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Conserved domains on  [gi|119390044]
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Chain B, Adrenocortical dysplasia protein homolog

Protein Classification

TPP1 domain-containing protein( domain architecture ID 10563477)

TPP1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPP1 pfam10341
Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, ...
 8-117 4.49e-27

Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, involved in telomere replication. It has been demonstrated that TPP1 dimerizes and binds to DNA and RNA. Furthermore, TPP1 stimulates the dissociation of RNA/DNA hetero-duplexes. Yeast telomerase protein TPP1 (Est3 in yeast) is a novel type of GTPase. The key residues in Swiss:Q03096 are an Asp at residue 86 and the Arg at residue 110. The Asp is totally conserved in the family, whereas the Arg is not so well conserved. The N-terminal of TPP1 is likely to be the binding surface for TINF2, whereas the C-terminus probably binds to POT1, thereby tethering POT1 to the shelterin complex. The complex bound to telomeric DNA increases the activity and processivity of the human telomerase core enzyme, thus helping to maintain the length of the telomeres. This domain is conserved from fungi to mammals, hence family Telomere_Pot1 has been merged into the family. The human shelterin complex includes six proteins: telomere repeat binding factor 1 (TRF1), TRF2, repressor/activator protein 1 (RAP1), TRF1-interacting nuclear protein 2 (TIN2), TIN2-interacting protein 1 (TPP1) and protection of telomeres 1 (POT1).


:

Pssm-ID: 431220  Cd Length: 107  Bit Score: 97.75  E-value: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119390044    8 PWIRELILGSETPSS-----PRAGQLLEVLQdaeaavagpsHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKE 82
Cdd:pfam10341   1 PWILKLVLGAIKLSLdypntPSKAQLLKVVK----------FAQTTDNYAITAVLSDSTHKILAIFTREAVSNFEREEKS 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119390044   83 FGFRGTEGRLLLLQDCGVHVQVAEG--GAPAEFYLQV 117
Cdd:pfam10341  71 RITSGTVNCLILIKDASLVFQTVSElrKNFGEFLLSV 107
 
Name Accession Description Interval E-value
TPP1 pfam10341
Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, ...
 8-117 4.49e-27

Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, involved in telomere replication. It has been demonstrated that TPP1 dimerizes and binds to DNA and RNA. Furthermore, TPP1 stimulates the dissociation of RNA/DNA hetero-duplexes. Yeast telomerase protein TPP1 (Est3 in yeast) is a novel type of GTPase. The key residues in Swiss:Q03096 are an Asp at residue 86 and the Arg at residue 110. The Asp is totally conserved in the family, whereas the Arg is not so well conserved. The N-terminal of TPP1 is likely to be the binding surface for TINF2, whereas the C-terminus probably binds to POT1, thereby tethering POT1 to the shelterin complex. The complex bound to telomeric DNA increases the activity and processivity of the human telomerase core enzyme, thus helping to maintain the length of the telomeres. This domain is conserved from fungi to mammals, hence family Telomere_Pot1 has been merged into the family. The human shelterin complex includes six proteins: telomere repeat binding factor 1 (TRF1), TRF2, repressor/activator protein 1 (RAP1), TRF1-interacting nuclear protein 2 (TIN2), TIN2-interacting protein 1 (TPP1) and protection of telomeres 1 (POT1).


Pssm-ID: 431220  Cd Length: 107  Bit Score: 97.75  E-value: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119390044    8 PWIRELILGSETPSS-----PRAGQLLEVLQdaeaavagpsHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKE 82
Cdd:pfam10341   1 PWILKLVLGAIKLSLdypntPSKAQLLKVVK----------FAQTTDNYAITAVLSDSTHKILAIFTREAVSNFEREEKS 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119390044   83 FGFRGTEGRLLLLQDCGVHVQVAEG--GAPAEFYLQV 117
Cdd:pfam10341  71 RITSGTVNCLILIKDASLVFQTVSElrKNFGEFLLSV 107
 
Name Accession Description Interval E-value
TPP1 pfam10341
Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, ...
 8-117 4.49e-27

Shelterin complex subunit, TPP1/ACD; TPP1 is a component of the telomerase holoenzyme, involved in telomere replication. It has been demonstrated that TPP1 dimerizes and binds to DNA and RNA. Furthermore, TPP1 stimulates the dissociation of RNA/DNA hetero-duplexes. Yeast telomerase protein TPP1 (Est3 in yeast) is a novel type of GTPase. The key residues in Swiss:Q03096 are an Asp at residue 86 and the Arg at residue 110. The Asp is totally conserved in the family, whereas the Arg is not so well conserved. The N-terminal of TPP1 is likely to be the binding surface for TINF2, whereas the C-terminus probably binds to POT1, thereby tethering POT1 to the shelterin complex. The complex bound to telomeric DNA increases the activity and processivity of the human telomerase core enzyme, thus helping to maintain the length of the telomeres. This domain is conserved from fungi to mammals, hence family Telomere_Pot1 has been merged into the family. The human shelterin complex includes six proteins: telomere repeat binding factor 1 (TRF1), TRF2, repressor/activator protein 1 (RAP1), TRF1-interacting nuclear protein 2 (TIN2), TIN2-interacting protein 1 (TPP1) and protection of telomeres 1 (POT1).


Pssm-ID: 431220  Cd Length: 107  Bit Score: 97.75  E-value: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119390044    8 PWIRELILGSETPSS-----PRAGQLLEVLQdaeaavagpsHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKE 82
Cdd:pfam10341   1 PWILKLVLGAIKLSLdypntPSKAQLLKVVK----------FAQTTDNYAITAVLSDSTHKILAIFTREAVSNFEREEKS 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119390044   83 FGFRGTEGRLLLLQDCGVHVQVAEG--GAPAEFYLQV 117
Cdd:pfam10341  71 RITSGTVNCLILIKDASLVFQTVSElrKNFGEFLLSV 107
 
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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