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Conserved domains on  [gi|1039761706|ref|XP_017174701|]
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26S proteasome non-ATPase regulatory subunit 5 isoform X1 [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 ...
1-275 5.58e-146

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: 418.42  E-value: 5.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706   1 MVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDP 80
Cdd:pfam10508 223 LLTDLALSKHGLEYLAQRGVVDKISNLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDP 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706  81 TMIGVAVDTVGILGSSVEGKQVL-QKTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWF 159
Cdd:pfam10508 302 TMRPVAMDTLGNLASSVEGKEVLeFKNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWY 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706 160 SSMSRDSLE-LFRGISNQPFPELHCAALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSK 238
Cdd:pfam10508 381 ELLAGKALEnVIRDNVKQPFPELKCAALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLS 460
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039761706 239 TVAEIFGNSNYLRLRAYLSEGPYYVKPVATTAVE--GAD 275
Cdd:pfam10508 461 EASQIFADPELIRLKAYLREGPYYVQAVAAVATEprGAE 499
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
1-275 5.58e-146

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: 418.42  E-value: 5.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706   1 MVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDP 80
Cdd:pfam10508 223 LLTDLALSKHGLEYLAQRGVVDKISNLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDP 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706  81 TMIGVAVDTVGILGSSVEGKQVL-QKTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWF 159
Cdd:pfam10508 302 TMRPVAMDTLGNLASSVEGKEVLeFKNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWY 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706 160 SSMSRDSLE-LFRGISNQPFPELHCAALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSK 238
Cdd:pfam10508 381 ELLAGKALEnVIRDNVKQPFPELKCAALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLS 460
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039761706 239 TVAEIFGNSNYLRLRAYLSEGPYYVKPVATTAVE--GAD 275
Cdd:pfam10508 461 EASQIFADPELIRLKAYLREGPYYVQAVAAVATEprGAE 499
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
1-275 5.58e-146

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: 418.42  E-value: 5.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706   1 MVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMdSPQQICERYPVFLEKVFEMADSQDP 80
Cdd:pfam10508 223 LLTDLALSKHGLEYLAQRGVVDKISNLMERVEEDPLGELYLPGIVKFFGYLAVM-SPLQVLKTYPDFLERLFRMIQSLDP 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706  81 TMIGVAVDTVGILGSSVEGKQVL-QKTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDfLGMTESWF 159
Cdd:pfam10508 302 TMRPVAMDTLGNLASSVEGKEVLeFKNSGRLEKTLKAIGAHAKSGSVELKKRTLQAITSIFYNKTEQQTED-LAIAESWY 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761706 160 SSMSRDSLE-LFRGISNQPFPELHCAALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSK 238
Cdd:pfam10508 381 ELLAGKALEnVIRDNVKQPFPELKCAALDFLQQIAKYPWGVQLMINTPGFVEFLLDRKTELHKEYKDRKYQLIKRLVHLS 460
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039761706 239 TVAEIFGNSNYLRLRAYLSEGPYYVKPVATTAVE--GAD 275
Cdd:pfam10508 461 EASQIFADPELIRLKAYLREGPYYVQAVAAVATEprGAE 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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