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Conserved domains on  [gi|767939998|ref|XP_011512896|]
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proteasome assembly chaperone 4 isoform X2 [Homo sapiens]

Protein Classification

proteasome assembly chaperone 4 family protein( domain architecture ID 11240890)

proteasome assembly chaperone 4 (PAC-4) family protein similar to human PAC-4, also called PSMG4, that is a chaperone protein which promotes assembly of the 20S proteasome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAC4 pfam16093
Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes ...
 30-85 1.37e-14

Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes assembly of the 20S proteasome. It interacts with PSMG3. It associates with alpha subunits of the 20S proteasome. At the very C-terminal is a crucial HbYX or hydrophobic-tyrosine-X sequence motif that, in proteasome activators, opens the 20S proteasome entry pore.


:

Pssm-ID: 465017  Cd Length: 72  Bit Score: 62.97  E-value: 1.37e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939998   30 VMRLTDSLFLWVGAT--PHLRNLAVAMCSRYDSIP-VSTSLLGDT-SDTTSTGLAQRLGR 85
Cdd:pfam16093   1 LTKLAKSIFLWVGTAspEELGSLAVAMPTRYNSTPpLSTTLLGDPsSDDFSTRLAQRLAR 60
 
Name Accession Description Interval E-value
PAC4 pfam16093
Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes ...
 30-85 1.37e-14

Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes assembly of the 20S proteasome. It interacts with PSMG3. It associates with alpha subunits of the 20S proteasome. At the very C-terminal is a crucial HbYX or hydrophobic-tyrosine-X sequence motif that, in proteasome activators, opens the 20S proteasome entry pore.


Pssm-ID: 465017  Cd Length: 72  Bit Score: 62.97  E-value: 1.37e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939998   30 VMRLTDSLFLWVGAT--PHLRNLAVAMCSRYDSIP-VSTSLLGDT-SDTTSTGLAQRLGR 85
Cdd:pfam16093   1 LTKLAKSIFLWVGTAspEELGSLAVAMPTRYNSTPpLSTTLLGDPsSDDFSTRLAQRLAR 60
 
Name Accession Description Interval E-value
PAC4 pfam16093
Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes ...
 30-85 1.37e-14

Proteasome assembly chaperone 4; PAC4 or proteasome assembly chaperone 4 protein promotes assembly of the 20S proteasome. It interacts with PSMG3. It associates with alpha subunits of the 20S proteasome. At the very C-terminal is a crucial HbYX or hydrophobic-tyrosine-X sequence motif that, in proteasome activators, opens the 20S proteasome entry pore.


Pssm-ID: 465017  Cd Length: 72  Bit Score: 62.97  E-value: 1.37e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939998   30 VMRLTDSLFLWVGAT--PHLRNLAVAMCSRYDSIP-VSTSLLGDT-SDTTSTGLAQRLGR 85
Cdd:pfam16093   1 LTKLAKSIFLWVGTAspEELGSLAVAMPTRYNSTPpLSTTLLGDPsSDDFSTRLAQRLAR 60
 
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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