NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1020738621|ref|NP_001310338|]
View 

proteasome inhibitor PI31 subunit isoform 5 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 11-148 5.95e-37

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: 127.78  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738621  11 AAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1020738621  85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEH-----------LGDFHRTYKNSEELRSRIVSGIITPIHEQWEK 148
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdekLGDLFISYPRLEDLISLFKSNIIQKLVPGLRK 155
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 182-248 5.72e-09

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: 51.67  E-value: 5.72e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738621 182 PPWCDPLGPFVVGGEDLDPF--GPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 248
Cdd:pfam08577   8 PPGLGPHDPLRGPGGLPRPGggGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-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 ...
 11-148 5.95e-37

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: 127.78  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738621  11 AAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1020738621  85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEH-----------LGDFHRTYKNSEELRSRIVSGIITPIHEQWEK 148
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdekLGDLFISYPRLEDLISLFKSNIIQKLVPGLRK 155
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 182-248 5.72e-09

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: 51.67  E-value: 5.72e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738621 182 PPWCDPLGPFVVGGEDLDPF--GPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 248
Cdd:pfam08577   8 PPGLGPHDPLRGPGGLPRPGggGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-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 ...
 11-148 5.95e-37

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: 127.78  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738621  11 AAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSEL------LPAGWNNNKDLYVLRYEYKDGSRKLLVKAIT 84
Cdd:pfam11566   1 TSSDLKSPYDALALLVHACMTALGFRLVGLGEDKKIEESPSELqslaprLPPGWNAGSGSYAFRYAHKQSSMEYLLKVDR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1020738621  85 VESSMILNVLEYGSQQVADLTLNLDDYIDAEH-----------LGDFHRTYKNSEELRSRIVSGIITPIHEQWEK 148
Cdd:pfam11566  81 LGNKLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdekLGDLFISYPRLEDLISLFKSNIIQKLVPGLRK 155
PI31_Prot_C pfam08577
PI31 proteasome regulator; PI31 is a cellular regulator of proteasome formation and of ...
 182-248 5.72e-09

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: 51.67  E-value: 5.72e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738621 182 PPWCDPLGPFVVGGEDLDPF--GPRRGGMIVDPLRSGFPRALIDPSS-----GLPNRLPPGaVPPGARFDPFGP 248
Cdd:pfam08577   8 PPGLGPHDPLRGPGGLPRPGggGGGGGGMHPGPDHPLFGDPPNGPGGrggpsGPGPGFPPQ-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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH