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Conserved domains on  [gi|446151443|ref|WP_000229298|]
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MULTISPECIES: 50S ribosomal protein L7/L12-serine acetyltransferase [Salmonella]

Protein Classification

50S ribosomal protein L7/L12-serine acetyltransferase( domain architecture ID 10013440)

50S ribosomal protein L7/L12-serine acetyltransferase which acetylates the N-terminal serine of ribosomal protein L7/L12, similar to Escherichia coli RimL

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.08e-131

50S ribosomal protein L7/L12-serine acetyltransferase;


:

Pssm-ID: 182270  Cd Length: 179  Bit Score: 366.01  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   1 MVEIIPVSTTLELQAADESHVPALHQLVLKNKAWLQQSLDWPQYVTSQEETRKHVQGNMLLHQRGYAKMYLIFCQNEMAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  81 VLSFNVIEPVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160
                        170
                 ....*....|....*....
gi 446151443 161 YLNGDYHDVNMYARIIDAD 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.08e-131

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 366.01  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   1 MVEIIPVSTTLELQAADESHVPALHQLVLKNKAWLQQSLDWPQYVTSQEETRKHVQGNMLLHQRGYAKMYLIFCQNEMAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  81 VLSFNVIEPVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160
                        170
                 ....*....|....*....
gi 446151443 161 YLNGDYHDVNMYARIIDAD 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-177 3.18e-36

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: 123.96  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  11 LELQAADESHVPALHQLvLKNKAWLQQsldWPQYVTSQEETRKHVQGNMLLHQRGYAKMYLIFCQ--NEMAGVLSFNVIE 88
Cdd:COG1670    8 LRLRPLRPEDAEALAEL-LNDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYDID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  89 PVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAEYLNGDYHD 168
Cdd:COG1670   84 RANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163

                 ....*....
gi 446151443 169 VNMYARIID 177
Cdd:COG1670  164 HVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-151 2.67e-18

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 76.62  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   11 LELQAADESHVPALHQLvLKNKAWLQQSLDWPqyvTSQEETRKHVQGNMLLHQRGYAKMYLIFCQNE-MAGVLSFNVIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFEL-LSDPEVMRYGVPWP---LTLEEAREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446151443   90 VNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFT 151
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
68-169 4.23e-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: 36.18  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   68 KMYLIFCQ-NEMAGVLSFNVIEPVNKAAYIGYWLDESLQ---GQGIMSQSLQALMTHYARRGdirrfvIKCRV--DNQAS 141
Cdd:TIGR03585  51 RRYWIVCQeSRPIGVISFTDINLVHKSAFWGIYANPFCKpgvGSVLEEAALEYAFEHLGLHK------LSLEVleSNNKA 124
                          90       100
                  ....*....|....*....|....*...
gi 446151443  142 NAVARRNHFTLEGCMKQaeylNGDYHDV 169
Cdd:TIGR03585 125 LKLYEKFGFEREGVFRQ----GGEYYDV 148
 
Name Accession Description Interval E-value
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
1-179 1.08e-131

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 366.01  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   1 MVEIIPVSTTLELQAADESHVPALHQLVLKNKAWLQQSLDWPQYVTSQEETRKHVQGNMLLHQRGYAKMYLIFCQNEMAG 80
Cdd:PRK10151   1 MTEIIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  81 VLSFNVIEPVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAE 160
Cdd:PRK10151  81 VLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAE 160
                        170
                 ....*....|....*....
gi 446151443 161 YLNGDYHDVNMYARIIDAD 179
Cdd:PRK10151 161 YLNGAYDDVNLYARIIDSD 179
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-177 3.18e-36

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: 123.96  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  11 LELQAADESHVPALHQLvLKNKAWLQQsldWPQYVTSQEETRKHVQGNMLLHQRGYAKMYLIFCQ--NEMAGVLSFNVIE 88
Cdd:COG1670    8 LRLRPLRPEDAEALAEL-LNDPEVARY---LPGPPYSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYDID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  89 PVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAEYLNGDYHD 168
Cdd:COG1670   84 RANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163

                 ....*....
gi 446151443 169 VNMYARIID 177
Cdd:COG1670  164 HVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-151 2.67e-18

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 76.62  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   11 LELQAADESHVPALHQLvLKNKAWLQQSLDWPqyvTSQEETRKHVQGNMLLHQRGYAKMYLIFCQNE-MAGVLSFNVIEP 89
Cdd:pfam13302   2 LLLRPLTEEDAEALFEL-LSDPEVMRYGVPWP---LTLEEAREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446151443   90 VNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVDNQASNAVARRNHFT 151
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
70-150 3.06e-09

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: 52.13  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   70 YLIFCQNEMAGVLSFNVIEPVNKAAYI-GYWLDESLQGQGIMSQSLQALMtHYARRGDIRRFVIKCRVDNQASNAVARRN 148
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALL-EWARERGCERIFLEVAADNLAAIALYEKL 114

                  ..
gi 446151443  149 HF 150
Cdd:pfam00583 115 GF 116
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
61-168 1.33e-08

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 52.05  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  61 LHQRGYAKMYLIFC--QNEMAGVLSF-NVIEPVNKAAYIGYWLDESLQGQGIMSQSLQALMTHYARRGDIRRFVIKCRVD 137
Cdd:PRK10809  69 FHKQGSAFYFALLDpdEKEIIGVANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPH 148
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446151443 138 NQASNAVARRNHFTLEGCMKQAEYLNGDYHD 168
Cdd:PRK10809 149 NKRSGDLLARLGFEKEGYAKDYLLIDGQWRD 179
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
16-176 2.09e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.07  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  16 ADESHVPALHQLVlkNKAWLQQSLDWPQYVTSQEETRKHVQGnmlLHQRGYAkmYLIFCQN-EMAGVLSFNVIEPVNKAA 94
Cdd:COG1247    7 ATPEDAPAIAAIY--NEAIAEGTATFETEPPSEEEREAWFAA---ILAPGRP--VLVAEEDgEVVGFASLGPFRPRPAYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443  95 YIGYW---LDESLQGQGIMSQSLQALMTHyARRGDIRRFVIKCRVDNQASNAVARRNHFTLEGCMKQAEYLNGDYHDVNM 171
Cdd:COG1247   80 GTAEEsiyVDPDARGRGIGRALLEALIER-ARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158

                 ....*
gi 446151443 172 YARII 176
Cdd:COG1247  159 MQKRL 163
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
68-169 4.23e-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: 36.18  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446151443   68 KMYLIFCQ-NEMAGVLSFNVIEPVNKAAYIGYWLDESLQ---GQGIMSQSLQALMTHYARRGdirrfvIKCRV--DNQAS 141
Cdd:TIGR03585  51 RRYWIVCQeSRPIGVISFTDINLVHKSAFWGIYANPFCKpgvGSVLEEAALEYAFEHLGLHK------LSLEVleSNNKA 124
                          90       100
                  ....*....|....*....|....*...
gi 446151443  142 NAVARRNHFTLEGCMKQaeylNGDYHDV 169
Cdd:TIGR03585 125 LKLYEKFGFEREGVFRQ----GGEYYDV 148
 
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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