NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71892460|ref|NP_001025446|]
View 

putative peptidyl-tRNA hydrolase PTRHD1 [Danio rerio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
12-125 7.80e-70

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: 204.95  E-value: 7.80e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  12 LVQYVIVRSDLIHSLSWPLGAVITQACHAATAAIHLHYSDPDTQQ--YLAELDSMHKVVLQAPDEASLSTLSSTLEEKDI 89
Cdd:cd02429   1 LVQYVILRRDLQTKLSWPLGAVIAQACHAAVAVIHLFRSDPDTKKyaYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71892460  90 AHKLWMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
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 ...
12-125 7.80e-70

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: 204.95  E-value: 7.80e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  12 LVQYVIVRSDLIHSLSWPLGAVITQACHAATAAIHLHYSDPDTQQ--YLAELDSMHKVVLQAPDEASLSTLSSTLEEKDI 89
Cdd:cd02429   1 LVQYVILRRDLQTKLSWPLGAVIAQACHAAVAVIHLFRSDPDTKKyaYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71892460  90 AHKLWMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:cd02429  81 KHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
12-125 2.17e-35

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: 117.55  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460    12 LVQYVIVRSDLihslSWPLGAVITQACHAATAAIHLHYSDPDTQQYLAELDSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:pfam01981   1 LKQVLVVRTDL----KMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPH 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 71892460    92 KLWME------QPeNIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:pfam01981  77 ALIRDagrtqiAP-GTPTVLAIGPAPKELVDKITGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
14-125 4.93e-06

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 42.46  E-value: 4.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  14 QYVIVRSDLihSLSwpLGAVITQACHAA-TAAIHLHYSDPDT-QQYLAEldSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:COG1990   5 QVIVVRKDL--KMS--KGKLAAQVAHAAvSAALDALKKDKEWfEEWKDE--GQKKVVLKVNSEEELFELKEKAERLGLPT 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71892460  92 KL-----WMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:COG1990  79 ALirdagLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
14-125 5.33e-04

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: 37.13  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460    14 QYVIVRSDLIHSLswplGAVITQACHAATAA-IHLHYSDPD-TQQYLAEldSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:TIGR00283   3 MVIVIRDDLGMGK----GKIAAQVCHAAIIGfLKSKRKNPSlRRKWLDE--GQKKVVLKVNSLEELLEIYHKAESLGLVT 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71892460    92 KL-----WMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:TIGR00283  77 GLirdagHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
 
Name Accession Description Interval E-value
PTH2_like cd02429
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
12-125 7.80e-70

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: 204.95  E-value: 7.80e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  12 LVQYVIVRSDLIHSLSWPLGAVITQACHAATAAIHLHYSDPDTQQ--YLAELDSMHKVVLQAPDEASLSTLSSTLEEKDI 89
Cdd:cd02429   1 LVQYVILRRDLQTKLSWPLGAVIAQACHAAVAVIHLFRSDPDTKKyaYLSNLDNMHKVVLEVPDEAALKNLSSKLTENSI 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71892460  90 AHKLWMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:cd02429  81 KHKLWIEQPENIPTCIALKPYPKETVASYLKKLKLL 116
PTH2_family cd02407
Peptidyl-tRNA hydrolase, type 2 (PTH2)_like . Peptidyl-tRNA hydrolase activity releases tRNA ...
12-125 2.80e-48

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: 150.38  E-value: 2.80e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  12 LVQYVIVRSDLihslSWPLGAVITQACHAATAAIHLHYSDPDTQQYLAELDSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:cd02407   1 YKMVIVVRNDL----KMGKGKIAAQCAHAALAAYKKAMKDPPTLLRAWELEGQKKVVLKVPSEEELLELAKKAKELGLPH 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71892460  92 KLWME-----QPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:cd02407  77 SLIQDagrtqIPPGTPTVLAIGPAPKEKVDKVTGHLKLL 115
PTH2 pfam01981
Peptidyl-tRNA hydrolase PTH2; Peptidyl-tRNA hydrolases are enzymes that release tRNAs from ...
12-125 2.17e-35

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: 117.55  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460    12 LVQYVIVRSDLihslSWPLGAVITQACHAATAAIHLHYSDPDTQQYLAELDSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:pfam01981   1 LKQVLVVRTDL----KMSKGKIAAQCAHAAVAAYEKALKPNPELLREWEREGQKKVVLKVPSEEELLELAEKAKSLGLPH 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 71892460    92 KLWME------QPeNIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:pfam01981  77 ALIRDagrtqiAP-GTPTVLAIGPAPKELVDKITGHLKLL 115
Pth2 COG1990
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis];
14-125 4.93e-06

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


Pssm-ID: 441593  Cd Length: 117  Bit Score: 42.46  E-value: 4.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  14 QYVIVRSDLihSLSwpLGAVITQACHAA-TAAIHLHYSDPDT-QQYLAEldSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:COG1990   5 QVIVVRKDL--KMS--KGKLAAQVAHAAvSAALDALKKDKEWfEEWKDE--GQKKVVLKVNSEEELFELKEKAERLGLPT 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71892460  92 KL-----WMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:COG1990  79 ALirdagLTELEPGTVTCLGIGPAPEEKIDKITGDLKLL 117
PTH2 cd02430
Peptidyl-tRNA hydrolase, type 2 (PTH2). Peptidyl-tRNA hydrolase (PTH) activity releases tRNA ...
14-125 7.00e-06

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: 42.13  E-value: 7.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460  14 QYVIVRSDLIHSLswplGAVITQACHAA-TAAIHLHYSDPD-TQQYLAEldSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:cd02430   3 MVLVVRNDLKMGK----GKIAAQCAHAAlGAYKKAMKSNPElLRAWERE--GQKKIVLKVNSEEELLELKKKAKSLGLPT 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71892460  92 KL-----WMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:cd02430  77 SLiqdagRTQIAPGTITVLGIGPAPEELIDKVTGHLKLL 115
arch_pth2 TIGR00283
peptidyl-tRNA hydrolase; This model describes an archaeal/eukaryotic form of peptidyl-tRNA ...
14-125 5.33e-04

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: 37.13  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71892460    14 QYVIVRSDLIHSLswplGAVITQACHAATAA-IHLHYSDPD-TQQYLAEldSMHKVVLQAPDEASLSTLSSTLEEKDIAH 91
Cdd:TIGR00283   3 MVIVIRDDLGMGK----GKIAAQVCHAAIIGfLKSKRKNPSlRRKWLDE--GQKKVVLKVNSLEELLEIYHKAESLGLVT 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71892460    92 KL-----WMEQPENIPTCLALKPYPKETVQPYLKKFKLF 125
Cdd:TIGR00283  77 GLirdagHTQIPPGTITAVGIGPDEDEKIDKITGDLKLL 115
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH