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Conserved domains on  [gi|767958696|ref|XP_011517487|]
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ribosome-recycling factor, mitochondrial isoform X2 [Homo sapiens]

Protein Classification

ribosome-recycling factor( domain architecture ID 10484758)

ribosome-recycling factor is responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
124-213 4.45e-24

Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) dissociates the ribosome from the mRNA after termination of translation, and is essential bacterial growth. Thus ribosomes are "recycled" and ready for another round of protein synthesis.


:

Pssm-ID: 460316  Cd Length: 158  Bit Score: 93.27  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696  124 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 203
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79
                          90
                  ....*....|
gi 767958696  204 PqsakwPMTQ 213
Cdd:pfam01765  80 P-----PLTE 84
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
124-213 4.45e-24

Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) dissociates the ribosome from the mRNA after termination of translation, and is essential bacterial growth. Thus ribosomes are "recycled" and ready for another round of protein synthesis.


Pssm-ID: 460316  Cd Length: 158  Bit Score: 93.27  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696  124 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 203
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79
                          90
                  ....*....|
gi 767958696  204 PqsakwPMTQ 213
Cdd:pfam01765  80 P-----PLTE 84
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
105-213 2.48e-19

Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination complex, composed of the ribosome, deacylated tRNA, and mRNA, after termination of translation. Thus ribosomes are "recycled" and ready for another round of protein synthesis. RRF is believed to bind the ribosome at the A-site in a manner that mimics tRNA, but the specific mechanisms remain unclear. RRF is essential for bacterial growth. It is not necessary for cell growth in archaea or eukaryotes, but is found in mitochondria or chloroplasts of some eukaryotic species.


Pssm-ID: 238288  Cd Length: 179  Bit Score: 81.54  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696 105 NLEEVNEEMKSVIEALKDNFNKTLNIRTSPGSLDKIaVVTADGK-LALNQISQISMKSPQLILVNMasFPECTAAAI-KA 182
Cdd:cd00520    1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSI-TVEYYGApTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKA 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767958696 183 IRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:cd00520   78 ILNSDLGLNPNNDGAVIRVNLP-----PLTE 103
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
100-213 5.61e-19

Ribosome recycling factor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440003  Cd Length: 185  Bit Score: 80.85  E-value: 5.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696 100 VEDIINleEVNEEMKSVIEALKDNFNKtlnIRT---SPGSLDKIAVVTADGKLALNQISQISMKSPQLILV-----NMAS 171
Cdd:COG0233    2 IDEILK--DAEEKMEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958696 172 fpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:COG0233   77 -------AIeKAIRKSDLGLNPSNDGNVIRIPIP-----PLTE 107
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
111-213 5.60e-13

ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or chloroplast forms might be expected but are not currently known. This protein was previously called ribosome releasing factor. By releasing ribosomes from mRNA at the end of protein biosynthesis, it prevents inappropriate translation from 3-prime regions of the mRNA and frees the ribosome for new rounds of translation. EGAD|53116|YHR038W is part of the frr superfamily. [Protein synthesis, Translation factors]


Pssm-ID: 129587  Cd Length: 176  Bit Score: 64.79  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696  111 EEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMN 189
Cdd:TIGR00496   2 ERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLG 79
                          90       100
                  ....*....|....*....|....
gi 767958696  190 LNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:TIGR00496  80 LNPNNDGSVIRVNFP-----PLTE 98
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
124-213 4.45e-24

Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) dissociates the ribosome from the mRNA after termination of translation, and is essential bacterial growth. Thus ribosomes are "recycled" and ready for another round of protein synthesis.


Pssm-ID: 460316  Cd Length: 158  Bit Score: 93.27  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696  124 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 203
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79
                          90
                  ....*....|
gi 767958696  204 PqsakwPMTQ 213
Cdd:pfam01765  80 P-----PLTE 84
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
105-213 2.48e-19

Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination complex, composed of the ribosome, deacylated tRNA, and mRNA, after termination of translation. Thus ribosomes are "recycled" and ready for another round of protein synthesis. RRF is believed to bind the ribosome at the A-site in a manner that mimics tRNA, but the specific mechanisms remain unclear. RRF is essential for bacterial growth. It is not necessary for cell growth in archaea or eukaryotes, but is found in mitochondria or chloroplasts of some eukaryotic species.


Pssm-ID: 238288  Cd Length: 179  Bit Score: 81.54  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696 105 NLEEVNEEMKSVIEALKDNFNKTLNIRTSPGSLDKIaVVTADGK-LALNQISQISMKSPQLILVNMasFPECTAAAI-KA 182
Cdd:cd00520    1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSI-TVEYYGApTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKA 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767958696 183 IRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:cd00520   78 ILNSDLGLNPNNDGAVIRVNLP-----PLTE 103
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
100-213 5.61e-19

Ribosome recycling factor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440003  Cd Length: 185  Bit Score: 80.85  E-value: 5.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696 100 VEDIINleEVNEEMKSVIEALKDNFNKtlnIRT---SPGSLDKIAVVTADGKLALNQISQISMKSPQLILV-----NMAS 171
Cdd:COG0233    2 IDEILK--DAEEKMEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958696 172 fpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:COG0233   77 -------AIeKAIRKSDLGLNPSNDGNVIRIPIP-----PLTE 107
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
111-213 5.60e-13

ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or chloroplast forms might be expected but are not currently known. This protein was previously called ribosome releasing factor. By releasing ribosomes from mRNA at the end of protein biosynthesis, it prevents inappropriate translation from 3-prime regions of the mRNA and frees the ribosome for new rounds of translation. EGAD|53116|YHR038W is part of the frr superfamily. [Protein synthesis, Translation factors]


Pssm-ID: 129587  Cd Length: 176  Bit Score: 64.79  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958696  111 EEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMN 189
Cdd:TIGR00496   2 ERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLG 79
                          90       100
                  ....*....|....*....|....
gi 767958696  190 LNPEVEGTLIRVPIPqsakwPMTQ 213
Cdd:TIGR00496  80 LNPNNDGSVIRVNFP-----PLTE 98
 
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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