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Conserved domains on  [gi|62865879|ref|NP_001015509|]
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peptidyl-tRNA hydrolase 2, mitochondrial isoform a [Homo sapiens]

Protein Classification

peptidyl-tRNA hydrolase 2( domain architecture ID 10116187)

peptidyl-tRNA hydrolase 2 releases tRNA from the premature translation termination product peptidyl-tRNA

CATH:  3.40.50.1470
EC:  3.1.1.29
Gene Symbol:  PTRH2
Gene Ontology:  GO:0004045|GO:0006412
PubMed:  16849786|24768774
SCOP:  4000577

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
66-180 1.18e-72

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: 214.31  E-value: 1.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:cd02430   1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 62865879 146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:cd02430  81 DAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
 
Name Accession Description Interval E-value
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
66-180 1.18e-72

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: 214.31  E-value: 1.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:cd02430   1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 62865879 146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:cd02430  81 DAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
66-180 3.91e-68

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: 202.68  E-value: 3.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879    66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62865879   146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:pfam01981  81 DAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
65-180 1.27e-60

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 183.83  E-value: 1.27e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  65 EYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLI 144
Cdd:COG1990   2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62865879 145 QDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:COG1990  82 RDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
68-180 3.90e-57

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 175.02  E-value: 3.90e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879   68 MILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDA 147
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62865879  148 GRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
67-180 2.00e-48

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: 153.08  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879    67 KMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQD 146
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 62865879   147 AGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:TIGR00283  82 AGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
 
Name Accession Description Interval E-value
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
66-180 1.18e-72

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: 214.31  E-value: 1.18e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:cd02430   1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 62865879 146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:cd02430  81 DAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
66-180 3.91e-68

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: 202.68  E-value: 3.91e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879    66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62865879   146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:pfam01981  81 DAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
66-180 2.22e-66

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: 198.53  E-value: 2.22e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  66 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 145
Cdd:cd02407   1 YKMVIVVRNDLKMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPHSLIQ 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 62865879 146 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:cd02407  81 DAGRTQIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
65-180 1.27e-60

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 183.83  E-value: 1.27e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879  65 EYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLI 144
Cdd:COG1990   2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 62865879 145 QDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:COG1990  82 RDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
68-180 3.90e-57

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 175.02  E-value: 3.90e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879   68 MILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDA 147
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62865879  148 GRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
67-180 2.00e-48

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: 153.08  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62865879    67 KMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQD 146
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 62865879   147 AGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 180
Cdd:TIGR00283  82 AGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
68-130 1.23e-05

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: 42.39  E-value: 1.23e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62865879  68 MILVVRNDL----KMGKGKVAAQCSHAAVSAykqIQR-RNPEMLKQWEYCGQ----PKVVVKAPDEETLIAL 130
Cdd:cd02429   3 QYVILRRDLqtklSWPLGAVIAQACHAAVAV---IHLfRSDPDTKKYAYLSNldnmHKVVLEVPDEAALKNL 71
 
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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