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Conserved domains on  [gi|116006497|ref|NP_013416|]
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mitochondrial 54S ribosomal protein YmL15 [Saccharomyces cerevisiae S288C]

Protein Classification

RIBOc domain-containing protein( domain architecture ID 10650201)

RIBOc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RIBOc smart00535
Ribonuclease III family;
85-221 1.19e-24

Ribonuclease III family;


:

Pssm-ID: 197778  Cd Length: 129  Bit Score: 94.98  E-value: 1.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497    85 ELILQCLTHKSFAHgSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAEsceNGQLSLQFSNLGtkfakeltSKNTACTFVK 164
Cdd:smart00535   1 SLLLRALTHASYSN-EHEHNERLEFLGDAVLELVVTEYLYKKYPDLS---EGDLSRLRSALV--------SNETLARLAK 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116006497   165 LHNLDPFIFWKMRDPIKDGhiNGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLL 221
Cdd:smart00535  69 KLGLGEFIRLGRGEAISGG--RDKPKILADVFEALIGAIYLDSGLEAAREFIRDLLG 123
 
Name Accession Description Interval E-value
RIBOc smart00535
Ribonuclease III family;
85-221 1.19e-24

Ribonuclease III family;


Pssm-ID: 197778  Cd Length: 129  Bit Score: 94.98  E-value: 1.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497    85 ELILQCLTHKSFAHgSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAEsceNGQLSLQFSNLGtkfakeltSKNTACTFVK 164
Cdd:smart00535   1 SLLLRALTHASYSN-EHEHNERLEFLGDAVLELVVTEYLYKKYPDLS---EGDLSRLRSALV--------SNETLARLAK 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116006497   165 LHNLDPFIFWKMRDPIKDGhiNGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLL 221
Cdd:smart00535  69 KLGLGEFIRLGRGEAISGG--RDKPKILADVFEALIGAIYLDSGLEAAREFIRDLLG 123
RIBOc cd00593
RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and ...
85-229 4.80e-19

RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosomal RNA precursors. Prokaryotic RNAse III also plays a role in the maturation of tRNA precursors and in the processing of phage and plasmid transcripts. Eukaryotic RNase III's participate (through direct cleavage) in rRNA processing, in processing of small nucleolar RNAs (snoRNAs) and snRNA's (components of the spliceosome). In eukaryotes RNase III or RNaseIII like enzymes such as Dicer are involved in RNAi (RNA interference) and miRNA (micro-RNA) gene silencing.


Pssm-ID: 238333  Cd Length: 133  Bit Score: 80.35  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497  85 ELILQCLTHKSFA-HGSKPYNEKLNLLGAQFLKLQTCIHSLKNGSpaeSCENGQLSLQFSNLgtkfakelTSKNTACTFV 163
Cdd:cd00593    1 SLLLEALTHPSYAnEHGRFNNERLEFLGDAVLELVVTEYLFKKFP---DLSEGDLTRLRSAL--------VSNETLARLA 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116006497 164 KLHNLDPFIFWKMRDPIKDGHINgeTTIFASVLNAFIGAILSTNGSEKAAKFIQGSLLDKEDLHSL 229
Cdd:cd00593   70 RELGLGKYLRLGKGEEKSGGRLR--PKILADVFEALIGAIYLDGGFEAARKFLLRLLGPLIEEISL 133
Ribonucleas_3_3 pfam14622
Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA ...
84-221 1.14e-15

Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA processing. They probably also cleave a stem-loop structure at the 3' end of U2 snRNA to ensure formation of the correct U2 3' end; they are involved in polyadenylation-independent transcription termination. Some members may be mitochondrial ribosomal protein subunit L15, others may be 60S ribosomal protein L3.


Pssm-ID: 434075  Cd Length: 127  Bit Score: 71.05  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497   84 NELILQCLTHKSFAHGSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAEscenGQLSLQFSNLGT-----KFAKELtsknt 158
Cdd:pfam14622   1 EELLLQALTHKSYANGRKPYNERLEFLGDAVLELSVSEYLFKKPDLDE----GGLTKLRASIVSeeslaEIAREI----- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116006497  159 actfvklhNLDPFIFWkmRDPIKDGHINGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLL 221
Cdd:pfam14622  72 --------GLGKYLRL--GKGEEETGGSGRESILADALEALIGAIYLDGGFEVAKEFILKKIL 124
 
Name Accession Description Interval E-value
RIBOc smart00535
Ribonuclease III family;
85-221 1.19e-24

Ribonuclease III family;


Pssm-ID: 197778  Cd Length: 129  Bit Score: 94.98  E-value: 1.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497    85 ELILQCLTHKSFAHgSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAEsceNGQLSLQFSNLGtkfakeltSKNTACTFVK 164
Cdd:smart00535   1 SLLLRALTHASYSN-EHEHNERLEFLGDAVLELVVTEYLYKKYPDLS---EGDLSRLRSALV--------SNETLARLAK 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116006497   165 LHNLDPFIFWKMRDPIKDGhiNGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLL 221
Cdd:smart00535  69 KLGLGEFIRLGRGEAISGG--RDKPKILADVFEALIGAIYLDSGLEAAREFIRDLLG 123
RIBOc cd00593
RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and ...
85-229 4.80e-19

RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosomal RNA precursors. Prokaryotic RNAse III also plays a role in the maturation of tRNA precursors and in the processing of phage and plasmid transcripts. Eukaryotic RNase III's participate (through direct cleavage) in rRNA processing, in processing of small nucleolar RNAs (snoRNAs) and snRNA's (components of the spliceosome). In eukaryotes RNase III or RNaseIII like enzymes such as Dicer are involved in RNAi (RNA interference) and miRNA (micro-RNA) gene silencing.


Pssm-ID: 238333  Cd Length: 133  Bit Score: 80.35  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497  85 ELILQCLTHKSFA-HGSKPYNEKLNLLGAQFLKLQTCIHSLKNGSpaeSCENGQLSLQFSNLgtkfakelTSKNTACTFV 163
Cdd:cd00593    1 SLLLEALTHPSYAnEHGRFNNERLEFLGDAVLELVVTEYLFKKFP---DLSEGDLTRLRSAL--------VSNETLARLA 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116006497 164 KLHNLDPFIFWKMRDPIKDGHINgeTTIFASVLNAFIGAILSTNGSEKAAKFIQGSLLDKEDLHSL 229
Cdd:cd00593   70 RELGLGKYLRLGKGEEKSGGRLR--PKILADVFEALIGAIYLDGGFEAARKFLLRLLGPLIEEISL 133
Ribonucleas_3_3 pfam14622
Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA ...
84-221 1.14e-15

Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA processing. They probably also cleave a stem-loop structure at the 3' end of U2 snRNA to ensure formation of the correct U2 3' end; they are involved in polyadenylation-independent transcription termination. Some members may be mitochondrial ribosomal protein subunit L15, others may be 60S ribosomal protein L3.


Pssm-ID: 434075  Cd Length: 127  Bit Score: 71.05  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497   84 NELILQCLTHKSFAHGSKPYNEKLNLLGAQFLKLQTCIHSLKNGSPAEscenGQLSLQFSNLGT-----KFAKELtsknt 158
Cdd:pfam14622   1 EELLLQALTHKSYANGRKPYNERLEFLGDAVLELSVSEYLFKKPDLDE----GGLTKLRASIVSeeslaEIAREI----- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116006497  159 actfvklhNLDPFIFWkmRDPIKDGHINGETTIFASVLNAFIGAILSTNGSEKAAKFIQGSLL 221
Cdd:pfam14622  72 --------GLGKYLRL--GKGEEETGGSGRESILADALEALIGAIYLDGGFEVAKEFILKKIL 124
Ribonuclease_3 pfam00636
Ribonuclease III domain;
105-208 3.02e-06

Ribonuclease III domain;


Pssm-ID: 459883  Cd Length: 101  Bit Score: 44.57  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006497  105 EKLNLLGAQFLKLQTCIHSLKNGSPAEScenGQLslqfsnlgTKFAKELTSKNTACTFVKLHNLDPFIFWKMRDPIKDG- 183
Cdd:pfam00636   1 ERLEFLGDAVLELYVREYLFEKFPDLRE---GDL--------HRLRSALVSNEALAKLARKLGLEKFLTEEELDIRRRNn 69
                          90       100       110
                  ....*....|....*....|....*....|..
gi 116006497  184 -------HINGETTIFASVLNAFIGAILSTNG 208
Cdd:pfam00636  70 algkgpkRADGKEKVLADAFEALIGALYLDGG 101
 
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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