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Conserved domains on  [gi|501020507|ref|WP_012073178|]
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ribosomal protein S18-alanine N-acetyltransferase [Actinobacillus succinogenes]

Protein Classification

ribosomal-protein-alanine N-acetyltransferase( domain architecture ID 10013255)

ribosomal-protein-alanine N-acetyltransferase acetylates the N-terminal alanine of ribosomal protein S18; similar to Escherichia coli K-12 RimI

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 3-149 1.55e-95

ribosomal-protein-alanine N-acetyltransferase; Provisional


:

Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 271.80  E-value: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   3 VIRIEPVTENEMESLYPIETAAHSVPWSLGTLKNNVGNRYHNLKILLDDQIVGFAICQIVLDEATLFNITVHPDFQGQKL 82
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501020507  83 GHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYPTADGkRENAVIMAAYL 149
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADG-REDAIIMALPL 146
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 3-149 1.55e-95

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 271.80  E-value: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   3 VIRIEPVTENEMESLYPIETAAHSVPWSLGTLKNNVGNRYHNLKILLDDQIVGFAICQIVLDEATLFNITVHPDFQGQKL 82
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501020507  83 GHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYPTADGkRENAVIMAAYL 149
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADG-REDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 15-145 9.35e-49

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: 153.25  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   15 ESLYPIETAAHSVPWSLGTLKNNVGNRYHNLKILL-DDQIVGFAICQIVLDEATLFNITVHPDFQGQKLGHMLLNALIEQ 93
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 501020507   94 LRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYPTADgkrENAVIM 145
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPG---EDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-149 6.65e-25

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 91.26  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  55 GFAICQIVL--DEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYY 132
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*..
gi 501020507 133 PtadgkrENAVIMAAYL 149
Cdd:COG0456   81 G------DDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-122 7.72e-20

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: 79.10  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   14 MESLYPIETAAHSVPWSLGTL----KNNVGNRYHNLKILLDDQIVGFAICQIVLDE---ATLFNITVHPDFQGQKLGHML 86
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 501020507   87 LNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-105 1.14e-11

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: 56.52  E-value: 1.14e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501020507  47 ILLDDQIVGFAICQI---VLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLE 105
Cdd:cd04301    4 AEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 3-149 1.55e-95

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 271.80  E-value: 1.55e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   3 VIRIEPVTENEMESLYPIETAAHSVPWSLGTLKNNVGNRYHNLKILLDDQIVGFAICQIVLDEATLFNITVHPDFQGQKL 82
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501020507  83 GHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYPTADGkRENAVIMAAYL 149
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADG-REDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 15-145 9.35e-49

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: 153.25  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   15 ESLYPIETAAHSVPWSLGTLKNNVGNRYHNLKILL-DDQIVGFAICQIVLDEATLFNITVHPDFQGQKLGHMLLNALIEQ 93
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 501020507   94 LRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYPTADgkrENAVIM 145
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPG---EDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-149 6.65e-25

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 91.26  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  55 GFAICQIVL--DEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYY 132
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*..
gi 501020507 133 PtadgkrENAVIMAAYL 149
Cdd:COG0456   81 G------DDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-122 7.72e-20

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: 79.10  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   14 MESLYPIETAAHSVPWSLGTL----KNNVGNRYHNLKILLDDQIVGFAICQIVLDE---ATLFNITVHPDFQGQKLGHML 86
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 501020507   87 LNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNF 122
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
6-145 2.47e-18

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 76.57  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   6 IEPVTENEMESLypietaahsvpwslgtLKNNVGNRYHNLKILLDDQIVGFAICQIV-----LDEATLFNITVHPDFQGQ 80
Cdd:COG1247   32 TEPPSEEEREAW----------------FAAILAPGRPVLVAEEDGEVVGFASLGPFrprpaYRGTAEESIYVDPDARGR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501020507  81 KLGHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNYYpTADGKRENAVIM 145
Cdd:COG1247   96 GIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVG-FKFGRWLDLVLM 159
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 47-145 1.20e-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: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  47 ILLDDQIVGF-AICQIVLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLevrESNRHAIKLYEKLNFNEV 125
Cdd:COG1246   33 AEEDGEIVGCaALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEEI 109

                         90       100
                 ....*....|....*....|
gi 501020507 126 DvrKNYYPTADGKRENAVIM 145
Cdd:COG1246  110 D--KEDLPYAKVWQRDSVVM 127
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-124 2.48e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 66.71  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   47 ILLDDQIVGFAICQIVLDEATLFNIT--VHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVREsnrHAIKLYEKLNFNE 124
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRlaVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-126 1.48e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.87  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   6 IEPVTENEMESLYPIETAAHSVPWSLGTLKN--NVGNRYHNLKILLDDQIVGFAICQIV-----LDEATLFNITVHPDFQ 78
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRlrEDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEYR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501020507  79 GQKLGHMLLNALIEQLRKKGILSLWLevrESNRHAIKLYEKLNFNEVD 126
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFRPAG 125
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
47-125 2.83e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 59.81  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  47 ILLDDQIVGFA-ICQIVLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVREsnrHAIKLYEKLNFNEV 125
Cdd:COG2153   39 AYDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA---HAVGFYEKLGFVPV 115
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
52-125 1.00e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 57.23  E-value: 1.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501020507  52 QIVGFAICQIVLDE-ATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEV 125
Cdd:COG3393    1 ELVAMAGVRAESPGvAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-105 1.14e-11

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: 56.52  E-value: 1.14e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501020507  47 ILLDDQIVGFAICQI---VLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLE 105
Cdd:cd04301    4 AEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 40-127 4.35e-11

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: 56.51  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   40 NRYHNLKILLDDQIVGFAIcqiVLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESNrHAIKLYEK 119
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIA---LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFYEK 104


                  ....*...
gi 501020507  120 LNFNEVDV 127
Cdd:pfam13673 105 LGFRATGP 112
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 50-146 3.30e-09

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 52.69  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  50 DDQIVGFA-ICQIVLDEATL-FNITVHPDFQGQKLGHMLLNALIEQLRKK-GILSLWLEVRESNRHAIKLYEKLNFNEVD 126
Cdd:COG1670   70 DGELIGVVgLYDIDRANRSAeIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149

                         90       100
                 ....*....|....*....|
gi 501020507 127 VRKNYYPtADGKRENAVIMA 146
Cdd:COG1670  150 TLRDALV-IDGRYRDHVLYS 168
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 61-128 1.35e-08

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: 49.25  E-value: 1.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501020507   61 IVLDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGILSLwLEVRESNRHAIKLYEKLNFNEVDVR 128
Cdd:pfam08445  17 LRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPF-AVVVAGNTPSRRLYEKLGFRKIDET 83
PRK03624 PRK03624
putative acetyltransferase; Provisional
 73-127 1.54e-08

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 50.31  E-value: 1.54e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501020507  73 VHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDV 127
Cdd:PRK03624  76 VHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDR 130
PRK07757 PRK07757
N-acetyltransferase;
50-133 3.49e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 44.03  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507  50 DDQIVGFAICQIV-LDEATLFNITVHPDFQGQKLGHMLLNALIEQLRKKGI---LSLWLEVResnrhaikLYEKLNFNEV 125
Cdd:PRK07757  49 EGEIVGCCALHILwEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVkrvFALTYQPE--------FFEKLGFREV 120


                 ....*...
gi 501020507 126 DvrKNYYP 133
Cdd:PRK07757 121 D--KEALP 126
PTZ00330 PTZ00330
acetyltransferase; Provisional
 70-122 6.14e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.90  E-value: 6.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501020507  70 NITVHPDFQGQKLGHMLLNALIEQLRKKGILSLWLEVRESnrhAIKLYEKLNF 122
Cdd:PTZ00330  87 DVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTED---MVAFYKKLGF 136
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 83-131 1.22e-03

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: 36.95  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 501020507   83 GHMLLNALIEQ-LRKKGILSLWLEVRESNRHAIKLYEKLNFNEVDVRKNY 131
Cdd:TIGR03585  93 GSVLEEAALEYaFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG 142
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 47-122 2.38e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 36.87  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501020507   47 ILLDDQIV----------GFAICQIvldeATlfnitvHPDFQGQKLGHMLLNALIEQLRKKGILSLWlevRESNRHAIKL 116
Cdd:pfam12746 158 ILKDGEIVsgassysvyeGGIEIEI----DT------HPDYRGKGLATICAAALILECLKRGLYPSW---DAHNEASVAL 224


                  ....*.
gi 501020507  117 YEKLNF 122
Cdd:pfam12746 225 AEKLGY 230
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 72-102 2.76e-03

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 36.67  E-value: 2.76e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 501020507  72 TVHPDFQGQKLGHMLLNALIEQLRKKGILSL 102
Cdd:PRK05279 366 AVHPDYRGSGRGERLLKRIEQRARQLGLKRL 396
 
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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