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Conserved domains on  [gi|968090841|ref|XP_015024280|]
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proteasome inhibitor PI31 subunit [Drosophila virilis]

Protein Classification

PI31_Prot_N domain-containing protein( domain architecture ID 10568993)

PI31_Prot_N domain-containing protein

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 ...
 32-166 2.70e-33

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: 118.93  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968090841   32 IDKKADVLMVLAHFLLTKHyKFRCVGIGDDKTLPED----EVGSELLPDHWNGDSSKYSLRYVHNKVL--YLLLGHITED 105
Cdd:pfam11566   5 LKSPYDALALLVHACMTAL-GFRLVGLGEDKKIEESpselQSLAPRLPPGWNAGSGSYAFRYAHKQSSmeYLLKVDRLGN 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968090841  106 ALIVNLLDINTKNVSNICITPESLVAEVK------------GGITKIMPTATDIVERFRKELCDPVFTGNSRE 166
Cdd:pfam11566  84 KLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdeklGDLFISYPRLEDLISLFKSNIIQKLVPGLRKE 156
 
Name Accession Description Interval E-value
PI31_Prot_N pfam11566
PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome ...
 32-166 2.70e-33

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: 118.93  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968090841   32 IDKKADVLMVLAHFLLTKHyKFRCVGIGDDKTLPED----EVGSELLPDHWNGDSSKYSLRYVHNKVL--YLLLGHITED 105
Cdd:pfam11566   5 LKSPYDALALLVHACMTAL-GFRLVGLGEDKKIEESpselQSLAPRLPPGWNAGSGSYAFRYAHKQSSmeYLLKVDRLGN 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968090841  106 ALIVNLLDINTKNVSNICITPESLVAEVK------------GGITKIMPTATDIVERFRKELCDPVFTGNSRE 166
Cdd:pfam11566  84 KLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdeklGDLFISYPRLEDLISLFKSNIIQKLVPGLRKE 156
 
Name Accession Description Interval E-value
PI31_Prot_N pfam11566
PI31 proteasome regulator N-terminal; PI31 is a regulatory subunit of the immuno-proteasome ...
 32-166 2.70e-33

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: 118.93  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968090841   32 IDKKADVLMVLAHFLLTKHyKFRCVGIGDDKTLPED----EVGSELLPDHWNGDSSKYSLRYVHNKVL--YLLLGHITED 105
Cdd:pfam11566   5 LKSPYDALALLVHACMTAL-GFRLVGLGEDKKIEESpselQSLAPRLPPGWNAGSGSYAFRYAHKQSSmeYLLKVDRLGN 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968090841  106 ALIVNLLDINTKNVSNICITPESLVAEVK------------GGITKIMPTATDIVERFRKELCDPVFTGNSRE 166
Cdd:pfam11566  84 KLVINGLALGDDKVASFEINVKDYVSSSAlplredrsdeklGDLFISYPRLEDLISLFKSNIIQKLVPGLRKE 156
 
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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