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Conserved domains on  [gi|1052836955|emb|SCI64786|]
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Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase ybaK [uncultured Clostridium sp.]

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 ...
 9-160 2.53e-73

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: 216.55  E-value: 2.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEvGEHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKK 88
Cdd:cd00002     2 TPAIRLLDKAKIPYELHEYEHDE-DASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADI 160
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 ...
 9-160 2.53e-73

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: 216.55  E-value: 2.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEvGEHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKK 88
Cdd:cd00002     2 TPAIRLLDKAKIPYELHEYEHDE-DASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADI 160
Cdd:cd00002    81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 9-161 4.18e-61

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: 185.51  E-value: 4.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEVGEhFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKK 88
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKGPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADIT 161
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 9-163 4.63e-56

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: 172.97  E-value: 4.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEvgeHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVsCIAVNHEVDLKKLAKVSGNKK 88
Cdd:COG2606     1 TPVRRALDAAGIPYEVVEHPEPA---ATAEEAAEALGVPPEQIAKTLVFRGDGGPVLA-VVPGDRRLDLKKLAAALGAKK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADITKE 163
Cdd:COG2606    77 VEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
9-162 2.18e-33

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 115.61  E-value: 2.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEVGEHFGEAIAEMTGIPAEKSFKTLVA--RGDKTGIMVSCIAVNHEVDLKKLAKVSGN 86
Cdd:PRK10670    2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVavNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052836955  87 KKVEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADITK 162
Cdd:PRK10670   82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIAR 157
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 38-152 1.38e-25

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: 94.59  E-value: 1.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  38 EAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKKVEMIHVKELLGLTGYIRGGVSPVGMKKK- 116
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGLKAKg 87

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1052836955 117 YPTYINETAQNFETIAISGGRCGTTLILSPNDVQKA 152
Cdd:pfam04073  88 VPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 9-160 2.53e-73

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: 216.55  E-value: 2.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEvGEHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKK 88
Cdd:cd00002     2 TPAIRLLDKAKIPYELHEYEHDE-DASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADI 160
Cdd:cd00002    81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 9-161 4.18e-61

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: 185.51  E-value: 4.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEVGEhFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKK 88
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKGPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADIT 161
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 9-163 4.63e-56

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: 172.97  E-value: 4.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEvgeHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVsCIAVNHEVDLKKLAKVSGNKK 88
Cdd:COG2606     1 TPVRRALDAAGIPYEVVEHPEPA---ATAEEAAEALGVPPEQIAKTLVFRGDGGPVLA-VVPGDRRLDLKKLAAALGAKK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052836955  89 VEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADITKE 163
Cdd:COG2606    77 VEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 23-154 7.43e-37

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: 123.42  E-value: 7.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  23 ETVEYEADEvGEHFGEAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKKVEMIHVKELLGLTG 102
Cdd:cd04332     1 EYLEYEHTP-GAKTIEEAAEALGVPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052836955 103 YIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATD 154
Cdd:cd04332    80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLG 131
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
9-162 2.18e-33

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 115.61  E-value: 2.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955   9 TNAMRLLNASKIKYETVEYEADEVGEHFGEAIAEMTGIPAEKSFKTLVA--RGDKTGIMVSCIAVNHEVDLKKLAKVSGN 86
Cdd:PRK10670    2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVavNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052836955  87 KKVEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIAISGGRCGTTLILSPNDVQKATDCVFADITK 162
Cdd:PRK10670   82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIAR 157
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 38-152 1.38e-25

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: 94.59  E-value: 1.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  38 EAIAEMTGIPAEKSFKTLVARGDKTGIMVSCIAVNHEVDLKKLAKVSGNKKVEMIHVKELLGLTGYIRGGVSPVGMKKK- 116
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGLKAKg 87

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1052836955 117 YPTYINETAQNFETIAISGGRCGTTLILSPNDVQKA 152
Cdd:pfam04073  88 VPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 53-160 4.40e-11

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: 57.51  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  53 KTLVARGDKTGIMVsCIAVNHEVDLKKLAKVSGnKKVEMIHVKELLGLTGYIRGGVSPVGMKKKYPTYINETAQNFETIA 132
Cdd:cd04333    43 KSLVFRVDDEPVLV-VTSGDARVDNKKFKALFG-EKLKMADAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVW 120

                          90       100
                  ....*....|....*....|....*...
gi 1052836955 133 ISGGRCGTTLILSPNDVQKATDCVFADI 160
Cdd:cd04333   121 AAAGTPNAAFRLTPDELERLTGAEWVDV 148
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 38-127 5.31e-09

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 53.93  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  38 EAIAEMTGIPAEKSFKTLVARGDKTGIMVsCIAVNHEVDLKKLAKVSGNKKVEMIHVKELLGLTGYIRGGVSPVGMKKKY 117
Cdd:PRK09194  262 EELAEFLNVPAEKTVKTLLVKADGELVAV-LVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPKDV 340

                          90
                  ....*....|
gi 1052836955 118 PTYINETAQN 127
Cdd:PRK09194  341 PIIADRSVAD 350
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 14-148 1.41e-07

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: 48.11  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  14 LLNASKIKYETVEYEAdevgEHFGEAIAEMTGIPAEKSFKTLVARgDKTGIMVSCIAV---NHEVDLKKLAKVSGNKKVE 90
Cdd:cd04336     7 LLNTNGARFRVLDHPP----EGTSEEVAAIRGTELGQGAKALLCK-VKDGSRRFVLAVlpaDKKLDLKAVAAAVGGKKAD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  91 MIHVKELLGLTGYIRGGVSPVGMKKKYPTYINE--TAQNFEtIAISGGRCGTTLILSPND 148
Cdd:cd04336    82 LASPEEAEELTGCVIGAVPPFSFDPKLKLIADPslLDRGDE-IAFNAGRLDASVVLDTAD 140
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 38-115 2.90e-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: 44.81  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  38 EAIAEMTGIPAEKSFKTLVARGDKTG--IMVsCIAVNHEVDLKKLAKVSGNKKVEMIHVKELLGLTGYIRGGVSPVGMKK 115
Cdd:cd04334    39 EELAEFLGVPPSQTVKTLLVKADGEEelVAV-LLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLKK 117
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 38-146 1.64e-03

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: 36.94  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836955  38 EAIAEMTGIPAEKSFKTLVARGDKTGI--MVSCIAV-NHEVDLKKLAKVS-GNKKVEMIHVKELLGLTGYIRGGVSPVGM 113
Cdd:cd04939    15 AAFCARYGFGLEDSANCVVVAGKRGGEerYAACVVLaTTRADVNGVVKRRlGARKASFAPMETAVELTGMEYGGITPVGL 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1052836955 114 KKKYPTYINETAQNFETIAISGGRCGTTLILSP 146
Cdd:cd04939    95 PAGWPILVDSAVAERPAVVIGSGVRRSKLLLPG 127
 
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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