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Conserved domains on  [gi|6323472|ref|NP_013544|]
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mitochondrial 54S ribosomal protein YmL4 [Saccharomyces cerevisiae S288C]

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 ...
 68-159 4.33e-30

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: 109.45  E-value: 4.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323472     68 LWQFFSNKKfirsadDLPPSSHI--RPWSIPELRHKSFNDLHSLWYNCLREQNVL-ARENHLLKNIVGsthDEFSELSNS 144
Cdd:pfam06984   1 LEEFFDDKK------NWPEEEVKvgRAWPAEELRHKSFNDLHKLWYVCLKEKNMLlTMEQELLRNQEV---MPSPERLDK 71

                          90
                  ....*....|....*
gi 6323472    145 IRTTMWQIRHVLNER 159
Cdd:pfam06984  72 VKISMENIKTVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 68-159 4.33e-30

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: 109.45  E-value: 4.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323472     68 LWQFFSNKKfirsadDLPPSSHI--RPWSIPELRHKSFNDLHSLWYNCLREQNVL-ARENHLLKNIVGsthDEFSELSNS 144
Cdd:pfam06984   1 LEEFFDDKK------NWPEEEVKvgRAWPAEELRHKSFNDLHKLWYVCLKEKNMLlTMEQELLRNQEV---MPSPERLDK 71

                          90
                  ....*....|....*
gi 6323472    145 IRTTMWQIRHVLNER 159
Cdd:pfam06984  72 VKISMENIKTVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 68-159 4.33e-30

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: 109.45  E-value: 4.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323472     68 LWQFFSNKKfirsadDLPPSSHI--RPWSIPELRHKSFNDLHSLWYNCLREQNVL-ARENHLLKNIVGsthDEFSELSNS 144
Cdd:pfam06984   1 LEEFFDDKK------NWPEEEVKvgRAWPAEELRHKSFNDLHKLWYVCLKEKNMLlTMEQELLRNQEV---MPSPERLDK 71

                          90
                  ....*....|....*
gi 6323472    145 IRTTMWQIRHVLNER 159
Cdd:pfam06984  72 VKISMENIKTVLRER 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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