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Conserved domains on  [gi|291042689|ref|NP_001166983|]
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ribosome-recycling factor, mitochondrial isoform 3 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) ...
 62-208 4.25e-50

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: 159.91  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689   62 GSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPIPQVTREHREML 141
Cdd:pfam01765  12 SLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPIPPLTEERRKEL 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291042689  142 VKLAKQNTNKAKDSLRKVRTNSMNKLKK-SKDTVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKEL 208
Cdd:pfam01765  91 VKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
 62-208 4.25e-50

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: 159.91  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689   62 GSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPIPQVTREHREML 141
Cdd:pfam01765  12 SLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPIPPLTEERRKEL 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291042689  142 VKLAKQNTNKAKDSLRKVRTNSMNKLKK-SKDTVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKEL 208
Cdd:pfam01765  91 VKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
78-209 3.27e-29

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 107.04  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689  78 LNQISQISMKSPQLILV-----NMASfpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLVKLAKQNTNK 151
Cdd:COG0233   51 LNQVANISVPEARTLVIqpwdkSMLK-------AIeKAIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEE 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689 152 AKDSLRKVRTNSMNKLKKS-KD-TVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:COG0233  124 AKVAIRNIRRDANDDLKKLeKDkEISEDELKRAEDEIQKLTDKYIKKIDELLKAKEKEIM 183
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 64-209 4.50e-29

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: 106.58  E-value: 4.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689  64 LDKIAVVTADGKLALNQISQISMKSPQLILVNMasFPECTAAAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLV 142
Cdd:cd00520   33 LDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAILNSDLGLNPNNDGAVIRVNLPPLTEERRKELV 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291042689 143 KLAKQNTNKAKDSLRKVRTNSMNKLKK--SKDTVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:cd00520  111 KDAKKIAEEAKVAIRNIRRDANDKIKKleKEKEISEDEVKKAEEDLQKLTDEYIKKIDELLKSKEKELL 179
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 64-209 5.33e-22

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: 88.29  E-value: 5.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689   64 LDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLV 142
Cdd:TIGR00496  28 LDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLGLNPNNDGSVIRVNFPPLTEERRKELV 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291042689  143 KLAKQNTNKAKDSLRKVRTNSMNKLKK-SKDT-VSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:TIGR00496 106 KHAKKIAEQAKVAVRNVRRDANDKVKKlEKDKeISEDEERRLQEEIQKLTDEYIKKIDEILKDKEKELM 174
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
 62-208 4.25e-50

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: 159.91  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689   62 GSLDKIAVVTADGKLALNQISQISMKSPQLILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPIPQVTREHREML 141
Cdd:pfam01765  12 SLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPIPPLTEERRKEL 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291042689  142 VKLAKQNTNKAKDSLRKVRTNSMNKLKK-SKDTVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKEL 208
Cdd:pfam01765  91 VKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
78-209 3.27e-29

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 107.04  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689  78 LNQISQISMKSPQLILV-----NMASfpectaaAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLVKLAKQNTNK 151
Cdd:COG0233   51 LNQVANISVPEARTLVIqpwdkSMLK-------AIeKAIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEE 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689 152 AKDSLRKVRTNSMNKLKKS-KD-TVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:COG0233  124 AKVAIRNIRRDANDDLKKLeKDkEISEDELKRAEDEIQKLTDKYIKKIDELLKAKEKEIM 183
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 64-209 4.50e-29

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: 106.58  E-value: 4.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689  64 LDKIAVVTADGKLALNQISQISMKSPQLILVNMasFPECTAAAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLV 142
Cdd:cd00520   33 LDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAILNSDLGLNPNNDGAVIRVNLPPLTEERRKELV 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291042689 143 KLAKQNTNKAKDSLRKVRTNSMNKLKK--SKDTVSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:cd00520  111 KDAKKIAEEAKVAIRNIRRDANDKIKKleKEKEISEDEVKKAEEDLQKLTDEYIKKIDELLKSKEKELL 179
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 64-209 5.33e-22

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: 88.29  E-value: 5.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291042689   64 LDKIAVVTADGKLALNQISQISMKSPQLILVNmaSFPECTAAAI-KAIRESGMNLNPEVEGTLIRVPIPQVTREHREMLV 142
Cdd:TIGR00496  28 LDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLGLNPNNDGSVIRVNFPPLTEERRKELV 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291042689  143 KLAKQNTNKAKDSLRKVRTNSMNKLKK-SKDT-VSEDTIRLIEKQISQMADDTVAELDRHLAVKTKELL 209
Cdd:TIGR00496 106 KHAKKIAEQAKVAVRNVRRDANDKVKKlEKDKeISEDEERRLQEEIQKLTDEYIKKIDEILKDKEKELM 174
 
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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