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Conserved domains on  [gi|2462549320|ref|XP_054236453|]
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telomeric repeat-binding factor 2-interacting protein 1 isoform X1 [Homo sapiens]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein( domain architecture ID 11244295)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein binds DNA and may function as a transcription factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myb_DNA-bind_2 pfam08914
Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, ...
 132-196 3.43e-34

Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, with the second and third helices forming a helix-turn-helix variant motif. The function of this domain is unclear: it may either interact with DNA via an adaptor protein or it may be only involved in protein-protein interactions.


:

Pssm-ID: 286058  Cd Length: 65  Bit Score: 119.16  E-value: 3.43e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549320 132 GRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYL 196
Cdd:pfam08914   1 GRLPYTPEEDAAILHYVLEKERSPASVRGNAIWKEMEKKHLTRHSWQSMKDRYLKHLRGQHREGL 65
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 17-99 8.21e-17

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


:

Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 73.94  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549320  17 SSTLFvrddgSSMSFYV--RPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGE----ALAEASGDFISTQYILDCVER 90
Cdd:pfam16589   1 LPNLF-----EPLRFYInaIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNktdkLAENTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 2462549320  91 NERLELEAY 99
Cdd:pfam16589  76 GKLLPLENY 84
 
Name Accession Description Interval E-value
Myb_DNA-bind_2 pfam08914
Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, ...
 132-196 3.43e-34

Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, with the second and third helices forming a helix-turn-helix variant motif. The function of this domain is unclear: it may either interact with DNA via an adaptor protein or it may be only involved in protein-protein interactions.


Pssm-ID: 286058  Cd Length: 65  Bit Score: 119.16  E-value: 3.43e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549320 132 GRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYL 196
Cdd:pfam08914   1 GRLPYTPEEDAAILHYVLEKERSPASVRGNAIWKEMEKKHLTRHSWQSMKDRYLKHLRGQHREGL 65
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 17-99 8.21e-17

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 73.94  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549320  17 SSTLFvrddgSSMSFYV--RPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGE----ALAEASGDFISTQYILDCVER 90
Cdd:pfam16589   1 LPNLF-----EPLRFYInaIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNktdkLAENTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 2462549320  91 NERLELEAY 99
Cdd:pfam16589  76 GKLLPLENY 84
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 133-189 1.27e-15

DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is mediated by a pair of DNA-binding modules comprised of 2 3-helix bundles with an N-terminal arm, closely matching the structure of homeodomain and myb-type proteins. Human Rap1 has a single myb-like module, and may not bind DNA directly. Rap1, identified in budding yeast as repressor-activator protein 1, is a conserved telomere binding protein, also identified in fission yeast and mammals. In Saccharomyces cerevisiae, Rap1 directly binds DNA and is involved in transcriptional activation, gene silencing, as well as binding at numerous binding sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human Rap1 apparently does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the Rap C-terminal domain (RCT). Rap1 may act by suppressing non-homologous end-joining. Yeast Rap1 has 2 myb-type DNA binding modules, a BRCT domain, and a RCT domain that recruits Sir3 and Sir4 proteins for gene silencing and Rif1 and Rif2 for telomere length maintenance. Human Rap1 has a similar domain architecture but has a single myb-like domain.


Pssm-ID: 212554  Cd Length: 57  Bit Score: 69.95  E-value: 1.27e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549320 133 RIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSlTQHSWQSLKDRYLKHLR 189
Cdd:cd11655     1 RTKFTAEDDYILCKYVAKYGRRGRGRLGNSFYKELAEEH-PRHTWQSWRDRYRKFLS 56
 
Name Accession Description Interval E-value
Myb_DNA-bind_2 pfam08914
Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, ...
 132-196 3.43e-34

Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, with the second and third helices forming a helix-turn-helix variant motif. The function of this domain is unclear: it may either interact with DNA via an adaptor protein or it may be only involved in protein-protein interactions.


Pssm-ID: 286058  Cd Length: 65  Bit Score: 119.16  E-value: 3.43e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549320 132 GRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYL 196
Cdd:pfam08914   1 GRLPYTPEEDAAILHYVLEKERSPASVRGNAIWKEMEKKHLTRHSWQSMKDRYLKHLRGQHREGL 65
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 17-99 8.21e-17

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 73.94  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549320  17 SSTLFvrddgSSMSFYV--RPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGE----ALAEASGDFISTQYILDCVER 90
Cdd:pfam16589   1 LPNLF-----EPLRFYInaIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNktdkLAENTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 2462549320  91 NERLELEAY 99
Cdd:pfam16589  76 GKLLPLENY 84
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 133-189 1.27e-15

DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is mediated by a pair of DNA-binding modules comprised of 2 3-helix bundles with an N-terminal arm, closely matching the structure of homeodomain and myb-type proteins. Human Rap1 has a single myb-like module, and may not bind DNA directly. Rap1, identified in budding yeast as repressor-activator protein 1, is a conserved telomere binding protein, also identified in fission yeast and mammals. In Saccharomyces cerevisiae, Rap1 directly binds DNA and is involved in transcriptional activation, gene silencing, as well as binding at numerous binding sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human Rap1 apparently does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the Rap C-terminal domain (RCT). Rap1 may act by suppressing non-homologous end-joining. Yeast Rap1 has 2 myb-type DNA binding modules, a BRCT domain, and a RCT domain that recruits Sir3 and Sir4 proteins for gene silencing and Rif1 and Rif2 for telomere length maintenance. Human Rap1 has a similar domain architecture but has a single myb-like domain.


Pssm-ID: 212554  Cd Length: 57  Bit Score: 69.95  E-value: 1.27e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549320 133 RIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSlTQHSWQSLKDRYLKHLR 189
Cdd:cd11655     1 RTKFTAEDDYILCKYVAKYGRRGRGRLGNSFYKELAEEH-PRHTWQSWRDRYRKFLS 56
 
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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