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Conserved domains on  [gi|40317624|ref|NP_954646|]
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ribosome-recycling factor, mitochondrial isoform 2 precursor [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

CATH:  1.10.132.20|3.30.1360.40
Gene Ontology:  GO:0043023|GO:0006412|GO:0032790

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) ...
 103-192 1.56e-23

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: 91.34  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624   103 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 182
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90
                  ....*....|
gi 40317624   183 PqsakwPMTQ 192
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) ...
 103-192 1.56e-23

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: 91.34  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624   103 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 182
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90
                  ....*....|
gi 40317624   183 PqsakwPMTQ 192
Cdd:pfam01765  80 P-----PLTE 84
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 84-192 1.26e-18

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: 79.23  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624  84 NLEEVNEEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMasFPECTAAAI-KAI 162
Cdd:cd00520   1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAI 78

                        90       100       110
                ....*....|....*....|....*....|
gi 40317624 163 RESGMNLNPEVEGTLIRVPIPqsakwPMTQ 192
Cdd:cd00520  79 LNSDLGLNPNNDGAVIRVNLP-----PLTE 103
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
79-192 2.18e-18

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 78.54  E-value: 2.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624  79 VEDIINleEVNEEMKSVIEALKDNFNKtlnIRT---SPGSLDKIAVVTADGKLALNQISQISMKSPQLILV-----NMAS 150
Cdd:COG0233   2 IDEILK--DAEEKMEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 40317624 151 fpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 192
Cdd:COG0233  77 -------AIeKAIRKSDLGLNPSNDGNVIRIPIP-----PLTE 107
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 90-192 1.81e-12

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: 62.86  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624    90 EEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMN 168
Cdd:TIGR00496   2 ERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLG 79

                          90       100
                  ....*....|....*....|....
gi 40317624   169 LNPEVEGTLIRVPIPqsakwPMTQ 192
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) ...
 103-192 1.56e-23

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: 91.34  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624   103 FNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 182
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90
                  ....*....|
gi 40317624   183 PqsakwPMTQ 192
Cdd:pfam01765  80 P-----PLTE 84
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 84-192 1.26e-18

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: 79.23  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624  84 NLEEVNEEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNMasFPECTAAAI-KAI 162
Cdd:cd00520   1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAI 78

                        90       100       110
                ....*....|....*....|....*....|
gi 40317624 163 RESGMNLNPEVEGTLIRVPIPqsakwPMTQ 192
Cdd:cd00520  79 LNSDLGLNPNNDGAVIRVNLP-----PLTE 103
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
79-192 2.18e-18

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 78.54  E-value: 2.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624  79 VEDIINleEVNEEMKSVIEALKDNFNKtlnIRT---SPGSLDKIAVVTADGKLALNQISQISMKSPQLILV-----NMAS 150
Cdd:COG0233   2 IDEILK--DAEEKMEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 40317624 151 fpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPqsakwPMTQ 192
Cdd:COG0233  77 -------AIeKAIRKSDLGLNPSNDGNVIRIPIP-----PLTE 107
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 90-192 1.81e-12

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: 62.86  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40317624    90 EEMKSVIEALKDNFNKTLNIRTSPGSLDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMN 168
Cdd:TIGR00496   2 ERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLG 79

                          90       100
                  ....*....|....*....|....
gi 40317624   169 LNPEVEGTLIRVPIPqsakwPMTQ 192
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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