NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30689758|ref|NP_849488|]
View 

UvrB/UvrC domain protein (DUF3506) [Arabidopsis thaliana]

Protein Classification

cyclin D1-binding domain-containing protein( domain architecture ID 10489987)

cyclin D1-binding domain-containing protein is a DUF3506 domain-containing protein; similar to Oryza sativa chloroplastic protein EXECUTER 1 and 2, which work together to enable higher plants to perceive singlet oxygen as a stress signal in plastid that activates a genetically determined nuclear stress response program which triggers a programmed cell death (PCD)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 528-682 6.05e-40

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


:

Pssm-ID: 463431  Cd Length: 147  Bit Score: 143.52  E-value: 6.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   528 FRRIDVTPSL-DPLDGLYIGAHGLYTSEVIHLKRKFGqwkggkeskkptDIEFYEYVEAVKLTGDPYVPAGKVAFRAKIG 606
Cdd:pfam12014   1 YRRLYLPPTLiRPFRGLFVGDYGGHGLEILLLSFPDG------------AREHGKYAEATKLTGDPNVPAGEVTFEAHDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   607 RRYELPHKGLIPEEFGV---------IARYKGQGRLADPGFRNPRWVDGELVILDGKYvkggpvVGFVYWapEYHFVMFF 677
Cdd:pfam12014  69 EIFREFNEGSRVVQVGVrsrdqnyprTCRFYGVGHIAGHGFRNPRRIPGVLILFDEDH------LGFIWL--ELKHFSLF 140


                  ....*
gi 30689758   678 NRLRL 682
Cdd:pfam12014 141 SRVDQ 145
UVR pfam02151
UvrB/uvrC motif;
127-153 1.36e-03

UvrB/uvrC motif;


:

Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 36.61  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 30689758   127 DRLLSVLKSQLNRAIKREDYEDAARLK 153
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLR 27
 
Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 528-682 6.05e-40

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


Pssm-ID: 463431  Cd Length: 147  Bit Score: 143.52  E-value: 6.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   528 FRRIDVTPSL-DPLDGLYIGAHGLYTSEVIHLKRKFGqwkggkeskkptDIEFYEYVEAVKLTGDPYVPAGKVAFRAKIG 606
Cdd:pfam12014   1 YRRLYLPPTLiRPFRGLFVGDYGGHGLEILLLSFPDG------------AREHGKYAEATKLTGDPNVPAGEVTFEAHDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   607 RRYELPHKGLIPEEFGV---------IARYKGQGRLADPGFRNPRWVDGELVILDGKYvkggpvVGFVYWapEYHFVMFF 677
Cdd:pfam12014  69 EIFREFNEGSRVVQVGVrsrdqnyprTCRFYGVGHIAGHGFRNPRRIPGVLILFDEDH------LGFIWL--ELKHFSLF 140


                  ....*
gi 30689758   678 NRLRL 682
Cdd:pfam12014 141 SRVDQ 145
UVR pfam02151
UvrB/uvrC motif;
127-153 1.36e-03

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 36.61  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 30689758   127 DRLLSVLKSQLNRAIKREDYEDAARLK 153
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLR 27
 
Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 528-682 6.05e-40

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


Pssm-ID: 463431  Cd Length: 147  Bit Score: 143.52  E-value: 6.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   528 FRRIDVTPSL-DPLDGLYIGAHGLYTSEVIHLKRKFGqwkggkeskkptDIEFYEYVEAVKLTGDPYVPAGKVAFRAKIG 606
Cdd:pfam12014   1 YRRLYLPPTLiRPFRGLFVGDYGGHGLEILLLSFPDG------------AREHGKYAEATKLTGDPNVPAGEVTFEAHDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689758   607 RRYELPHKGLIPEEFGV---------IARYKGQGRLADPGFRNPRWVDGELVILDGKYvkggpvVGFVYWapEYHFVMFF 677
Cdd:pfam12014  69 EIFREFNEGSRVVQVGVrsrdqnyprTCRFYGVGHIAGHGFRNPRRIPGVLILFDEDH------LGFIWL--ELKHFSLF 140


                  ....*
gi 30689758   678 NRLRL 682
Cdd:pfam12014 141 SRVDQ 145
UVR pfam02151
UvrB/uvrC motif;
127-153 1.36e-03

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 36.61  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 30689758   127 DRLLSVLKSQLNRAIKREDYEDAARLK 153
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLR 27
 
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