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Conserved domains on  [gi|1237938296|ref|NP_001341028|]
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PSME3-interacting protein isoform a [Homo sapiens]

Protein Classification

PSME3-interacting protein( domain architecture ID 12103847)

PSME3-interacting protein promotes the association of the proteasome activator complex subunit PSME3 with the 20S proteasome and regulates its activity

Gene Ontology:  GO:0032091|GO:1901799

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAM192A_Fyv6_N pfam10187
FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30 ...
 15-103 3.57e-33

FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30/FAM192A protein and the fungal Fyv6 protein. PIP30/FAM192A acts as a regulator PA28-gamma, a nuclear activator of the 20S proteasome. PIP30 favors PA28-gamma interaction with the 20S proteasome while inhibiting its association with coilin, a central component of nuclear Cajal bodies. Fyv6 is involved in telomere length regulation and required for survival upon exposure to K1 killer toxin. It promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase.


:

Pssm-ID: 462987 [Multi-domain]  Cd Length: 102  Bit Score: 116.15  E-value: 3.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938296  15 FVSEAELDERRKRRQEEWEKVRKPEDPEECPEEVYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVS 94
Cdd:pfam10187   1 FVSESELEEAREKRQEEWEKARAELEPEEEPEEEYDGRSLYERLQENKAAKQEEFEEKLKLKNQFRGLDEDEAEFLDEVE 80


                  ....*....
gi 1237938296  95 RQQELIEKQ 103
Cdd:pfam10187  81 EKKREEERR 89
 
Name Accession Description Interval E-value
FAM192A_Fyv6_N pfam10187
FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30 ...
 15-103 3.57e-33

FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30/FAM192A protein and the fungal Fyv6 protein. PIP30/FAM192A acts as a regulator PA28-gamma, a nuclear activator of the 20S proteasome. PIP30 favors PA28-gamma interaction with the 20S proteasome while inhibiting its association with coilin, a central component of nuclear Cajal bodies. Fyv6 is involved in telomere length regulation and required for survival upon exposure to K1 killer toxin. It promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase.


Pssm-ID: 462987 [Multi-domain]  Cd Length: 102  Bit Score: 116.15  E-value: 3.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938296  15 FVSEAELDERRKRRQEEWEKVRKPEDPEECPEEVYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVS 94
Cdd:pfam10187   1 FVSESELEEAREKRQEEWEKARAELEPEEEPEEEYDGRSLYERLQENKAAKQEEFEEKLKLKNQFRGLDEDEAEFLDEVE 80


                  ....*....
gi 1237938296  95 RQQELIEKQ 103
Cdd:pfam10187  81 EKKREEERR 89
 
Name Accession Description Interval E-value
FAM192A_Fyv6_N pfam10187
FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30 ...
 15-103 3.57e-33

FAM192A/Fyv6, N-terminal domain; This is a the N-terminal domain of the mammalian PIP30/FAM192A protein and the fungal Fyv6 protein. PIP30/FAM192A acts as a regulator PA28-gamma, a nuclear activator of the 20S proteasome. PIP30 favors PA28-gamma interaction with the 20S proteasome while inhibiting its association with coilin, a central component of nuclear Cajal bodies. Fyv6 is involved in telomere length regulation and required for survival upon exposure to K1 killer toxin. It promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase.


Pssm-ID: 462987 [Multi-domain]  Cd Length: 102  Bit Score: 116.15  E-value: 3.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938296  15 FVSEAELDERRKRRQEEWEKVRKPEDPEECPEEVYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVS 94
Cdd:pfam10187   1 FVSESELEEAREKRQEEWEKARAELEPEEEPEEEYDGRSLYERLQENKAAKQEEFEEKLKLKNQFRGLDEDEAEFLDEVE 80


                  ....*....
gi 1237938296  95 RQQELIEKQ 103
Cdd:pfam10187  81 EKKREEERR 89
 
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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