NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490570396|ref|WP_004435416|]
View 

MULTISPECIES: Cys-tRNA(Pro) deacylase [Sinorhizobium]

Protein Classification

aminoacyl-tRNA deacylase( domain architecture ID 10025411)

aminoacyl-tRNA deacylase of the YbaK/EbsC family

Gene Ontology:  GO:0016829

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 5-143 9.33e-61

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: 184.58  E-value: 9.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYDYDPGAErVGLQAAEALGEDPSRVLKTLMAEVDGK-PVCCIVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396  84 ASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQD 140
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 5-143 9.33e-61

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: 184.58  E-value: 9.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYDYDPGAErVGLQAAEALGEDPSRVLKTLMAEVDGK-PVCCIVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396  84 ASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQD 140
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 5-143 1.10e-55

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: 171.65  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396    5 TRATQALAKAGVIFTVHSYDYDPGAErVGLQAAEALGEDPSRVLKTLMAEVDGK-PVCCIVPSDREVSMKKLAAAFGGKS 83
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKgPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   84 ASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDD 139
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-143 3.85e-51

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: 160.26  E-value: 3.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYdydPGAERVGLQAAEALGEDPSRVLKTLMAEVDGKPVCCIVPSDREVSMKKLAAAFGGKSA 84
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490570396  85 SMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:COG2606   78 EMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPAD 136
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
5-143 3.35e-32

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 112.15  E-value: 3.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYDYDPGAERVGLQAAEALGEDPSRVLKTLMAEVDGKP---VCCIVPSDREVSMKKLAAAFGG 81
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMkhlAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490570396  82 KSASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGD 143
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 35-143 4.30e-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: 79.95  E-value: 4.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   35 QAAEALGEDPSRVLKTLMAEV-DGKPVCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTGYHVGGISPFG-QRKTV 112
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGV 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 490570396  113 PTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:pfam04073  89 PVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 5-143 9.33e-61

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: 184.58  E-value: 9.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYDYDPGAErVGLQAAEALGEDPSRVLKTLMAEVDGK-PVCCIVPSDREVSMKKLAAAFGGKS 83
Cdd:cd00002    2 TPAIRLLDKAKIPYELHEYEHDEDAS-DGLEAAEKLGLDPEQVFKTLVVEGDKKgLVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396  84 ASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQD 140
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 5-143 1.10e-55

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: 171.65  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396    5 TRATQALAKAGVIFTVHSYDYDPGAErVGLQAAEALGEDPSRVLKTLMAEVDGK-PVCCIVPSDREVSMKKLAAAFGGKS 83
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHL-DGESAAEKLGVDPHRVFKTLVAEGDKKgPVVAVIPGDEELDLKKLAKASGGKK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   84 ASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:TIGR00011  80 AEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDD 139
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-143 3.85e-51

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: 160.26  E-value: 3.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYdydPGAERVGLQAAEALGEDPSRVLKTLMAEVDGKPVCCIVPSDREVSMKKLAAAFGGKSA 84
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEH---PEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490570396  85 SMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:COG2606   78 EMADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPAD 136
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
5-143 3.35e-32

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 112.15  E-value: 3.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   5 TRATQALAKAGVIFTVHSYDYDPGAERVGLQAAEALGEDPSRVLKTLMAEVDGKP---VCCIVPSDREVSMKKLAAAFGG 81
Cdd:PRK10670   2 TPAVKLLEKNKISFTLHTYEHDPAETNFGDEVVRKLGLNADQVYKTLLVAVNGDMkhlAVAVTPVAGQLDLKKVAKALGA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490570396  82 KSASMMKPADAERLTGYHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:PRK10670  82 KKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGD 143
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 19-143 3.74e-32

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: 111.48  E-value: 3.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396  19 TVHSYDYDPGAeRVGLQAAEALGEDPSRVLKTLMAEVD-GKPVCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTG 97
Cdd:cd04332    1 EYLEYEHTPGA-KTIEEAAEALGVPPGQIAKTLVLKDDkGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490570396  98 YHVGGISPFGQRKTVPTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:cd04332   80 CEPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPAD 125
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 35-143 4.30e-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: 79.95  E-value: 4.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   35 QAAEALGEDPSRVLKTLMAEV-DGKPVCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTGYHVGGISPFG-QRKTV 112
Cdd:pfam04073   9 ELAAALGVPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGV 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 490570396  113 PTAIEEAALAEALVFINGGQRGLQVRLAPKD 143
Cdd:pfam04073  89 PVLVDESLKDLPDVVVGAGENGATLRLSNAD 119
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 6-114 7.18e-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: 7.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396   6 RATQALAKAGVIFTVHSYdydPGAERVGLQAAEALGEDPSRVLKTLMAEVDGKPVCCIVPSDREVSMKKLAAAFGGKsAS 85
Cdd:cd04333    3 RVRAFLAARGLDLEVIEL---PESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEK-LK 78

                         90       100
                 ....*....|....*....|....*....
gi 490570396  86 MMKPADAERLTGYHVGGISPFGQRKTVPT 114
Cdd:cd04333   79 MADAEEVRELTGFAIGGVCPFGHPEPLPV 107
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 37-113 5.94e-12

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 62.02  E-value: 5.94e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490570396  37 AEALGEDPSRVLKTLMAEVDGKPVCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTGYHVGGISPFGQRKTVP 113
Cdd:PRK09194 265 AEFLNVPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPKDVP 341
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 29-107 2.56e-11

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


Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 58.12  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490570396  29 AERVGLQAAEALGEDPSRVLKTLMAEVDGKP---VCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTGYHVGGISP 105
Cdd:cd04336   22 PEGTSEEVAAIRGTELGQGAKALLCKVKDGSrrfVLAVLPADKKLDLKAVAAAVGGKKADLASPEEAEELTGCVIGAVPP 101


                 ..
gi 490570396 106 FG 107
Cdd:cd04336  102 FS 103
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 37-107 1.02e-09

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: 54.06  E-value: 1.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490570396  37 AEALGEDPSRVLKTL--MAEVDGKPVCCIVPSDREVSMKKLAAAFGGKSASMMKPADAERLTGYHVGGISPFG 107
Cdd:cd04334   42 AEFLGVPPSQTVKTLlvKADGEEELVAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVG 114
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH