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Conserved domains on  [gi|446545072|ref|WP_000622418|]
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MULTISPECIES: ribosome recycling factor [Enterobacteriaceae]

Protein Classification

ribosome-recycling factor( domain architecture ID 10000748)

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
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
1-185 1.31e-115

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


:

Pssm-ID: 440003  Cd Length: 185  Bit Score: 325.83  E-value: 1.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   1 MISDIRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEK 80
Cdd:COG0233    1 MIDEILKDAEEKMEKAIEALKEELAKIRTGRASPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIQPWDKSMLKAIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072  81 AIMASDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDV 160
Cdd:COG0233   81 AIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLKKLEKDKEISEDELKRAEDEI 160
                        170       180
                 ....*....|....*....|....*
gi 446545072 161 QKLTDAAIKKIEAALADKEAELMQF 185
Cdd:COG0233  161 QKLTDKYIKKIDELLKAKEKEIMEV 185
 
Name Accession Description Interval E-value
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
1-185 1.31e-115

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 325.83  E-value: 1.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   1 MISDIRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEK 80
Cdd:COG0233    1 MIDEILKDAEEKMEKAIEALKEELAKIRTGRASPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIQPWDKSMLKAIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072  81 AIMASDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDV 160
Cdd:COG0233   81 AIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLKKLEKDKEISEDELKRAEDEI 160
                        170       180
                 ....*....|....*....|....*
gi 446545072 161 QKLTDAAIKKIEAALADKEAELMQF 185
Cdd:COG0233  161 QKLTDKYIKKIDELLKAKEKEIMEV 185
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
10-185 1.26e-94

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: 272.41  E-value: 1.26e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   10 EVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMASDLGL 89
Cdd:TIGR00496   1 KERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQPFDKSNINAIEKAIQRSDLGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   90 NPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDVQKLTDAAIK 169
Cdd:TIGR00496  81 NPNNDGSVIRVNFPPLTEERRKELVKHAKKIAEQAKVAVRNVRRDANDKVKKLEKDKEISEDEERRLQEEIQKLTDEYIK 160
                         170
                  ....*....|....*.
gi 446545072  170 KIEAALADKEAELMQF 185
Cdd:TIGR00496 161 KIDEILKDKEKELMEV 176
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
24-182 2.19e-86

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: 250.82  E-value: 2.19e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   24 ISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMASDLGLNPNSAGSDIRVPLP 103
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITPWDKSMLKAIEKAILASDLGLNPQNDGQVIRLPIP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446545072  104 PLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDkEISEDDDRRSQDDVQKLTDAAIKKIEAALADKEAEL 182
Cdd:pfam01765  81 PLTEERRKELVKQAKKLAEEAKVAIRNIRRDANDKLKKLEKD-EISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
5-183 2.49e-83

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: 243.71  E-value: 2.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   5 IRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMA 84
Cdd:cd00520    1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINPFDKSAIKAIEKAILN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072  85 SDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDVQKLT 164
Cdd:cd00520   81 SDLGLNPNNDGAVIRVNLPPLTEERRKELVKDAKKIAEEAKVAIRNIRRDANDKIKKLEKEKEISEDEVKKAEEDLQKLT 160
                        170
                 ....*....|....*....
gi 446545072 165 DAAIKKIEAALADKEAELM 183
Cdd:cd00520  161 DEYIKKIDELLKSKEKELL 179
 
Name Accession Description Interval E-value
Frr COG0233
Ribosome recycling factor [Translation, ribosomal structure and biogenesis];
1-185 1.31e-115

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


Pssm-ID: 440003  Cd Length: 185  Bit Score: 325.83  E-value: 1.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   1 MISDIRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEK 80
Cdd:COG0233    1 MIDEILKDAEEKMEKAIEALKEELAKIRTGRASPSLLDGIKVDYYGSPTPLNQVANISVPEARTLVIQPWDKSMLKAIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072  81 AIMASDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDV 160
Cdd:COG0233   81 AIRKSDLGLNPSNDGNVIRIPIPPLTEERRKELVKVVKKEAEEAKVAIRNIRRDANDDLKKLEKDKEISEDELKRAEDEI 160
                        170       180
                 ....*....|....*....|....*
gi 446545072 161 QKLTDAAIKKIEAALADKEAELMQF 185
Cdd:COG0233  161 QKLTDKYIKKIDELLKAKEKEIMEV 185
frr TIGR00496
ribosome recycling factor; This model finds only eubacterial proteins. Mitochondrial and/or ...
10-185 1.26e-94

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: 272.41  E-value: 1.26e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   10 EVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMASDLGL 89
Cdd:TIGR00496   1 KERMDKSIQALKRELSKIRTGRANPSLLDRILVEYYGAPTPLRQLASVTVPDARTLVIQPFDKSNINAIEKAIQRSDLGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   90 NPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDVQKLTDAAIK 169
Cdd:TIGR00496  81 NPNNDGSVIRVNFPPLTEERRKELVKHAKKIAEQAKVAVRNVRRDANDKVKKLEKDKEISEDEERRLQEEIQKLTDEYIK 160
                         170
                  ....*....|....*.
gi 446545072  170 KIEAALADKEAELMQF 185
Cdd:TIGR00496 161 KIDEILKDKEKELMEV 176
RRF pfam01765
Ribosome recycling factor; The ribosome recycling factor (RRF / ribosome release factor) ...
24-182 2.19e-86

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: 250.82  E-value: 2.19e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   24 ISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMASDLGLNPNSAGSDIRVPLP 103
Cdd:pfam01765   1 LAKIRTGRANPSLLDNIKVDYYGSPTPLNQLAQVSVPEARTLVITPWDKSMLKAIEKAILASDLGLNPQNDGQVIRLPIP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446545072  104 PLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDkEISEDDDRRSQDDVQKLTDAAIKKIEAALADKEAEL 182
Cdd:pfam01765  81 PLTEERRKELVKQAKKLAEEAKVAIRNIRRDANDKLKKLEKD-EISEDELKKAEKEIQKLTDKYIKKIDELLKAKEKEI 158
RRF cd00520
Ribosome recycling factor (RRF). Ribosome recycling factor dissociates the posttermination ...
5-183 2.49e-83

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: 243.71  E-value: 2.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072   5 IRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMA 84
Cdd:cd00520    1 ILKEAKEKMEKSLEALKEELNKIRTGRANPALLDSITVEYYGAPTPLNQLASISVPEPRTIVINPFDKSAIKAIEKAILN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446545072  85 SDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDVQKLT 164
Cdd:cd00520   81 SDLGLNPNNDGAVIRVNLPPLTEERRKELVKDAKKIAEEAKVAIRNIRRDANDKIKKLEKEKEISEDEVKKAEEDLQKLT 160
                        170
                 ....*....|....*....
gi 446545072 165 DAAIKKIEAALADKEAELM 183
Cdd:cd00520  161 DEYIKKIDELLKSKEKELL 179
 
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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