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Conserved domains on  [gi|398364875|ref|NP_012931|]
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mitochondrial 54S ribosomal protein YmL13 [Saccharomyces cerevisiae S288C]

Protein Classification

mL50 family ribosomal protein( domain architecture ID 10564704)

mL50 family ribosomal protein similar to Saccharomyces cerevisiae 54S ribosomal protein L13, which is a component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_L50 pfam10501
Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger ...
 124-229 1.22e-20

Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger mitochondrial 66S or 70S units. Under conditions of ethanol-stress in rats the larger subunit is largely dissociated into its smaller components. In E. coli, in the absence of the enzyme pseudouridine synthase (RluD) synthase, there is an accumulation of 50S and 30S subunits and the appearance of abnormal particles (62S and 39S), with concomitant loss of 70S ribosomes.


:

Pssm-ID: 402226  Cd Length: 109  Bit Score: 84.25  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364875  124 TSDNQLDDMILQATEKTLGKVDQ------DVQFSDLVAKFQFTKFLQSKSGYLIPDYELTTLSTPLQFKRYIKEKIlpsa 197
Cdd:pfam10501   2 SESEELDEIVAETYSEAFGAPGDgdkgflSLSLDDLSFKFAFLKRLQQLTGHDIPDYKLTKLHTVADLVNYLEEVL---- 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 398364875  198 nDPKLA-YKEAEPNAIHPFSDNYASPNIYVVND 229
Cdd:pfam10501  78 -SPKPKkLAERLPNAIVLRREDFKLPNVYINEE 109
 
Name Accession Description Interval E-value
Ribosomal_L50 pfam10501
Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger ...
 124-229 1.22e-20

Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger mitochondrial 66S or 70S units. Under conditions of ethanol-stress in rats the larger subunit is largely dissociated into its smaller components. In E. coli, in the absence of the enzyme pseudouridine synthase (RluD) synthase, there is an accumulation of 50S and 30S subunits and the appearance of abnormal particles (62S and 39S), with concomitant loss of 70S ribosomes.


Pssm-ID: 402226  Cd Length: 109  Bit Score: 84.25  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364875  124 TSDNQLDDMILQATEKTLGKVDQ------DVQFSDLVAKFQFTKFLQSKSGYLIPDYELTTLSTPLQFKRYIKEKIlpsa 197
Cdd:pfam10501   2 SESEELDEIVAETYSEAFGAPGDgdkgflSLSLDDLSFKFAFLKRLQQLTGHDIPDYKLTKLHTVADLVNYLEEVL---- 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 398364875  198 nDPKLA-YKEAEPNAIHPFSDNYASPNIYVVND 229
Cdd:pfam10501  78 -SPKPKkLAERLPNAIVLRREDFKLPNVYINEE 109
 
Name Accession Description Interval E-value
Ribosomal_L50 pfam10501
Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger ...
 124-229 1.22e-20

Ribosomal subunit 39S; The 39S ribosomal protein appears to be a subunit of one of the larger mitochondrial 66S or 70S units. Under conditions of ethanol-stress in rats the larger subunit is largely dissociated into its smaller components. In E. coli, in the absence of the enzyme pseudouridine synthase (RluD) synthase, there is an accumulation of 50S and 30S subunits and the appearance of abnormal particles (62S and 39S), with concomitant loss of 70S ribosomes.


Pssm-ID: 402226  Cd Length: 109  Bit Score: 84.25  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364875  124 TSDNQLDDMILQATEKTLGKVDQ------DVQFSDLVAKFQFTKFLQSKSGYLIPDYELTTLSTPLQFKRYIKEKIlpsa 197
Cdd:pfam10501   2 SESEELDEIVAETYSEAFGAPGDgdkgflSLSLDDLSFKFAFLKRLQQLTGHDIPDYKLTKLHTVADLVNYLEEVL---- 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 398364875  198 nDPKLA-YKEAEPNAIHPFSDNYASPNIYVVND 229
Cdd:pfam10501  78 -SPKPKkLAERLPNAIVLRREDFKLPNVYINEE 109
 
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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