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Conserved domains on  [gi|410084735|ref|XP_003959944|]
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hypothetical protein KAFR_0L01980 [Kazachstania africana CBS 2517]

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 ...
12-190 4.55e-45

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: 146.85  E-value: 4.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  12 CITGIGNMEPQYAMTRHNVGICFVDYLKDyllrgQQPKEFKKCRSAPYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS 91
Cdd:cd00462    1 LIVGLGNPGPKYENTRHNVGFMVLDALAE-----RYGVSFKKKKKKGLVGEGRIGGEKVLLLKPQTYMNLSGEAVAALAN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  92 QLPNRHEvRHIVVHDDLSLPVGKVQLRKPESSlRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFNTR 170
Cdd:cd00462   76 FYKIPPE-DILVIHDDLDLPLGKIRLKKGGGS-GGHNGLKSIIAHLGTEdFPRLRIGIGRPPNKMD--VADYVLSKFSKE 151
                        170       180
                 ....*....|....*....|
gi 410084735 171 EVEVLQSESFPSACNLLEKM 190
Cdd:cd00462  152 ERELLEEAIEKAADALEDIL 171
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
12-190 4.55e-45

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: 146.85  E-value: 4.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  12 CITGIGNMEPQYAMTRHNVGICFVDYLKDyllrgQQPKEFKKCRSAPYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS 91
Cdd:cd00462    1 LIVGLGNPGPKYENTRHNVGFMVLDALAE-----RYGVSFKKKKKKGLVGEGRIGGEKVLLLKPQTYMNLSGEAVAALAN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  92 QLPNRHEvRHIVVHDDLSLPVGKVQLRKPESSlRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFNTR 170
Cdd:cd00462   76 FYKIPPE-DILVIHDDLDLPLGKIRLKKGGGS-GGHNGLKSIIAHLGTEdFPRLRIGIGRPPNKMD--VADYVLSKFSKE 151
                        170       180
                 ....*....|....*....|
gi 410084735 171 EVEVLQSESFPSACNLLEKM 190
Cdd:cd00462  152 ERELLEEAIEKAADALEDIL 171
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
13-167 1.09e-36

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: 125.93  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   13 ITGIGNMEPQYAMTRHNVGICFVDYL-KDYLLRGQQPKEFkkcrsAPYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS 91
Cdd:TIGR00447   4 IVGLGNPGKKYAGTRHNAGFWVLDLLaSRLGLSLRTEKKF-----FGYTERGLLSGKKVILLKPLTYMNLSGEAVRALAS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410084735   92 --QLPNRhevRHIVVHDDLSLPVGKVQLRKPESSlRGHNGLKDIAKYYG-NRFHKLSVGVDRPEsrDSDIVAKYVLNKF 167
Cdd:TIGR00447  79 fyRIKPA---ELLVVHDELDLPLGKVRLKMGGGA-GGHNGLKSIISHLGtNNFNRLRIGIGSPG--GSNKVVEFVLSKF 151
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
13-191 8.48e-35

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 121.00  E-value: 8.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   13 ITGIGNMEPQYAMTRHNVGICFVDYL-KDYLLRgqqpkeFKKCRSAPYVKYLCISNQLVLLrydgnFMNLSGKYVVPIWS 91
Cdd:pfam01195   2 IVGLGNPGPEYAGTRHNVGFMVVDALaERYGIS------LWKHKFKALFGEGRIGGEKVLLlkpqtYMNLSGEAVAALAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   92 --QLPNRHeVrhIVVHDDLSLPVGKVQLRKpESSLRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFN 168
Cdd:pfam01195  76 fyKIPPED-I--LVIHDDLDLPLGKLRLKK-GGSAGGHNGLKSIIAHLGTDdFPRLRIGIGRPPGDKD--VADYVLGKFS 149
                         170       180
                  ....*....|....*....|...
gi 410084735  169 TREVEVLQsESFPSACNLLEKML 191
Cdd:pfam01195 150 KEERKLLD-EALDKAADAVELLL 171
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
13-191 5.63e-29

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: 105.87  E-value: 5.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  13 ITGIGNMEPQYAMTRHNVGICFVDYLKDYLlrGQQPKEfKKCRSApYVKYLCISNQLVLLRYDgNFMNLSGKYVVPI--W 90
Cdd:COG0193    5 IVGLGNPGPEYANTRHNIGFMVVDELARRH--GVSFKK-KKFKGL-VAEGRIGGEKVLLLKPQ-TYMNLSGEAVAALarF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  91 SQLPnrheVRHI-VVHDDLSLPVGKVQLRKpESSLRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFN 168
Cdd:COG0193   80 YKIP----PEDIlVVHDDLDLPPGKIRLKK-GGGHGGHNGLKSIIAHLGTQdFPRLRIGIGRPGGKGD--VADYVLGKFS 152
                        170       180
                 ....*....|....*....|...
gi 410084735 169 TREVEVLQsESFPSACNLLEKML 191
Cdd:COG0193  153 KEERELLD-EAIDRAADAVELLL 174
 
Name Accession Description Interval E-value
PTH cd00462
Peptidyl-tRNA hydrolase (PTH) is a monomeric protein that cleaves the ester bond linking the ...
12-190 4.55e-45

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: 146.85  E-value: 4.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  12 CITGIGNMEPQYAMTRHNVGICFVDYLKDyllrgQQPKEFKKCRSAPYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS 91
Cdd:cd00462    1 LIVGLGNPGPKYENTRHNVGFMVLDALAE-----RYGVSFKKKKKKGLVGEGRIGGEKVLLLKPQTYMNLSGEAVAALAN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  92 QLPNRHEvRHIVVHDDLSLPVGKVQLRKPESSlRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFNTR 170
Cdd:cd00462   76 FYKIPPE-DILVIHDDLDLPLGKIRLKKGGGS-GGHNGLKSIIAHLGTEdFPRLRIGIGRPPNKMD--VADYVLSKFSKE 151
                        170       180
                 ....*....|....*....|
gi 410084735 171 EVEVLQSESFPSACNLLEKM 190
Cdd:cd00462  152 ERELLEEAIEKAADALEDIL 171
pth TIGR00447
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs that ...
13-167 1.09e-36

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: 125.93  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   13 ITGIGNMEPQYAMTRHNVGICFVDYL-KDYLLRGQQPKEFkkcrsAPYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS 91
Cdd:TIGR00447   4 IVGLGNPGKKYAGTRHNAGFWVLDLLaSRLGLSLRTEKKF-----FGYTERGLLSGKKVILLKPLTYMNLSGEAVRALAS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410084735   92 --QLPNRhevRHIVVHDDLSLPVGKVQLRKPESSlRGHNGLKDIAKYYG-NRFHKLSVGVDRPEsrDSDIVAKYVLNKF 167
Cdd:TIGR00447  79 fyRIKPA---ELLVVHDELDLPLGKVRLKMGGGA-GGHNGLKSIISHLGtNNFNRLRIGIGSPG--GSNKVVEFVLSKF 151
Pept_tRNA_hydro pfam01195
Peptidyl-tRNA hydrolase;
13-191 8.48e-35

Peptidyl-tRNA hydrolase;


Pssm-ID: 460105  Cd Length: 182  Bit Score: 121.00  E-value: 8.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   13 ITGIGNMEPQYAMTRHNVGICFVDYL-KDYLLRgqqpkeFKKCRSAPYVKYLCISNQLVLLrydgnFMNLSGKYVVPIWS 91
Cdd:pfam01195   2 IVGLGNPGPEYAGTRHNVGFMVVDALaERYGIS------LWKHKFKALFGEGRIGGEKVLLlkpqtYMNLSGEAVAALAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735   92 --QLPNRHeVrhIVVHDDLSLPVGKVQLRKpESSLRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFN 168
Cdd:pfam01195  76 fyKIPPED-I--LVIHDDLDLPLGKLRLKK-GGSAGGHNGLKSIIAHLGTDdFPRLRIGIGRPPGDKD--VADYVLGKFS 149
                         170       180
                  ....*....|....*....|...
gi 410084735  169 TREVEVLQsESFPSACNLLEKML 191
Cdd:pfam01195 150 KEERKLLD-EALDKAADAVELLL 171
Pth COG0193
Peptidyl-tRNA hydrolase [Translation, ribosomal structure and biogenesis]; Peptidyl-tRNA ...
13-191 5.63e-29

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: 105.87  E-value: 5.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  13 ITGIGNMEPQYAMTRHNVGICFVDYLKDYLlrGQQPKEfKKCRSApYVKYLCISNQLVLLRYDgNFMNLSGKYVVPI--W 90
Cdd:COG0193    5 IVGLGNPGPEYANTRHNIGFMVVDELARRH--GVSFKK-KKFKGL-VAEGRIGGEKVLLLKPQ-TYMNLSGEAVAALarF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  91 SQLPnrheVRHI-VVHDDLSLPVGKVQLRKpESSLRGHNGLKDIAKYYGNR-FHKLSVGVDRPESRDSdiVAKYVLNKFN 168
Cdd:COG0193   80 YKIP----PEDIlVVHDDLDLPPGKIRLKK-GGGHGGHNGLKSIIAHLGTQdFPRLRIGIGRPGGKGD--VADYVLGKFS 152
                        170       180
                 ....*....|....*....|...
gi 410084735 169 TREVEVLQsESFPSACNLLEKML 191
Cdd:COG0193  153 KEERELLD-EAIDRAADAVELLL 174
CRS2 cd02406
Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of ...
13-175 5.93e-19

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: 80.22  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  13 ITGIGNMEPQYAMTRHNVGICFVDYLKDYLLRGQQPKEFKKcrsapYVKYLCISNQLVLLRYDGNFMNLSGKYVVPIWS- 91
Cdd:cd02406    5 IAGLGNPGNKYKGTRHNVGFEMVDRIAEAEGITMNTIQFKS-----LLGIGSIGDVPVLLAKPQTYMNYSGESVGPLAAy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410084735  92 -QLPNRHEvrhIVVHDDLSLPVGKVQLrKPESSLRGHNGLKDIAKYY-GNR-FHKLSVGVDRPESRdSDIVAkYVLNKFN 168
Cdd:cd02406   80 yKVPLRHI---LVIYDDMSLPNGVLRL-QPKGGHGRHNGLQSVIEHLdGSReFPRLSIGIGSPPGK-MDPRA-FLLQKFS 153

                 ....*..
gi 410084735 169 TREVEVL 175
Cdd:cd02406  154 SEEREQI 160
 
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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