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Conserved domains on  [gi|518394258|ref|WP_019564465|]
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MULTISPECIES: Cys-tRNA(Pro) deacylase [Agrobacterium]

Protein Classification

aminoacyl-tRNA deacylase( domain architecture ID 10025411)

aminoacyl-tRNA deacylase of the YbaK/EbsC family

Gene Ontology:  GO:0016829

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 5-155 5.51e-68

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


:

Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 202.68  E-value: 5.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYDYDPNADrIGLQAAEAIGEPPHLVLKTLMAELDGK-PVCVVVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518394258  84 ASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPL 155
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 5-155 5.51e-68

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 202.68  E-value: 5.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYDYDPNADrIGLQAAEAIGEPPHLVLKTLMAELDGK-PVCVVVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518394258  84 ASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPL 155
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 5-156 5.35e-67

Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272853 [Multi-domain]  Cd Length: 152  Bit Score: 200.54  E-value: 5.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258    5 TRATQMLTKAGVNFTTVTYDYDPNADrIGLQAAEAIGEPPHLVLKTLMAELDGK-PVCVVVPSDREVSMKKLAAAFGGKS 83
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKgPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518394258   84 ASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPLV 156
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-158 8.19e-57

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 174.51  E-value: 8.19e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYdydPNADRIGLQAAEAIGEPPHLVLKTLMAELDGKPVCVVVPSDREVSMKKLAAAFGGKSA 84
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518394258  85 SMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPLVAD 158
Cdd:COG2606   78 EMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
5-153 1.70e-33

Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;


Pssm-ID: 182634  Cd Length: 159  Bit Score: 115.61  E-value: 1.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYDYDPNADRIGLQAAEAIGEPPHLVLKTLMAELDGKP---VCVVVPSDREVSMKKLAAAFGG 81
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMkhlAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518394258  82 KSASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVA 153
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFA 153
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 35-143 3.07e-24

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: 90.74  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   35 QAAEAIGEPPHLVLKTL-MAELDGKPVCVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHVGGISPFG-QKKQV 112
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLvLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGV 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 518394258  113 PTAIEAGAMTHSHVYMNGGQRGLQVRLSPGD 143
Cdd:pfam04073  89 PVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 5-155 5.51e-68

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 202.68  E-value: 5.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYDYDPNADrIGLQAAEAIGEPPHLVLKTLMAELDGK-PVCVVVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518394258  84 ASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPL 155
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 5-156 5.35e-67

Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272853 [Multi-domain]  Cd Length: 152  Bit Score: 200.54  E-value: 5.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258    5 TRATQMLTKAGVNFTTVTYDYDPNADrIGLQAAEAIGEPPHLVLKTLMAELDGK-PVCVVVPSDREVSMKKLAAAFGGKS 83
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKgPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518394258   84 ASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPLV 156
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-158 8.19e-57

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 174.51  E-value: 8.19e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYdydPNADRIGLQAAEAIGEPPHLVLKTLMAELDGKPVCVVVPSDREVSMKKLAAAFGGKSA 84
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518394258  85 SMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAPLVAD 158
Cdd:COG2606   78 EMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 22-153 1.37e-36

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: 122.65  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258  22 TYDYDPNADRIgLQAAEAIGEPPHLVLKTLMAELD-GKPVCVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHV 100
Cdd:cd04332    4 EYEHTPGAKTI-EEAAEALGVPPGQIAKTLVLKDDkGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTGCEP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518394258 101 GGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALK-AVVA 153
Cdd:cd04332   83 GGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGeAEVA 136
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
5-153 1.70e-33

Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;


Pssm-ID: 182634  Cd Length: 159  Bit Score: 115.61  E-value: 1.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   5 TRATQMLTKAGVNFTTVTYDYDPNADRIGLQAAEAIGEPPHLVLKTLMAELDGKP---VCVVVPSDREVSMKKLAAAFGG 81
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMkhlAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518394258  82 KSASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVA 153
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFA 153
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 35-143 3.07e-24

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: 90.74  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   35 QAAEAIGEPPHLVLKTL-MAELDGKPVCVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHVGGISPFG-QKKQV 112
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLvLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGV 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 518394258  113 PTAIEAGAMTHSHVYMNGGQRGLQVRLSPGD 143
Cdd:pfam04073  89 PVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 35-154 1.93e-17

This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.


Pssm-ID: 239825 [Multi-domain]  Cd Length: 148  Bit Score: 74.08  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258  35 QAAEAIGEPPHLVLKTLMAELDGKPVCVVVPSDREVSMKKLAAAFGGKsASMMKPADAERATGYHVGGISPFGQKKQVPT 114
Cdd:cd04333   29 LAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEK-LKMADAEEVRELTGFAIGGVCPFGHPEPLPV 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518394258 115 AIEAGAMTHSHVYMNGGQRGLQVRLSPGDAQAALKAVVAP 154
Cdd:cd04333  108 YLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVD 147
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 6-158 5.41e-13

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: 62.36  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258   6 RATQMLTKAGVNFTTVTYDYDPNADriglQAAEAIGEPPHLVLKTLMAELDGKP---VCVVVPSDREVSMKKLAAAFGGK 82
Cdd:cd04336    3 RLQELLNTNGARFRVLDHPPEGTSE----EVAAIRGTELGQGAKALLCKVKDGSrrfVLAVLPADKKLDLKAVAAAVGGK 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518394258  83 SASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMT-HSHVYMNGGQRGLQVRLSPGDaqaALKaVVAPLVAD 158
Cdd:cd04336   79 KADLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDrGDEIAFNAGRLDASVVLDTAD---YLR-IARPLVLQ 151
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 37-113 2.21e-11

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 60.48  E-value: 2.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518394258  37 AEAIGEPPHLVLKTLMAELDGKPVCVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHVGGISPFGQKKQVP 113
Cdd:PRK09194 265 AEFLNVPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPKDVP 341
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 37-110 3.71e-09

INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA synthetase (ProRS) however, this CD is not exclusively bacterial. It is also found at the N-terminus of the eukaryotic/archaea-like ProRS's of yeasts and single-celled parasites. ProRS catalyzes the attachment of proline to tRNA(Pro); proline is first activated by ATP, and then transferred to the acceptor end of tRNA(Pro). ProRS can inadvertently process noncognate amino acids such as alanine and cysteine, and to avoid such errors, in post-transfer editing, the INS domain deacylates mischarged Ala-tRNA(Pro), thus ensuring the fidelity of translation. Misacylated Cys-tRNA(Pro) is not edited by ProRS. In addition to the INS editing domain, the prokaryote-like ProRS protein contains catalytic and anticodon-binding domains which form a dimeric interface.


Pssm-ID: 239826 [Multi-domain]  Cd Length: 160  Bit Score: 52.51  E-value: 3.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518394258  37 AEAIGEPPHLVLKTL--MAELDGKPVCVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHVGGISPFGQKK 110
Cdd:cd04334   42 AEFLGVPPSQTVKTLlvKADGEEELVAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLKK 117
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 61-152 8.17e-04

PA2301 is an uncharacterized Pseudomonas aeruginosa 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: 240137  Cd Length: 139  Bit Score: 37.32  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518394258  61 CVVVPSDREVSMKKLAAAFGGKSASMMKPADAERATGYHVGGISPFGQKKQVPTAIEAGAMTHSHVYMNGGQRGLQVrLS 140
Cdd:cd04939   47 CVVLATTRADVNGVVKRRLGARKASFAPMETAVELTGMEYGGITPVGLPAGWPILVDSAVAERPAVVIGSGVRRSKL-LL 125

                         90
                 ....*....|..
gi 518394258 141 PGDAQAALKAVV 152
Cdd:cd04939  126 PGAALAELPGAE 137
 
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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