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Conserved domains on  [gi|1243913942]
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Chain Y, 39S ribosomal protein L47, mitochondrial

Protein Classification

ribosomal protein L29 family protein( domain architecture ID 10536699)

ribosomal protein L29 family protein such as mammalian mitochondrial 39S ribosomal protein L47 and fungal mitochondrial 54S ribosomal protein L4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 64-149 2.93e-41

Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal region (approximately 8 residues) of the eukaryotic mitochondrial 39-S ribosomal protein L47 (MRP-L47). Mitochondrial ribosomal proteins (MRPs) are the counterparts of the cytoplasmic ribosomal proteins, in that they fulfil similar functions in protein biosynthesis. However, they are distinct in number, features and primary structure.


:

Pssm-ID: 369158  Cd Length: 86  Bit Score: 136.41  E-value: 2.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243913942  64 LEEFFDDPKNWGQEKVKSGAAWTCQQLRNKSNEDLHKLWYVLLKERNMLLTLEQEAKRQRLPMPSPERLDKVVDSMDALD 143
Cdd:pfam06984   1 LEEFFDDKKNWPEEEVKVGRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMENIK 80


                  ....*.
gi 1243913942 144 KVVQER 149
Cdd:pfam06984  81 TVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 64-149 2.93e-41

Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal region (approximately 8 residues) of the eukaryotic mitochondrial 39-S ribosomal protein L47 (MRP-L47). Mitochondrial ribosomal proteins (MRPs) are the counterparts of the cytoplasmic ribosomal proteins, in that they fulfil similar functions in protein biosynthesis. However, they are distinct in number, features and primary structure.


Pssm-ID: 369158  Cd Length: 86  Bit Score: 136.41  E-value: 2.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243913942  64 LEEFFDDPKNWGQEKVKSGAAWTCQQLRNKSNEDLHKLWYVLLKERNMLLTLEQEAKRQRLPMPSPERLDKVVDSMDALD 143
Cdd:pfam06984   1 LEEFFDDKKNWPEEEVKVGRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMENIK 80


                  ....*.
gi 1243913942 144 KVVQER 149
Cdd:pfam06984  81 TVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 64-149 2.93e-41

Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal region (approximately 8 residues) of the eukaryotic mitochondrial 39-S ribosomal protein L47 (MRP-L47). Mitochondrial ribosomal proteins (MRPs) are the counterparts of the cytoplasmic ribosomal proteins, in that they fulfil similar functions in protein biosynthesis. However, they are distinct in number, features and primary structure.


Pssm-ID: 369158  Cd Length: 86  Bit Score: 136.41  E-value: 2.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243913942  64 LEEFFDDPKNWGQEKVKSGAAWTCQQLRNKSNEDLHKLWYVLLKERNMLLTLEQEAKRQRLPMPSPERLDKVVDSMDALD 143
Cdd:pfam06984   1 LEEFFDDKKNWPEEEVKVGRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMENIK 80


                  ....*.
gi 1243913942 144 KVVQER 149
Cdd:pfam06984  81 TVLRER 86
 
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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