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Conserved domains on  [gi|194376632|dbj|BAG57462|]
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unnamed protein product [Homo sapiens]

Protein Classification

proteasome inhibitor PI31 family protein( domain architecture ID 10569006)

proteasome inhibitor PI31 family protein plays an important role in control of proteasome function; it inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI31_Prot_N pfam11566
PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome ...
 11-117 1.03e-30

PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome which is an inhibitor of the 20 S proteasome in vitro.PI31 is also an F-box protein Fbxo7.Skp1 binding partner which requires an N terminal FP domain in both proteins for the interaction to occur via the FP beta sheets. The structure of PI31 FP domain contains a novel alpha/beta-fold and two intermolecular contact surfaces. This is the N-terminal domain of the members.


:

Pssm-ID: 463296  Cd Length: 156  Bit Score: 110.07  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376632   11 AAPAITCRQDALACFLHWEVVTHGYCGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194376632   85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEHL 117
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAL 113
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 124-186 9.06e-08

PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of proteasome-mediated antigen processing.


:

Pssm-ID: 430086  Cd Length: 80  Bit Score: 47.82  E-value: 9.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194376632  124 DPLgPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 186
Cdd:pfam08577  15 DPL-RGPGGLPRPGGGGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-VPPGARFDPFGP 80
 
Name Accession Description Interval E-value
PI31_Prot_N pfam11566
PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome ...
 11-117 1.03e-30

PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome which is an inhibitor of the 20 S proteasome in vitro.PI31 is also an F-box protein Fbxo7.Skp1 binding partner which requires an N terminal FP domain in both proteins for the interaction to occur via the FP beta sheets. The structure of PI31 FP domain contains a novel alpha/beta-fold and two intermolecular contact surfaces. This is the N-terminal domain of the members.


Pssm-ID: 463296  Cd Length: 156  Bit Score: 110.07  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376632   11 AAPAITCRQDALACFLHWEVVTHGYCGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194376632   85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEHL 117
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAL 113
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 124-186 9.06e-08

PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of proteasome-mediated antigen processing.


Pssm-ID: 430086  Cd Length: 80  Bit Score: 47.82  E-value: 9.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194376632  124 DPLgPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 186
Cdd:pfam08577  15 DPL-RGPGGLPRPGGGGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-VPPGARFDPFGP 80
 
Name Accession Description Interval E-value
PI31_Prot_N pfam11566
PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome ...
 11-117 1.03e-30

PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome which is an inhibitor of the 20 S proteasome in vitro.PI31 is also an F-box protein Fbxo7.Skp1 binding partner which requires an N terminal FP domain in both proteins for the interaction to occur via the FP beta sheets. The structure of PI31 FP domain contains a novel alpha/beta-fold and two intermolecular contact surfaces. This is the N-terminal domain of the members.


Pssm-ID: 463296  Cd Length: 156  Bit Score: 110.07  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376632   11 AAPAITCRQDALACFLHWEVVTHGYCGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194376632   85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEHL 117
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAL 113
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 124-186 9.06e-08

PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of proteasome-mediated antigen processing.


Pssm-ID: 430086  Cd Length: 80  Bit Score: 47.82  E-value: 9.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194376632  124 DPLgPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 186
Cdd:pfam08577  15 DPL-RGPGGLPRPGGGGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-VPPGARFDPFGP 80
 
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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