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Conserved domains on  [gi|398365235|ref|NP_009726|]
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ribonuclease P/MRP protein subunit POP7 [Saccharomyces cerevisiae S288C]

Protein Classification

ribonuclease P subunit p20 family protein( domain architecture ID 10574286)

ribonuclease P (RNase P) protein subunit p20 family protein similar to Homo sapiens ribonuclease P protein subunit p20 and Saccharomyces cerevisiae ribonucleases P/MRP protein subunit POP7, is an AlbA family DNA/RNA-binding protein that belongs to a family of small basic dimeric nucleic acid-binding proteins which may be regulated via acetylation/deacetylation

CATH:  3.30.110.20
Gene Ontology:  GO:0003676
PubMed:  26900088
SCOP:  3000507

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rpp20 pfam12328
Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is ...
 28-137 9.39e-34

Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is made up of at least nine protein subunits; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1. Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 (Rpp21) which is unique to RNase P. Human nuclear RNase P and MRP appear to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5, although there is recent evidence that not all of these subunits are shared between P and MRP. Archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins. In the yeast RNase P, Pop6 and Pop7 (the Rpp20 homolog) interact with each other and they are both interaction partners of Pop4; in the human MRP Rpp25 and Rpp20 interact with each other and Rpp25 binds to Rpp29 (Pop4).


:

Pssm-ID: 372048  Cd Length: 118  Bit Score: 114.31  E-value: 9.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365235   28 QIHTTIFVKSTTPYVSALKRINKFLDSVHKQ-------------GSSYVAVLGMGKAVEKTLALGCHFQDQKNKKIEVYT 94
Cdd:pfam12328   1 KVPKTIYVKSKTPFISAVKRIQKLLDKAEKRakgskknkgdeslKLEEVVVKGMGKAIEKALSLALWFQEKGNYKVDVRT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 398365235   95 KTIEVLDEVITEgqadiDMESDVEDDDKETQLKKRAVSGVELR 137
Cdd:pfam12328  81 GTVEVVDDIVEE-----DEEDEDDDDDEEPETRKRTVSAVEVR 118
 
Name Accession Description Interval E-value
Rpp20 pfam12328
Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is ...
 28-137 9.39e-34

Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is made up of at least nine protein subunits; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1. Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 (Rpp21) which is unique to RNase P. Human nuclear RNase P and MRP appear to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5, although there is recent evidence that not all of these subunits are shared between P and MRP. Archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins. In the yeast RNase P, Pop6 and Pop7 (the Rpp20 homolog) interact with each other and they are both interaction partners of Pop4; in the human MRP Rpp25 and Rpp20 interact with each other and Rpp25 binds to Rpp29 (Pop4).


Pssm-ID: 372048  Cd Length: 118  Bit Score: 114.31  E-value: 9.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365235   28 QIHTTIFVKSTTPYVSALKRINKFLDSVHKQ-------------GSSYVAVLGMGKAVEKTLALGCHFQDQKNKKIEVYT 94
Cdd:pfam12328   1 KVPKTIYVKSKTPFISAVKRIQKLLDKAEKRakgskknkgdeslKLEEVVVKGMGKAIEKALSLALWFQEKGNYKVDVRT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 398365235   95 KTIEVLDEVITEgqadiDMESDVEDDDKETQLKKRAVSGVELR 137
Cdd:pfam12328  81 GTVEVVDDIVEE-----DEEDEDDDDDEEPETRKRTVSAVEVR 118
 
Name Accession Description Interval E-value
Rpp20 pfam12328
Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is ...
 28-137 9.39e-34

Rpp20 subunit of nuclear RNase MRP and P; The nuclear RNase P of Saccharomyces cerevisiae is made up of at least nine protein subunits; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1. Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 (Rpp21) which is unique to RNase P. Human nuclear RNase P and MRP appear to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5, although there is recent evidence that not all of these subunits are shared between P and MRP. Archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins. In the yeast RNase P, Pop6 and Pop7 (the Rpp20 homolog) interact with each other and they are both interaction partners of Pop4; in the human MRP Rpp25 and Rpp20 interact with each other and Rpp25 binds to Rpp29 (Pop4).


Pssm-ID: 372048  Cd Length: 118  Bit Score: 114.31  E-value: 9.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365235   28 QIHTTIFVKSTTPYVSALKRINKFLDSVHKQ-------------GSSYVAVLGMGKAVEKTLALGCHFQDQKNKKIEVYT 94
Cdd:pfam12328   1 KVPKTIYVKSKTPFISAVKRIQKLLDKAEKRakgskknkgdeslKLEEVVVKGMGKAIEKALSLALWFQEKGNYKVDVRT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 398365235   95 KTIEVLDEVITEgqadiDMESDVEDDDKETQLKKRAVSGVELR 137
Cdd:pfam12328  81 GTVEVVDDIVEE-----DEEDEDDDDDEEPETRKRTVSAVEVR 118
 
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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