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Conserved domains on  [gi|21356545|ref|NP_650073|]
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ribosomal protein L24-like [Drosophila melanogaster]

Protein Classification

ribosomal eL24 family protein( domain architecture ID 11112902)

ribosomal L24e family protein such as 60S ribosomal protein L24 and ribosome biogenesis protein RLP24

PubMed:  24524803

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_L24e pfam01246
Ribosomal protein L24e;
2-64 4.19e-34

Ribosomal protein L24e;


:

Pssm-ID: 460131  Cd Length: 63  Bit Score: 115.32  E-value: 4.19e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356545     2 RIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKELA 64
Cdd:pfam01246   1 KTETCSFSGYKIYPGHGKRFVRNDGKVFRFCSSKCEKLFKQKRNPRKLKWTKAYRRAHKKELT 63
 
Name Accession Description Interval E-value
Ribosomal_L24e pfam01246
Ribosomal protein L24e;
2-64 4.19e-34

Ribosomal protein L24e;


Pssm-ID: 460131  Cd Length: 63  Bit Score: 115.32  E-value: 4.19e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356545     2 RIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKELA 64
Cdd:pfam01246   1 KTETCSFSGYKIYPGHGKRFVRNDGKVFRFCSSKCEKLFKQKRNPRKLKWTKAYRRAHKKELT 63
Ribosomal_L24e_L24 cd00472
Ribosomal protein L24e/L24 is a ribosomal protein found in eukaryotes (L24) and in archaea ...
 1-54 1.11e-27

Ribosomal protein L24e/L24 is a ribosomal protein found in eukaryotes (L24) and in archaea (L24e, distinct from archaeal L24). L24e/L24 is located on the surface of the large subunit, adjacent to proteins L14 and L3, and near the translation factor binding site. L24e/L24 appears to play a role in the kinetics of peptide synthesis, and may be involved in interactions between the large and small subunits, either directly or through other factors. In mouse, a deletion mutation in L24 has been identified as the cause for the belly spot and tail (Bst) mutation that results in disrupted pigmentation, somitogenesis and retinal cell fate determination. L24 may be an important protein in eukaryotic reproduction: in shrimp, L24 expression is elevated in the ovary, suggesting a role in oogenesis, and in Arabidopsis, L24 has been proposed to have a specific function in gynoecium development. No protein with sequence or structural homology to L24e/L24 has been identified in bacteria, but a functionally equivalent protein may exist. Bacterial L19 forms an interprotein beta sheet with L14 that is similar to the L24e/L14 interprotein beta sheet observed in the archaeal L24e structures. Some eukaryotic L24 proteins were initially identified as L30, and this alignment model contains several sequences called L30.


Pssm-ID: 100103  Cd Length: 54  Bit Score: 98.80  E-value: 1.11e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21356545   1 MRIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKA 54
Cdd:cd00472   1 MKTEKCSFCGYKIYPGHGKMYVRNDGKVFRFCSSKCEKNFLRKRNPRKLKWTVA 54
RPL24A COG2075
Ribosomal protein L24E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ...
 1-62 1.71e-17

Ribosomal protein L24E [Translation, ribosomal structure and biogenesis]; Ribosomal protein L24E is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 441678  Cd Length: 63  Bit Score: 72.64  E-value: 1.71e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356545   1 MRIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKE 62
Cdd:COG2075   2 VETRTCSFCGREIEPGTGKMYVRNDGTVLWFCSSKCEKNMKLGRDPRKLKWTRKYRKGKEKR 63
PRK00807 PRK00807
50S ribosomal protein L24e; Validated
 3-54 1.61e-13

50S ribosomal protein L24e; Validated


Pssm-ID: 179131  Cd Length: 52  Bit Score: 61.92  E-value: 1.61e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21356545    3 IQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKA 54
Cdd:PRK00807   1 TRTCSFCGKEIEPGTGKMYVKKDGTILYFCSSKCEKNYKLGRVPRKLKWTKA 52
TRASH smart00746
metallochaperone-like domain;
6-44 4.15e-08

metallochaperone-like domain;


Pssm-ID: 214799  Cd Length: 39  Bit Score: 47.37  E-value: 4.15e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 21356545      6 CYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKK 44
Cdd:smart00746   1 CSFCGKDIYNPGTGIMVVNDGKVYYFCSSKCLSKFKKKR 39
 
Name Accession Description Interval E-value
Ribosomal_L24e pfam01246
Ribosomal protein L24e;
2-64 4.19e-34

Ribosomal protein L24e;


Pssm-ID: 460131  Cd Length: 63  Bit Score: 115.32  E-value: 4.19e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356545     2 RIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKELA 64
Cdd:pfam01246   1 KTETCSFSGYKIYPGHGKRFVRNDGKVFRFCSSKCEKLFKQKRNPRKLKWTKAYRRAHKKELT 63
Ribosomal_L24e_L24 cd00472
Ribosomal protein L24e/L24 is a ribosomal protein found in eukaryotes (L24) and in archaea ...
 1-54 1.11e-27

Ribosomal protein L24e/L24 is a ribosomal protein found in eukaryotes (L24) and in archaea (L24e, distinct from archaeal L24). L24e/L24 is located on the surface of the large subunit, adjacent to proteins L14 and L3, and near the translation factor binding site. L24e/L24 appears to play a role in the kinetics of peptide synthesis, and may be involved in interactions between the large and small subunits, either directly or through other factors. In mouse, a deletion mutation in L24 has been identified as the cause for the belly spot and tail (Bst) mutation that results in disrupted pigmentation, somitogenesis and retinal cell fate determination. L24 may be an important protein in eukaryotic reproduction: in shrimp, L24 expression is elevated in the ovary, suggesting a role in oogenesis, and in Arabidopsis, L24 has been proposed to have a specific function in gynoecium development. No protein with sequence or structural homology to L24e/L24 has been identified in bacteria, but a functionally equivalent protein may exist. Bacterial L19 forms an interprotein beta sheet with L14 that is similar to the L24e/L14 interprotein beta sheet observed in the archaeal L24e structures. Some eukaryotic L24 proteins were initially identified as L30, and this alignment model contains several sequences called L30.


Pssm-ID: 100103  Cd Length: 54  Bit Score: 98.80  E-value: 1.11e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21356545   1 MRIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKA 54
Cdd:cd00472   1 MKTEKCSFCGYKIYPGHGKMYVRNDGKVFRFCSSKCEKNFLRKRNPRKLKWTVA 54
RPL24A COG2075
Ribosomal protein L24E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ...
 1-62 1.71e-17

Ribosomal protein L24E [Translation, ribosomal structure and biogenesis]; Ribosomal protein L24E is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 441678  Cd Length: 63  Bit Score: 72.64  E-value: 1.71e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356545   1 MRIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKE 62
Cdd:COG2075   2 VETRTCSFCGREIEPGTGKMYVRNDGTVLWFCSSKCEKNMKLGRDPRKLKWTRKYRKGKEKR 63
PRK00807 PRK00807
50S ribosomal protein L24e; Validated
 3-54 1.61e-13

50S ribosomal protein L24e; Validated


Pssm-ID: 179131  Cd Length: 52  Bit Score: 61.92  E-value: 1.61e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21356545    3 IQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKA 54
Cdd:PRK00807   1 TRTCSFCGKEIEPGTGKMYVKKDGTILYFCSSKCEKNYKLGRVPRKLKWTKA 52
PRK14891 PRK14891
50S ribosomal protein L24e/unknown domain fusion protein; Provisional
 2-64 1.16e-10

50S ribosomal protein L24e/unknown domain fusion protein; Provisional


Pssm-ID: 184885 [Multi-domain]  Cd Length: 131  Bit Score: 56.88  E-value: 1.16e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356545    2 RIQTCYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRKAAGKELA 64
Cdd:PRK14891   3 ETRTCDYTGEEIEPGTGTMFVRKDGTVLHFVDSKCEKNYDLGREARDLEWTEAGRAEKGPAAA 65
TRASH smart00746
metallochaperone-like domain;
6-44 4.15e-08

metallochaperone-like domain;


Pssm-ID: 214799  Cd Length: 39  Bit Score: 47.37  E-value: 4.15e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 21356545      6 CYFCSSKIYPGHGVQFVRNDCKVFKFCRGKCHKAFKRKK 44
Cdd:smart00746   1 CSFCGKDIYNPGTGIMVVNDGKVYYFCSSKCLSKFKKKR 39
PTZ00033 PTZ00033
60S ribosomal protein L24; Provisional
 1-57 1.26e-07

60S ribosomal protein L24; Provisional


Pssm-ID: 140068  Cd Length: 125  Bit Score: 48.47  E-value: 1.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356545    1 MRIQTCYFCSSKIYPGHGVQFV----RNDCKVFKFCRGKCHKAFKRKKNPRKVGWTKAYRK 57
Cdd:PTZ00033   1 MRTIACEFSHFAVHPGHGRRYVpfafLSTKPVLTFLRPKCFALYMRKKNPRFLPWTRTYRR 61
 
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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