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Conserved domains on  [gi|124512624|ref|XP_001349445|]
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26S proteasome regulatory subunit RPN10, putative [Plasmodium falciparum 3D7]

Protein Classification

26S proteasome regulatory subunit RPN10( domain architecture ID 10106897)

26S proteasome regulatory subunit RPN10 is a multiubiquitin binding protein

CATH:  3.40.50.410
Gene Ontology:  GO:0008540|GO:0006511|GO:0043130|GO:0031593
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 2-188 3.92e-95

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


:

Pssm-ID: 238729  Cd Length: 187  Bit Score: 285.41  E-value: 3.92e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624   2 SNIEATIICIDNSDYNRNEDIVPNRFLSQIDCVNVLCCNKTSLHYKNNIGILMMAGDKIKVKVSLTNDIGQLLSCIHDIK 81
Cdd:cd01452    1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624  82 LDGTCDIIRSLLIAQLALKHRVDKNLDQKIILFIGSPFHVNEKQLINTGKQLKKNNISVDIISFGNIDKNRDKLMMLFES 161
Cdd:cd01452   81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                        170       180
                 ....*....|....*....|....*..
gi 124512624 162 VNNNDNCRFIECPEYENNLSKFVLNSF 188
Cdd:cd01452  161 VNGKDGSHLVSVPPGENLLSDALLSSP 187
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 2-188 3.92e-95

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 285.41  E-value: 3.92e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624   2 SNIEATIICIDNSDYNRNEDIVPNRFLSQIDCVNVLCCNKTSLHYKNNIGILMMAGDKIKVKVSLTNDIGQLLSCIHDIK 81
Cdd:cd01452    1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624  82 LDGTCDIIRSLLIAQLALKHRVDKNLDQKIILFIGSPFHVNEKQLINTGKQLKKNNISVDIISFGNIDKNRDKLMMLFES 161
Cdd:cd01452   81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                        170       180
                 ....*....|....*....|....*..
gi 124512624 162 VNNNDNCRFIECPEYENNLSKFVLNSF 188
Cdd:cd01452  161 VNGKDGSHLVSVPPGENLLSDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
7-115 1.12e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624    7 TIICIDNSDYNRNEDIVPNRFLSQIDCVNVLCcnkTSLHyKNNIGILMMaGDKIKVKVSLTNDIGQLLSCIHDIK-LDGT 85
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL---KSLP-GDRVGLVTF-GDGPEVLIPLTKDRAKILRALRRLEpKGGG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 124512624   86 CDIIRSLLIAQLALKHRvdKNLDQKIILFI 115
Cdd:pfam13519  76 TNLAAALQLARAALKHR--RKNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 8-158 4.99e-05

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624     8 IICIDNSdynrnEDIVPNRFLSQIDCVNVLCCNKTSLHYKNNIGILMMAGD-KIKVKVSLTNDIGQLLSCIHDIKLD--G 84
Cdd:smart00327   3 VFLLDGS-----GSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDaRVLFPLNDSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512624    85 TCDIIRSLLIAQLALKHRVDKNLD--QKIILFI--GSPfHVNEKQLINTGKQLKKNNISVDIISFGNiDKNRDKLMML 158
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRgaPKVVILItdGES-NDGPKDLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL 153
 
Name Accession Description Interval E-value
VWA_26S_proteasome_subunit cd01452
26S proteasome plays a major role in eukaryotic protein breakdown, especially for ...
 2-188 3.92e-95

26S proteasome plays a major role in eukaryotic protein breakdown, especially for ubiquitin-tagged proteins. It is an ATP-dependent protease responsible for the bulk of non-lysosomal proteolysis in eukaryotes, often using covalent modification of proteins by ubiquitylation. It consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP). The CP is an ATP independent peptidase consisting of hydrolyzing activities. One or both ends of CP carry the RP that confers both ubiquitin and ATP dependence to the 26S proteosome. The RP's proposed functions include recognition of substrates and translocation of these to CP for proteolysis. The RP can dissociate into a stable lid and base subcomplexes. The base is composed of three non-ATPase subunits (Rpn 1, 2 and 10). A single residue in the vWA domain of Rpn10 has been implicated to be responsible for stabilizing the lid-base association.


Pssm-ID: 238729  Cd Length: 187  Bit Score: 285.41  E-value: 3.92e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624   2 SNIEATIICIDNSDYNRNEDIVPNRFLSQIDCVNVLCCNKTSLHYKNNIGILMMAGDKIKVKVSLTNDIGQLLSCIHDIK 81
Cdd:cd01452    1 MVLEATMICIDNSEYMRNGDYPPTRFQAQADAVNLICQAKTRSNPENNVGLMTMAGNSPEVLVTLTNDQGKILSKLHDVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624  82 LDGTCDIIRSLLIAQLALKHRVDKNLDQKIILFIGSPFHVNEKQLINTGKQLKKNNISVDIISFGNIDKNRDKLMMLFES 161
Cdd:cd01452   81 PKGKANFITGIQIAQLALKHRQNKNQKQRIVAFVGSPIEEDEKDLVKLAKRLKKNNVSVDIINFGEIDDNTEKLTAFIDA 160

                        170       180
                 ....*....|....*....|....*..
gi 124512624 162 VNNNDNCRFIECPEYENNLSKFVLNSF 188
Cdd:cd01452  161 VNGKDGSHLVSVPPGENLLSDALLSSP 187
VWA_2 pfam13519
von Willebrand factor type A domain;
7-115 1.12e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624    7 TIICIDNSDYNRNEDIVPNRFLSQIDCVNVLCcnkTSLHyKNNIGILMMaGDKIKVKVSLTNDIGQLLSCIHDIK-LDGT 85
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALL---KSLP-GDRVGLVTF-GDGPEVLIPLTKDRAKILRALRRLEpKGGG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 124512624   86 CDIIRSLLIAQLALKHRvdKNLDQKIILFI 115
Cdd:pfam13519  76 TNLAAALQLARAALKHR--RKNQPRRIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 8-158 4.99e-05

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512624     8 IICIDNSdynrnEDIVPNRFLSQIDCVNVLCCNKTSLHYKNNIGILMMAGD-KIKVKVSLTNDIGQLLSCIHDIKLD--G 84
Cdd:smart00327   3 VFLLDGS-----GSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDaRVLFPLNDSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512624    85 TCDIIRSLLIAQLALKHRVDKNLD--QKIILFI--GSPfHVNEKQLINTGKQLKKNNISVDIISFGNiDKNRDKLMML 158
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRgaPKVVILItdGES-NDGPKDLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL 153
 
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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