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Conserved domains on  [gi|9257097|pdb|1DBX|A]
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Chain A, cysteinyl-tRNA(Pro) deacylase

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 ...
 1-155 5.80e-80

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: 233.11  E-value: 5.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        1 MTPAIDLLKKQKIPFILHTYDHDPNNqHFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIG 80
Cdd:cd00002   1 KTPAIRLLDKAKIPYELHEYEHDEDA-SDGLEAAEKLGLDPEQVFKTLVVE--GDKKGLVVAVVPVDEELDLKKLAKALG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A       81 VKKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:cd00002  78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 5.80e-80

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: 233.11  E-value: 5.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        1 MTPAIDLLKKQKIPFILHTYDHDPNNqHFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIG 80
Cdd:cd00002   1 KTPAIRLLDKAKIPYELHEYEHDEDA-SDGLEAAEKLGLDPEQVFKTLVVE--GDKKGLVVAVVPVDEELDLKKLAKALG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A       81 VKKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:cd00002  78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-155 7.01e-75

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 220.77  E-value: 7.01e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A         1 MTPAIDLLKKQKIPFILHTYDHDPNNQHFGDEAAEKLGIDPNRSFKTLLVAENGDQKKLACFVLATAN*LNLKKAAKSIG 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A        81 VKKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 2.37e-60

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: 183.59  E-value: 2.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A          2 TPAIDLLKKQKIPFILHTYDHDPNNQhFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIGV 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAE--GDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A         82 KKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDIV 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-158 4.54e-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: 175.28  E-value: 4.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        2 TPAIDLLKKQKIPFILHTYDHDPnnqHFGDEAAEKLGIDPNRSFKTLLVAengDQKKLACFVLATAN*LNLKKAAKSIGV 81
Cdd:COG2606   1 TPVRRALDAAGIPYEVVEHPEPA---ATAEEAAEALGVPPEQIAKTLVFR---GDGGPVLAVVPGDRRLDLKKLAAALGA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DBX_A       82 KKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDIVDE 158
Cdd:COG2606  75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-146 1.93e-22

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: 86.12  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A         32 EAAEKLGIDPNRSFKTLLVaENGDQKKLACFVLATAn*LNLKKAAKSIGVKKVE*ADKDAAQKSTGYLVGGISPLG-QKK 110
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVL-KDKKGKYVLVVVPGDR-EVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAK 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
1DBX_A        111 RVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAK 146
Cdd:pfam04073  87 GVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRK 122
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 5.80e-80

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: 233.11  E-value: 5.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        1 MTPAIDLLKKQKIPFILHTYDHDPNNqHFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIG 80
Cdd:cd00002   1 KTPAIRLLDKAKIPYELHEYEHDEDA-SDGLEAAEKLGLDPEQVFKTLVVE--GDKKGLVVAVVPVDEELDLKKLAKALG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A       81 VKKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:cd00002  78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-155 7.01e-75

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 220.77  E-value: 7.01e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A         1 MTPAIDLLKKQKIPFILHTYDHDPNNQHFGDEAAEKLGIDPNRSFKTLLVAENGDQKKLACFVLATAN*LNLKKAAKSIG 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A        81 VKKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 2.37e-60

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: 183.59  E-value: 2.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A          2 TPAIDLLKKQKIPFILHTYDHDPNNQhFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIGV 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAE--GDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DBX_A         82 KKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDIV 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-158 4.54e-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: 175.28  E-value: 4.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        2 TPAIDLLKKQKIPFILHTYDHDPnnqHFGDEAAEKLGIDPNRSFKTLLVAengDQKKLACFVLATAN*LNLKKAAKSIGV 81
Cdd:COG2606   1 TPVRRALDAAGIPYEVVEHPEPA---ATAEEAAEALGVPPEQIAKTLVFR---GDGGPVLAVVPGDRRLDLKKLAAALGA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DBX_A       82 KKVE*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDIVDE 158
Cdd:COG2606  75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 18-150 4.85e-41

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: 134.21  E-value: 4.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A       18 HTYDHDPNnQHFGDEAAEKLGIDPNRSFKTLLVAenGDQKKLACFVLATAN*LNLKKAAKSIGVKKVE*ADKDAAQKSTG 97
Cdd:cd04332   3 LEYEHTPG-AKTIEEAAEALGVPPGQIAKTLVLK--DDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
1DBX_A       98 YLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGA 150
Cdd:cd04332  80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGE 132
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-146 1.93e-22

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: 86.12  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A         32 EAAEKLGIDPNRSFKTLLVaENGDQKKLACFVLATAn*LNLKKAAKSIGVKKVE*ADKDAAQKSTGYLVGGISPLG-QKK 110
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVL-KDKKGKYVLVVVPGDR-EVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAK 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
1DBX_A        111 RVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAK 146
Cdd:pfam04073  87 GVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRK 122
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 32-155 5.26e-16

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: 70.22  E-value: 5.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A       32 EAAEKLGIDPNRSFKTLLVAENGdqkKLACFVLATAN*LNLKKAAKSIGvKKVE*ADKDAAQKSTGYLVGGISPLGQKKR 111
Cdd:cd04333  29 LAAEALGCEPGQIAKSLVFRVDD---EPVLVVTSGDARVDNKKFKALFG-EKLKMADAEEVRELTGFAIGGVCPFGHPEP 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1DBX_A      112 VKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDI 155
Cdd:cd04333 105 LPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 5-153 4.33e-11

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: 57.35  E-value: 4.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        5 IDLLKKQKIPFilHTYDHDPNNQhfGDEAAEKLGIDPNRSFKTLLVAENGDQKKLACFVLATAN*LNLKKAAKSIGVKKV 84
Cdd:cd04336   5 QELLNTNGARF--RVLDHPPEGT--SEEVAAIRGTELGQGAKALLCKVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DBX_A       85 E*ADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALE-FETIYVSGGKRGLSVEIAPQD---LAKVLGAEFT 153
Cdd:cd04336  81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDrGDEIAFNAGRLDASVVLDTADylrIARPLVLQFT 153
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 31-151 5.90e-08

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: 48.88  E-value: 5.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A       31 DEAA--EKLGIDPNRSFKTLLVA--ENGDQKKLACFVLATAN*LNLKKAAKS-IGVKKVE*ADKDAAQKSTGYLVGGISP 105
Cdd:cd04939  13 DTAAfcARYGFGLEDSANCVVVAgkRGGEERYAACVVLATTR-ADVNGVVKRrLGARKASFAPMETAVELTGMEYGGITP 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
1DBX_A      106 LGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAE 151
Cdd:cd04939  92 VGLPAGWPILVDSAVAERPAVVIGSGVRRSKLLLPGAALAELPGAE 137
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 31-120 1.38e-06

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 46.62  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        31 DEAAEKLGIDPNRSFKTLLVAENGdqkKLACFVLATAN*LNLKKAAKSIGVKKVE*ADKDAAQKSTGYLVGGISPLGQKK 110
Cdd:PRK09194 262 EELAEFLNVPAEKTVKTLLVKADG---ELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPK 338

                         90
                 ....*....|
1DBX_A       111 RVKTVINSTA 120
Cdd:PRK09194 339 DVPIIADRSV 348
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 26-120 1.50e-06

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: 45.20  E-value: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A       26 NQHFGDEAAEKLGIDPNRSFKTLLVAENGDQKKLACFVLATAN*LNLKKAAKSIGVKKVE*ADKDAAQKSTGYLVGGISP 105
Cdd:cd04334  34 GQKTIEELAEFLGVPPSQTVKTLLVKADGEEELVAVLLRGDHE-LNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGP 112

                        90
                ....*....|....*
1DBX_A      106 LGQKKrVKTVINSTA 120
Cdd:cd04334 113 VGLKK-IPIIADRSV 126
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 5-150 1.40e-04

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


Pssm-ID: 442974  Cd Length: 162  Bit Score: 39.73  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DBX_A        5 IDLLKKQKIPFilHTYDHDPnnqHFGDEAAEKLGID-PNRSFKTLLVaENGDQKKLACFVLATAN*LNLKKAAKSIGVKK 83
Cdd:COG3760   8 YALLDELGIPY--ETVEHPP---VFTVEEAEALRGDlPGAHTKNLFL-RDKKGTRFYLVVVPEDKRVDLKALSKQLGSGR 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1DBX_A       84 VE*ADKDAAQKSTGYLVGGISPLG----QKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGA 150
Cdd:COG3760  82 LSFASPERLEEYLGVTPGSVTPFGlindTENRVTVVLDADLLEAELINCHPLVNTATLKISTDDLLRFLEA 152
 
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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