NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|40889674|pdb|1RLK|A]
View 

Chain A, Hypothetical protein Ta0108

Protein Classification

peptidyl-tRNA hydrolase( domain architecture ID 10701833)

peptidyl-tRNA hydrolase belonging to the PTH2 family releases tRNA from the premature translation termination product peptidyl-tRNA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
1-117 9.69e-67

Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 441593  Cd Length: 117  Bit Score: 196.54  E-value: 9.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        1 MVKKMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEI 80
Cdd:COG1990   1 MEMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTAL 80
                        90       100       110
                ....*....|....*....|....*....|....*..
1RLK_A       81 VQDRGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:COG1990  81 IRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
 
Name Accession Description Interval E-value
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
1-117 9.69e-67

Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441593  Cd Length: 117  Bit Score: 196.54  E-value: 9.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        1 MVKKMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEI 80
Cdd:COG1990   1 MEMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTAL 80
                        90       100       110
                ....*....|....*....|....*....|....*..
1RLK_A       81 VQDRGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:COG1990  81 IRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
5-117 2.11e-64

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 190.81  E-value: 2.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A         5 MVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQDR 84
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
1RLK_A        85 GYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
4-117 9.44e-63

Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA from the premature translation termination product peptidyl-tRNA, therefore allowing the tRNA and peptide to be reused in protein synthesis. PTH2 is present in archaea and eukaryotes.


Pssm-ID: 239108  Cd Length: 115  Bit Score: 186.58  E-value: 9.44e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:cd02430   2 KMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQD 81
                        90       100       110
                ....*....|....*....|....*....|....
1RLK_A       84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:cd02430  82 AGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
4-117 3.61e-57

Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.


Pssm-ID: 460403  Cd Length: 115  Bit Score: 172.25  E-value: 3.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A          4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:pfam01981   2 KQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
1RLK_A         84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:pfam01981  82 AGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
4-117 7.72e-47

peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA hydrolase. Most bacterial forms are described by TIGR00447. [Protein synthesis, Other]


Pssm-ID: 161803  Cd Length: 115  Bit Score: 146.53  E-value: 7.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A          4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
1RLK_A         84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:TIGR00283  82 AGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
 
Name Accession Description Interval E-value
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
1-117 9.69e-67

Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441593  Cd Length: 117  Bit Score: 196.54  E-value: 9.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        1 MVKKMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEI 80
Cdd:COG1990   1 MEMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTAL 80
                        90       100       110
                ....*....|....*....|....*....|....*..
1RLK_A       81 VQDRGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:COG1990  81 IRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
5-117 2.11e-64

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 190.81  E-value: 2.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A         5 MVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQDR 84
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
1RLK_A        85 GYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
4-117 9.44e-63

Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA from the premature translation termination product peptidyl-tRNA, therefore allowing the tRNA and peptide to be reused in protein synthesis. PTH2 is present in archaea and eukaryotes.


Pssm-ID: 239108  Cd Length: 115  Bit Score: 186.58  E-value: 9.44e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:cd02430   2 KMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQD 81
                        90       100       110
                ....*....|....*....|....*....|....
1RLK_A       84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:cd02430  82 AGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
4-117 8.30e-59

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes.


Pssm-ID: 239091  Cd Length: 115  Bit Score: 176.58  E-value: 8.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:cd02407   2 KMVIVVRNDLKMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPHSLIQD 81
                        90       100       110
                ....*....|....*....|....*....|....
1RLK_A       84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:cd02407  82 AGRTQIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
4-117 3.61e-57

Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.


Pssm-ID: 460403  Cd Length: 115  Bit Score: 172.25  E-value: 3.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A          4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:pfam01981   2 KQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
1RLK_A         84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:pfam01981  82 AGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
4-117 7.72e-47

peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA hydrolase. Most bacterial forms are described by TIGR00447. [Protein synthesis, Other]


Pssm-ID: 161803  Cd Length: 115  Bit Score: 146.53  E-value: 7.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A          4 KMVIAVRKDLDMGKGKIAAQVAHAAVTCAIRSMKINRDVFNEWYDEGQRKIVVKVNDLDEIMEIKRMADSMGIVNEIVQD 83
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
1RLK_A         84 RGYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:TIGR00283  82 AGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
5-117 7.74e-07

Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two structurally different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes. There is no functional information for this eukaryote-specific subgroup.


Pssm-ID: 239107  Cd Length: 116  Bit Score: 44.32  E-value: 7.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RLK_A        5 MVIAVRKDLDMGK----GKIAAQVAHAAVTcAIRSMKINRDVFNEWYDEG---QRKIVVKVNDLDEIMEIKRMADSMGIV 77
Cdd:cd02429   3 QYVILRRDLQTKLswplGAVIAQACHAAVA-VIHLFRSDPDTKKYAYLSNldnMHKVVLEVPDEAALKNLSSKLTENSIK 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1RLK_A       78 NEIvqdrgYTQVEPGTITCIGLGPDEEEKLDKITGKYKLL 117
Cdd:cd02429  82 HKL-----WIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
 
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