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Conserved domains on  [gi|742395903|ref|WP_038875028|]
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MULTISPECIES: Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK [Serratia]

Protein Classification

aminoacyl-tRNA deacylase( domain architecture ID 10793438)

aminoacyl-tRNA deacylase of the YbaK/EbsC family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 2.83e-111

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


:

Pssm-ID: 182634  Cd Length: 159  Bit Score: 312.83  E-value: 2.83e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   1 MTPAVVLLEKQKVTFTLHPYHHDSEETNFGDEAVRKLGLDADRVYKTLLVALNGDAKHLAVAVTPVATQLDLKKVARALG 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395903  81 AKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIAKRD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
 
Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 2.83e-111

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 312.83  E-value: 2.83e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   1 MTPAVVLLEKQKVTFTLHPYHHDSEETNFGDEAVRKLGLDADRVYKTLLVALNGDAKHLAVAVTPVATQLDLKKVARALG 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395903  81 AKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIAKRD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 1.75e-81

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: 236.96  E-value: 1.75e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   1 MTPAVVLLEKQKVTFTLHPYHHDsEETNFGDEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVTPVATQLDLKKVARALG 80
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHD-EDASDGLEAAEKLGLDPEQVFKTLVVE--GDKKGLVVAVVPVDEELDLKKLAKALG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395903  81 AKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADI 155
Cdd:cd00002   78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 8.81e-64

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: 192.45  E-value: 8.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903    2 TPAVVLLEKQKVTFTLHPYHHDsEETNFGDEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVTPVATQLDLKKVARALGA 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVD-PDHLDGESAAEKLGVDPHRVFKTLVAE--GDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395903   82 KKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIA 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-159 8.19e-58

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: 177.20  E-value: 8.19e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   2 TPAVVLLEKQKVTFTLHPYHHDseeTNFGDEAVRKLGLDADRVYKTLLVALNGDakhLAVAVTPVATQLDLKKVARALGA 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEP---AATAEEAAEALGVPPEQIAKTLVFRGDGG---PVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395903  82 KKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIAKRD 159
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-147 1.81e-20

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: 81.11  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   32 EAVRKLGLDADRVYKTLLVAlNGDAKHLAVAVtPVATQLDLKKVARALGAKKAEMADPQLAQRVTGYLVGGISPLG-QKK 110
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVLK-DKKGKYVLVVV-PGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAK 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 742395903  111 RLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRL 147
Cdd:pfam04073  87 GVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
 
Name Accession Description Interval E-value
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-159 2.83e-111

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 312.83  E-value: 2.83e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   1 MTPAVVLLEKQKVTFTLHPYHHDSEETNFGDEAVRKLGLDADRVYKTLLVALNGDAKHLAVAVTPVATQLDLKKVARALG 80
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395903  81 AKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIAKRD 159
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARRD 159
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-155 1.75e-81

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: 236.96  E-value: 1.75e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   1 MTPAVVLLEKQKVTFTLHPYHHDsEETNFGDEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVTPVATQLDLKKVARALG 80
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHD-EDASDGLEAAEKLGLDPEQVFKTLVVE--GDKKGLVVAVVPVDEELDLKKLAKALG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395903  81 AKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADI 155
Cdd:cd00002   78 AKKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-156 8.81e-64

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: 192.45  E-value: 8.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903    2 TPAVVLLEKQKVTFTLHPYHHDsEETNFGDEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVTPVATQLDLKKVARALGA 81
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVD-PDHLDGESAAEKLGVDPHRVFKTLVAE--GDKKGPVVAVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395903   82 KKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIA 156
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-159 8.19e-58

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: 177.20  E-value: 8.19e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   2 TPAVVLLEKQKVTFTLHPYHHDseeTNFGDEAVRKLGLDADRVYKTLLVALNGDakhLAVAVTPVATQLDLKKVARALGA 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEP---AATAEEAAEALGVPPEQIAKTLVFRGDGG---PVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395903  82 KKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIAKRD 159
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 18-149 1.48e-40

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: 132.67  E-value: 1.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903  18 HPYHHDsEETNFGDEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVTPVATQLDLKKVARALGAKKAEMADPQLAQRVTG 97
Cdd:cd04332    3 LEYEHT-PGAKTIEEAAEALGVPPGQIAKTLVLK--DDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742395903  98 YLVGGISPLGQKKRLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLA 149
Cdd:cd04332   80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLG 131
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-147 1.81e-20

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: 81.11  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   32 EAVRKLGLDADRVYKTLLVAlNGDAKHLAVAVtPVATQLDLKKVARALGAKKAEMADPQLAQRVTGYLVGGISPLG-QKK 110
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVLK-DKKGKYVLVVV-PGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAK 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 742395903  111 RLPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRL 147
Cdd:pfam04073  87 GVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 5-156 3.48e-16

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: 70.84  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903   5 VVLLEKQKVTFTLhpYHHDSEETNfgDEAVRKLGLDADRVYKTLLVALNGDAKHLAVAVTPVATQLDLKKVARALGAKKA 84
Cdd:cd04336    5 QELLNTNGARFRV--LDHPPEGTS--EEVAAIRGTELGQGAKALLCKVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395903  85 EMADPQLAQRVTGYLVGGISPLGQKKRLPTVID-SPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADIA 156
Cdd:cd04336   81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADpSLLDRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQFT 153
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 32-155 5.64e-14

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: 64.83  E-value: 5.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903  32 EAVRKLGLDADRVYKTLLVALNGDAkhlAVAVTPVATQLDLKKVARALGaKKAEMADPQLAQRVTGYLVGGISPLGQKKR 111
Cdd:cd04333   29 LAAEALGCEPGQIAKSLVFRVDDEP---VLVVTSGDARVDNKKFKALFG-EKLKMADAEEVRELTGFAIGGVCPFGHPEP 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742395903 112 LPTVIDSPAQAFATIYVSGGKRGLDIELAAADLCRLLAGSFADI 155
Cdd:cd04333  105 LPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 31-117 8.83e-07

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 47.39  E-value: 8.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903  31 DEAVRKLGLDADRVYKTLLVAlnGDAKHLAVAVtPVATQLDLKKVARALGAKKAEMADPQLAQRVTGYLVGGISPLGQKK 110
Cdd:PRK09194 262 EELAEFLNVPAEKTVKTLLVK--ADGELVAVLV-RGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPK 338


                 ....*..
gi 742395903 111 RLPTVID 117
Cdd:PRK09194 339 DVPIIAD 345
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 38-147 5.37e-05

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: 40.79  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903  38 GLDADRVYKTLLVALN-GDAKHLAVAVTPVATQLDLKKVARA-LGAKKAEMADPQLAQRVTGYLVGGISPLGQKKRLPTV 115
Cdd:cd04939   22 GFGLEDSANCVVVAGKrGGEERYAACVVLATTRADVNGVVKRrLGARKASFAPMETAVELTGMEYGGITPVGLPAGWPIL 101

                         90       100       110
                 ....*....|....*....|....*....|..
gi 742395903 116 IDSPAQAFATIYVSGGKRGLDIELAAADLCRL 147
Cdd:cd04939  102 VDSAVAERPAVVIGSGVRRSKLLLPGAALAEL 133
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 31-117 5.65e-05

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: 40.96  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395903  31 DEAVRKLGLDADRVYKTLLVALNGDAKHLAVAVtpvatQLDLKKVARALGAKKAEMADPQLAQRVTGYLVGGISPLGQKK 110
Cdd:cd04334   39 EELAEFLGVPPSQTVKTLLVKADGEEELVAVLLrg-dhELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLKK 117


                 ....*..
gi 742395903 111 rLPTVID 117
Cdd:cd04334  118 -IPIIAD 123
 
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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