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Conserved domains on  [gi|1063726430|ref|NP_001328355|]
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Peptidyl-tRNA hydrolase II (PTH2) family protein [Arabidopsis thaliana]

Protein Classification

aminoacyl-tRNA hydrolase( domain architecture ID 10487989)

aminoacyl-tRNA hydrolase catalyzes the hydolysis of an N-substituted aminoacyl-tRNA to yield the N-substituted amino acid and tRNA to ensure the recycling of peptidyl-tRNAs produced when translation is aborted

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
 79-165 3.59e-42

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: 136.42  E-value: 3.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:pfam01981  81 DAGRTQI 87
 
Name Accession Description Interval E-value
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
 79-165 3.59e-42

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: 136.42  E-value: 3.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:pfam01981  81 DAGRTQI 87
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
 80-165 9.71e-41

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: 133.03  E-value: 9.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  80 KMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVAD 159
Cdd:cd02430     2 KMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQD 81


                  ....*.
gi 1063726430 160 AGRTEV 165
Cdd:cd02430    82 AGRTQI 87
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
78-165 2.29e-32

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 111.80  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  78 ELKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVV 157
Cdd:COG1990     2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81


                  ....*...
gi 1063726430 158 ADAGRTEV 165
Cdd:COG1990    82 RDAGLTEL 89
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
 81-165 7.97e-30

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 105.29  E-value: 7.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  81 MVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVADA 160
Cdd:PRK04322    1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80


                  ....*
gi 1063726430 161 GRTEV 165
Cdd:PRK04322   81 GLTQL 85
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
 79-165 1.30e-27

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: 99.53  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:TIGR00283   1 MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIR 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:TIGR00283  81 DAGHTQI 87
 
Name Accession Description Interval E-value
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
 79-165 3.59e-42

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: 136.42  E-value: 3.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPHALIR 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:pfam01981  81 DAGRTQI 87
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
 80-165 9.71e-41

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: 133.03  E-value: 9.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  80 KMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVAD 159
Cdd:cd02430     2 KMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAMKSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGLPTSLIQD 81


                  ....*.
gi 1063726430 160 AGRTEV 165
Cdd:cd02430    82 AGRTQI 87
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
 79-165 1.29e-36

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: 122.65  E-value: 1.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:cd02407     1 YKMVIVVRNDLKMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPHSLIQ 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:cd02407    81 DAGRTQI 87
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
78-165 2.29e-32

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 111.80  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  78 ELKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVV 157
Cdd:COG1990     2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWFEEWKDEGQKKVVLKVNSEEELFELKEKAERLGLPTALI 81


                  ....*...
gi 1063726430 158 ADAGRTEV 165
Cdd:COG1990    82 RDAGLTEL 89
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
 81-165 7.97e-30

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 105.29  E-value: 7.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  81 MVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVADA 160
Cdd:PRK04322    1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKSNREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTALIRDA 80


                  ....*
gi 1063726430 161 GRTEV 165
Cdd:PRK04322   81 GLTQL 85
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
 79-165 1.30e-27

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: 99.53  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726430  79 LKMVLVVRQDLKMRTGKIASQCAHAATGMYAELMQSDRYLLRRWEENGQPKIVVTCKNQQEMNKITEAAESVGLPTFVVA 158
Cdd:TIGR00283   1 MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKRKNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGLVTGLIR 80


                  ....*..
gi 1063726430 159 DAGRTEV 165
Cdd:TIGR00283  81 DAGHTQI 87
 
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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