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Conserved domains on  [gi|974005338|ref|NP_001305746|]
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large ribosomal subunit protein uL18m isoform 2 [Homo sapiens]

Protein Classification

uL18 family ribosomal protein( domain architecture ID 227)

uL18 family ribosomal protein such as bacteria 50S ribosomal protein L18, chloroplast 50S ribosomal protein L18, and mitochondrial 39S ribosomal protein L18.

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_L18_L5e super family cl00379
Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of ...
68-109 3.16e-10

Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of the large subunit. L18 binds 5S rRNA and induces a conformational change that stimulates the binding of L5 to 5S rRNA. Association of 5S rRNA with 23S rRNA depends on the binding of L18 and L5 to 5S rRNA. L18/L5e is generally described as L18 in prokaryotes and archaea, and as L5e (or L5) in eukaryotes. In bacteria, the CP proteins L5, L18, and L25 are required for the ribosome to incorporate 5S rRNA into the large subunit, one of the last steps in ribosome assembly. In archaea, both L18 and L5 bind 5S rRNA; in eukaryotes, only the L18 homolog (L5e) binds 5S rRNA but a homolog to L5 is also identified.


The actual alignment was detected with superfamily member cd00432:

Pssm-ID: 444873  Cd Length: 103  Bit Score: 53.31  E-value: 3.16e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 974005338  68 WRTVFPSREFWHRLRVIRTQHHVEALVEH-QNGKVVVSASTHE 109
Cdd:cd00432    1 RRRKRLGTQERPRLVVRKSNKHIYAQIIDdSGDKTLVSASTLE 43
 
Name Accession Description Interval E-value
Ribosomal_L18_L5e cd00432
Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of ...
68-109 3.16e-10

Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of the large subunit. L18 binds 5S rRNA and induces a conformational change that stimulates the binding of L5 to 5S rRNA. Association of 5S rRNA with 23S rRNA depends on the binding of L18 and L5 to 5S rRNA. L18/L5e is generally described as L18 in prokaryotes and archaea, and as L5e (or L5) in eukaryotes. In bacteria, the CP proteins L5, L18, and L25 are required for the ribosome to incorporate 5S rRNA into the large subunit, one of the last steps in ribosome assembly. In archaea, both L18 and L5 bind 5S rRNA; in eukaryotes, only the L18 homolog (L5e) binds 5S rRNA but a homolog to L5 is also identified.


Pssm-ID: 238246  Cd Length: 103  Bit Score: 53.31  E-value: 3.16e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 974005338  68 WRTVFPSREFWHRLRVIRTQHHVEALVEH-QNGKVVVSASTHE 109
Cdd:cd00432    1 RRRKRLGTQERPRLVVRKSNKHIYAQIIDdSGDKTLVSASTLE 43
 
Name Accession Description Interval E-value
Ribosomal_L18_L5e cd00432
Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of ...
68-109 3.16e-10

Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein found in the central protuberance (CP) of the large subunit. L18 binds 5S rRNA and induces a conformational change that stimulates the binding of L5 to 5S rRNA. Association of 5S rRNA with 23S rRNA depends on the binding of L18 and L5 to 5S rRNA. L18/L5e is generally described as L18 in prokaryotes and archaea, and as L5e (or L5) in eukaryotes. In bacteria, the CP proteins L5, L18, and L25 are required for the ribosome to incorporate 5S rRNA into the large subunit, one of the last steps in ribosome assembly. In archaea, both L18 and L5 bind 5S rRNA; in eukaryotes, only the L18 homolog (L5e) binds 5S rRNA but a homolog to L5 is also identified.


Pssm-ID: 238246  Cd Length: 103  Bit Score: 53.31  E-value: 3.16e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 974005338  68 WRTVFPSREFWHRLRVIRTQHHVEALVEH-QNGKVVVSASTHE 109
Cdd:cd00432    1 RRRKRLGTQERPRLVVRKSNKHIYAQIIDdSGDKTLVSASTLE 43
 
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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