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Conserved domains on  [gi|488992982|ref|WP_002903719|]
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MULTISPECIES: spermidine N1-acetyltransferase [Klebsiella]

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 6.33e-142

spermidine N1-acetyltransferase; Provisional


:

Pssm-ID: 237916  Cd Length: 186  Bit Score: 392.24  E-value: 6.33e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   1 MTDALHVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVIECNGDKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  81 HRRAEFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 488992982 161 RMCLFQHQYLAEHKTPGPSLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 6.33e-142

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 392.24  E-value: 6.33e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   1 MTDALHVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVIECNGDKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  81 HRRAEFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 488992982 161 RMCLFQHQYLAEHKTPGPSLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-164 5.07e-42

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: 138.98  E-value: 5.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   6 HVKLRPLEREDLRFVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVIECNGDKA--GLVELVEINHVH 81
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEDKEDGEliGVVGLYDIDRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  82 RRAEFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTIR 161
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ...
gi 488992982 162 MCL 164
Cdd:COG1670  167 YSL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-140 4.58e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.33  E-value: 4.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982    9 LRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVIECNGDKA-GLVELVEINHVHRRA 84
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488992982   85 EFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-146 3.12e-04

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: 38.85  E-value: 3.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488992982   86 FQIIISPDFQGKGLATRAARLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFMVEGEL 146
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIR 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 7.16e-04

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: 36.48  E-value: 7.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488992982  60 FVIECNGDKAGLVELVEINHVHRRAEFQ-IIISPDFQGKGLATRAARLAMDY 110
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 6.33e-142

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 392.24  E-value: 6.33e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   1 MTDALHVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVIECNGDKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  81 HRRAEFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 488992982 161 RMCLFQHQYLAEHKTPGPSLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-164 5.07e-42

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: 138.98  E-value: 5.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   6 HVKLRPLEREDLRFVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVIECNGDKA--GLVELVEINHVH 81
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEDKEDGEliGVVGLYDIDRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  82 RRAEFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTIR 161
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ...
gi 488992982 162 MCL 164
Cdd:COG1670  167 YSL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-140 4.58e-25

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.33  E-value: 4.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982    9 LRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVIECNGDKA-GLVELVEINHVHRRA 84
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488992982   85 EFQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-140 8.01e-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: 72.55  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   32 YWFEEPYEAFVELSDLYDKHIHDQSERRFVIECNGDKAGLVELVEINHVHRRAE-FQIIISPDFQGKGLATRAARLAMDY 110
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEiEGLAVAPEYRGKGIGTALLQALLEW 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 488992982  111 GFTvLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam00583  88 ARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-162 5.47e-15

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 68.87  E-value: 5.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   7 VKLRPLEREDLRFVHQLDNNA---SVMRYWFEEPYEAFVELsdlYDKHIHDQSERRFVIECNGDKAGLVELV---EINHV 80
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAiaeGTATFETEPPSEEEREA---WFAAILAPGRPVLVAEEDGEVVGFASLGpfrPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  81 HRRAEFQIIISPDFQGKGLAT----RAARLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEY 156
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRalleALIERARARGYR-----RLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRW 153


                 ....*.
gi 488992982 157 RNTIRM 162
Cdd:COG1247  154 LDLVLM 159
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-148 5.86e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 51.19  E-value: 5.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  74 LVEINHVHRRAE-FQIIISPDFQGKGLATR----AARLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFMVEGELIH 148
Cdd:COG0456    4 LLGLVDGGDEAEiEDLAVDPEYRGRGIGRAlleaALERARERGAR-----RLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-140 6.51e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 6.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   60 FVIECNGDKAGLVELVEINHVHRRAEFQIIISPDFQGKGLATraaRLaMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLG 139
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGR---AL-LEAAEAAAKEGGIKLLELETTNRAAAFYEKLG 81


                  .
gi 488992982  140 F 140
Cdd:pfam13508  82 F 82
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
92-151 3.03e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 3.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488992982  92 PDFQGKGLATR----AARLAMDYGFTVLnlyklYLIVDKENEKAIHIYRKLGFMVEGELIHEFF 151
Cdd:COG3393   25 PEYRGRGLASAlvaaLAREALARGARTP-----FLYVDADNPAARRLYERLGFRPVGEYATVLF 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-151 4.03e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 44.31  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   9 LRPLEREDLRFVHQLDNNAsvmrywFEEPYEAfvELSDLYDKHIHDqsERRFVIECNGDKAGLVELVEINHVHRRAEFQI 88
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA------FGPGREA--ELVDRLREDPAA--GLSLVAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488992982  89 ---IISPDFQGKGLATRAARLAMDYgFTVLNLYKLYLIVDkenEKAIHIYRKLGFMVEGELIHEFF 151
Cdd:COG3153   71 gplAVDPEYRGQGIGRALMRAALEA-ARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-164 1.08e-05

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: 43.06  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   7 VKLRPLEREDLRFVHQLdnnasVMRYWFEEPYEAFvelsdlydkhihdqserrFVIECNGDKAGLVELVEINHvhRRAEF 86
Cdd:COG1246    1 MTIRPATPDDVPAILEL-----IRPYALEEEIGEF------------------WVAEEDGEIVGCAALHPLDE--DLAEL 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982  87 Q-IIISPDFQGKGLATR----AARLAMDYGFTvlnlyKLYLIVdkeNEKAIHIYRKLGFmVEGELIHEFFINGEYRNTIR 161
Cdd:COG1246   56 RsLAVHPDYRGRGIGRRlleaLLAEARELGLK-----RLFLLT---TSAAIHFYEKLGF-EEIDKEDLPYAKVWQRDSVV 126


                 ...
gi 488992982 162 MCL 164
Cdd:COG1246  127 MEK 129
PRK10140 PRK10140
N-acetyltransferase;
9-162 1.48e-05

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 43.43  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   9 LRPLEREDLRFVHQLDNNASVMRYWFEEPYEAfvelSDLYDKHIHDQSERRFVIEC-NGDKAGLVELVEINHVHRR--AE 85
Cdd:PRK10140   6 IRHAETRDYEAIRQIHAQPEVYHNTLQVPHPS----DHMWQERLADRPGIKQLVACiDGDVVGHLTIDVQQRPRRShvAD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488992982  86 FQIIISPDFQGKGLATRAARLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVEGELIHEFFINGEYRNTIRM 162
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-146 3.12e-04

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: 38.85  E-value: 3.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488992982   86 FQIIISPDFQGKGLATRAARLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFMVEGEL 146
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIR 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 7.16e-04

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: 36.48  E-value: 7.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488992982  60 FVIECNGDKAGLVELVEINHVHRRAEFQ-IIISPDFQGKGLATRAARLAMDY 110
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-154 4.21e-03

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: 35.71  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488992982   35 EEPYEAFVE--LSDLYDKHIHDQSERRFVIECNGDKAGLVELVEINHVHRraefqIIISPDFQGKGLATR----AARLAM 108
Cdd:pfam13673   7 EEGIETFYEfiSPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKAlleaVEDYAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488992982  109 DYGFTvlnlyKLYLIVDKENEkAIHIYRKLGFMVEGElihEFFING 154
Cdd:pfam13673  82 KDGIK-----LSELTVNASPY-AVPFYEKLGFRATGP---EQEFNG 118
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 87-140 5.84e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 35.41  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488992982  87 QIIISPDFQGKGLATR----AARLAMDYGFTVLnlyklYLIVDKENEKAIHIYRKLGF 140
Cdd:COG0454   63 RLYVLPEYRGKGIGKAlleaLLEWARERGCTAL-----ELDTLDGNPAAIRFYERLGF 115
PRK03624 PRK03624
putative acetyltransferase; Provisional
 81-143 7.13e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 35.29  E-value: 7.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488992982  81 HRRAEFQIIISPDFQGKGLATRAARLAMDYgFTVLNLYKLYLIVDKENEKAIHIYRKLGFMVE 143
Cdd:PRK03624  67 HRGWAYYLAVHPDFRGRGIGRALVARLEKK-LIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 86-140 8.28e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 35.29  E-value: 8.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488992982  86 FQIIISPDFQGKGLatraARLAMDYGFTVL---NLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:PRK09491  67 FNIAVDPDYQRQGL----GRALLEHLIDELekrGVATLWLEVRASNAAAIALYESLGF 120
 
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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