NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24667521|ref|NP_649227|]
View 

uncharacterized protein Dmel_CG5199, isoform A [Drosophila melanogaster]

Protein Classification

cut8/STS1 family protein( domain architecture ID 10554109)

cut8/STS1 family protein such as tethering factor for nuclear proteasome STS1 that functions as a regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cut8 pfam08559
Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear ...
 189-377 3.99e-57

Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear envelope protein that physically interacts with and tethers 26S proteasome in the nucleus resulting in the nuclear accumulation of proteasome. Cut8 comprises three functional domains. An N-terminal lysine-rich segment which binds to the proteasome when ubiquitinated, a central dimerization domain and a C-terminal nine-helix, pdb:3q5w, bundle which shows structural similarity to 14-3-3 phosphoprotein-binding domains. The helical bundle is necessary for liposome and cholesterol binding. Cut8 is a proteasome substrate and the N-terminal segment is polyubiquitinated and functions as a degron tag. Ubiquitination of the amino N-terminal segment is essential for the function of Cut8. Lysine residues in the N-terminal segment of Cut8 are required for physical interaction with proteasome. In fission yeast the function of Cut8 has been demonstrated to be regulated by ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1. Cut8 homologs have been identified in Drosophila melanogaster, Anopheles gambiae and Dictyostelium discoideum.


:

Pssm-ID: 462518  Cd Length: 203  Bit Score: 185.10  E-value: 3.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   189 TNTDATLPSLLQGLSQEQLIDLIMNNI-KSASDEGEIRTQLPTPDISALEQDLHHAKRLIFKSLPTSrlCKKTDAAAYSK 267
Cdd:pfam08559   9 LSDTDPLPRLLETLDKEQLRSLLQSLVeRHPELQQEVVSKAPRPDIQSLLQVLSEKQENIFKSLPYS--GDSTDDYAYNR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   268 ASMHLNEFKRVLQSQAKRLHDSTH--WDALVDYVSMAWQCVASTPNWESHAHNAVRRQCFKLLACSCYAAIKH----GGM 341
Cdd:pfam08559  87 VKPHLLEFLDALSDFTLNFLPPNEtqWSTSLKFLDGATNIVHRLPNWDNQSHNYYKDKCYEQLSNAWALVIKEaakrGGG 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24667521   342 RLGQLRLETLERNLREWSKDYEDVL-SCVNALQRTLN 377
Cdd:pfam08559 167 LLGQLHLGGWDQKLAKHNEDSGGRLqSALNLLKSLLG 203
 
Name Accession Description Interval E-value
Cut8 pfam08559
Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear ...
 189-377 3.99e-57

Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear envelope protein that physically interacts with and tethers 26S proteasome in the nucleus resulting in the nuclear accumulation of proteasome. Cut8 comprises three functional domains. An N-terminal lysine-rich segment which binds to the proteasome when ubiquitinated, a central dimerization domain and a C-terminal nine-helix, pdb:3q5w, bundle which shows structural similarity to 14-3-3 phosphoprotein-binding domains. The helical bundle is necessary for liposome and cholesterol binding. Cut8 is a proteasome substrate and the N-terminal segment is polyubiquitinated and functions as a degron tag. Ubiquitination of the amino N-terminal segment is essential for the function of Cut8. Lysine residues in the N-terminal segment of Cut8 are required for physical interaction with proteasome. In fission yeast the function of Cut8 has been demonstrated to be regulated by ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1. Cut8 homologs have been identified in Drosophila melanogaster, Anopheles gambiae and Dictyostelium discoideum.


Pssm-ID: 462518  Cd Length: 203  Bit Score: 185.10  E-value: 3.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   189 TNTDATLPSLLQGLSQEQLIDLIMNNI-KSASDEGEIRTQLPTPDISALEQDLHHAKRLIFKSLPTSrlCKKTDAAAYSK 267
Cdd:pfam08559   9 LSDTDPLPRLLETLDKEQLRSLLQSLVeRHPELQQEVVSKAPRPDIQSLLQVLSEKQENIFKSLPYS--GDSTDDYAYNR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   268 ASMHLNEFKRVLQSQAKRLHDSTH--WDALVDYVSMAWQCVASTPNWESHAHNAVRRQCFKLLACSCYAAIKH----GGM 341
Cdd:pfam08559  87 VKPHLLEFLDALSDFTLNFLPPNEtqWSTSLKFLDGATNIVHRLPNWDNQSHNYYKDKCYEQLSNAWALVIKEaakrGGG 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24667521   342 RLGQLRLETLERNLREWSKDYEDVL-SCVNALQRTLN 377
Cdd:pfam08559 167 LLGQLHLGGWDQKLAKHNEDSGGRLqSALNLLKSLLG 203
 
Name Accession Description Interval E-value
Cut8 pfam08559
Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear ...
 189-377 3.99e-57

Cut8, nuclear proteasome tether protein; In Schizosaccharomyces pombe, Cut8 is a nuclear envelope protein that physically interacts with and tethers 26S proteasome in the nucleus resulting in the nuclear accumulation of proteasome. Cut8 comprises three functional domains. An N-terminal lysine-rich segment which binds to the proteasome when ubiquitinated, a central dimerization domain and a C-terminal nine-helix, pdb:3q5w, bundle which shows structural similarity to 14-3-3 phosphoprotein-binding domains. The helical bundle is necessary for liposome and cholesterol binding. Cut8 is a proteasome substrate and the N-terminal segment is polyubiquitinated and functions as a degron tag. Ubiquitination of the amino N-terminal segment is essential for the function of Cut8. Lysine residues in the N-terminal segment of Cut8 are required for physical interaction with proteasome. In fission yeast the function of Cut8 has been demonstrated to be regulated by ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1. Cut8 homologs have been identified in Drosophila melanogaster, Anopheles gambiae and Dictyostelium discoideum.


Pssm-ID: 462518  Cd Length: 203  Bit Score: 185.10  E-value: 3.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   189 TNTDATLPSLLQGLSQEQLIDLIMNNI-KSASDEGEIRTQLPTPDISALEQDLHHAKRLIFKSLPTSrlCKKTDAAAYSK 267
Cdd:pfam08559   9 LSDTDPLPRLLETLDKEQLRSLLQSLVeRHPELQQEVVSKAPRPDIQSLLQVLSEKQENIFKSLPYS--GDSTDDYAYNR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24667521   268 ASMHLNEFKRVLQSQAKRLHDSTH--WDALVDYVSMAWQCVASTPNWESHAHNAVRRQCFKLLACSCYAAIKH----GGM 341
Cdd:pfam08559  87 VKPHLLEFLDALSDFTLNFLPPNEtqWSTSLKFLDGATNIVHRLPNWDNQSHNYYKDKCYEQLSNAWALVIKEaakrGGG 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24667521   342 RLGQLRLETLERNLREWSKDYEDVL-SCVNALQRTLN 377
Cdd:pfam08559 167 LLGQLHLGGWDQKLAKHNEDSGGRLqSALNLLKSLLG 203
 
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