NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|459371609|gb|EMG49340|]
View 

CaRap1p [Candida maltosa Xu316]

Protein Classification

BRCT_2 and rap1_myb-like domain-containing protein( domain architecture ID 11244278)

BRCT_2 and rap1_myb-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SANT super family cl21498
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 296-366 2.32e-19

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


The actual alignment was detected with superfamily member pfam09197:

Pssm-ID: 473887  Cd Length: 108  Bit Score: 82.46  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609  296 KFTAEDDYFLCSEAIKS------------------------------ENINYTFFSNLYRKRSSHTLNSWRDRYRKYVDE 345
Cdd:pfam09197   1 KFTAEDDYALCKEVKKQfysdiyqkdpdtgsslisdgdppeheakrdMTVPREFFKDFAKTNPSHTENSWRDRYRKFVLE 80

                          90       100
                  ....*....|....*....|.
gi 459371609  346 DTIPQYIEYYENCMELGEEPQ 366
Cdd:pfam09197  81 YGIQKYIKYYEKERASGEEPE 101
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 72-150 6.58e-13

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: 63.54  E-value: 6.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609   72 PKTIFvdkdnKTMLFYI-PKEEPNRIKYRELIIKHGGLLVDKQIPTAYHLSNNE---------KMLGYFKLKFIDDCIAN 141
Cdd:pfam16589   1 LPNLF-----EPLRFYInAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYnktdklaenTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 459371609  142 GGLVPLLDY 150
Cdd:pfam16589  76 GKLLPLENY 84
SANT super family cl21498
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 205-259 1.89e-05

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


The actual alignment was detected with superfamily member cd11655:

Pssm-ID: 473887  Cd Length: 57  Bit Score: 41.84  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 459371609 205 NRFTAEQDEFILEQVRMKPR---YRHSHQFYHDLSqtRELHGHTGNSIRSRYRRHLEP 259
Cdd:cd11655    2 TKFTAEDDYILCKYVAKYGRrgrGRLGNSFYKELA--EEHPRHTWQSWRDRYRKFLSK 57
 
Name Accession Description Interval E-value
Rap1-DNA-bind pfam09197
Rap1, DNA-binding; Members of this family, which are predominantly found in the yeast protein ...
 296-366 2.32e-19

Rap1, DNA-binding; Members of this family, which are predominantly found in the yeast protein rap1, assume a secondary structure consisting of a three-helix bundle and an N-terminal arm. They contain an Arg-Asp-Arg-Lys sequence that interacts with an ACACC region in the 3' region of the DNA-binding site.


Pssm-ID: 401223  Cd Length: 108  Bit Score: 82.46  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609  296 KFTAEDDYFLCSEAIKS------------------------------ENINYTFFSNLYRKRSSHTLNSWRDRYRKYVDE 345
Cdd:pfam09197   1 KFTAEDDYALCKEVKKQfysdiyqkdpdtgsslisdgdppeheakrdMTVPREFFKDFAKTNPSHTENSWRDRYRKFVLE 80

                          90       100
                  ....*....|....*....|.
gi 459371609  346 DTIPQYIEYYENCMELGEEPQ 366
Cdd:pfam09197  81 YGIQKYIKYYEKERASGEEPE 101
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 72-150 6.58e-13

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: 63.54  E-value: 6.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609   72 PKTIFvdkdnKTMLFYI-PKEEPNRIKYRELIIKHGGLLVDKQIPTAYHLSNNE---------KMLGYFKLKFIDDCIAN 141
Cdd:pfam16589   1 LPNLF-----EPLRFYInAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYnktdklaenTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 459371609  142 GGLVPLLDY 150
Cdd:pfam16589  76 GKLLPLENY 84
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 294-343 2.01e-12

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: 61.48  E-value: 2.01e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459371609 294 KNKFTAEDDYFLCSEAIK-----SENINYTFFSNLYRKRSSHTLNSWRDRYRKYV 343
Cdd:cd11655    1 RTKFTAEDDYILCKYVAKygrrgRGRLGNSFYKELAEEHPRHTWQSWRDRYRKFL 55
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 205-259 1.89e-05

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: 41.84  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 459371609 205 NRFTAEQDEFILEQVRMKPR---YRHSHQFYHDLSqtRELHGHTGNSIRSRYRRHLEP 259
Cdd:cd11655    2 TKFTAEDDYILCKYVAKYGRrgrGRLGNSFYKELA--EEHPRHTWQSWRDRYRKFLSK 57
Myb_DNA-bind_2 pfam08914
Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, ...
 207-262 1.50e-04

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: 39.42  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 459371609  207 FTAEQDEFILEQVRMKPRYRHS---HQFYHDLSQTReLHGHTGNSIRSRYRRHLEPLLS 262
Cdd:pfam08914   5 YTPEEDAAILHYVLEKERSPASvrgNAIWKEMEKKH-LTRHSWQSMKDRYLKHLRGQHR 62
 
Name Accession Description Interval E-value
Rap1-DNA-bind pfam09197
Rap1, DNA-binding; Members of this family, which are predominantly found in the yeast protein ...
 296-366 2.32e-19

Rap1, DNA-binding; Members of this family, which are predominantly found in the yeast protein rap1, assume a secondary structure consisting of a three-helix bundle and an N-terminal arm. They contain an Arg-Asp-Arg-Lys sequence that interacts with an ACACC region in the 3' region of the DNA-binding site.


Pssm-ID: 401223  Cd Length: 108  Bit Score: 82.46  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609  296 KFTAEDDYFLCSEAIKS------------------------------ENINYTFFSNLYRKRSSHTLNSWRDRYRKYVDE 345
Cdd:pfam09197   1 KFTAEDDYALCKEVKKQfysdiyqkdpdtgsslisdgdppeheakrdMTVPREFFKDFAKTNPSHTENSWRDRYRKFVLE 80

                          90       100
                  ....*....|....*....|.
gi 459371609  346 DTIPQYIEYYENCMELGEEPQ 366
Cdd:pfam09197  81 YGIQKYIKYYEKERASGEEPE 101
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 72-150 6.58e-13

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: 63.54  E-value: 6.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459371609   72 PKTIFvdkdnKTMLFYI-PKEEPNRIKYRELIIKHGGLLVDKQIPTAYHLSNNE---------KMLGYFKLKFIDDCIAN 141
Cdd:pfam16589   1 LPNLF-----EPLRFYInAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYnktdklaenTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 459371609  142 GGLVPLLDY 150
Cdd:pfam16589  76 GKLLPLENY 84
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 294-343 2.01e-12

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: 61.48  E-value: 2.01e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459371609 294 KNKFTAEDDYFLCSEAIK-----SENINYTFFSNLYRKRSSHTLNSWRDRYRKYV 343
Cdd:cd11655    1 RTKFTAEDDYILCKYVAKygrrgRGRLGNSFYKELAEEHPRHTWQSWRDRYRKFL 55
rap1_myb-like cd11655
DNA-binding modules of yeast Rap1 and related proteins; Yeast Rap1 DNA-binding activity is ...
 205-259 1.89e-05

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: 41.84  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 459371609 205 NRFTAEQDEFILEQVRMKPR---YRHSHQFYHDLSqtRELHGHTGNSIRSRYRRHLEP 259
Cdd:cd11655    2 TKFTAEDDYILCKYVAKYGRrgrGRLGNSFYKELA--EEHPRHTWQSWRDRYRKFLSK 57
Myb_DNA-bind_2 pfam08914
Rap1 Myb domain; The Rap1 Myb domain adopts a canonical three-helix bundle tertiary structure, ...
 207-262 1.50e-04

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: 39.42  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 459371609  207 FTAEQDEFILEQVRMKPRYRHS---HQFYHDLSQTReLHGHTGNSIRSRYRRHLEPLLS 262
Cdd:pfam08914   5 YTPEEDAAILHYVLEKERSPASvrgNAIWKEMEKKH-LTRHSWQSMKDRYLKHLRGQHR 62
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH