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Conserved domains on  [gi|727170777|ref|WP_033638511|]
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MULTISPECIES: ribosomal protein S5-alanine N-acetyltransferase [Serratia]

Protein Classification

ribosomal protein S5-alanine N-acetyltransferase( domain architecture ID 10013654)

ribosomal protein S5-alanine N-acetyltransferase acetylates the N-terminal alanine of ribosomal protein S5; also plays a role in maturation of the 30S ribosomal subunit as well as in the temperature regulation of pap pilin transcription

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
1-194 1.81e-155

30S ribosomal protein S5 alanine N-acetyltransferase;


:

Pssm-ID: 182749  Cd Length: 194  Bit Score: 427.23  E-value: 1.81e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   1 MFGYRSASPKVRLTTDRMVVRLVNERDAYRLADYYAENRAFLKPWEPVRDESHCYPSGWQARLGMITEMQKQGSAYYFIL 80
Cdd:PRK10809   1 MFGYRSNVPKVRLTTDRLVVRLVHERDAWRLADYYAENRHFLKPWEPVRDESHCYPSGWQARLGMINEFHKQGSAFYFAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  81 LDPEEQEVRGVANFSNVLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLG 160
Cdd:PRK10809  81 LDPDEKEIIGVANFSNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLG 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 727170777 161 FEREGYAKDYLLIDGQWQDHVLTAYTNKEWLPPR 194
Cdd:PRK10809 161 FEKEGYAKDYLLIDGQWRDHVLTALTTPEWTPGR 194
 
Name Accession Description Interval E-value
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
1-194 1.81e-155

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 427.23  E-value: 1.81e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   1 MFGYRSASPKVRLTTDRMVVRLVNERDAYRLADYYAENRAFLKPWEPVRDESHCYPSGWQARLGMITEMQKQGSAYYFIL 80
Cdd:PRK10809   1 MFGYRSNVPKVRLTTDRLVVRLVHERDAWRLADYYAENRHFLKPWEPVRDESHCYPSGWQARLGMINEFHKQGSAFYFAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  81 LDPEEQEVRGVANFSNVLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLG 160
Cdd:PRK10809  81 LDPDEKEIIGVANFSNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLG 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 727170777 161 FEREGYAKDYLLIDGQWQDHVLTAYTNKEWLPPR 194
Cdd:PRK10809 161 FEKEGYAKDYLLIDGQWRDHVLTALTTPEWTPGR 194
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-189 4.80e-41

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: 136.67  E-value: 4.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  11 VRLTTDRMVVRLVNERDAYRLADYYAeNRAFLKPWEPVRDEshcyPSGWQARLGMITEMQKQGSAYYFILLDPEEQEVRG 90
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLN-DPEVARYLPGPPYS----LEEARAWLERLLADWADGGALPFAIEDKEDGELIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  91 VANFSNVlRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLGFEREGYAKDY 170
Cdd:COG1670   76 VVGLYDI-DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
                        170
                 ....*....|....*....
gi 727170777 171 LLIDGQWQDHVLTAYTNKE 189
Cdd:COG1670  155 LVIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
17-162 3.27e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 82.01  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   17 RMVVRLVNERDAYRLADYYAENRA--FLKPWEPVRDESHcypsgwqARLGMITEMQKQGSAYYFILLDPEEQEVrGVANF 94
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVmrYGVPWPLTLEEAR-------EWLARIWAADEAERGYGWAIELKDTGFI-GSIGL 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727170777   95 SNvLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLGFE 162
Cdd:pfam13302  73 YD-IDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
1-194 1.81e-155

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 427.23  E-value: 1.81e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   1 MFGYRSASPKVRLTTDRMVVRLVNERDAYRLADYYAENRAFLKPWEPVRDESHCYPSGWQARLGMITEMQKQGSAYYFIL 80
Cdd:PRK10809   1 MFGYRSNVPKVRLTTDRLVVRLVHERDAWRLADYYAENRHFLKPWEPVRDESHCYPSGWQARLGMINEFHKQGSAFYFAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  81 LDPEEQEVRGVANFSNVLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLG 160
Cdd:PRK10809  81 LDPDEKEIIGVANFSNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLG 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 727170777 161 FEREGYAKDYLLIDGQWQDHVLTAYTNKEWLPPR 194
Cdd:PRK10809 161 FEKEGYAKDYLLIDGQWRDHVLTALTTPEWTPGR 194
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-189 4.80e-41

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: 136.67  E-value: 4.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  11 VRLTTDRMVVRLVNERDAYRLADYYAeNRAFLKPWEPVRDEshcyPSGWQARLGMITEMQKQGSAYYFILLDPEEQEVRG 90
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLN-DPEVARYLPGPPYS----LEEARAWLERLLADWADGGALPFAIEDKEDGELIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  91 VANFSNVlRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLGFEREGYAKDY 170
Cdd:COG1670   76 VVGLYDI-DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
                        170
                 ....*....|....*....
gi 727170777 171 LLIDGQWQDHVLTAYTNKE 189
Cdd:COG1670  155 LVIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
17-162 3.27e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 82.01  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   17 RMVVRLVNERDAYRLADYYAENRA--FLKPWEPVRDESHcypsgwqARLGMITEMQKQGSAYYFILLDPEEQEVrGVANF 94
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVmrYGVPWPLTLEEAR-------EWLARIWAADEAERGYGWAIELKDTGFI-GSIGL 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727170777   95 SNvLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLGFE 162
Cdd:pfam13302  73 YD-IDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
18-182 3.41e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.46  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  18 MVVRLVNERDAYRLADYYAE---NRAFLKPWEPVRDEShcypsgWQARLGmitemQKQGSAYYFILLDpEEQEVRGVANF 94
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEaiaEGTATFETEPPSEEE------REAWFA-----AILAPGRPVLVAE-EDGEVVGFASL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  95 SNV--LRGSFHACFLGYSLGEKWQGQGL---MFEALqsaIRYmLRQQRMHRIMANYMPHNQRSGALLTRLGFEREGYAKD 169
Cdd:COG1247   70 GPFrpRPAYRGTAEESIYVDPDARGRGIgraLLEAL---IER-ARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
                        170
                 ....*....|...
gi 727170777 170 YLLIDGQWQDHVL 182
Cdd:COG1247  146 VGFKFGRWLDLVL 158
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
45-161 3.35e-08

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: 49.82  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777   45 WEPVRDESHCYPSGWQARLGMITEMQKQGSAYYFILLDPEEQEVRGVANFSNVLRGSFHACFLGYSLGEKWQGQGLMFEA 124
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 727170777  125 LQSAIRYMlRQQRMHRIMANYMPHNQRSGALLTRLGF 161
Cdd:pfam00583  81 LQALLEWA-RERGCERIFLEVAADNLAAIALYEKLGF 116
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
77-179 1.81e-07

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 48.99  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170777  77 YFILLDpeeQEVRGVANFsNVLRGSFHACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALL 156
Cdd:PRK10151  70 FMIFKE---DELIGVLSF-NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVA 145
                         90       100
                 ....*....|....*....|...
gi 727170777 157 TRLGFEREGYAKDYLLIDGQWQD 179
Cdd:PRK10151 146 LRNGFTLEGCLKQAEYLNGAYDD 168
PRK10140 PRK10140
N-acetyltransferase;
103-179 8.03e-03

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 35.73  E-value: 8.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727170777 103 HACFLGYSLGEKWQGQGLMFEALQSAIRYMLRQQRMHRIMANYMPHNQRSGALLTRLGFEREGYAKDYLLIDGQWQD 179
Cdd:PRK10140  78 HVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVD 154
 
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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