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Conserved domains on  [gi|16764847|ref|NP_460462|]
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spermidine N1-acetyltransferase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

spermidine N1-acetyltransferase( domain architecture ID 10014985)

spermidine N1-acetyltransferase which catalyzes the transfer of acetyl groups from acetyl-CoA to spermidine, similar to Escherichia coli SpeG; it is a key enzyme in controlling polyamine levels in prokaryotic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 2.39e-140

spermidine N1-acetyltransferase; Provisional


:

Pssm-ID: 237916  Cd Length: 186  Bit Score: 388.39  E-value: 2.39e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    1 MTSDYKVRLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   81 HRRAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 16764847  161 RMCIFQQQYLDEHKTSGSTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 2.39e-140

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 388.39  E-value: 2.39e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    1 MTSDYKVRLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   81 HRRAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 16764847  161 RMCIFQQQYLDEHKTSGSTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-168 2.88e-43

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: 142.06  E-value: 2.88e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   7 VRLRPLEREDLRFVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVVE--CDGENAGLVELVEINHVHR 82
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847  83 RAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTIRM 162
Cdd:COG1670  88 SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167


                ....*.
gi 16764847 163 CIFQQQ 168
Cdd:COG1670 168 SLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-141 3.32e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.72  E-value: 3.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847     7 VRLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVVECDGENA-GLVELVEINHVHR 82
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16764847    83 RAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFR 141
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-146 2.27e-05

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: 42.32  E-value: 2.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16764847    86 FQIIISPEYQGKGLASRAAKLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFRVEGEL 146
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIR 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 7.28e-05

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: 39.18  E-value: 7.28e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16764847  60 FVVECDGENAGLVELVEINHVHRRAEFQ-IIISPEYQGKGLASRAAKLAMDY 110
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 2.39e-140

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 388.39  E-value: 2.39e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    1 MTSDYKVRLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   81 HRRAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 16764847  161 RMCIFQQQYLDEHKTSGSTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-168 2.88e-43

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: 142.06  E-value: 2.88e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   7 VRLRPLEREDLRFVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVVE--CDGENAGLVELVEINHVHR 82
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847  83 RAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTIRM 162
Cdd:COG1670  88 SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167


                ....*.
gi 16764847 163 CIFQQQ 168
Cdd:COG1670 168 SLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-141 3.32e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.72  E-value: 3.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847     7 VRLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVVECDGENA-GLVELVEINHVHR 82
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16764847    83 RAEFQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFR 141
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-140 6.90e-18

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: 75.25  E-value: 6.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    32 YWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHVHRRAE-FQIIISPEYQGKGLASRAAKLAMDY 110
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEiEGLAVAPEYRGKGIGTALLQALLEW 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 16764847   111 GFTvLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam00583  88 ARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-162 8.40e-18

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: 8.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   7 VRLRPLEREDLRFVHQLDNNA---SVMRYWFEEPYEAFVELsdlYDKHIHDQSERRFVVECDGENAGLVELV---EINHV 80
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEAiaeGTATFETEPPSEEEREA---WFAAILAPGRPVLVAEEDGEVVGFASLGpfrPRPAY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847  81 HRRAEFQIIISPEYQGKGLAS----RAAKLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEY 156
Cdd:COG1247  79 RGTAEESIYVDPDARGRGIGRalleALIERARARGYR-----RLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRW 153


                ....*.
gi 16764847 157 RNTIRM 162
Cdd:COG1247 154 LDLVLM 159
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-142 2.94e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 54.38  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    60 FVVECDGENAGLVELVEINHVHRRAEFQIIISPEYQGKGLASRaakLaMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLG 139
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRA---L-LEAAEAAAKEGGIKLLELETTNRAAAFYEKLG 81


                  ...
gi 16764847   140 FRV 142
Cdd:pfam13508  82 FEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-148 3.99e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 3.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847  74 LVEINHVHRRAE-FQIIISPEYQGKGLASR----AAKLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFRVEGELIH 148
Cdd:COG0456   4 LLGLVDGGDEAEiEDLAVDPEYRGRGIGRAlleaALERARERGAR-----RLRLEVREDNEAAIALYEKLGFEEVGERPN 78
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
92-151 9.71e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.99  E-value: 9.71e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16764847  92 PEYQGKGLASR----AAKLAMDYGFTVLnlyklYLIVDKENEKAIHIYRKLGFRVEGELIHEFF 151
Cdd:COG3393  25 PEYRGRGLASAlvaaLAREALARGARTP-----FLYVDADNPAARRLYERLGFRPVGEYATVLF 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-142 9.06e-08

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: 48.83  E-value: 9.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   7 VRLRPLEREDLRFVHQLdnnasVMRYWFEEPYEAFvelsdlydkhihdqserrFVVECDGENAGLVELVEINHvhRRAEF 86
Cdd:COG1246   1 MTIRPATPDDVPAILEL-----IRPYALEEEIGEF------------------WVAEEDGEIVGCAALHPLDE--DLAEL 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16764847  87 Q-IIISPEYQGKGLASR----AAKLAMDYGFTvlnlyKLYLIVdkeNEKAIHIYRKLGFRV 142
Cdd:COG1246  56 RsLAVHPDYRGRGIGRRlleaLLAEARELGLK-----RLFLLT---TSAAIHFYEKLGFEE 108
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-151 9.99e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 9.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   9 LRPLEREDLRFVHQLDNNAsvmrywFEEPYEAfvELSDLYDKHIHDqsERRFVVECDGENAGLVELVEINHVHRRAEFQI 88
Cdd:COG3153   1 IRPATPEDAEAIAALLRAA------FGPGREA--ELVDRLREDPAA--GLSLVAEDDGEIVGHVALSPVDIDGEGPALLL 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16764847  89 ---IISPEYQGKGLASRAAKLAMDYgFTVLNLYKLYLIVDkenEKAIHIYRKLGFRVEGELIHEFF 151
Cdd:COG3153  71 gplAVDPEYRGQGIGRALMRAALEA-ARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
PRK10140 PRK10140
N-acetyltransferase;
9-162 1.19e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 46.13  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    9 LRPLEREDLRFVHQLDNNASVMRYWFEEPYEAfvelSDLYDKHIHDQSERRFVVEC-DGENAGLVELVEINHVHRR--AE 85
Cdd:PRK10140   6 IRHAETRDYEAIRQIHAQPEVYHNTLQVPHPS----DHMWQERLADRPGIKQLVACiDGDVVGHLTIDVQQRPRRShvAD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16764847   86 FQIIISPEYQGKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEYRNTIRM 162
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-154 2.18e-05

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: 42.26  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    35 EEPYEAFVE--LSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHVHRraefqIIISPEYQGKGLASRAAKLAMDYGF 112
Cdd:pfam13673   7 EEGIETFYEfiSPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16764847   113 TvLNLYKLYLIVDKENEkAIHIYRKLGFRVEGElihEFFING 154
Cdd:pfam13673  82 K-DGIKLSELTVNASPY-AVPFYEKLGFRATGP---EQEFNG 118
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-146 2.27e-05

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: 42.32  E-value: 2.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16764847    86 FQIIISPEYQGKGLASRAAKLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFRVEGEL 146
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIR 117
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 60-146 2.97e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 41.96  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847  60 FVVECDGENAGLVELVEINHVHrrAEF-QIIISPEYQGKGLASR----AAKLAMDYGFTVLnlyklYLIVDKENEKAIHI 134
Cdd:COG0454  37 IAVDDKGEPIGFAGLRRLDDKV--LELkRLYVLPEYRGKGIGKAlleaLLEWARERGCTAL-----ELDTLDGNPAAIRF 109

                        90
                ....*....|..
gi 16764847 135 YRKLGFRVEGEL 146
Cdd:COG0454 110 YERLGFKEIERY 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 7.28e-05

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: 39.18  E-value: 7.28e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16764847  60 FVVECDGENAGLVELVEINHVHRRAEFQ-IIISPEYQGKGLASRAAKLAMDY 110
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
PRK10562 PRK10562
putative acetyltransferase; Provisional
 9-149 5.00e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.51  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847    9 LRPLEREDLrfvhqldnnASVMRYWFEEPYEA--FVELSDLYD-----KHIHDQSERRFVVECDGENAGLVELVEINHVH 81
Cdd:PRK10562   2 IREYQPSDL---------PAILQLWLESTIWAhpFIKEQYWREsaplvRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVG 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16764847   82 rrAEFqiiISPEYQGKGLAsraaKLAMDYgftVLNLYK-LYLIVDKENEKAIHIYRKLGFRVEGELIHE 149
Cdd:PRK10562  73 --ALF---VAPKAVRRGIG----KALMQH---VQQRYPhLSLEVYQKNQRAVNFYHAQGFRIVDSAWQE 129
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-143 4.10e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.06  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847   60 FVVECDGENAGLVeLVEINHvHRRAEFQIIISPEYQGKGLAsRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLG 139
Cdd:PRK03624  48 LVAEVGGEVVGTV-MGGYDG-HRGWAYYLAVHPDFRGRGIG-RALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALG 124


                 ....
gi 16764847  140 FRVE 143
Cdd:PRK03624 125 YEEQ 128
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
52-110 4.25e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 34.75  E-value: 4.25e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16764847  52 IHDQSERRFVVECDGENAGLVE------LVEINHVhrraefqiIISPEYQGKGLASRAAKLAMDY 110
Cdd:COG2388   4 THNEEKGRFELEVDGELAGELTyrleggVIIITHT--------EVPPALRGQGIASALVEAALDD 60
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 81-145 7.93e-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: 35.71  E-value: 7.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16764847    81 HRRAEFQIIISPEYQGKGLASR-AAKL---AMDYGftvlnlykLYLIVDKENEKAIHIYRKLGFRVEGE 145
Cdd:pfam12746 175 EGGIEIEIDTHPDYRGKGLATIcAAALileCLKRG--------LYPSWDAHNEASVALAEKLGYEFVKE 235
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
9-156 9.09e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 35.04  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16764847     9 LRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGENAGLVELVEINHVHRRA---E 85
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLSPGEIVFGVAESDRLIGYATLRQFDYVKTHKaelS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16764847    86 FQIIISPEyqgKGLASRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFRVEGELIHEFFINGEY 156
Cdd:pfam13420  81 FYVVKNND---EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRW 148
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 92-142 9.88e-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: 33.84  E-value: 9.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16764847    92 PEYQGKGLASRAAKlAMDYGFTVLNlYKLYLIVDKENEKAIHIYRKLGFRV 142
Cdd:pfam08445  31 PEHRRRGLGSRLVA-ALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFRK 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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