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Conserved domains on  [gi|330443413|ref|NP_009496|]
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aminoacyl-tRNA hydrolase [Saccharomyces cerevisiae S288C]

Protein Classification

peptidyl-tRNA hydrolase 2( domain architecture ID 10794499)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
88-208 3.39e-65

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: 196.60  E-value: 3.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413   88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATnparasYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:TIGR00283   1 MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKR------KNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443413  168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:TIGR00283  75 VTGLIRDAGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
 
Name Accession Description Interval E-value
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
88-208 3.39e-65

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: 196.60  E-value: 3.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413   88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATnparasYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:TIGR00283   1 MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKR------KNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443413  168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:TIGR00283  75 VTGLIRDAGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
88-208 6.45e-61

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: 185.80  E-value: 6.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIAtnparaSYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:cd02430    1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAM------KSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGL 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 330443413 168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:cd02430   75 PTSLIQDAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
88-208 1.70e-60

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: 184.57  E-value: 1.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413   88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNparasyNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKP------NPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443413  168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:pfam01981  75 PHALIRDAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
87-208 1.39e-46

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 149.55  E-value: 1.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  87 EVRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNPARASynpimtQRWLNAGQAKITLKCPDKFTMDELYAKAISLG 166
Cdd:COG1990    2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWF------EEWKDEGQKKVVLKVNSEEELFELKEKAERLG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 330443413 167 VNAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:COG1990   76 LPTALIRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
90-208 9.38e-44

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 141.89  E-value: 9.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  90 MALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNparasyNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNA 169
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKS------NREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPT 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330443413 170 AVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:PRK04322  75 ALIRDAGLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
 
Name Accession Description Interval E-value
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
88-208 3.39e-65

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: 196.60  E-value: 3.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413   88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATnparasYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:TIGR00283   1 MKMVIVIRDDLGMGKGKIAAQVCHAAIIGFLKSKR------KNPSLRRKWLDEGQKKVVLKVNSLEELLEIYHKAESLGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443413  168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:TIGR00283  75 VTGLIRDAGHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
88-208 6.45e-61

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: 185.80  E-value: 6.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIAtnparaSYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:cd02430    1 YKMVLVVRNDLKMGKGKIAAQCAHAALGAYKKAM------KSNPELLRAWEREGQKKIVLKVNSEEELLELKKKAKSLGL 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 330443413 168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:cd02430   75 PTSLIQDAGRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
88-208 1.70e-60

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: 184.57  E-value: 1.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413   88 VRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNparasyNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGV 167
Cdd:pfam01981   1 LKQVLVVRTDLKMSKGKIAAQCAHAAVAAYEKALKP------NPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 330443413  168 NAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:pfam01981  75 PHALIRDAGRTQIAPGTPTVLAIGPAPKELVDKITGHLKLL 115
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
90-208 7.62e-56

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: 172.73  E-value: 7.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  90 MALVIRQDLGMTKGKIAAQCCHAALSCFRHIAtnparaSYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNA 169
Cdd:cd02407    3 MVIVVRNDLKMGKGKIAAQCAHAALAAYKKAM------KDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPH 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330443413 170 AVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:cd02407   77 SLIQDAGRTQIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
87-208 1.39e-46

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 149.55  E-value: 1.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  87 EVRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNPARASynpimtQRWLNAGQAKITLKCPDKFTMDELYAKAISLG 166
Cdd:COG1990    2 EMKQVIVVRKDLKMSKGKLAAQVAHAAVSAALDALKKDKEWF------EEWKDEGQKKVVLKVNSEEELFELKEKAERLG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 330443413 167 VNAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:COG1990   76 LPTALIRDAGLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PRK04322 PRK04322
peptidyl-tRNA hydrolase; Provisional
90-208 9.38e-44

peptidyl-tRNA hydrolase; Provisional


Pssm-ID: 235280  Cd Length: 113  Bit Score: 141.89  E-value: 9.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443413  90 MALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNparasyNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNA 169
Cdd:PRK04322   1 QVIVVRTDLKMGKGKLAAQVAHAAVSAYEKADKS------NREWLEEWLNEGQKKVVLKVNSEEELLELKEKAERLGLPT 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330443413 170 AVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY 208
Cdd:PRK04322  75 ALIRDAGLTQLPPGTVTALGIGPAPEEKIDKITGDLKLL 113
 
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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