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Conserved domains on  [gi|50897284|ref|NP_001002913|]
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peptidyl-tRNA hydrolase isoform 1 [Homo sapiens]

Protein Classification

aminoacyl-tRNA hydrolase( domain architecture ID 10087440)

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
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
32-203 2.15e-67

Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the nascent peptide and tRNA when peptidyl-tRNA is released prematurely from the ribosome. This ensures the recycling of peptidyl-tRNAs into tRNAs produced through abortion of translation and is essential for cell viability.This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts.


:

Pssm-ID: 238259  Cd Length: 171  Bit Score: 204.25  E-value: 2.15e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCAaDLALAPLGDAQLVLLRPRRLMNANGRSVARAAELF 109
Cdd:cd00462   1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKKG-LVGEGRIGGEKVLLLKPQTYMNLSGEAVAALANFY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 110 GLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELLP 189
Cdd:cd00462  78 KIPPEDILVIHDDLDLPLGKIRLKKGGGSGGHNGLKSIIAHLGTEDFPRLRIGIGRPPNKMDVADYVLSKFSKEERELLE 157
                       170
                ....*....|....
gi 50897284 190 LLLDRATDLILDHI 203
Cdd:cd00462 158 EAIEKAADALEDIL 171
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
32-203 2.15e-67

Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the nascent peptide and tRNA when peptidyl-tRNA is released prematurely from the ribosome. This ensures the recycling of peptidyl-tRNAs into tRNAs produced through abortion of translation and is essential for cell viability.This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts.


Pssm-ID: 238259  Cd Length: 171  Bit Score: 204.25  E-value: 2.15e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCAaDLALAPLGDAQLVLLRPRRLMNANGRSVARAAELF 109
Cdd:cd00462   1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKKG-LVGEGRIGGEKVLLLKPQTYMNLSGEAVAALANFY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 110 GLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELLP 189
Cdd:cd00462  78 KIPPEDILVIHDDLDLPLGKIRLKKGGGSGGHNGLKSIIAHLGTEDFPRLRIGIGRPPNKMDVADYVLSKFSKEERELLE 157
                       170
                ....*....|....
gi 50897284 190 LLLDRATDLILDHI 203
Cdd:cd00462 158 EAIEKAADALEDIL 171
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
32-205 6.92e-60

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 185.71  E-value: 6.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284    32 MVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHcAADLALAPLGDAQLVLLRPRRLMNANGRSVARAAEL 108
Cdd:pfam01195   1 LIVGLGNPG-PeyaGTRHNVGFMVVDALAERYGI--SLWKHKF-KALFGEGRIGGEKVLLLKPQTYMNLSGEAVAALANF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284   109 FGLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELL 188
Cdd:pfam01195  77 YKIPPEDILVIHDDLDLPLGKLRLKKGGSAGGHNGLKSIIAHLGTDDFPRLRIGIGRPPGDKDVADYVLGKFSKEERKLL 156
                         170
                  ....*....|....*..
gi 50897284   189 PLLLDRATDLILDHIRE 205
Cdd:pfam01195 157 DEALDKAADAVELLLKG 173
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
31-201 9.86e-55

Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA hydrolase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439963  Cd Length: 187  Bit Score: 172.89  E-value: 9.86e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  31 WMVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHCAaDLALAPLGDAQLVLLRPRRLMNANGRSVARAAE 107
Cdd:COG0193   3 KLIVGLGNPG-PeyaNTRHNIGFMVVDELARRHGV--SFKKKKFKG-LVAEGRIGGEKVLLLKPQTYMNLSGEAVAALAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 108 LFGLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQEL 187
Cdd:COG0193  79 FYKIPPEDILVVHDDLDLPPGKIRLKKGGGHGGHNGLKSIIAHLGTQDFPRLRIGIGRPGGKGDVADYVLGKFSKEEREL 158
                       170
                ....*....|....
gi 50897284 188 LPLLLDRATDLILD 201
Cdd:COG0193 159 LDEAIDRAADAVEL 172
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
32-205 4.26e-46

aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that drop off the ribosome during protein synthesis. Peptidyl-tRNA hydrolase is a bacterial protein; YHR189W from Saccharomyces cerevisiae appears to be orthologous and likely has the same function. [Protein synthesis, Other]


Pssm-ID: 213531  Cd Length: 188  Bit Score: 150.96  E-value: 4.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284    32 MVAGLGNPGL--PGTRHSVGMAVLGQLARRLGVaeSWTRDRHCAADLALAPLGDAQLVLLRPRRLMNANGRSVARAAELF 109
Cdd:TIGR00447   3 LIVGLGNPGKkyAGTRHNAGFWVLDLLASRLGL--SLRTEKKFFGYTERGLLSGKKVILLKPLTYMNLSGEAVRALASFY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284   110 GLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELLP 189
Cdd:TIGR00447  81 RIKPAELLVVHDELDLPLGKVRLKMGGGAGGHNGLKSIISHLGTNNFNRLRIGIGSPGGSNKVVEFVLSKFTKSELPLLE 160
                         170
                  ....*....|....*.
gi 50897284   190 LLLDRATDLILDHIRE 205
Cdd:TIGR00447 161 KALDKAVEALEMSFSE 176
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
32-203 2.15e-67

Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the nascent peptide and tRNA when peptidyl-tRNA is released prematurely from the ribosome. This ensures the recycling of peptidyl-tRNAs into tRNAs produced through abortion of translation and is essential for cell viability.This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts.


Pssm-ID: 238259  Cd Length: 171  Bit Score: 204.25  E-value: 2.15e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCAaDLALAPLGDAQLVLLRPRRLMNANGRSVARAAELF 109
Cdd:cd00462   1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKKG-LVGEGRIGGEKVLLLKPQTYMNLSGEAVAALANFY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 110 GLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELLP 189
Cdd:cd00462  78 KIPPEDILVIHDDLDLPLGKIRLKKGGGSGGHNGLKSIIAHLGTEDFPRLRIGIGRPPNKMDVADYVLSKFSKEERELLE 157
                       170
                ....*....|....
gi 50897284 190 LLLDRATDLILDHI 203
Cdd:cd00462 158 EAIEKAADALEDIL 171
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
32-205 6.92e-60

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 185.71  E-value: 6.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284    32 MVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHcAADLALAPLGDAQLVLLRPRRLMNANGRSVARAAEL 108
Cdd:pfam01195   1 LIVGLGNPG-PeyaGTRHNVGFMVVDALAERYGI--SLWKHKF-KALFGEGRIGGEKVLLLKPQTYMNLSGEAVAALANF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284   109 FGLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELL 188
Cdd:pfam01195  77 YKIPPEDILVIHDDLDLPLGKLRLKKGGSAGGHNGLKSIIAHLGTDDFPRLRIGIGRPPGDKDVADYVLGKFSKEERKLL 156
                         170
                  ....*....|....*..
gi 50897284   189 PLLLDRATDLILDHIRE 205
Cdd:pfam01195 157 DEALDKAADAVELLLKG 173
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
31-201 9.86e-55

Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA hydrolase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439963  Cd Length: 187  Bit Score: 172.89  E-value: 9.86e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  31 WMVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHCAaDLALAPLGDAQLVLLRPRRLMNANGRSVARAAE 107
Cdd:COG0193   3 KLIVGLGNPG-PeyaNTRHNIGFMVVDELARRHGV--SFKKKKFKG-LVAEGRIGGEKVLLLKPQTYMNLSGEAVAALAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 108 LFGLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQEL 187
Cdd:COG0193  79 FYKIPPEDILVVHDDLDLPPGKIRLKKGGGHGGHNGLKSIIAHLGTQDFPRLRIGIGRPGGKGDVADYVLGKFSKEEREL 158
                       170
                ....*....|....
gi 50897284 188 LPLLLDRATDLILD 201
Cdd:COG0193 159 LDEAIDRAADAVEL 172
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
32-205 4.26e-46

aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that drop off the ribosome during protein synthesis. Peptidyl-tRNA hydrolase is a bacterial protein; YHR189W from Saccharomyces cerevisiae appears to be orthologous and likely has the same function. [Protein synthesis, Other]


Pssm-ID: 213531  Cd Length: 188  Bit Score: 150.96  E-value: 4.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284    32 MVAGLGNPGL--PGTRHSVGMAVLGQLARRLGVaeSWTRDRHCAADLALAPLGDAQLVLLRPRRLMNANGRSVARAAELF 109
Cdd:TIGR00447   3 LIVGLGNPGKkyAGTRHNAGFWVLDLLASRLGL--SLRTEKKFFGYTERGLLSGKKVILLKPLTYMNLSGEAVRALASFY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284   110 GLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSNAMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQELLP 189
Cdd:TIGR00447  81 RIKPAELLVVHDELDLPLGKVRLKMGGGAGGHNGLKSIISHLGTNNFNRLRIGIGSPGGSNKVVEFVLSKFTKSELPLLE 160
                         170
                  ....*....|....*.
gi 50897284   190 LLLDRATDLILDHIRE 205
Cdd:TIGR00447 161 KALDKAVEALEMSFSE 176
CRS2 cd02406
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
31-199 7.70e-32

Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of group II introns in the chloroplast. CRS2 forms stable complexes with two CRS2-associated factors, CAF1 and CAF2, which are required for the splicing of distinct subsets of CRS2-dependent introns. CRS2 is closely related to bacterial peptidyl-tRNA hydrolases (PTH).


Pssm-ID: 239090  Cd Length: 191  Bit Score: 114.50  E-value: 7.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284  31 WMVAGLGNPG--LPGTRHSVGMAVLGQLARRLGVAESWTRDRhcaADLALAPLGDAQLVLLRPRRLMNANGRSVARAAEL 108
Cdd:cd02406   3 WLIAGLGNPGnkYKGTRHNVGFEMVDRIAEAEGITMNTIQFK---SLLGIGSIGDVPVLLAKPQTYMNYSGESVGPLAAY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897284 109 FGLTAEEVYLVHDELDKPLGRLALKLGGSARGHNGVRSCISCLNSN-AMPRLRVGIGRPAHPEAVQAHVLGCFSPAEQEL 187
Cdd:cd02406  80 YKVPLRHILVIYDDMSLPNGVLRLQPKGGHGRHNGLQSVIEHLDGSrEFPRLSIGIGSPPGKMDPRAFLLQKFSSEEREQ 159
                       170
                ....*....|..
gi 50897284 188 LPLLLDRATDLI 199
Cdd:cd02406 160 IDTALEQGVDAV 171
 
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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