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Conserved domains on  [gi|1129021608|gb|APT48695|]
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deacylase [Bacillus safensis]

Protein Classification

aminoacyl-tRNA deacylase( domain architecture ID 10006507)

aminoacyl-tRNA deacylase of the YbaK/EbsC family, such as Haemophilus influenzae cysteinyl-tRNA(Pro) deacylase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-158 8.37e-43

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: 139.07  E-value: 8.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   5 PAHDFLDKHGIPYEIKTFSAETeKGAANVATALGFRERQMIKTLIFEtGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKM 84
Cdd:COG2606     2 PVRRALDAAGIPYEVVEHPEPA-ATAEEAAEALGVPPEQIAKTLVFR-GDGGPVLAVVPGDRRLDLKKLAAALGAKKVEM 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129021608  85 ASPEKVLEVTGYRIGSIPPFCwQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPFDIVQPA 158
Cdd:COG2606    80 ADPEEVERLTGYEVGGVSPFG-LKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
 
Name Accession Description Interval E-value
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-158 8.37e-43

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: 139.07  E-value: 8.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   5 PAHDFLDKHGIPYEIKTFSAETeKGAANVATALGFRERQMIKTLIFEtGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKM 84
Cdd:COG2606     2 PVRRALDAAGIPYEVVEHPEPA-ATAEEAAEALGVPPEQIAKTLVFR-GDGGPVLAVVPGDRRLDLKKLAAALGAKKVEM 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129021608  85 ASPEKVLEVTGYRIGSIPPFCwQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPFDIVQPA 158
Cdd:COG2606    80 ADPEEVERLTGYEVGGVSPFG-LKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 25-146 2.71e-35

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: 118.86  E-value: 2.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  25 ETEKGAANVATALGFRERQMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPF 104
Cdd:pfam04073   2 PPAATIEELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1129021608 105 CWQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKA 146
Cdd:pfam04073  82 GLKAKGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 28-152 7.67e-30

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: 105.70  E-value: 7.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  28 KGAANVATALGFRERQMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFCwQ 107
Cdd:cd04332    12 KTIEEAAEALGVPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTGCEPGGVGPFG-L 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1129021608 108 PEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPF 152
Cdd:cd04332    91 KKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGEAEV 135
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 31-133 2.64e-06

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 45.85  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  31 ANVATALGFRERQMIKTLIFeTGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFCwQPEG 110
Cdd:PRK09194  262 EELAEFLNVPAEKTVKTLLV-KADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVG-LPKD 339

                          90       100
                  ....*....|....*....|...
gi 1129021608 111 FRTIIEASLLEEEILGVGAGEWG 133
Cdd:PRK09194  340 VPIIADRSVADMSNFVVGANEDD 362
 
Name Accession Description Interval E-value
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 5-158 8.37e-43

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: 139.07  E-value: 8.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   5 PAHDFLDKHGIPYEIKTFSAETeKGAANVATALGFRERQMIKTLIFEtGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKM 84
Cdd:COG2606     2 PVRRALDAAGIPYEVVEHPEPA-ATAEEAAEALGVPPEQIAKTLVFR-GDGGPVLAVVPGDRRLDLKKLAAALGAKKVEM 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129021608  85 ASPEKVLEVTGYRIGSIPPFCwQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPFDIVQPA 158
Cdd:COG2606    80 ADPEEVERLTGYEVGGVSPFG-LKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARPA 152
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 25-146 2.71e-35

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: 118.86  E-value: 2.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  25 ETEKGAANVATALGFRERQMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPF 104
Cdd:pfam04073   2 PPAATIEELAAALGVPPGRIAKTLVLKDKKGKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1129021608 105 CWQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKA 146
Cdd:pfam04073  82 GLKAKGVPVLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 28-152 7.67e-30

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: 105.70  E-value: 7.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  28 KGAANVATALGFRERQMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFCwQ 107
Cdd:cd04332    12 KTIEEAAEALGVPPGQIAKTLVLKDDKGGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTGCEPGGVGPFG-L 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1129021608 108 PEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPF 152
Cdd:cd04332    91 KKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLGEAEV 135
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 3-154 5.88e-29

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: 103.69  E-value: 5.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   3 KLPAHDFLDKHGIPYEIKTFSAETEKG-AANVATALGFRERQMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRN 81
Cdd:cd00002     1 KTPAIRLLDKAKIPYELHEYEHDEDASdGLEAAEKLGLDPEQVFKTLVVEGDKKGLVVAVVPVDEELDLKKLAKALGAKK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129021608  82 IKMASPEKVLEVTGYRIGSIPPFCwQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPFDI 154
Cdd:cd00002    81 VEMAPPKDAERLTGYIRGGISPLG-QKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 8-154 2.00e-20

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: 81.78  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   8 DFLDKHGIPYEIKTFSAETeKGAANVATALGFRERQMIKTLIFEtGEGEQLLVMVGADQHIKSGKLKKAAGSRnIKMASP 87
Cdd:cd04333     6 AFLAARGLDLEVIELPEST-RTAALAAEALGCEPGQIAKSLVFR-VDDEPVLVVTSGDARVDNKKFKALFGEK-LKMADA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129021608  88 EKVLEVTGYRIGSIPPFCwQPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQLVKASKAVPFDI 154
Cdd:cd04333    83 EEVRELTGFAIGGVCPFG-HPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 8-121 1.46e-13

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: 63.90  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   8 DFLDKHGIPYEIKTFSAE--TEKGAANVATALGfrerQMIKTLI--FETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIK 83
Cdd:cd04336     6 ELLNTNGARFRVLDHPPEgtSEEVAAIRGTELG----QGAKALLckVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKAD 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1129021608  84 MASPEKVLEVTGYRIGSIPPFCWQPEgFRTIIEASLLE 121
Cdd:cd04336    82 LASPEEAEELTGCVIGAVPPFSFDPK-LKLIADPSLLD 118
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 33-133 1.50e-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: 56.37  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  33 VATALGFRERQMIKTLIFETGEGEQL-LVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFcwQPEGF 111
Cdd:cd04334    41 LAEFLGVPPSQTVKTLLVKADGEEELvAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPV--GLKKI 118

                          90       100
                  ....*....|....*....|..
gi 1129021608 112 RTIIEASLLEEEILGVGAGEWG 133
Cdd:cd04334   119 PIIADRSVADLKNFVCGANEDD 140
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 8-145 1.33e-08

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: 50.98  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   8 DFLDKHGIPYEIKTFSAetekgAANVATALGFRER---QMIKTLIFETGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKM 84
Cdd:cd04335     6 ALLDELGIAYETVEHPP-----VFTVEEADEVLGElpgAHTKNLFLKDKKGRLYLVTALHDKKVDLKALSKQLGASRLSF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129021608  85 ASPEKVLEVTGYRIGSIPPF---CWQPEGFRTIIEASLLEEEILGVGAGEwgNE--ILITPEQLVK 145
Cdd:cd04335    81 ASEERLEEKLGVTPGSVTPFaliNDKENDVQVVLDKDLLEEERVGFHPLT--NTatVGISTEDLLK 144
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 7-127 2.29e-08

Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only];


Pssm-ID: 442974  Cd Length: 162  Bit Score: 50.51  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608   7 HDFLDKHGIPYEIKT----FSAEtekGAANVATALGFrerQMIKTLIFETGEGEQL-LVMVGADQHIKSGKLKKAAGSRN 81
Cdd:COG3760     8 YALLDELGIPYETVEhppvFTVE---EAEALRGDLPG---AHTKNLFLRDKKGTRFyLVVVPEDKRVDLKALSKQLGSGR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1129021608  82 IKMASPEKVLEVTGYRIGSIPPFCW---QPEGFRTIIEASLLEEEILGV 127
Cdd:COG3760    82 LSFASPERLEEYLGVTPGSVTPFGLindTENRVTVVLDADLLEAELINC 130
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 31-133 2.64e-06

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 45.85  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129021608  31 ANVATALGFRERQMIKTLIFeTGEGEQLLVMVGADQHIKSGKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFCwQPEG 110
Cdd:PRK09194  262 EELAEFLNVPAEKTVKTLLV-KADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVG-LPKD 339

                          90       100
                  ....*....|....*....|...
gi 1129021608 111 FRTIIEASLLEEEILGVGAGEWG 133
Cdd:PRK09194  340 VPIIADRSVADMSNFVVGANEDD 362
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 71-143 7.89e-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: 7.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129021608  71 GKLKKAAGSRNIKMASPEKVLEVTGYRIGSIPPFCWqPEGFRTIIEASLLEEEILGVGAGEWGNEILITPEQL 143
Cdd:cd04939    59 GVVKRRLGARKASFAPMETAVELTGMEYGGITPVGL-PAGWPILVDSAVAERPAVVIGSGVRRSKLLLPGAAL 130
 
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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