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Conserved domains on  [gi|48526512|ref|NP_079820|]
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small ribosomal subunit protein uS15m precursor [Mus musculus]

Protein Classification

uS15 family ribosomal protein( domain architecture ID 11092050)

uS15 family ribosomal protein such as metazoan mitochondrial 28S ribosomal protein S15, fungal mitochondrial 37S ribosomal protein S28, and bacterial 30S ribosomal protein S15.

Gene Ontology:  GO:0003723|GO:0003735|GO:0006412
PubMed:  24524803

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_S15 pfam00312
Ribosomal protein S15;
110-187 6.19e-23

Ribosomal protein S15;


:

Pssm-ID: 459756  Cd Length: 81  Bit Score: 89.02  E-value: 6.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48526512   110 EQLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELG 187
Cdd:pfam00312   2 QEIIKEFGRHPGDTGSPEVQIALLTERINNLTEHLKEHKKDKHSRRGLLKLVGKRRRLLKYLKRKDVERYRYLIEKLG 79
 
Name Accession Description Interval E-value
Ribosomal_S15 pfam00312
Ribosomal protein S15;
110-187 6.19e-23

Ribosomal protein S15;


Pssm-ID: 459756  Cd Length: 81  Bit Score: 89.02  E-value: 6.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48526512   110 EQLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELG 187
Cdd:pfam00312   2 QEIIKEFGRHPGDTGSPEVQIALLTERINNLTEHLKEHKKDKHSRRGLLKLVGKRRRLLKYLKRKDVERYRYLIEKLG 79
Ribosomal_S15p_S13e cd00353
Ribosomal protein S15 (prokaryotic)_S13 (eukaryotic) binds the central domain of 16S rRNA and ...
 108-187 3.95e-19

Ribosomal protein S15 (prokaryotic)_S13 (eukaryotic) binds the central domain of 16S rRNA and is required for assembly of the small ribosomal subunit and for intersubunit association, thus representing a key element in the assembly of the whole ribosome. S15 also plays an important autoregulatory role by binding and preventing its own mRNA from being translated. S15 has a predominantly alpha-helical fold that is highly structured except for the N-terminal alpha helix.


Pssm-ID: 238213  Cd Length: 80  Bit Score: 79.08  E-value: 3.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512 108 KQEQLMNKIVENPeDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELG 187
Cdd:cd00353   2 KQEILKEFGLAEG-DTGSPEVQLALLTERIVNLTEHLEKNKKDKHSKRGLLLLVSKRRRLLKYLKRKDRLRYEWLIEKLG 80
RpsO COG0184
Ribosomal protein S15P/S13E [Translation, ribosomal structure and biogenesis]; Ribosomal ...
 98-189 6.50e-10

Ribosomal protein S15P/S13E [Translation, ribosomal structure and biogenesis]; Ribosomal protein S15P/S13E is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 439954  Cd Length: 89  Bit Score: 54.68  E-value: 6.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512  98 MASRKEKlkiKQEqLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYD 177
Cdd:COG0184   1 MPLTKEE---KEE-IIKEYGRHEGDTGSPEVQIALLTERINNLTEHLKEHKKDHHSRRGLLKMVGKRRRLLDYLKKKDIE 76

                        90
                ....*....|..
gi 48526512 178 VFEKTCKELGVE 189
Cdd:COG0184  77 RYRALIAKLGLR 88
PTZ00119 PTZ00119
40S ribosomal protein S15; Provisional
 82-192 1.11e-09

40S ribosomal protein S15; Provisional


Pssm-ID: 240278  Cd Length: 302  Bit Score: 57.65  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512   82 NIEKVDDVVKRILSLEMASRKEKLKIKQEQLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSI 161
Cdd:PTZ00119  83 DIKHLRKNIINMLHLNCANSKQIHKYKKLCIRRCLQRRPFDTGSAPVQIGCLTEKILNLRAHLILRCKDHPKKRTMSILL 162

                         90       100       110
                 ....*....|....*....|....*....|.
gi 48526512  162 DRRKKLLKILRQTNYDVFEKTCKELGVEYTL 192
Cdd:PTZ00119 163 ARRQKLMKYLYKTDFELYKHTCNLLKIKCIL 193
 
Name Accession Description Interval E-value
Ribosomal_S15 pfam00312
Ribosomal protein S15;
110-187 6.19e-23

Ribosomal protein S15;


Pssm-ID: 459756  Cd Length: 81  Bit Score: 89.02  E-value: 6.19e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48526512   110 EQLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELG 187
Cdd:pfam00312   2 QEIIKEFGRHPGDTGSPEVQIALLTERINNLTEHLKEHKKDKHSRRGLLKLVGKRRRLLKYLKRKDVERYRYLIEKLG 79
Ribosomal_S15p_S13e cd00353
Ribosomal protein S15 (prokaryotic)_S13 (eukaryotic) binds the central domain of 16S rRNA and ...
 108-187 3.95e-19

Ribosomal protein S15 (prokaryotic)_S13 (eukaryotic) binds the central domain of 16S rRNA and is required for assembly of the small ribosomal subunit and for intersubunit association, thus representing a key element in the assembly of the whole ribosome. S15 also plays an important autoregulatory role by binding and preventing its own mRNA from being translated. S15 has a predominantly alpha-helical fold that is highly structured except for the N-terminal alpha helix.


Pssm-ID: 238213  Cd Length: 80  Bit Score: 79.08  E-value: 3.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512 108 KQEQLMNKIVENPeDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELG 187
Cdd:cd00353   2 KQEILKEFGLAEG-DTGSPEVQLALLTERIVNLTEHLEKNKKDKHSKRGLLLLVSKRRRLLKYLKRKDRLRYEWLIEKLG 80
RpsO COG0184
Ribosomal protein S15P/S13E [Translation, ribosomal structure and biogenesis]; Ribosomal ...
 98-189 6.50e-10

Ribosomal protein S15P/S13E [Translation, ribosomal structure and biogenesis]; Ribosomal protein S15P/S13E is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 439954  Cd Length: 89  Bit Score: 54.68  E-value: 6.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512  98 MASRKEKlkiKQEqLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYD 177
Cdd:COG0184   1 MPLTKEE---KEE-IIKEYGRHEGDTGSPEVQIALLTERINNLTEHLKEHKKDHHSRRGLLKMVGKRRRLLDYLKKKDIE 76

                        90
                ....*....|..
gi 48526512 178 VFEKTCKELGVE 189
Cdd:COG0184  77 RYRALIAKLGLR 88
PTZ00119 PTZ00119
40S ribosomal protein S15; Provisional
 82-192 1.11e-09

40S ribosomal protein S15; Provisional


Pssm-ID: 240278  Cd Length: 302  Bit Score: 57.65  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48526512   82 NIEKVDDVVKRILSLEMASRKEKLKIKQEQLMNKIVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSI 161
Cdd:PTZ00119  83 DIKHLRKNIINMLHLNCANSKQIHKYKKLCIRRCLQRRPFDTGSAPVQIGCLTEKILNLRAHLILRCKDHPKKRTMSILL 162

                         90       100       110
                 ....*....|....*....|....*....|.
gi 48526512  162 DRRKKLLKILRQTNYDVFEKTCKELGVEYTL 192
Cdd:PTZ00119 163 ARRQKLMKYLYKTDFELYKHTCNLLKIKCIL 193
S15_NS1_EPRS_RNA-bind cd00677
S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, ...
 127-172 4.61e-09

S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic aminoacyl tRNA synthetases (aaRSs), where it occurs as a single or a repeated unit. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions in the formation of tRNA-synthetases into multienzyme complexes. While this domain lacks significant sequence similarity between the subgroups in which it is found, they share similar electrostatic surface potentials and thus are likely to bind to RNA via the same mechanism.


Pssm-ID: 238361  Cd Length: 46  Bit Score: 50.97  E-value: 4.61e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 48526512 127 EAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILR 172
Cdd:cd00677   1 EVQIALLTERIRNLKEHLAKNKKDKHSKRGLDLLVSKRLRLLKYLK 46
rps15 CHL00027
ribosomal protein S15
 116-188 1.59e-04

ribosomal protein S15


Pssm-ID: 214339  Cd Length: 90  Bit Score: 39.56  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48526512  116 IVENPEDSRTLEAQIIALTVRIRNYEEHMQKHRKDKAHKRHLLMSIDRRKKLLKILRQTNYDVFEKTCKELGV 188
Cdd:CHL00027  12 QEEKEENRGSVEFQVFSFTNKIRRLTSHLELHKKDYSSQRGLRKILGKRQRLLAYLSKKNRVRYKKLISQLGI 84
 
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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