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Conserved domains on  [gi|446472587|ref|WP_000550441|]
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MULTISPECIES: elongation factor P hydroxylase [Acinetobacter]

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 ...
42-220 1.73e-93

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


:

Pssm-ID: 442335  Cd Length: 180  Bit Score: 270.92  E-value: 1.73e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587  42 ESEQVDWLILHFNHWFS-HHNVTLVRGEFEPEYFPANEHEP-AKIQFAHGFFNSALHEISHWTIAGAKRRLLPDLGYWYA 119
Cdd:COG3101    1 MTHQYQDLIELFNQCFAeSYNTRLVKGDDEPIYLPADEECPyHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587 120 PDGRTKEQQDLFEQVEIKPQAIEWLFAQSFGRKFRVSLDNLTGDG-GDGRKFKDNVYAQVQRYFsgEAKLPADAARFIEC 198
Cdd:COG3101   81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAePDREAFKRAVHAQVLRYL--EQGLPERAARFIQA 158
                        170       180
                 ....*....|....*....|..
gi 446472587 199 ICQCTRAGAALQLNEFKRELLD 220
Cdd:COG3101  159 LAAFYGTPLPLTAADFPLPELL 180
 
Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
42-220 1.73e-93

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 270.92  E-value: 1.73e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587  42 ESEQVDWLILHFNHWFS-HHNVTLVRGEFEPEYFPANEHEP-AKIQFAHGFFNSALHEISHWTIAGAKRRLLPDLGYWYA 119
Cdd:COG3101    1 MTHQYQDLIELFNQCFAeSYNTRLVKGDDEPIYLPADEECPyHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587 120 PDGRTKEQQDLFEQVEIKPQAIEWLFAQSFGRKFRVSLDNLTGDG-GDGRKFKDNVYAQVQRYFsgEAKLPADAARFIEC 198
Cdd:COG3101   81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAePDREAFKRAVHAQVLRYL--EQGLPERAARFIQA 158
                        170       180
                 ....*....|....*....|..
gi 446472587 199 ICQCTRAGAALQLNEFKRELLD 220
Cdd:COG3101  159 LAAFYGTPLPLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
53-201 2.22e-82

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: 242.51  E-value: 2.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587   53 FNHWFSH-HNVTLVRGEFEPEYFPANEHEP-AKIQFAHGFFNSALHEISHWTIAGAKRRLLPDLGYWYAPDGRTKEQQDL 130
Cdd:pfam04315   2 FNACFFEsYNTRLVKGGDEPIYLPADDEVPyHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQAE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446472587  131 FEQVEIKPQAIEWLFAQSFGRKFRVSLDNLTGDGGDGRKFKDNVYAQVQRYFsgEAKLPADAARFIECICQ 201
Cdd:pfam04315  82 FEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGEEGDRQAFKRAVHAQVMRYL--AQGLPARAARFIQALQA 150
 
Name Accession Description Interval E-value
EpmC COG3101
Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal ...
42-220 1.73e-93

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


Pssm-ID: 442335  Cd Length: 180  Bit Score: 270.92  E-value: 1.73e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587  42 ESEQVDWLILHFNHWFS-HHNVTLVRGEFEPEYFPANEHEP-AKIQFAHGFFNSALHEISHWTIAGAKRRLLPDLGYWYA 119
Cdd:COG3101    1 MTHQYQDLIELFNQCFAeSYNTRLVKGDDEPIYLPADEECPyHRIVFAHGFFASALHEIAHWCIAGEERRLLEDYGYWYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587 120 PDGRTKEQQDLFEQVEIKPQAIEWLFAQSFGRKFRVSLDNLTGDG-GDGRKFKDNVYAQVQRYFsgEAKLPADAARFIEC 198
Cdd:COG3101   81 PDGRDAEQQAEFEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGDAePDREAFKRAVHAQVLRYL--EQGLPERAARFIQA 158
                        170       180
                 ....*....|....*....|..
gi 446472587 199 ICQCTRAGAALQLNEFKRELLD 220
Cdd:COG3101  159 LAAFYGTPLPLTAADFPLPELL 180
EpmC pfam04315
Elongation factor P hydroxylase; This family catalyzes the final step in the elongation factor ...
53-201 2.22e-82

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: 242.51  E-value: 2.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446472587   53 FNHWFSH-HNVTLVRGEFEPEYFPANEHEP-AKIQFAHGFFNSALHEISHWTIAGAKRRLLPDLGYWYAPDGRTKEQQDL 130
Cdd:pfam04315   2 FNACFFEsYNTRLVKGGDEPIYLPADDEVPyHRIVFAHGFFASALHEIAHWCIAGKERRLLVDYGYWYCPDGRDAEQQAE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446472587  131 FEQVEIKPQAIEWLFAQSFGRKFRVSLDNLTGDGGDGRKFKDNVYAQVQRYFsgEAKLPADAARFIECICQ 201
Cdd:pfam04315  82 FEKVEVKPQALEWIFSVAAGFPFRVSCDNLNGEEGDRQAFKRAVHAQVMRYL--AQGLPARAARFIQALQA 150
MPTase-PolyVal pfam18818
Zincin-like metallopeptidase; Zincin-like Metallopeptidase frequently found in polyvalent ...
79-115 3.54e-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: 3.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446472587   79 HEPAKIQF--AHGFFNSALHEISHWTiaGAKRRLLPDLG 115
Cdd:pfam18818  31 QMPPFEAFrdAENYYATLLHELGHWT--GHESRLDRDLS 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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