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Conserved domains on  [gi|502926101|ref|WP_013161077|]
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MULTISPECIES: Cys-tRNA(Pro) deacylase [Propionibacterium]

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 ...
 11-164 3.52e-70

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: 208.85  E-value: 3.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSRYfGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKA 90
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASD-GLEAAEKLGLDPEQVFKTLVVEGDKK-GLVV-AVVPVDEELDLKKLAKALGA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTI 164
Cdd:cd00002   79 KKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 11-164 3.52e-70

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: 208.85  E-value: 3.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSRYfGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKA 90
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASD-GLEAAEKLGLDPEQVFKTLVVEGDKK-GLVV-AVVPVDEELDLKKLAKALGA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTI 164
Cdd:cd00002   79 KKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 11-164 2.51e-56

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: 173.96  E-value: 2.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101   11 TPATVALARTGLPHTLHPYVHDPRSRYfGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKA 90
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLD-GESAAEKLGVDPHRVFKTLVAEGDKK-GPVV-AVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502926101   91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTI 164
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADI 151
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 11-167 9.30e-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: 172.58  E-value: 9.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSryfGEEAAAALHVDPARVFKTLVVELTSGPeplVTAVIPADNHLDLKQIAALSKA 90
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAAT---AEEAAEALGVPPEQIAKTLVFRGDGGP---VLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTISRP 167
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
11-167 4.52e-53

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 166.07  E-value: 4.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSRYFGEEAAAALHVDPARVFKTLVVELTSGPEPLVTAVIPADNHLDLKQIAALSKA 90
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTISRP 167
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARR 158
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 40-156 4.03e-26

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: 96.13  E-value: 4.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101   40 EEAAAALHVDPARVFKTLVVElTSGPEPLVtAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLG-QK 118
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLK-DKKGKYVL-VVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKA 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502926101  119 RQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRA 156
Cdd:pfam04073  86 KGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 11-164 3.52e-70

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: 208.85  E-value: 3.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSRYfGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKA 90
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDASD-GLEAAEKLGLDPEQVFKTLVVEGDKK-GLVV-AVVPVDEELDLKKLAKALGA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTI 164
Cdd:cd00002   79 KKVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 11-164 2.51e-56

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: 173.96  E-value: 2.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101   11 TPATVALARTGLPHTLHPYVHDPRSRYfGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKA 90
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLD-GESAAEKLGVDPHRVFKTLVAEGDKK-GPVV-AVIPGDEELDLKKLAKASGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502926101   91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTI 164
Cdd:TIGR00011  78 KKAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADI 151
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 11-167 9.30e-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: 172.58  E-value: 9.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSryfGEEAAAALHVDPARVFKTLVVELTSGPeplVTAVIPADNHLDLKQIAALSKA 90
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAAT---AEEAAEALGVPPEQIAKTLVFRGDGGP---VLAVVPGDRRLDLKKLAAALGA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTISRP 167
Cdd:COG2606   75 KKVEMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
11-167 4.52e-53

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 166.07  E-value: 4.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  11 TPATVALARTGLPHTLHPYVHDPRSRYFGEEAAAALHVDPARVFKTLVVELTSGPEPLVTAVIPADNHLDLKQIAALSKA 90
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502926101  91 KRAALADPAVAQRVTGFVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGRLGTISRP 167
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADIARR 158
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 27-157 1.06e-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: 136.13  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  27 HPYVHDPrSRYFGEEAAAALHVDPARVFKTLVVELTSGpEPLVtAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTG 106
Cdd:cd04332    3 LEYEHTP-GAKTIEEAAEALGVPPGQIAKTLVLKDDKG-GLVL-VVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502926101 107 FVRGGISPLGQKRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRAT 157
Cdd:cd04332   80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLL 130
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 40-156 4.03e-26

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: 96.13  E-value: 4.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101   40 EEAAAALHVDPARVFKTLVVElTSGPEPLVtAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLG-QK 118
Cdd:pfam04073   8 EELAAALGVPPGRIAKTLVLK-DKKGKYVL-VVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKA 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 502926101  119 RQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRA 156
Cdd:pfam04073  86 KGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 40-160 8.21e-18

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: 75.23  E-value: 8.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  40 EEAAAALHVDPARVFKTLVVELTSGPeplVTAVIPADNHLDLKQIAALSKAKrAALADPAVAQRVTGFVRGGISPLGQKR 119
Cdd:cd04333   28 ALAAEALGCEPGQIAKSLVFRVDDEP---VLVVTSGDARVDNKKFKALFGEK-LKMADAEEVRELTGFAIGGVCPFGHPE 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502926101 120 QTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDLVRATHGR 160
Cdd:cd04333  104 PLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAE 144
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 40-155 5.86e-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: 5.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  40 EEAAAALHVDPARVFKTLVVELTSGPEPLVTAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLGQKR 119
Cdd:cd04336   27 EEVAAIRGTELGQGAKALLCKVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKADLASPEEAEELTGCVIGAVPPFSFDP 106

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502926101 120 QTPVIIDQS-AAAAPTIFVSGGRRGLSVEMAPDDLVR 155
Cdd:cd04336  107 KLKLIADPSlLDRGDEIAFNAGRLDASVVLDTADYLR 143
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 40-140 1.83e-12

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 64.33  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  40 EEAAAALHVDPARVFKTLVVEltsGPEPLVTAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLGQKR 119
Cdd:PRK09194 262 EELAEFLNVPAEKTVKTLLVK---ADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPK 338

                         90       100
                 ....*....|....*....|.
gi 502926101 120 QTPVIIDQSAAAApTIFVSGG 140
Cdd:PRK09194 339 DVPIIADRSVADM-SNFVVGA 358
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 40-140 4.50e-10

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: 55.21  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  40 EEAAAALHVDPARVFKTLVVeLTSGPEPLVTAVIPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLGQKr 119
Cdd:cd04334   39 EELAEFLGVPPSQTVKTLLV-KADGEEELVAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLK- 116

                         90       100
                 ....*....|....*....|.
gi 502926101 120 QTPVIIDQSAAAApTIFVSGG 140
Cdd:cd04334  117 KIPIIADRSVADL-KNFVCGA 136
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 40-153 8.47e-04

PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


Pssm-ID: 240137  Cd Length: 139  Bit Score: 37.71  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  40 EEAAAALHVDPARVFKTLVVELT-SGPEPLVTAVIPADNHLDL-KQIAALSKAKRAALADPAVAQRVTGFVRGGISPLGQ 117
Cdd:cd04939   15 AAFCARYGFGLEDSANCVVVAGKrGGEERYAACVVLATTRADVnGVVKRRLGARKASFAPMETAVELTGMEYGGITPVGL 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502926101 118 KRQTPVIIDQSAAAAPTIFVSGGRRGLSVEMAPDDL 153
Cdd:cd04939   95 PAGWPILVDSAVAERPAVVIGSGVRRSKLLLPGAAL 130
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 68-155 1.22e-03

This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins.


Pssm-ID: 239827  Cd Length: 156  Bit Score: 37.50  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502926101  68 LVTAviPADNHLDLKQIAALSKAKRAALADPAVAQRVTGFVRGGISPLG----QKRQTPVIIDQSAAAAPTIFVSGGRRG 143
Cdd:cd04335   55 LVTA--LHDKKVDLKALSKQLGASRLSFASEERLEEKLGVTPGSVTPFAlindKENDVQVVLDKDLLEEERVGFHPLTNT 132

                         90
                 ....*....|..
gi 502926101 144 LSVEMAPDDLVR 155
Cdd:cd04335  133 ATVGISTEDLLK 144
 
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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