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Conserved domains on  [gi|700258668|gb|AIU50940|]
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ARM repeat superfamily protein, partial [Cabomba caroliniana]

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 ...
5-254 6.94e-08

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: 53.64  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668    5 RIRIFSFTAKLFSISTVAASAvrRSGLLDVLVSEVNSSsDVLMTLSILEVLYELASTPHGSEYLLSSTLLQLLMSLIRTS 84
Cdd:pfam10508 177 RYRIYELAVERASISPTALCI--CTFLYDKLLSELDGD-DVLVQADAIELLTDLALSKHGLEYLAQRGVVDKISNLMERV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668   85 EGSVLKSRAIVILGRLLSSME------------DALSSISEILEDSDECIN--AIDAIGQIGASLKGAELL---FALMVE 147
Cdd:pfam10508 254 EEDPLGELYLPGIVKFFGYLAvmsplqvlktypDFLERLFRMIQSLDPTMRpvAMDTLGNLASSVEGKEVLefkNSGRLE 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668  148 HVIRTAFLRKGRAT---RLASLHALGSIVgeDRSTLSNPSEERLRKLIYETAAASSkLTPSgILHSVLQQDAEIRLAAYR 224
Cdd:pfam10508 334 KTLKAIGAHAKSGSvelKKRTLQAITSIF--YNKTEQQTEDLAIAESWYELLAGKA-LENV-IRDNVKQPFPELKCAALD 409
                         250       260       270
                  ....*....|....*....|....*....|
gi 700258668  225 VIAGLVVRPWFLLEVCLKGEFIDIITDETT 254
Cdd:pfam10508 410 FLQQIAKYPWGVQLMINTPGFVEFLLDRKT 439
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
5-254 6.94e-08

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: 53.64  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668    5 RIRIFSFTAKLFSISTVAASAvrRSGLLDVLVSEVNSSsDVLMTLSILEVLYELASTPHGSEYLLSSTLLQLLMSLIRTS 84
Cdd:pfam10508 177 RYRIYELAVERASISPTALCI--CTFLYDKLLSELDGD-DVLVQADAIELLTDLALSKHGLEYLAQRGVVDKISNLMERV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668   85 EGSVLKSRAIVILGRLLSSME------------DALSSISEILEDSDECIN--AIDAIGQIGASLKGAELL---FALMVE 147
Cdd:pfam10508 254 EEDPLGELYLPGIVKFFGYLAvmsplqvlktypDFLERLFRMIQSLDPTMRpvAMDTLGNLASSVEGKEVLefkNSGRLE 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668  148 HVIRTAFLRKGRAT---RLASLHALGSIVgeDRSTLSNPSEERLRKLIYETAAASSkLTPSgILHSVLQQDAEIRLAAYR 224
Cdd:pfam10508 334 KTLKAIGAHAKSGSvelKKRTLQAITSIF--YNKTEQQTEDLAIAESWYELLAGKA-LENV-IRDNVKQPFPELKCAALD 409
                         250       260       270
                  ....*....|....*....|....*....|
gi 700258668  225 VIAGLVVRPWFLLEVCLKGEFIDIITDETT 254
Cdd:pfam10508 410 FLQQIAKYPWGVQLMINTPGFVEFLLDRKT 439
 
Name Accession Description Interval E-value
Proteasom_PSMB pfam10508
Proteasome non-ATPase 26S subunit; The 26S proteasome, a eukaryotic ATP-dependent, dumb-bell ...
5-254 6.94e-08

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: 53.64  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668    5 RIRIFSFTAKLFSISTVAASAvrRSGLLDVLVSEVNSSsDVLMTLSILEVLYELASTPHGSEYLLSSTLLQLLMSLIRTS 84
Cdd:pfam10508 177 RYRIYELAVERASISPTALCI--CTFLYDKLLSELDGD-DVLVQADAIELLTDLALSKHGLEYLAQRGVVDKISNLMERV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668   85 EGSVLKSRAIVILGRLLSSME------------DALSSISEILEDSDECIN--AIDAIGQIGASLKGAELL---FALMVE 147
Cdd:pfam10508 254 EEDPLGELYLPGIVKFFGYLAvmsplqvlktypDFLERLFRMIQSLDPTMRpvAMDTLGNLASSVEGKEVLefkNSGRLE 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700258668  148 HVIRTAFLRKGRAT---RLASLHALGSIVgeDRSTLSNPSEERLRKLIYETAAASSkLTPSgILHSVLQQDAEIRLAAYR 224
Cdd:pfam10508 334 KTLKAIGAHAKSGSvelKKRTLQAITSIF--YNKTEQQTEDLAIAESWYELLAGKA-LENV-IRDNVKQPFPELKCAALD 409
                         250       260       270
                  ....*....|....*....|....*....|
gi 700258668  225 VIAGLVVRPWFLLEVCLKGEFIDIITDETT 254
Cdd:pfam10508 410 FLQQIAKYPWGVQLMINTPGFVEFLLDRKT 439
 
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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