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Conserved domains on  [gi|767994998|ref|XP_011523189|]
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peptidyl-tRNA hydrolase 2, mitochondrial isoform X1 [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 ...
65-179 1.09e-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: 1.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:cd02430    1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767994998 145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
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 ...
65-179 1.09e-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: 1.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:cd02430    1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767994998 145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:cd02430   81 DAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
65-179 3.33e-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: 203.06  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998   65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767994998  145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:pfam01981  81 DAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
64-179 1.17e-60

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 183.83  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  64 EYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLI 143
Cdd:COG1990    2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767994998 144 QDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:COG1990   82 RDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
67-179 4.24e-57

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 174.63  E-value: 4.24e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  67 MILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDA 146
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767994998 147 GRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
66-179 1.93e-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: 1.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998   66 KMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQD 145
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767994998  146 AGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
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 ...
65-179 1.09e-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: 1.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:cd02430    1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767994998 145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:cd02430   81 DAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
65-179 3.33e-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: 203.06  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998   65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767994998  145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:pfam01981  81 DAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
65-179 2.12e-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: 2.12e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  65 YKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQ 144
Cdd:cd02407    1 YKMVIVVRNDLKMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPHSLIQ 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767994998 145 DAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:cd02407   81 DAGRTQIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
64-179 1.17e-60

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 183.83  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  64 EYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLI 143
Cdd:COG1990    2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767994998 144 QDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:COG1990   82 RDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
67-179 4.24e-57

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 174.63  E-value: 4.24e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998  67 MILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDA 146
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767994998 147 GRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:PRK04322  81 GLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
66-179 1.93e-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: 1.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994998   66 KMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQD 145
Cdd:TIGR00283   2 KMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIRD 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767994998  146 AGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY 179
Cdd:TIGR00283  82 AGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
67-129 1.25e-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: 1.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767994998  67 MILVVRNDL----KMGKGKVAAQCSHAAVSAykqIQR-RNPEMLKQWEYCGQ----PKVVVKAPDEETLIAL 129
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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