVDNVPALALYERFG 130
Cdd:COG1670    65 IEDKEDGELIGVVGLYDIDRANRSAEIGywLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG 144

                          90       100
                  ....*....|....*....|....*
gi 1765042305 131 FTRMGLRKRYYQPEG--IDAYTMSL 153
Cdd:COG1670   145 FRLEGTLRDALVIDGryRDHVLYSL 169
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
66-135 7.84e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 58.38  E-value: 7.84e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  66 AGYWYDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFTRMG 135
Cdd:COG3393     7 GVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 64-135 2.70e-11

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: 58.08  E-value: 2.70e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765042305  64 GYAG-YWYDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRvdnVPALALYERFGFTRMG 135
Cdd:COG1246    41 GCAAlHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT---SAAIHFYEKLGFEEID 110
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-155 8.59e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.02  E-value: 8.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305   9 PEDtaVGQIAALEKDLFGRGAWSEQSVR-QEFHAPARTYLLDIEGDAVqtadpvvrGYAGYW-----YDGDDAEIMTIGV 82
Cdd:COG3153     6 PED--AEAIAALLRAAFGPGREAELVDRlREDPAAGLSLVAEDDGEIV--------GHVALSpvdidGEGPALLLGPLAV 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765042305  83 GRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPalaLYERFGFTRMGLRKRYYQPegiDAYTMSLDL 155
Cdd:COG3153    76 DPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP---FYERFGFRPAGELGLTLGP---DEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 64-133 1.13e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765042305  64 GYAGYWYDGDDAEIMTIGVG-RP-YQRQGIAAALLETLIVSARRQGAKRMLLEVRvdnVPALALYERFGFTR 133
Cdd:pfam13508  16 GFAALLPLDDEGALAELRLAvHPeYRGQGIGRALLEAAEAAAKEGGIKLLELETT---NRAAAFYEKLGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 82-135 1.87e-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: 50.35  E-value: 1.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1765042305  82 VGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNvPALALYERFGFTRMG 135
Cdd:pfam13673  59 VDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFYEKLGFRATG 111
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
68-156 4.85e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 49.41  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  68 YWYDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDnvpALALYERFGFTRMGlrkRYYQPEGID 147
Cdd:COG2153    52 LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPVG---EEFLEAGIP 125


                  ....*....
gi 1765042305 148 AYTMSLDLE 156
Cdd:COG2153   126 HIDMRKPLS 134
PRK10140 PRK10140
N-acetyltransferase;
80-152 2.43e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.05  E-value: 2.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765042305  80 IGVGRPYQRQGIAAALLETLI-VSARRQGAKRMLLEVRVDNVPALALYERFGFTRMGLRKRY--YQPEGIDAYTMS 152
Cdd:PRK10140   84 ICVDSRWKNRGVASALMREMIeMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYalRNGEYVDAYYMA 159
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-114 8.63e-07

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: 44.57  E-value: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1765042305  64 GYAGYWYDG---DDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLE 114
Cdd:cd04301    12 GFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 78-151 2.74e-05

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 42.35  E-value: 2.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765042305  78 MTIGV-GRPYQRQGIAAALLETLIVSARRQ-GAKRMLLEVRVDNVPALALYERFGFTRMGLRKRYyqPEGIDAYTM 151
Cdd:TIGR03585  78 AFWGIyANPFCKPGVGSVLEEAALEYAFEHlGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG--GEYYDVLLM 151
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
74-132 1.72e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.30  E-value: 1.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1765042305  74 DAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFT 132
Cdd:PRK10975  126 DARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
PRK12308 PRK12308
argininosuccinate lyase;
49-132 8.00e-04

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 39.38  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  49 DIEGDAVQTADPVVRGYAG-YWYDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRvdnVPALALYE 127
Cdd:PRK12308  501 DIGSFAVAEHHGEVTGCASlYIYDSGLAEIRSLGVEAGWQVQGQGSALVQYLVEKARQMAIKKVFVLTR---VPEFFMKQ 577


                  ....*
gi 1765042305 128 RFGFT 132
Cdd:PRK12308  578 GFSPT 582
PRK03624 PRK03624
putative acetyltransferase; Provisional
 70-132 1.83e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765042305  70 YDGDDAEIMTIGVGRPYQRQGIAAALLETLIVSARRQGAKRMLLEVRVDNVPALALYERFGFT 132
Cdd:PRK03624   64 YDGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYE 126
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-132 4.82e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 35.78  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765042305  54 AVQTADPVVRGYAGYWYDGDDAEIMTIG--VGRPYQRQGIA----AALLEtliVSARRQGAKRMLLEVRVDNVPALALYE 127
Cdd:pfam13302  58 AIELKDTGFIGSIGLYDIDGEPERAELGywLGPDYWGKGYAteavRALLE---YAFEELGLPRLVARIDPENTASRRVLE 134


                  ....*
gi 1765042305 128 RFGFT 132
Cdd:pfam13302 135 KLGFK 139
 
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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