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Conserved domains on  [gi|447061325|ref|WP_001138581|]
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MULTISPECIES: spermidine N1-acetyltransferase [Enterobacteriaceae]

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 4.72e-141

spermidine N1-acetyltransferase; Provisional


:

Pssm-ID: 237916  Cd Length: 186  Bit Score: 390.31  E-value: 4.72e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   1 MPSAHSVKLRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 447061325 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 4.72e-141

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 390.31  E-value: 4.72e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   1 MPSAHSVKLRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 447061325 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-164 2.12e-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: 139.75  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   7 VKLRPLEREDLRYVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVVE--CDGEKAGLVELVEINHVHR 82
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  83 RAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAIRM 162
Cdd:COG1670   88 SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167


                 ..
gi 447061325 163 CI 164
Cdd:COG1670  168 SL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-140 3.01e-24

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 92.41  E-value: 3.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325    9 LRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVVECDGEKA-GLVELVEINHVHRRA 84
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 447061325   85 EFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-162 3.15e-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: 41.93  E-value: 3.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447061325   86 FQIIISPEYQGKGLATRAAKLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHefFINGQYRNAIRM 162
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRN--YYPDPGEDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 4.38e-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: 39.95  E-value: 4.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447061325  60 FVVECDGEKAGLVELVEINHVHRRAEFQ-IIISPEYQGKGLATRAAKLAMDY 110
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-186 4.72e-141

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 390.31  E-value: 4.72e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   1 MPSAHSVKLRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80
Cdd:PRK15130   1 MPSAHSVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAI 160
Cdd:PRK15130  81 HRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160

                        170       180
                 ....*....|....*....|....*.
gi 447061325 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
Cdd:PRK15130 161 RMCIFQHQYLAEHKTPGQTLLKPTAQ 186
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-164 2.12e-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: 139.75  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   7 VKLRPLEREDLRYVHQLDNNASVMRYWFEEPY--EAFVELSDLYDKHIHDQSERRFVVE--CDGEKAGLVELVEINHVHR 82
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYslEEARAWLERLLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  83 RAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAIRM 162
Cdd:COG1670   88 SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167


                 ..
gi 447061325 163 CI 164
Cdd:COG1670  168 SL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-140 3.01e-24

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 92.41  E-value: 3.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325    9 LRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFvELSDLYDKHIHDQSERR---FVVECDGEKA-GLVELVEINHVHRRA 84
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERgygWAIELKDTGFiGSIGLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 447061325   85 EFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam13302  83 ELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-140 3.76e-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: 76.02  E-value: 3.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   32 YWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAE-FQIIISPEYQGKGLATRAAKLAMDY 110
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEiEGLAVAPEYRGKGIGTALLQALLEW 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 447061325  111 GFTvLNLYKLYLIVDKENEKAIHIYRKLGF 140
Cdd:pfam00583  88 ARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
6-162 1.91e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 72.72  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   6 SVKLRPLEREDLRYVHQLDNNA---SVMRYWFEEPYEAFVELsdlYDKHIHDQSERRFVVECDGEKAGLVELV---EINH 79
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAiaeGTATFETEPPSEEEREA---WFAAILAPGRPVLVAEEDGEVVGFASLGpfrPRPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  80 VHRRAEFQIIISPEYQGKGLAT----RAAKLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQ 155
Cdd:COG1247   78 YRGTAEESIYVDPDARGRGIGRalleALIERARARGYR-----RLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGR 152


                 ....*..
gi 447061325 156 YRNAIRM 162
Cdd:COG1247  153 WLDLVLM 159
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-142 6.11e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.61  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   60 FVVECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRaakLaMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLG 139
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRA---L-LEAAEAAAKEGGIKLLELETTNRAAAFYEKLG 81


                  ...
gi 447061325  140 FSV 142
Cdd:pfam13508  82 FEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-148 8.72e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 53.12  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  74 LVEINHVHRRAE-FQIIISPEYQGKGLATR----AAKLAMDYGFTvlnlyKLYLIVDKENEKAIHIYRKLGFSVEGELMH 148
Cdd:COG0456    4 LLGLVDGGDEAEiEDLAVDPEYRGRGIGRAlleaALERARERGAR-----RLRLEVREDNEAAIALYEKLGFEEVGERPN 78
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
92-151 3.46e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.45  E-value: 3.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447061325  92 PEYQGKGLATR----AAKLAMDYGFTVLnlyklYLIVDKENEKAIHIYRKLGFSVEGELMHEFF 151
Cdd:COG3393   25 PEYRGRGLASAlvaaLAREALARGARTP-----FLYVDADNPAARRLYERLGFRPVGEYATVLF 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-142 1.11e-07

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: 48.45  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   7 VKLRPLEREDLRYVHQLdnnasVMRYWFEEPYEAFvelsdlydkhihdqserrFVVECDGEKAGLVELVEINHvhRRAEF 86
Cdd:COG1246    1 MTIRPATPDDVPAILEL-----IRPYALEEEIGEF------------------WVAEEDGEIVGCAALHPLDE--DLAEL 55

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447061325  87 Q-IIISPEYQGKGLATR----AAKLAMDYGFTvlnlyKLYLIVdkeNEKAIHIYRKLGFSV 142
Cdd:COG1246   56 RsLAVHPDYRGRGIGRRlleaLLAEARELGLK-----RLFLLT---TSAAIHFYEKLGFEE 108
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-151 4.79e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.00  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   9 LRPLEREDLRYVHQLDNNAsvmrywFEEPYEAfvELSDLYDKHIHDqsERRFVVECDGEKAGLVELVEINHVHRRAEFQI 88
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA------FGPGREA--ELVDRLREDPAA--GLSLVAEDDGEIVGHVALSPVDIDGEGPALLL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447061325  89 ---IISPEYQGKGLATRAAKLAMDYgFTVLNLYKLYLIVDkenEKAIHIYRKLGFSVEGELMHEFF 151
Cdd:COG3153   71 gplAVDPEYRGQGIGRALMRAALEA-ARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTLG 132
PRK10140 PRK10140
N-acetyltransferase;
9-162 1.56e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 46.13  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   9 LRPLEREDLRYVHQLDNNASVMRYWFEEPYEAfvelSDLYDKHIHDQSERRFVVEC-DGEKAGLVELVEINHVHRR--AE 85
Cdd:PRK10140   6 IRHAETRDYEAIRQIHAQPEVYHNTLQVPHPS----DHMWQERLADRPGIKQLVACiDGDVVGHLTIDVQQRPRRShvAD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447061325  86 FQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAIRM 162
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-162 3.15e-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: 41.93  E-value: 3.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447061325   86 FQIIISPEYQGKGLATRAAKLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHefFINGQYRNAIRM 162
Cdd:TIGR01575  58 LNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRN--YYPDPGEDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-110 4.38e-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: 39.95  E-value: 4.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447061325  60 FVVECDGEKAGLVELVEINHVHRRAEFQ-IIISPEYQGKGLATRAAKLAMDY 110
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEE 53
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-162 5.64e-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: 41.10  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325   35 EEPYEAFVE--LSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRraefqIIISPEYQGKGLATRAAKLAMDYGF 112
Cdd:pfam13673   7 EEGIETFYEfiSPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYAE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 447061325  113 TvLNLYKLYLIVDKENEkAIHIYRKLGFSVEGELmheffingQYRNAIRM 162
Cdd:pfam13673  82 K-DGIKLSELTVNASPY-AVPFYEKLGFRATGPE--------QEFNGIRF 121
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 60-146 8.11e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.81  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  60 FVVECDGEKAGLVELVEINHVHrrAEF-QIIISPEYQGKGLATR----AAKLAMDYGFTVLnlyklYLIVDKENEKAIHI 134
Cdd:COG0454   37 IAVDDKGEPIGFAGLRRLDDKV--LELkRLYVLPEYRGKGIGKAlleaLLEWARERGCTAL-----ELDTLDGNPAAIRF 109

                         90
                 ....*....|..
gi 447061325 135 YRKLGFSVEGEL 146
Cdd:COG0454  110 YERLGFKEIERY 121
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
52-110 2.20e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 35.90  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447061325  52 IHDQSERRFVVECDGEKAGLVE------LVEINHVhrraefqiIISPEYQGKGLATRAAKLAMDY 110
Cdd:COG2388    4 THNEEKGRFELEVDGELAGELTyrleggVIIITHT--------EVPPALRGQGIASALVEAALDD 60
PRK10562 PRK10562
putative acetyltransferase; Provisional
 58-149 6.83e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.43  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  58 RRFVVECDGEKAGLVELVEINHVHrrAEFqiiISPEYQGKGLAtraaKLAMDYgftVLNLYK-LYLIVDKENEKAIHIYR 136
Cdd:PRK10562  49 QTWVWEEDGKLLGFVSVLEGRFVG--ALF---VAPKAVRRGIG----KALMQH---VQQRYPhLSLEVYQKNQRAVNFYH 116

                         90
                 ....*....|...
gi 447061325 137 KLGFSVEGELMHE 149
Cdd:PRK10562 117 AQGFRIVDSAWQE 129
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-143 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447061325  60 FVVECDGEKAGLVeLVEINHvHRRAEFQIIISPEYQGKGLATRAAKLAMDYgFTVLNLYKLYLIVDKENEKAIHIYRKLG 139
Cdd:PRK03624  48 LVAEVGGEVVGTV-MGGYDG-HRGWAYYLAVHPDFRGRGIGRALVARLEKK-LIARGCPKINLQVREDNDAVLGFYEALG 124


                 ....
gi 447061325 140 FSVE 143
Cdd:PRK03624 125 YEEQ 128
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 81-145 9.83e-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: 9.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447061325   81 HRRAEFQIIISPEYQGKGLATR-AAKL---AMDYGftvlnlykLYLIVDKENEKAIHIYRKLGFSVEGE 145
Cdd:pfam12746 175 EGGIEIEIDTHPDYRGKGLATIcAAALileCLKRG--------LYPSWDAHNEASVALAEKLGYEFVKE 235
 
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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