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Conserved domains on  [gi|15988502|pdb|1H6O|A]
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Chain A, TELOMERIC REPEAT BINDING FACTOR 1

Protein Classification

telomere repeat binding factor family protein( domain architecture ID 10084540)

telomere repeat binding factor (TRF) family protein binds directly to the telomeric double-stranded TTAGGG repeat through its SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain, and negatively regulates telomere length

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRFH cd00280
Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain ...
 15-203 3.84e-109

Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain Homology; TRFH. Telomeres are protein/DNA complexes that make up the physical ends of eukaryotic linear chromosomes and are essential for chromosome stability, protecting the chromosome ends from degradation and end-to-end fusion. Proteins TRF1, TRF2 and Taz1 bind telomeric DNA and are also involved in recruiting interacting proteins, TIN2, and Rap1, to the telomeres. It has also been demonstrated that PARP1 associates with TRF2 and is capable of poly(ADP-ribosyl)ation of TRF2, which affects binding of TRF2 to telomeric DNA. TRF1, TRF2 and Taz1 proteins contain three functional domains: an N-terminal acidic domain, a central TRF-specific/dimerization domain, and a C-terminal DNA binding domain with a single Myb-like repeat. Homodimerization, a prerequisite to DNA binding, results in the juxtaposition of two Myb DNA binding domains.


:

Pssm-ID: 238174  Cd Length: 200  Bit Score: 310.92  E-value: 3.84e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       15 GWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESAL 94
Cdd:cd00280  10 RWVLDFYFHSACRAFREGRYEDFRRTRDIAEALLVGPLKLTATQLKTLRIMQFLSRIAEGKNLDCQFENDEELTPLESAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       95 MIWGSIEKEHDK---LHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPfKSKLLMIISQKDTFHSFFQHFS 171
Cdd:cd00280  90 MVLESIEKEFSLpetLHEEIRKLIKEQAVAVCMENGEFKKAEEVLKRLFSDPESQKL-RMKLLMIIREKDPAHPVLQNFS 168

                       170       180       190
                ....*....|....*....|....*....|..
1H6O_A      172 YNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVV 203
Cdd:cd00280 169 YSHFMQKMKSYVELVLDEKESPFLLKAAAKVV 200
 
Name Accession Description Interval E-value
TRFH cd00280
Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain ...
 15-203 3.84e-109

Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain Homology; TRFH. Telomeres are protein/DNA complexes that make up the physical ends of eukaryotic linear chromosomes and are essential for chromosome stability, protecting the chromosome ends from degradation and end-to-end fusion. Proteins TRF1, TRF2 and Taz1 bind telomeric DNA and are also involved in recruiting interacting proteins, TIN2, and Rap1, to the telomeres. It has also been demonstrated that PARP1 associates with TRF2 and is capable of poly(ADP-ribosyl)ation of TRF2, which affects binding of TRF2 to telomeric DNA. TRF1, TRF2 and Taz1 proteins contain three functional domains: an N-terminal acidic domain, a central TRF-specific/dimerization domain, and a C-terminal DNA binding domain with a single Myb-like repeat. Homodimerization, a prerequisite to DNA binding, results in the juxtaposition of two Myb DNA binding domains.


Pssm-ID: 238174  Cd Length: 200  Bit Score: 310.92  E-value: 3.84e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       15 GWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESAL 94
Cdd:cd00280  10 RWVLDFYFHSACRAFREGRYEDFRRTRDIAEALLVGPLKLTATQLKTLRIMQFLSRIAEGKNLDCQFENDEELTPLESAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       95 MIWGSIEKEHDK---LHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPfKSKLLMIISQKDTFHSFFQHFS 171
Cdd:cd00280  90 MVLESIEKEFSLpetLHEEIRKLIKEQAVAVCMENGEFKKAEEVLKRLFSDPESQKL-RMKLLMIIREKDPAHPVLQNFS 168

                       170       180       190
                ....*....|....*....|....*....|..
1H6O_A      172 YNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVV 203
Cdd:cd00280 169 YSHFMQKMKSYVELVLDEKESPFLLKAAAKVV 200
TRF pfam08558
Telomere repeat binding factor (TRF); Telomere repeat binding factor (TRF) family proteins are ...
 16-181 1.79e-42

Telomere repeat binding factor (TRF); Telomere repeat binding factor (TRF) family proteins are important for the regulation of telomere stability. The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain pfam00249 at the carboxy terminus. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres. This domain is composed of multiple alpha helices arranged in a solenoid conformation similar to TPR repeats. The fungal members have now also been found to carry two double strand telomeric repeat binding factors.


Pssm-ID: 400735  Cd Length: 212  Bit Score: 142.16  E-value: 1.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A         16 WMLDFLCLSLCRAFRDGRSE-----------DFRRTRNSAEAIIHGLSSLTACQ----------LRTIYICQFLTRIAAG 74
Cdd:pfam08558   3 WVLDNLSTQLLRALREGPYTdvlaivsepdsEFRESFDILESLFERTKKLYSTRspllspsilkIRESYIMQTLRRINLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A         75 KTLDAQFENDErITPLESALMIWGSIEKEHDKL---HEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHM---- 147
Cdd:pfam08558  83 TFLDSVFGNLE-VGFLELAENFLDIFCPEDGKLlkpQGVLYLDLKTQAYIVALKEGPFKSASEILDKLFPDDLADIlkqr 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1H6O_A        148 -----------------PFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKS 181
Cdd:pfam08558 162 ndklltpsetdfverckKRREKLLNIINEKDPYHPLLQNFSWESFLKELLS 212
 
Name Accession Description Interval E-value
TRFH cd00280
Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain ...
 15-203 3.84e-109

Telomeric Repeat binding Factor or TTAGGG Repeat binding Factor, central (dimerization) domain Homology; TRFH. Telomeres are protein/DNA complexes that make up the physical ends of eukaryotic linear chromosomes and are essential for chromosome stability, protecting the chromosome ends from degradation and end-to-end fusion. Proteins TRF1, TRF2 and Taz1 bind telomeric DNA and are also involved in recruiting interacting proteins, TIN2, and Rap1, to the telomeres. It has also been demonstrated that PARP1 associates with TRF2 and is capable of poly(ADP-ribosyl)ation of TRF2, which affects binding of TRF2 to telomeric DNA. TRF1, TRF2 and Taz1 proteins contain three functional domains: an N-terminal acidic domain, a central TRF-specific/dimerization domain, and a C-terminal DNA binding domain with a single Myb-like repeat. Homodimerization, a prerequisite to DNA binding, results in the juxtaposition of two Myb DNA binding domains.


Pssm-ID: 238174  Cd Length: 200  Bit Score: 310.92  E-value: 3.84e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       15 GWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESAL 94
Cdd:cd00280  10 RWVLDFYFHSACRAFREGRYEDFRRTRDIAEALLVGPLKLTATQLKTLRIMQFLSRIAEGKNLDCQFENDEELTPLESAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A       95 MIWGSIEKEHDK---LHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPfKSKLLMIISQKDTFHSFFQHFS 171
Cdd:cd00280  90 MVLESIEKEFSLpetLHEEIRKLIKEQAVAVCMENGEFKKAEEVLKRLFSDPESQKL-RMKLLMIIREKDPAHPVLQNFS 168

                       170       180       190
                ....*....|....*....|....*....|..
1H6O_A      172 YNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVV 203
Cdd:cd00280 169 YSHFMQKMKSYVELVLDEKESPFLLKAAAKVV 200
TRF pfam08558
Telomere repeat binding factor (TRF); Telomere repeat binding factor (TRF) family proteins are ...
 16-181 1.79e-42

Telomere repeat binding factor (TRF); Telomere repeat binding factor (TRF) family proteins are important for the regulation of telomere stability. The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain pfam00249 at the carboxy terminus. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres. This domain is composed of multiple alpha helices arranged in a solenoid conformation similar to TPR repeats. The fungal members have now also been found to carry two double strand telomeric repeat binding factors.


Pssm-ID: 400735  Cd Length: 212  Bit Score: 142.16  E-value: 1.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A         16 WMLDFLCLSLCRAFRDGRSE-----------DFRRTRNSAEAIIHGLSSLTACQ----------LRTIYICQFLTRIAAG 74
Cdd:pfam08558   3 WVLDNLSTQLLRALREGPYTdvlaivsepdsEFRESFDILESLFERTKKLYSTRspllspsilkIRESYIMQTLRRINLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H6O_A         75 KTLDAQFENDErITPLESALMIWGSIEKEHDKL---HEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHM---- 147
Cdd:pfam08558  83 TFLDSVFGNLE-VGFLELAENFLDIFCPEDGKLlkpQGVLYLDLKTQAYIVALKEGPFKSASEILDKLFPDDLADIlkqr 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1H6O_A        148 -----------------PFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKS 181
Cdd:pfam08558 162 ndklltpsetdfverckKRREKLLNIINEKDPYHPLLQNFSWESFLKELLS 212
 
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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