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Conserved domains on  [gi|16130261|ref|NP_416829|]
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EF-P-Lys34 hydroxylase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

elongation factor P hydroxylase( domain architecture ID 10006931)

elongation factor P hydroxylase is involved in the final hydroxylation step of the post-translational modification of translation elongation factor P (EF-P) on a conserved lysine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
4-181 1.78e-133

Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442335  Cd Length: 180  Bit Score: 370.69  E-value: 1.78e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261   4 THHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101   2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261  84 DGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQN 163
Cdd:COG3101  82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                       170
                ....*....|....*....
gi 16130261 164 YYHTP-ELTAEQFPWPEAL 181
Cdd:COG3101 162 FYGTPlPLTAADFPLPELL 180
 
Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
4-181 1.78e-133

Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442335  Cd Length: 180  Bit Score: 370.69  E-value: 1.78e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261   4 THHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101   2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261  84 DGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQN 163
Cdd:COG3101  82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                       170
                ....*....|....*....
gi 16130261 164 YYHTP-ELTAEQFPWPEAL 181
Cdd:COG3101 162 FYGTPlPLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
13-175 7.14e-121

Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor P modification pathway. It hydroxylates Lys-34 of elongation factor P. Members of this family have a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold.


Pssm-ID: 427860  Cd Length: 162  Bit Score: 338.03  E-value: 7.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261    13 IFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCPDGRDAQTQS 92
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261    93 QFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGdFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQNYYHTPELTA 172
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 16130261   173 EQF 175
Cdd:pfam04315 160 AQF 162
 
Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
4-181 1.78e-133

Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442335  Cd Length: 180  Bit Score: 370.69  E-value: 1.78e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261   4 THHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101   2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261  84 DGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQN 163
Cdd:COG3101  82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                       170
                ....*....|....*....
gi 16130261 164 YYHTP-ELTAEQFPWPEAL 181
Cdd:COG3101 162 FYGTPlPLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
13-175 7.14e-121

Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor P modification pathway. It hydroxylates Lys-34 of elongation factor P. Members of this family have a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold.


Pssm-ID: 427860  Cd Length: 162  Bit Score: 338.03  E-value: 7.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261    13 IFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCPDGRDAQTQS 92
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130261    93 QFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGdFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQNYYHTPELTA 172
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 16130261   173 EQF 175
Cdd:pfam04315 160 AQF 162
 
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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