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Conserved domains on  [gi|1067605027|ref|NP_001332909|]
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peptidyl-tRNA hydrolase isoform 5 [Homo sapiens]

Protein Classification

aminoacyl-tRNA hydrolase family protein( domain architecture ID 358)

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
PubMed:  16849786|24768774
SCOP:  4000577

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTH super family cl00352
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
 32-105 8.87e-18

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.


The actual alignment was detected with superfamily member cd00462:

Pssm-ID: 469736  Cd Length: 171  Bit Score: 74.05  E-value: 8.87e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605027  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCaADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:cd00462     1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKK-GLVGEGRIGGEKVLLLKPQTYMNLSGEAVAAL 73
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
 32-105 8.87e-18

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: 74.05  E-value: 8.87e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605027  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCaADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:cd00462     1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKK-GLVGEGRIGGEKVLLLKPQTYMNLSGEAVAAL 73
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
32-105 1.43e-13

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 63.22  E-value: 1.43e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067605027  32 MVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHcAADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:pfam01195   1 LIVGLGNPG-PeyaGTRHNVGFMVVDALAERYGI--SLWKHKF-KALFGEGRIGGEKVLLLKPQTYMNLSGEAVAAL 73
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
 31-105 1.36e-11

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: 58.10  E-value: 1.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067605027  31 WMVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHCaADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:COG0193     3 KLIVGLGNPG-PeyaNTRHNIGFMVVDELARRHGV--SFKKKKFK-GLVAEGRIGGEKVLLLKPQTYMNLSGEAVAAL 76
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
 32-103 7.60e-08

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: 48.12  E-value: 7.60e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067605027  32 MVAGLGNPGL--PGTRHSVGMAVLGQLARRLGVaeSWTRDRHCAADLALAPLGDAQLVLLRPRRLMNANGRSVA 103
Cdd:TIGR00447   3 LIVGLGNPGKkyAGTRHNAGFWVLDLLASRLGL--SLRTEKKFFGYTERGLLSGKKVILLKPLTYMNLSGEAVR 74
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
 32-105 8.87e-18

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: 74.05  E-value: 8.87e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605027  32 MVAGLGNPGLP--GTRHSVGMAVLGQLARRLGVaeSWTRDRHCaADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:cd00462     1 LIVGLGNPGPKyeNTRHNVGFMVLDALAERYGV--SFKKKKKK-GLVGEGRIGGEKVLLLKPQTYMNLSGEAVAAL 73
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
32-105 1.43e-13

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 63.22  E-value: 1.43e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067605027  32 MVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHcAADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:pfam01195   1 LIVGLGNPG-PeyaGTRHNVGFMVVDALAERYGI--SLWKHKF-KALFGEGRIGGEKVLLLKPQTYMNLSGEAVAAL 73
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
 31-105 1.36e-11

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: 58.10  E-value: 1.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067605027  31 WMVAGLGNPGlP---GTRHSVGMAVLGQLARRLGVaeSWTRDRHCaADLALAPLGDAQLVLLRPRRLMNANGRSVARA 105
Cdd:COG0193     3 KLIVGLGNPG-PeyaNTRHNIGFMVVDELARRHGV--SFKKKKFK-GLVAEGRIGGEKVLLLKPQTYMNLSGEAVAAL 76
CRS2 cd02406
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
 31-103 1.42e-08

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: 50.17  E-value: 1.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067605027  31 WMVAGLGNPG--LPGTRHSVGMAVLGQLARRLGVAESWTRDRhcaADLALAPLGDAQLVLLRPRRLMNANGRSVA 103
Cdd:cd02406     3 WLIAGLGNPGnkYKGTRHNVGFEMVDRIAEAEGITMNTIQFK---SLLGIGSIGDVPVLLAKPQTYMNYSGESVG 74
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
 32-103 7.60e-08

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: 48.12  E-value: 7.60e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067605027  32 MVAGLGNPGL--PGTRHSVGMAVLGQLARRLGVaeSWTRDRHCAADLALAPLGDAQLVLLRPRRLMNANGRSVA 103
Cdd:TIGR00447   3 LIVGLGNPGKkyAGTRHNAGFWVLDLLASRLGL--SLRTEKKFFGYTERGLLSGKKVILLKPLTYMNLSGEAVR 74
 
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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