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Conserved domains on  [gi|1633185482|gb|TKG55700|]
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elongation factor P hydroxylase [Vibrio tasmaniensis]

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 ...
1-173 1.14e-116

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


:

Pssm-ID: 442335  Cd Length: 180  Bit Score: 327.93  E-value: 1.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482   1 MTHEYPDIIDIFNQTFFESFNTKLELGADEPIYLPADEEIPHHRIVFARGFYASALHEIAHWCVAGPERRLLEDFGYWYE 80
Cdd:COG3101     1 MTHQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  81 PDGRTESVQAEFEKVEIRPQAYEWIIATSAGFPFNVSCDNLHGDFEPDRLAFMNKVHSEVMGIFEAGLPPRVKMLSEALR 160
Cdd:COG3101    81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALA 160
                         170
                  ....*....|....
gi 1633185482 161 SFYDVE-PLCTSQF 173
Cdd:COG3101   161 AFYGTPlPLTAADF 174
 
Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
1-173 1.14e-116

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 327.93  E-value: 1.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482   1 MTHEYPDIIDIFNQTFFESFNTKLELGADEPIYLPADEEIPHHRIVFARGFYASALHEIAHWCVAGPERRLLEDFGYWYE 80
Cdd:COG3101     1 MTHQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  81 PDGRTESVQAEFEKVEIRPQAYEWIIATSAGFPFNVSCDNLHGDFEPDRLAFMNKVHSEVMGIFEAGLPPRVKMLSEALR 160
Cdd:COG3101    81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALA 160
                         170
                  ....*....|....
gi 1633185482 161 SFYDVE-PLCTSQF 173
Cdd:COG3101   161 AFYGTPlPLTAADF 174
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
11-173 7.75e-110

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: 309.92  E-value: 7.75e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  11 IFNQTFFESFNTKLELGADEPIYLPADEEIPHHRIVFARGFYASALHEIAHWCVAGPERRLLEDFGYWYEPDGRTESVQA 90
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  91 EFEKVEIRPQAYEWIIATSAGFPFNVSCDNLHGdFEPDRLAFMNKVHSEVMGIFEAGLPPRVKMLSEALRSFYDVEPLCT 170
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 1633185482 171 SQF 173
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 ...
1-173 1.14e-116

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 327.93  E-value: 1.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482   1 MTHEYPDIIDIFNQTFFESFNTKLELGADEPIYLPADEEIPHHRIVFARGFYASALHEIAHWCVAGPERRLLEDFGYWYE 80
Cdd:COG3101     1 MTHQYQDLIELFNQCFAESYNTRLVKGDDEPIYLPADEECPYHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  81 PDGRTESVQAEFEKVEIRPQAYEWIIATSAGFPFNVSCDNLHGDFEPDRLAFMNKVHSEVMGIFEAGLPPRVKMLSEALR 160
Cdd:COG3101    81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAEPDREAFKRAVHAQVLRYLEQGLPERAARFIQALA 160
                         170
                  ....*....|....
gi 1633185482 161 SFYDVE-PLCTSQF 173
Cdd:COG3101   161 AFYGTPlPLTAADF 174
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
11-173 7.75e-110

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: 309.92  E-value: 7.75e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  11 IFNQTFFESFNTKLELGADEPIYLPADEEIPHHRIVFARGFYASALHEIAHWCVAGPERRLLEDFGYWYEPDGRTESVQA 90
Cdd:pfam04315   1 LFNACFFESYNTRLVKGGDEPIYLPADDEVPYHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633185482  91 EFEKVEIRPQAYEWIIATSAGFPFNVSCDNLHGdFEPDRLAFMNKVHSEVMGIFEAGLPPRVKMLSEALRSFYDVEPLCT 170
Cdd:pfam04315  81 EFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNG-EEGDRQAFKRAVHAQVMRYLAQGLPARAARFIQALQAFYGTPPLTA 159

                  ...
gi 1633185482 171 SQF 173
Cdd:pfam04315 160 AQF 162
MPTase-PolyVal pfam18818
Zincin-like metallopeptidase; Zincin-like Metallopeptidase frequently found in polyvalent ...
27-76 2.50e-03

Zincin-like metallopeptidase; Zincin-like Metallopeptidase frequently found in polyvalent proteins of phages and conjugative elements. The active site is comprised of a HEXXH motif and a C-terminal glutamate.


Pssm-ID: 465878  Cd Length: 126  Bit Score: 36.30  E-value: 2.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1633185482  27 GADEPIYLPADEEI---PHHRIVFARGFYASALHEIAHWcvAGPERRLLEDFG 76
Cdd:pfam18818  17 GGDRAFYSPSTDHIqmpPFEAFRDAENYYATLLHELGHW--TGHESRLDRDLS 67
 
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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