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Conserved domains on  [gi|489715773|ref|WP_003619897|]
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aminoacyl-tRNA deacylase [Lactobacillus delbrueckii]

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 ...
 14-166 7.43e-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: 203.07  E-value: 7.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  14 TLVEKILDQHKIAYEQHISEISEDHGVAQVGTGKPVLDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKC 93
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKKV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489715773  94 EMIPLKQLEKTTGYVHGANTPIGIYhsKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:cd00002   82 EMAPPKDAERLTGYIRGGISPLGQK--KRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 14-166 7.43e-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: 203.07  E-value: 7.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  14 TLVEKILDQHKIAYEQHISEISEDHGVAQVGTGKPVLDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKC 93
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKKV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489715773  94 EMIPLKQLEKTTGYVHGANTPIGIYhsKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:cd00002   82 EMAPPKDAERLTGYIRGGISPLGQK--KRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 14-167 4.60e-51

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: 160.48  E-value: 4.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773   14 TLVEKILDQHKIAYEQHISEISEDHGVAQVGTGKPVLDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKC 93
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLDGESAAEKLGVDPHRVFKTLVAEGDKKGPVVAVIPGDEELDLKKLAKASGGKKA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489715773   94 EMIPLKQLEKTTGYVHGANTPIGIyhSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADLQ 167
Cdd:TIGR00011  81 EMADPKDAEKVTGYIRGGISPIGQ--KKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 14-166 8.18e-39

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: 129.44  E-value: 8.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  14 TLVEKILDQHKIAYEQHISEISEDHGV---AQVGtgkpvLDGHPVYKTLAVNGNKtGPIVGVVPLSGHLDLKKIAKASGN 90
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEeaaEALG-----VPPEQIAKTLVFRGDG-GPVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715773  91 KKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFG--LKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADI 148
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 50-158 1.61e-23

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: 89.20  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773   50 LDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKCEMIPLKQLEKTTGYVHGANTPIGIyHSKKFPIFLDE 129
Cdd:pfam04073  16 VPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGL-KAKGVPVLVDE 94

                          90       100
                  ....*....|....*....|....*....
gi 489715773  130 SVLKEDGIWVSSGEVGRSVMVNPLDLQKL 158
Cdd:pfam04073  95 SLKDLPDVVVGAGENGATLRLSNADLRKL 123
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
18-166 4.35e-23

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 89.42  E-value: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  18 KILDQHKIAYEQHiseiSEDHGVAQVGTGKPV-----LDGHPVYKTL--AVNGNKTGPIVGVVPLSGHLDLKKIAKASGN 90
Cdd:PRK10670   6 KLLEKNKISFTLH----TYEHDPAETNFGDEVvrklgLNADQVYKTLlvAVNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715773  91 KKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLG--QKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 14-166 7.43e-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: 203.07  E-value: 7.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  14 TLVEKILDQHKIAYEQHISEISEDHGVAQVGTGKPVLDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKC 93
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKKV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489715773  94 EMIPLKQLEKTTGYVHGANTPIGIYhsKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:cd00002   82 EMAPPKDAERLTGYIRGGISPLGQK--KRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 14-167 4.60e-51

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: 160.48  E-value: 4.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773   14 TLVEKILDQHKIAYEQHISEISEDHGVAQVGTGKPVLDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKC 93
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLDGESAAEKLGVDPHRVFKTLVAEGDKKGPVVAVIPGDEELDLKKLAKASGGKKA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489715773   94 EMIPLKQLEKTTGYVHGANTPIGIyhSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADLQ 167
Cdd:TIGR00011  81 EMADPKDAEKVTGYIRGGISPIGQ--KKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 14-166 8.18e-39

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: 129.44  E-value: 8.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  14 TLVEKILDQHKIAYEQHISEISEDHGV---AQVGtgkpvLDGHPVYKTLAVNGNKtGPIVGVVPLSGHLDLKKIAKASGN 90
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEeaaEALG-----VPPEQIAKTLVFRGDG-GPVLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715773  91 KKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFG--LKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADI 148
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 50-164 3.58e-31

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: 109.17  E-value: 3.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  50 LDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDE 129
Cdd:cd04332   23 VPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTGCEPGGVGPFG--LKKGVPVVVDE 100

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489715773 130 SVLKEDGIWVSSGEVGRSVMVNPLDLQKLVK-ATVA 164
Cdd:cd04332  101 SLLELEDVYVGAGERGADLHLSPADLLRLLGeAEVA 136
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 50-158 1.61e-23

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: 89.20  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773   50 LDGHPVYKTLAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKCEMIPLKQLEKTTGYVHGANTPIGIyHSKKFPIFLDE 129
Cdd:pfam04073  16 VPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGL-KAKGVPVLVDE 94

                          90       100
                  ....*....|....*....|....*....
gi 489715773  130 SVLKEDGIWVSSGEVGRSVMVNPLDLQKL 158
Cdd:pfam04073  95 SLKDLPDVVVGAGENGATLRLSNADLRKL 123
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
18-166 4.35e-23

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 89.42  E-value: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  18 KILDQHKIAYEQHiseiSEDHGVAQVGTGKPV-----LDGHPVYKTL--AVNGNKTGPIVGVVPLSGHLDLKKIAKASGN 90
Cdd:PRK10670   6 KLLEKNKISFTLH----TYEHDPAETNFGDEVvrklgLNADQVYKTLlvAVNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489715773  91 KKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVLKEDGIWVSSGEVGRSVMVNPLDLQKLVKATVADL 166
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLG--QKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 57-165 6.56e-09

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: 51.73  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  57 KTLAVNGnKTGPIVGVVPLSGHLDLKKIAKASGnKKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVLKEDG 136
Cdd:cd04333   43 KSLVFRV-DDEPVLVVTSGDARVDNKKFKALFG-EKLKMADAEEVRELTGFAIGGVCPFG--HPEPLPVYLDESLKRFDE 118

                         90       100       110
                 ....*....|....*....|....*....|
gi 489715773 137 IWVSSGEVgRSVM-VNPLDLQKLVKATVAD 165
Cdd:cd04333  119 VWAAAGTP-NAAFrLTPDELERLTGAEWVD 147
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 59-165 2.78e-06

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: 44.64  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489715773  59 LAVNGNKTGPIVGVVPLSGHLDLKKIAKASGNKKCEMIPLKQLEKTTGYVHGANTPIGiyHSKKFPIFLDESVL-KEDGI 137
Cdd:cd04336   46 CKVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKADLASPEEAEELTGCVIGAVPPFS--FDPKLKLIADPSLLdRGDEI 123

                         90       100
                 ....*....|....*....|....*...
gi 489715773 138 WVSSGEVGRSVMVNPLDLQKLVKATVAD 165
Cdd:cd04336  124 AFNAGRLDASVVLDTADYLRIARPLVLQ 151
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 57-131 3.92e-03

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: 35.95  E-value: 3.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489715773  57 KTLAVNGNKTGPIVGVVpLSG--HLDLKKIAKASGNKKCEMIPLKQLEKTTGYVHGAntpIGIYHSKKFPIFLDESV 131
Cdd:cd04334   54 KTLLVKADGEEELVAVL-LRGdhELNEVKLENLLGAAPLELASEEEIEAATGAPPGF---IGPVGLKKIPIIADRSV 126
 
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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