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Conserved domains on  [gi|479785861|gb|ENT55147|]
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hypothetical protein C007_02645 [Brucella suis F8/06-1]

Protein Classification

prolyl-tRNA synthetase associated domain-containing protein( domain architecture ID 10790401)

prolyl-tRNA synthetase associated domain-containing protein similar to Clostridium sticklandii prolyl-tRNA editing protein ProX, which edits the amino acid moiety from incorrectly charged Ala-tRNA(Pro), preventing translation errors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 2-163 7.10e-88

Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only];


:

Pssm-ID: 442974  Cd Length: 162  Bit Score: 254.28  E-value: 7.10e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   2 PLTPKELHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKKD-NFFLVTVEEDAVVDLKSIHQLIGAa 80
Cdd:COG3760    1 PLTEQELYALLDELGIPYETVEHPPVFTVEEAEALRGDLPGAHTKNLFLRDKKGtRFYLVVVPEDKRVDLKALSKQLGS- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861  81 SRVSFGKPEKLMEYLGVIPGSVTVFGAANDTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLKSTGHEPRI 160
Cdd:COG3760   80 GRLSFASPERLEEYLGVTPGSVTPFGLINDTENRVTVVLDADLLEAELINCHPLVNTATLKISTDDLLRFLEATGHEPLI 159


                 ...
gi 479785861 161 LAV 163
Cdd:COG3760  160 IDL 162
 
Name Accession Description Interval E-value
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 2-163 7.10e-88

Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only];


Pssm-ID: 442974  Cd Length: 162  Bit Score: 254.28  E-value: 7.10e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   2 PLTPKELHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKKD-NFFLVTVEEDAVVDLKSIHQLIGAa 80
Cdd:COG3760    1 PLTEQELYALLDELGIPYETVEHPPVFTVEEAEALRGDLPGAHTKNLFLRDKKGtRFYLVVVPEDKRVDLKALSKQLGS- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861  81 SRVSFGKPEKLMEYLGVIPGSVTVFGAANDTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLKSTGHEPRI 160
Cdd:COG3760   80 GRLSFASPERLEEYLGVTPGSVTPFGLINDTENRVTVVLDADLLEAELINCHPLVNTATLKISTDDLLRFLEATGHEPLI 159


                 ...
gi 479785861 161 LAV 163
Cdd:COG3760  160 IDL 162
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 5-161 6.95e-77

This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins.


Pssm-ID: 239827  Cd Length: 156  Bit Score: 226.25  E-value: 6.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   5 PKELHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKKDNFFLVTVEEDAVVDLKSIHQLIGAaSRVS 84
Cdd:cd04335    1 EDELLALLDELGIAYETVEHPPVFTVEEADEVLGELPGAHTKNLFLKDKKGRLYLVTALHDKKVDLKALSKQLGA-SRLS 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479785861  85 FGKPEKLMEYLGVIPGSVTVFGAANDTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLKSTGHEPRIL 161
Cdd:cd04335   80 FASEERLEEKLGVTPGSVTPFALINDKENDVQVVLDKDLLEEERVGFHPLTNTATVGISTEDLLKFLEATGHEPTVV 156
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 24-150 6.74e-27

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 98.06  E-value: 6.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   24 HPPLFTVADSQNLRGEIPGGHTKNLFLKDKKDNFFLVTVEEDAVVDLKSIHQLIGaASRVSFGKPEKLMEYLGVIPGSVT 103
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLG-VKRLRLASEEELLELTGVEPGGVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 479785861  104 VFGAandTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAF 150
Cdd:pfam04073  80 PFGL---KAKGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
 
Name Accession Description Interval E-value
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 2-163 7.10e-88

Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only];


Pssm-ID: 442974  Cd Length: 162  Bit Score: 254.28  E-value: 7.10e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   2 PLTPKELHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKKD-NFFLVTVEEDAVVDLKSIHQLIGAa 80
Cdd:COG3760    1 PLTEQELYALLDELGIPYETVEHPPVFTVEEAEALRGDLPGAHTKNLFLRDKKGtRFYLVVVPEDKRVDLKALSKQLGS- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861  81 SRVSFGKPEKLMEYLGVIPGSVTVFGAANDTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLKSTGHEPRI 160
Cdd:COG3760   80 GRLSFASPERLEEYLGVTPGSVTPFGLINDTENRVTVVLDADLLEAELINCHPLVNTATLKISTDDLLRFLEATGHEPLI 159


                 ...
gi 479785861 161 LAV 163
Cdd:COG3760  160 IDL 162
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 5-161 6.95e-77

This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins.


Pssm-ID: 239827  Cd Length: 156  Bit Score: 226.25  E-value: 6.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   5 PKELHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKKDNFFLVTVEEDAVVDLKSIHQLIGAaSRVS 84
Cdd:cd04335    1 EDELLALLDELGIAYETVEHPPVFTVEEADEVLGELPGAHTKNLFLKDKKGRLYLVTALHDKKVDLKALSKQLGA-SRLS 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479785861  85 FGKPEKLMEYLGVIPGSVTVFGAANDTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLKSTGHEPRIL 161
Cdd:cd04335   80 FASEERLEEKLGVTPGSVTPFALINDKENDVQVVLDKDLLEEERVGFHPLTNTATVGISTEDLLKFLEATGHEPTVV 156
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 24-150 6.74e-27

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 98.06  E-value: 6.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   24 HPPLFTVADSQNLRGEIPGGHTKNLFLKDKKDNFFLVTVEEDAVVDLKSIHQLIGaASRVSFGKPEKLMEYLGVIPGSVT 103
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLG-VKRLRLASEEELLELTGVEPGGVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 479785861  104 VFGAandTNHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAF 150
Cdd:pfam04073  80 PFGL---KAKGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 19-152 2.31e-26

YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).


Pssm-ID: 239824 [Multi-domain]  Cd Length: 136  Bit Score: 97.23  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861  19 VTTVEHPP-LFTVADSQNLRGEIPGGHTKNLFLKDKKDNFFLVTVEEDAVVDLKSIHQLIGAAsRVSFGKPEKLMEYLGV 97
Cdd:cd04332    2 YLEYEHTPgAKTIEEAAEALGVPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAK-KLRLASEEELEELTGC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 479785861  98 IPGSVTVFGAAndtnHRVQVILDAGLMKYDIINGHPLTNEATTSIRREDLIAFLK 152
Cdd:cd04332   81 EPGGVGPFGLK----KGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLG 131
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 8-130 3.56e-12

YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 60.82  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479785861   8 LHDLLHKLGIGVTTVEHPPLFTVADSQNLRGEIPGGHTKNLFLKDKK--DNFFLVTVEEDAVVDLKSIHQLIGaASRVSF 85
Cdd:cd04336    4 LQELLNTNGARFRVLDHPPEGTSEEVAAIRGTELGQGAKALLCKVKDgsRRFVLAVLPADKKLDLKAVAAAVG-GKKADL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 479785861  86 GKPEKLMEYLGVIPGSVTVFGaandTNHRVQVILDAGLM-KYDIIN 130
Cdd:cd04336   83 ASPEEAEELTGCVIGAVPPFS----FDPKLKLIADPSLLdRGDEIA 124
 
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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