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Conserved domains on  [gi|1734317114|ref|NP_001359789|]
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Large ribosomal subunit protein uL29m [Caenorhabditis elegans]

Protein Classification

uL29 family ribosomal protein( domain architecture ID 417)

uL29 family ribosomal protein such as archaeal 50S ribosomal protein L29, plasmodium 60S ribosomal protein L35, yeast mitochondrial 54S ribosomal protein L4, and chloroplast 50S ribosomal protein L29

Gene Ontology:  GO:0003735|GO:0006412
PubMed:  24524803

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_L29_HIP super family cl09943
Ribosomal L29 protein/HIP. L29 is a protein of the large ribosomal Subunit. A homolog, called ...
 47-134 4.25e-28

Ribosomal L29 protein/HIP. L29 is a protein of the large ribosomal Subunit. A homolog, called heparin/heparan sulfate interacting protein (HIP), has also been identified in mammals. L29 is located on the surface of the large ribosomal subunit, where it participates in forming a protein ring that surrounds the polypeptide exit channel, providing structural support for the ribosome. L29 is involved in forming the translocon binding site, along with L19, L22, L23, L24, and L31e. In addition, L29 and L23 form the interaction site for trigger factor (TF) on the ribosomal surface, adjacent to the exit tunnel. L29 forms numerous interactions with L23 and with the 23S rRNA. In some eukaryotes, L29 is referred to as L35, which is distinct from L35 found in bacteria and some eukaryotes (primarily plastids and mitochondria). The mammalian homolog, HIP, is found on the surface of many tissues and cell lines. It is believed to play a role in cell adhesion and modulation of blood coagulation. It has also been shown to inhibit apoptosis in cancer cells.


The actual alignment was detected with superfamily member pfam06984:

Pssm-ID: 471954  Cd Length: 86  Bit Score: 102.13  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734317114  47 QFFDDEANFGKAELRPkhrpGRSWTAEELRLKSNSDLHKLWYVCLKERNMLITMKKAHTSRARNMPNPERLDRVHETMDR 126
Cdd:pfam06984   3 EFFDDKKNWPEEEVKV----GRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMEN 78


                  ....*...
gi 1734317114 127 IESVVHER 134
Cdd:pfam06984  79 IKTVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 47-134 4.25e-28

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: 102.13  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734317114  47 QFFDDEANFGKAELRPkhrpGRSWTAEELRLKSNSDLHKLWYVCLKERNMLITMKKAHTSRARNMPNPERLDRVHETMDR 126
Cdd:pfam06984   3 EFFDDKKNWPEEEVKV----GRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMEN 78


                  ....*...
gi 1734317114 127 IESVVHER 134
Cdd:pfam06984  79 IKTVLRER 86
 
Name Accession Description Interval E-value
MRP-L47 pfam06984
Mitochondrial 39-S ribosomal protein L47 (MRP-L47); This family represents the N-terminal ...
 47-134 4.25e-28

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: 102.13  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734317114  47 QFFDDEANFGKAELRPkhrpGRSWTAEELRLKSNSDLHKLWYVCLKERNMLITMKKAHTSRARNMPNPERLDRVHETMDR 126
Cdd:pfam06984   3 EFFDDKKNWPEEEVKV----GRAWPAEELRHKSFNDLHKLWYVCLKEKNMLLTMEQELLRNQEVMPSPERLDKVKISMEN 78


                  ....*...
gi 1734317114 127 IESVVHER 134
Cdd:pfam06984  79 IKTVLRER 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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