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Conserved domains on  [gi|495778029|ref|WP_008502608|]
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MULTISPECIES: elongation factor P hydroxylase [Enterobacter]

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 7.62e-132

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


:

Pssm-ID: 442335  Cd Length: 180  Bit Score: 366.45  E-value: 7.62e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   4 THKYEQLIEIFDGCFADDFNTRLIKGDDEPIYLPADDEVPYNRIVFAHGFYASGLHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101    2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029  84 DGRDAATQGQFEDVEVKPQALEWLFCVAAGFPFNVSCDNLEGDFEPDRIVFQRRVHAQVMEYLEKGIPARPARLIEALQN 163
Cdd:COG3101   82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                        170
                 ....*....|....*....
gi 495778029 164 YYHTPA-IAAESFPWPEDL 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 7.62e-132

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 366.45  E-value: 7.62e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   4 THKYEQLIEIFDGCFADDFNTRLIKGDDEPIYLPADDEVPYNRIVFAHGFYASGLHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101    2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029  84 DGRDAATQGQFEDVEVKPQALEWLFCVAAGFPFNVSCDNLEGDFEPDRIVFQRRVHAQVMEYLEKGIPARPARLIEALQN 163
Cdd:COG3101   82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                        170
                 ....*....|....*....
gi 495778029 164 YYHTPA-IAAESFPWPEDL 181
Cdd:COG3101  162 FYGTPLpLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
13-175 3.49e-118

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: 331.10  E-value: 3.49e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   13 IFDGCFADDFNTRLIKGDDEPIYLPADDEVPYNRIVFAHGFYASGLHEISHWCIAGKARRELVDFGYWYCPDGRDAATQG 92
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   93 QFEDVEVKPQALEWLFCVAAGFPFNVSCDNLEGdFEPDRIVFQRRVHAQVMEYLEKGIPARPARLIEALQNYYHTPAIAA 172
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 495778029  173 ESF 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 7.62e-132

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 366.45  E-value: 7.62e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   4 THKYEQLIEIFDGCFADDFNTRLIKGDDEPIYLPADDEVPYNRIVFAHGFYASGLHEISHWCIAGKARRELVDFGYWYCP 83
Cdd:COG3101    2 THQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYCP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029  84 DGRDAATQGQFEDVEVKPQALEWLFCVAAGFPFNVSCDNLEGDFEPDRIVFQRRVHAQVMEYLEKGIPARPARLIEALQN 163
Cdd:COG3101   82 DGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALAA 161
                        170
                 ....*....|....*....
gi 495778029 164 YYHTPA-IAAESFPWPEDL 181
Cdd:COG3101  162 FYGTPLpLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
13-175 3.49e-118

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: 331.10  E-value: 3.49e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   13 IFDGCFADDFNTRLIKGDDEPIYLPADDEVPYNRIVFAHGFYASGLHEISHWCIAGKARRELVDFGYWYCPDGRDAATQG 92
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778029   93 QFEDVEVKPQALEWLFCVAAGFPFNVSCDNLEGdFEPDRIVFQRRVHAQVMEYLEKGIPARPARLIEALQNYYHTPAIAA 172
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 495778029  173 ESF 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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