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Conserved domains on  [gi|145361217|ref|NP_680763|]
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EKC/KEOPS complex subunit tprkb-like protein [Arabidopsis thaliana]

Protein Classification

EKC/KEOPS complex subunit CGI121/TPRKB( domain architecture ID 10554361)

EKC/KEOPS complex subunit CGI121/TPRKB, such as CGI21 from fungi and its homolog, TPRKB (TP53RK-binding protein) from mammals, acts as an allosteric effector that regulates the t(6)A activity of the EKC/KEOPS complex, which is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CGI-121 pfam08617
Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein ...
 17-170 2.59e-49

Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein kinase (PRPK). PRPK is a novel protein kinase which binds to and induces phosphorylation of the tumour suppressor protein p53. CGI-121 is part of a conserved protein complex, KEOPS. The KEOPS complex is involved in telomere uncapping and telomere elongation. Interestingly this family also include archaeal homologs, formerly in the DUF509 family. A structure for these proteins has been solved by structural genomics.


:

Pssm-ID: 462537  Cd Length: 160  Bit Score: 156.55  E-value: 2.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   17 FSGVTNSKELLNSMLDGSLKLEVSFLNASLIPDIFPLLAAAQKALISKSRDSLSTRTLHSELVYNYSGSKHITESLKRCG 96
Cdd:pfam08617   1 FKNVTNAAELREQLLSGNAEFEYAFIDASLIVSRFHLLSAIYRALLAQKRGKLKTKNVHSEILFNLSPSNNISEALKRFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   97 ISENTTYILAARFNASPVE--MEEVAKLINGKEIDLEE--LKTHANQANILKHYKITSQE--LGISSLGDAIVCRIAARD 170
Cdd:pfam08617  81 ISDDTSSLLVVKIGDSTNEdvLKHLLELVKGTEVPLSDenLSKLTDLAKIKKIYKLNGEEqeLERSELEDLVVGRIALKG 160
 
Name Accession Description Interval E-value
CGI-121 pfam08617
Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein ...
 17-170 2.59e-49

Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein kinase (PRPK). PRPK is a novel protein kinase which binds to and induces phosphorylation of the tumour suppressor protein p53. CGI-121 is part of a conserved protein complex, KEOPS. The KEOPS complex is involved in telomere uncapping and telomere elongation. Interestingly this family also include archaeal homologs, formerly in the DUF509 family. A structure for these proteins has been solved by structural genomics.


Pssm-ID: 462537  Cd Length: 160  Bit Score: 156.55  E-value: 2.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   17 FSGVTNSKELLNSMLDGSLKLEVSFLNASLIPDIFPLLAAAQKALISKSRDSLSTRTLHSELVYNYSGSKHITESLKRCG 96
Cdd:pfam08617   1 FKNVTNAAELREQLLSGNAEFEYAFIDASLIVSRFHLLSAIYRALLAQKRGKLKTKNVHSEILFNLSPSNNISEALKRFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   97 ISENTTYILAARFNASPVE--MEEVAKLINGKEIDLEE--LKTHANQANILKHYKITSQE--LGISSLGDAIVCRIAARD 170
Cdd:pfam08617  81 ISDDTSSLLVVKIGDSTNEdvLKHLLELVKGTEVPLSDenLSKLTDLAKIKKIYKLNGEEqeLERSELEDLVVGRIALKG 160
PRK14886 PRK14886
KEOPS complex subunit Cgi121;
34-167 2.75e-04

KEOPS complex subunit Cgi121;


Pssm-ID: 237848  Cd Length: 167  Bit Score: 39.60  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217  34 SLKLEVSFLNASLIPDIFPLLAAAQKALISKSRDSLSTRTLHSELVYNYSGSKHITESLKRCGISENTTYILAARFNASP 113
Cdd:PRK14886  28 EHGVTVQAFNADCIAGREHVEHAIILALRAFERGRNIAKDLGVEILLRAAGRRQISRAIKIIGAKEGENNIVVVVDEEEA 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145361217 114 VemEEVAKLINGKEIDLEELKTHANQANILKHYKITSQELGISSLG-DAIVC-RIA 167
Cdd:PRK14886 108 A--DAVIDLLGGLVDDSVLELDEAKEEKIRSLFDITEAELAACDGElVELVLeRVA 161
 
Name Accession Description Interval E-value
CGI-121 pfam08617
Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein ...
 17-170 2.59e-49

Kinase binding protein CGI-121; CGI-121 has been shown to bind to the p53-related protein kinase (PRPK). PRPK is a novel protein kinase which binds to and induces phosphorylation of the tumour suppressor protein p53. CGI-121 is part of a conserved protein complex, KEOPS. The KEOPS complex is involved in telomere uncapping and telomere elongation. Interestingly this family also include archaeal homologs, formerly in the DUF509 family. A structure for these proteins has been solved by structural genomics.


Pssm-ID: 462537  Cd Length: 160  Bit Score: 156.55  E-value: 2.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   17 FSGVTNSKELLNSMLDGSLKLEVSFLNASLIPDIFPLLAAAQKALISKSRDSLSTRTLHSELVYNYSGSKHITESLKRCG 96
Cdd:pfam08617   1 FKNVTNAAELREQLLSGNAEFEYAFIDASLIVSRFHLLSAIYRALLAQKRGKLKTKNVHSEILFNLSPSNNISEALKRFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217   97 ISENTTYILAARFNASPVE--MEEVAKLINGKEIDLEE--LKTHANQANILKHYKITSQE--LGISSLGDAIVCRIAARD 170
Cdd:pfam08617  81 ISDDTSSLLVVKIGDSTNEdvLKHLLELVKGTEVPLSDenLSKLTDLAKIKKIYKLNGEEqeLERSELEDLVVGRIALKG 160
PRK14886 PRK14886
KEOPS complex subunit Cgi121;
34-167 2.75e-04

KEOPS complex subunit Cgi121;


Pssm-ID: 237848  Cd Length: 167  Bit Score: 39.60  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145361217  34 SLKLEVSFLNASLIPDIFPLLAAAQKALISKSRDSLSTRTLHSELVYNYSGSKHITESLKRCGISENTTYILAARFNASP 113
Cdd:PRK14886  28 EHGVTVQAFNADCIAGREHVEHAIILALRAFERGRNIAKDLGVEILLRAAGRRQISRAIKIIGAKEGENNIVVVVDEEEA 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145361217 114 VemEEVAKLINGKEIDLEELKTHANQANILKHYKITSQELGISSLG-DAIVC-RIA 167
Cdd:PRK14886 108 A--DAVIDLLGGLVDDSVLELDEAKEEKIRSLFDITEAELAACDGElVELVLeRVA 161
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 63-135 6.07e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 6.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145361217   63 SKSRDSLSTRTLHSELVYNYSGSKHITESL-----KRCGISENTTYILAARFNASPVEMEEVAKLINGKEIDLEELKT 135
Cdd:pfam05483 335 AQMEELNKAKAAHSFVVTEFEATTCSLEELlrteqQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK 412
 
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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