NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720400393|ref|XP_030107858|]
View 

ribosome-recycling factor, mitochondrial isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
 12-169 1.25e-51

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: 162.22  E-value: 1.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  12 FNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 91
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400393  92 PKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK-SKDKTSEDTIRLIEKQISQMADDTVAELDQHLAAKTKEL 169
Cdd:pfam01765  80 PPLTEERRKELVKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
 12-169 1.25e-51

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: 162.22  E-value: 1.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  12 FNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 91
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400393  92 PKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK-SKDKTSEDTIRLIEKQISQMADDTVAELDQHLAAKTKEL 169
Cdd:pfam01765  80 PPLTEERRKELVKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
1-170 4.18e-36

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 123.60  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKtlnIRT---APGSLDHITVVTADGKVALNQIGQISMKSPQVILV-----NMASfpectaaAI-KAI 71
Cdd:COG0233    13 MEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK-------AIeKAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  72 RESGMNLNPEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKKS-KDKT-SEDTIRLIEKQISQ 149
Cdd:COG0233    83 RKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLKKLeKDKEiSEDELKRAEDEIQK 162

                         170       180
                  ....*....|....*....|.
gi 1720400393 150 MADDTVAELDQHLAAKTKELL 170
Cdd:COG0233   163 LTDKYIKKIDELLKAKEKEIM 183
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 1-170 3.00e-33

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: 116.21  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMasFPECTAAAI-KAIRESGMNLN 79
Cdd:cd00520     9 MEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAILNSDLGLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  80 PEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK--SKDKTSEDTIRLIEKQISQMADDTVAE 157
Cdd:cd00520    87 PNNDGAVIRVNLPPLTEERRKELVKDAKKIAEEAKVAIRNIRRDANDKIKKleKEKEISEDEVKKAEEDLQKLTDEYIKK 166

                         170
                  ....*....|...
gi 1720400393 158 LDQHLAAKTKELL 170
Cdd:cd00520   167 IDELLKSKEKELL 179
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 1-170 1.14e-25

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: 96.37  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNmaSFPECTAAAI-KAIRESGMNLN 79
Cdd:TIGR00496   4 MDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLGLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  80 PEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK-SKDK-TSEDTIRLIEKQISQMADDTVAE 157
Cdd:TIGR00496  82 PNNDGSVIRVNFPPLTEERRKELVKHAKKIAEQAKVAVRNVRRDANDKVKKlEKDKeISEDEERRLQEEIQKLTDEYIKK 161

                         170
                  ....*....|...
gi 1720400393 158 LDQHLAAKTKELL 170
Cdd:TIGR00496 162 IDEILKDKEKELM 174
 
Name Accession Description Interval E-value
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
 12-169 1.25e-51

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: 162.22  E-value: 1.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  12 FNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMaSFPECTAAAIKAIRESGMNLNPEVEGTLIRVPI 91
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITP-WDKSMLKAIEKAILASDLGLNPQNDGQVIRLPI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400393  92 PKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK-SKDKTSEDTIRLIEKQISQMADDTVAELDQHLAAKTKEL 169
Cdd:pfam01765  80 PPLTEERRKELVKQAKKLAEEAKVAIRNIRRDANDKLKKlEKDEISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
1-170 4.18e-36

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 123.60  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKtlnIRT---APGSLDHITVVTADGKVALNQIGQISMKSPQVILV-----NMASfpectaaAI-KAI 71
Cdd:COG0233    13 MEKAIEALKEELAK---IRTgraSPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIqpwdkSMLK-------AIeKAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  72 RESGMNLNPEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKKS-KDKT-SEDTIRLIEKQISQ 149
Cdd:COG0233    83 RKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLKKLeKDKEiSEDELKRAEDEIQK 162

                         170       180
                  ....*....|....*....|.
gi 1720400393 150 MADDTVAELDQHLAAKTKELL 170
Cdd:COG0233   163 LTDKYIKKIDELLKAKEKEIM 183
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
 1-170 3.00e-33

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: 116.21  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNMasFPECTAAAI-KAIRESGMNLN 79
Cdd:cd00520     9 MEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINP--FDKSAIKAIeKAILNSDLGLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  80 PEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK--SKDKTSEDTIRLIEKQISQMADDTVAE 157
Cdd:cd00520    87 PNNDGAVIRVNLPPLTEERRKELVKDAKKIAEEAKVAIRNIRRDANDKIKKleKEKEISEDEVKKAEEDLQKLTDEYIKK 166

                         170
                  ....*....|...
gi 1720400393 158 LDQHLAAKTKELL 170
Cdd:cd00520   167 IDELLKSKEKELL 179
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
 1-170 1.14e-25

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: 96.37  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393   1 MKSVVEALKDNFNKTLNIRTAPGSLDHITVVTADGKVALNQIGQISMKSPQVILVNmaSFPECTAAAI-KAIRESGMNLN 79
Cdd:TIGR00496   4 MDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQ--PFDKSNINAIeKAIQRSDLGLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400393  80 PEVEGTLIRVPIPKVTREHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKK-SKDK-TSEDTIRLIEKQISQMADDTVAE 157
Cdd:TIGR00496  82 PNNDGSVIRVNFPPLTEERRKELVKHAKKIAEQAKVAVRNVRRDANDKVKKlEKDKeISEDEERRLQEEIQKLTDEYIKK 161

                         170
                  ....*....|...
gi 1720400393 158 LDQHLAAKTKELL 170
Cdd:TIGR00496 162 IDEILKDKEKELM 174
BAR_GRAF2 cd07635
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion 2; BAR ...
 97-162 5.08e-03

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase 2 (GRAF2), also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA which regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle and also interacts with PKNbeta, which is a target of Rho. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of the related protein GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153319  Cd Length: 207  Bit Score: 36.13  E-value: 5.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720400393  97 EHREMLVKLAKQNTNKAKENLRKVRTNAMNKLKKSKDKTSEDTIRLIEKQIS----------QMADDTVAELDQHL 162
Cdd:cd07635    81 EQREIMALNVTETLIKPLERFRKEQLGAVKEEKKKFDKETEKNYSLLEKHLNlsakkkepqlQEADVQVEQNRQHF 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH