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Conserved domains on  [gi|1063731133|ref|NP_001331209|]
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Peptidyl-tRNA hydrolase II (PTH2) family protein [Arabidopsis thaliana]

Protein Classification

aminoacyl-tRNA hydrolase( domain architecture ID 10116186)

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 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_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
71-184 6.04e-69

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: 205.33  E-value: 6.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLID--SWPLGSVVTQGCHASVAAIWSFKDDPVTLQYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGI 148
Cdd:cd02429     1 LVQYVILRRDLQTklSWPLGAVIAQACHAAVAVIHLFRSDPDTKKYAYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063731133 149 SHKLWMEQPENIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:cd02429    81 KHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
 
Name Accession Description Interval E-value
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
71-184 6.04e-69

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: 205.33  E-value: 6.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLID--SWPLGSVVTQGCHASVAAIWSFKDDPVTLQYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGI 148
Cdd:cd02429     1 LVQYVILRRDLQTklSWPLGAVIAQACHAAVAVIHLFRSDPDTKKYAYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063731133 149 SHKLWMEQPENIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:cd02429    81 KHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
71-184 3.37e-33

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: 114.47  E-value: 3.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLidSWPLGSVVTQGCHASVAAIWSFKDDpvTLQYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGISH 150
Cdd:pfam01981   1 LKQVLVVRTDL--KMSKGKIAAQCAHAAVAAYEKALKP--NPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPH 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063731133 151 KLWME------QPeNIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:pfam01981  77 ALIRDagrtqiAP-GTPTVLAIGPAPKELVDKITGHLKLL 115
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
73-183 7.44e-05

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 40.20  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  73 QYVVLRRDLIDSwpLGSVVTQGCHASV-AAIWSFKDDPVTLqycDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGISHK 151
Cdd:PRK04322    1 QVIVVRTDLKMG--KGKLAAQVAHAAVsAYEKADKSNREWL---EEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTA 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063731133 152 L-----WMEQPENIPTCIATKPYPKSQVSSFFKKLKL 183
Cdd:PRK04322   76 LirdagLTQLPPGTVTALGIGPAPEEKIDKITGDLKL 112
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
73-183 3.04e-03

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: 35.97  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  73 QYVVLRRDLidSWPLGSVVTQGCHasvAAIWSFKDdpvtLQYCDPQHID-----SMHKVTLEVKGETQMMNLSEKLKLGG 147
Cdd:TIGR00283   3 MVIVIRDDL--GMGKGKIAAQVCH---AAIIGFLK----SKRKNPSLRRkwldeGQKKVVLKVNSLEELLEIYHKAESLG 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063731133 148 ISHKL-----WMEQPENIPTCIATKPYPKSQVSSFFKKLKL 183
Cdd:TIGR00283  74 LVTGLirdagHTQIPPGTITAVGIGPDEDEKIDKITGDLKL 114
 
Name Accession Description Interval E-value
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
71-184 6.04e-69

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: 205.33  E-value: 6.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLID--SWPLGSVVTQGCHASVAAIWSFKDDPVTLQYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGI 148
Cdd:cd02429     1 LVQYVILRRDLQTklSWPLGAVIAQACHAAVAVIHLFRSDPDTKKYAYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063731133 149 SHKLWMEQPENIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:cd02429    81 KHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
71-184 1.53e-44

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: 143.45  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLidSWPLGSVVTQGCHASVAAIWSFKDDPVTlqYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGISH 150
Cdd:cd02407     1 YKMVIVVRNDL--KMGKGKIAAQCAHAALAAYKKAMKDPPT--LLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPH 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063731133 151 KLWME-----QPENIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:cd02407    77 SLIQDagrtqIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
71-184 3.37e-33

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: 114.47  E-value: 3.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  71 VVQYVVLRRDLidSWPLGSVVTQGCHASVAAIWSFKDDpvTLQYCDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGISH 150
Cdd:pfam01981   1 LKQVLVVRTDL--KMSKGKIAAQCAHAAVAAYEKALKP--NPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPH 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063731133 151 KLWME------QPeNIPTCIATKPYPKSQVSSFFKKLKLC 184
Cdd:pfam01981  77 ALIRDagrtqiAP-GTPTVLAIGPAPKELVDKITGHLKLL 115
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
73-183 7.44e-05

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 40.20  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  73 QYVVLRRDLIDSwpLGSVVTQGCHASV-AAIWSFKDDPVTLqycDPQHIDSMHKVTLEVKGETQMMNLSEKLKLGGISHK 151
Cdd:PRK04322    1 QVIVVRTDLKMG--KGKLAAQVAHAAVsAYEKADKSNREWL---EEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPTA 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063731133 152 L-----WMEQPENIPTCIATKPYPKSQVSSFFKKLKL 183
Cdd:PRK04322   76 LirdagLTQLPPGTVTALGIGPAPEEKIDKITGDLKL 112
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
73-183 1.09e-03

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: 37.12  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  73 QYVVLRRDLidswPL--GSVVTQGCHASVAA-IWSFKDDPVTLQ---YCDPQhidsmhKVTLEVKGETQMMNLSEKLKLG 146
Cdd:cd02430     3 MVLVVRNDL----KMgkGKIAAQCAHAALGAyKKAMKSNPELLRaweREGQK------KIVLKVNSEEELLELKKKAKSL 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063731133 147 GISHKL-----WMEQPENIPTCIATKPYPKSQVSSFFKKLKL 183
Cdd:cd02430    73 GLPTSLiqdagRTQIAPGTITVLGIGPAPEELIDKVTGHLKL 114
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
73-183 3.04e-03

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: 35.97  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063731133  73 QYVVLRRDLidSWPLGSVVTQGCHasvAAIWSFKDdpvtLQYCDPQHID-----SMHKVTLEVKGETQMMNLSEKLKLGG 147
Cdd:TIGR00283   3 MVIVIRDDL--GMGKGKIAAQVCH---AAIIGFLK----SKRKNPSLRRkwldeGQKKVVLKVNSLEELLEIYHKAESLG 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063731133 148 ISHKL-----WMEQPENIPTCIATKPYPKSQVSSFFKKLKL 183
Cdd:TIGR00283  74 LVTGLirdagHTQIPPGTITAVGIGPDEDEKIDKITGDLKL 114
 
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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