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Conserved domains on  [gi|499840292|ref|WP_011521026|]
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ribonuclease P protein component [Candidatus Korobacter versatilis]

Protein Classification

ribonuclease P protein component( domain architecture ID 10467140)

ribonuclease P catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'terminus, and can also cleave other RNA substrates such as 4.5S RNA

CATH:  3.30.230.10
EC:  3.1.26.5
PubMed:  12831883
SCOP:  4000954

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ribonuclease_P pfam00825
Ribonuclease P;
18-126 3.67e-27

Ribonuclease P;


:

Pssm-ID: 425888  Cd Length: 107  Bit Score: 97.65  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292   18 KASRLLRHADFRLVYEQGRRHFSANFTAFYRANITEKSPRIGYTVSRALGGAVDRNRMKRRLREATRACWAGFRPtfAVD 97
Cdd:pfam00825   1 KKERLKKRSEFQRVFRKGKRVASRHFVLYYLPNDLDHPPRLGISVSKKVGKAVVRNRIKRLIREAFRLNKDELPP--GLD 78
                          90       100
                  ....*....|....*....|....*....
gi 499840292   98 VVVNPKKTVLATDFAVLTAEMQKALTVIE 126
Cdd:pfam00825  79 IVVIARPGAADADFAELLKELEKLLKKAG 107
 
Name Accession Description Interval E-value
Ribonuclease_P pfam00825
Ribonuclease P;
18-126 3.67e-27

Ribonuclease P;


Pssm-ID: 425888  Cd Length: 107  Bit Score: 97.65  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292   18 KASRLLRHADFRLVYEQGRRHFSANFTAFYRANITEKSPRIGYTVSRALGGAVDRNRMKRRLREATRACWAGFRPtfAVD 97
Cdd:pfam00825   1 KKERLKKRSEFQRVFRKGKRVASRHFVLYYLPNDLDHPPRLGISVSKKVGKAVVRNRIKRLIREAFRLNKDELPP--GLD 78
                          90       100
                  ....*....|....*....|....*....
gi 499840292   98 VVVNPKKTVLATDFAVLTAEMQKALTVIE 126
Cdd:pfam00825  79 IVVIARPGAADADFAELLKELEKLLKKAG 107
RnpA COG0594
RNase P protein component [Translation, ribosomal structure and biogenesis];
22-122 9.12e-25

RNase P protein component [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440359  Cd Length: 99  Bit Score: 91.34  E-value: 9.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292  22 LLRHADFRLVYEQGRRHFSANFTAFYRANiTEKSPRIGYTVSRALGGAVDRNRMKRRLREATRACWAGFRPtfAVDVVVN 101
Cdd:COG0594    1 LKKRKDFQRVFRKGKRVSSRYFVLYYLPN-DLDPPRLGFSVSKKVGNAVVRNRIKRRLREAFRLNKPELPP--GYDIVVI 77
                         90       100
                 ....*....|....*....|.
gi 499840292 102 PKKTVLATDFAVLTAEMQKAL 122
Cdd:COG0594   78 ARPGAAELDFAELEKELEKLL 98
rnpA TIGR00188
ribonuclease P protein component, eubacterial; This peptide is the protein component of a ...
18-126 3.27e-12

ribonuclease P protein component, eubacterial; This peptide is the protein component of a ribonucleoprotein that cleaves the leader sequence from each tRNA precursor to leave the mature 5'-terminus. The catalytic site is in the RNA component, M1 RNA. The yeast mitochondrial RNase P protein component gene RPM2 has no obvious sequence similarity to rnpA, but resembles eukaryotic nuclear RNase P instead. [Transcription, RNA processing]


Pssm-ID: 211560  Cd Length: 111  Bit Score: 59.25  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292   18 KASRLLRHADFRLVYEQGRRHFSANFTAFYRANITeKSPRIGYTVSR-ALGGAVDRNRMKRRLREATRACWAGFRptfAV 96
Cdd:TIGR00188   3 KPRRLRLKSEFQKVFQQGTRAFNPFLTIYVLKNEL-DHPRVGLSVSKkKVKNAVERNRIKRLIREVFRERQEELK---AL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 499840292   97 DVVVNPKKTVLATDFAVLTAEMQKALTVIE 126
Cdd:TIGR00188  79 DVVVIVRKGFSELTYEALLKLLLQLFLRCK 108
rnpA PRK03459
ribonuclease P; Reviewed
16-80 2.14e-06

ribonuclease P; Reviewed


Pssm-ID: 235126  Cd Length: 122  Bit Score: 44.40  E-value: 2.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499840292  16 IPKASRLLRHADFRLVYEQGRRHFSANFT--AFYRANITE----KSPRIGYTVSRALGGAVDRNRMKRRLR 80
Cdd:PRK03459   2 LPEQHKLRSSMQFRTTVRKGRRAGRRTVVvhLFDSAEAGEvasfGGPRFGLVVSKAVGNAVIRHRVSRRLR 72
 
Name Accession Description Interval E-value
Ribonuclease_P pfam00825
Ribonuclease P;
18-126 3.67e-27

Ribonuclease P;


Pssm-ID: 425888  Cd Length: 107  Bit Score: 97.65  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292   18 KASRLLRHADFRLVYEQGRRHFSANFTAFYRANITEKSPRIGYTVSRALGGAVDRNRMKRRLREATRACWAGFRPtfAVD 97
Cdd:pfam00825   1 KKERLKKRSEFQRVFRKGKRVASRHFVLYYLPNDLDHPPRLGISVSKKVGKAVVRNRIKRLIREAFRLNKDELPP--GLD 78
                          90       100
                  ....*....|....*....|....*....
gi 499840292   98 VVVNPKKTVLATDFAVLTAEMQKALTVIE 126
Cdd:pfam00825  79 IVVIARPGAADADFAELLKELEKLLKKAG 107
RnpA COG0594
RNase P protein component [Translation, ribosomal structure and biogenesis];
22-122 9.12e-25

RNase P protein component [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440359  Cd Length: 99  Bit Score: 91.34  E-value: 9.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292  22 LLRHADFRLVYEQGRRHFSANFTAFYRANiTEKSPRIGYTVSRALGGAVDRNRMKRRLREATRACWAGFRPtfAVDVVVN 101
Cdd:COG0594    1 LKKRKDFQRVFRKGKRVSSRYFVLYYLPN-DLDPPRLGFSVSKKVGNAVVRNRIKRRLREAFRLNKPELPP--GYDIVVI 77
                         90       100
                 ....*....|....*....|.
gi 499840292 102 PKKTVLATDFAVLTAEMQKAL 122
Cdd:COG0594   78 ARPGAAELDFAELEKELEKLL 98
rnpA TIGR00188
ribonuclease P protein component, eubacterial; This peptide is the protein component of a ...
18-126 3.27e-12

ribonuclease P protein component, eubacterial; This peptide is the protein component of a ribonucleoprotein that cleaves the leader sequence from each tRNA precursor to leave the mature 5'-terminus. The catalytic site is in the RNA component, M1 RNA. The yeast mitochondrial RNase P protein component gene RPM2 has no obvious sequence similarity to rnpA, but resembles eukaryotic nuclear RNase P instead. [Transcription, RNA processing]


Pssm-ID: 211560  Cd Length: 111  Bit Score: 59.25  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499840292   18 KASRLLRHADFRLVYEQGRRHFSANFTAFYRANITeKSPRIGYTVSR-ALGGAVDRNRMKRRLREATRACWAGFRptfAV 96
Cdd:TIGR00188   3 KPRRLRLKSEFQKVFQQGTRAFNPFLTIYVLKNEL-DHPRVGLSVSKkKVKNAVERNRIKRLIREVFRERQEELK---AL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 499840292   97 DVVVNPKKTVLATDFAVLTAEMQKALTVIE 126
Cdd:TIGR00188  79 DVVVIVRKGFSELTYEALLKLLLQLFLRCK 108
rnpA PRK03459
ribonuclease P; Reviewed
16-80 2.14e-06

ribonuclease P; Reviewed


Pssm-ID: 235126  Cd Length: 122  Bit Score: 44.40  E-value: 2.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499840292  16 IPKASRLLRHADFRLVYEQGRRHFSANFT--AFYRANITE----KSPRIGYTVSRALGGAVDRNRMKRRLR 80
Cdd:PRK03459   2 LPEQHKLRSSMQFRTTVRKGRRAGRRTVVvhLFDSAEAGEvasfGGPRFGLVVSKAVGNAVIRHRVSRRLR 72
 
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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