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Conserved domains on  [gi|1243457568|ref|NP_001342473|]
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26S proteasome non-ATPase regulatory subunit 5 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Proteasom_PSMB super family cl28774
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
1-330 2.25e-178

Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell shaped, protease complex with a molecular mass of approx 20kDa consists of a central 20S proteasome,functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles,composed of multiple subunits of 25- 110 kDa attached to the central portion in opposite orientations. It is responsible for degradation of abnormal intracellular proteins, including oxidatively damaged proteins, and may play a role as a component of a cellular anti-oxidative system. Expression of catalytic core subunits including PSMB5 and peptidase activities of the proteasome were elevated following incubation with 3-methylcholanthrene. The 20S proteasome comprises a cylindrical stack of four rings, two outer rings formed by seven alpha-subunits (alpha1-alpha7) and two inner rings of seven beta-subunits (beta1-beta7). Two outer rings of alpha subunits maintain structure, while the central beta rings contain the proteolytic active core subunits beta1 (PSMB6), beta2 (PSMB7), and beta5 (PSMB5). Expression of PSMB5 can be altered by chemical reactants, such as 3-methylcholanthrene.


The actual alignment was detected with superfamily member pfam10508:

Pssm-ID: 463124  Cd Length: 499  Bit Score: 503.17  E-value: 2.25e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568   1 MKTNDVVRYRVYELIIDISSVSSESLNYCTTsgLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQIS 80
Cdd:pfam10508 170 LKTNDIVRYRIYELAVERASISPTALCICTF--LYDKLLSELDGDDVLVQADAIELLTDLALSKHGLEYLAQRGVVDKIS 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568  81 NIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDPTMIGVAVDTVGILGSSVEGKQVL-Q 159
Cdd:pfam10508 248 NLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDPTMRPVAMDTLGNLASSVEGKEVLeF 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 160 KTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWFSSMSRDSLE-LFRGISNQPFPELHC 238
Cdd:pfam10508 327 KNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWYELLAGKALEnVIRDNVKQPFPELKC 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 239 AALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLRLRAYLSEGPYYV 318
Cdd:pfam10508 406 AALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLSEASQIFADPELIRLKAYLREGPYYV 485
                         330
                  ....*....|....
gi 1243457568 319 KPVATTAVE--GAD 330
Cdd:pfam10508 486 QAVAAVATEprGAE 499
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
1-330 2.25e-178

Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell shaped, protease complex with a molecular mass of approx 20kDa consists of a central 20S proteasome,functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles,composed of multiple subunits of 25- 110 kDa attached to the central portion in opposite orientations. It is responsible for degradation of abnormal intracellular proteins, including oxidatively damaged proteins, and may play a role as a component of a cellular anti-oxidative system. Expression of catalytic core subunits including PSMB5 and peptidase activities of the proteasome were elevated following incubation with 3-methylcholanthrene. The 20S proteasome comprises a cylindrical stack of four rings, two outer rings formed by seven alpha-subunits (alpha1-alpha7) and two inner rings of seven beta-subunits (beta1-beta7). Two outer rings of alpha subunits maintain structure, while the central beta rings contain the proteolytic active core subunits beta1 (PSMB6), beta2 (PSMB7), and beta5 (PSMB5). Expression of PSMB5 can be altered by chemical reactants, such as 3-methylcholanthrene.


Pssm-ID: 463124  Cd Length: 499  Bit Score: 503.17  E-value: 2.25e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568   1 MKTNDVVRYRVYELIIDISSVSSESLNYCTTsgLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQIS 80
Cdd:pfam10508 170 LKTNDIVRYRIYELAVERASISPTALCICTF--LYDKLLSELDGDDVLVQADAIELLTDLALSKHGLEYLAQRGVVDKIS 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568  81 NIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDPTMIGVAVDTVGILGSSVEGKQVL-Q 159
Cdd:pfam10508 248 NLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDPTMRPVAMDTLGNLASSVEGKEVLeF 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 160 KTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWFSSMSRDSLE-LFRGISNQPFPELHC 238
Cdd:pfam10508 327 KNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWYELLAGKALEnVIRDNVKQPFPELKC 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 239 AALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLRLRAYLSEGPYYV 318
Cdd:pfam10508 406 AALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLSEASQIFADPELIRLKAYLREGPYYV 485
                         330
                  ....*....|....
gi 1243457568 319 KPVATTAVE--GAD 330
Cdd:pfam10508 486 QAVAAVATEprGAE 499
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
1-330 2.25e-178

Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell shaped, protease complex with a molecular mass of approx 20kDa consists of a central 20S proteasome,functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles,composed of multiple subunits of 25- 110 kDa attached to the central portion in opposite orientations. It is responsible for degradation of abnormal intracellular proteins, including oxidatively damaged proteins, and may play a role as a component of a cellular anti-oxidative system. Expression of catalytic core subunits including PSMB5 and peptidase activities of the proteasome were elevated following incubation with 3-methylcholanthrene. The 20S proteasome comprises a cylindrical stack of four rings, two outer rings formed by seven alpha-subunits (alpha1-alpha7) and two inner rings of seven beta-subunits (beta1-beta7). Two outer rings of alpha subunits maintain structure, while the central beta rings contain the proteolytic active core subunits beta1 (PSMB6), beta2 (PSMB7), and beta5 (PSMB5). Expression of PSMB5 can be altered by chemical reactants, such as 3-methylcholanthrene.


Pssm-ID: 463124  Cd Length: 499  Bit Score: 503.17  E-value: 2.25e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568   1 MKTNDVVRYRVYELIIDISSVSSESLNYCTTsgLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQIS 80
Cdd:pfam10508 170 LKTNDIVRYRIYELAVERASISPTALCICTF--LYDKLLSELDGDDVLVQADAIELLTDLALSKHGLEYLAQRGVVDKIS 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568  81 NIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDPTMIGVAVDTVGILGSSVEGKQVL-Q 159
Cdd:pfam10508 248 NLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDPTMRPVAMDTLGNLASSVEGKEVLeF 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 160 KTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWFSSMSRDSLE-LFRGISNQPFPELHC 238
Cdd:pfam10508 327 KNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWYELLAGKALEnVIRDNVKQPFPELKC 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457568 239 AALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLRLRAYLSEGPYYV 318
Cdd:pfam10508 406 AALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLSEASQIFADPELIRLKAYLREGPYYV 485
                         330
                  ....*....|....
gi 1243457568 319 KPVATTAVE--GAD 330
Cdd:pfam10508 486 QAVAAVATEprGAE 499
 
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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