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Conserved domains on  [gi|555036833|gb|ESL81154|]
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prolyl-tRNA synthetase [Enterobacter roggenkampii]

Protein Classification

YbaK/EbsC family protein( domain architecture ID 10137841)

YbaK/EbsC family protein similar to Aeropyrum pernix Ape2540 YbaK a putative trans-editing enzyme for prolyl-tRNA synthetase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 3-150 8.58e-64

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: 191.95  E-value: 8.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   3 LQSVQQFFADNAPDIDVIELSQSTATVALAAAAHRVEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555036833  83 SSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDV 150
Cdd:cd04333   81 DAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
 
Name Accession Description Interval E-value
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 3-150 8.58e-64

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: 191.95  E-value: 8.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   3 LQSVQQFFADNAPDIDVIELSQSTATVALAAAAHRVEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555036833  83 SSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDV 150
Cdd:cd04333   81 DAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 4-151 3.55e-47

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: 149.86  E-value: 3.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   4 QSVQQFFADNAPDIDVIELSQSTATVALAAAAHRVEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGA-KARML 82
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAkKVEMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555036833  83 SSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDVC 151
Cdd:COG2606   81 DPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIA 149
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 38-142 6.04e-22

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: 84.58  E-value: 6.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   38 VEPGQIAKTLSLKV-KNEVILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGL-ENPLAVYCDIS 114
Cdd:pfam04073  16 VPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKrLRLASEEELLELTGVEPGGVTPFGLkAKGVPVLVDES 95

                          90       100
                  ....*....|....*....|....*...
gi 555036833  115 LKQYAEVLPAAGAIHSAVRISPDRMAEL 142
Cdd:pfam04073  96 LKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 38-151 9.94e-13

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: 61.48  E-value: 9.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   38 VEPGQIAKTLSLKV-KNEVILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISL 115
Cdd:TIGR00011  37 VDPHRVFKTLVAEGdKKGPVVAVIPGDEELDLKKLAKASGGKkAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESA 116

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 555036833  116 KQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDVC 151
Cdd:TIGR00011 117 KQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 38-116 4.36e-08

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 50.85  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGAKA-RMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISLK 116
Cdd:PRK09194 270 VPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPlELATEEEIRAALGAVPGFLGPVGLPKDVPIIADRSVA 349
 
Name Accession Description Interval E-value
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 3-150 8.58e-64

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: 191.95  E-value: 8.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   3 LQSVQQFFADNAPDIDVIELSQSTATVALAAAAHRVEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555036833  83 SSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDV 150
Cdd:cd04333   81 DAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 4-151 3.55e-47

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: 149.86  E-value: 3.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   4 QSVQQFFADNAPDIDVIELSQSTATVALAAAAHRVEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGA-KARML 82
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAkKVEMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555036833  83 SSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDVC 151
Cdd:COG2606   81 DPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIA 149
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 38-148 7.13e-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: 105.32  E-value: 7.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKVKN-EVILVVAKGDARLDNKKLKDTFGA-KARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISL 115
Cdd:cd04332   23 VPPGQIAKTLVLKDDKgGLVLVVVPGDHELDLKKLAKALGAkKLRLASEEELEELTGCEPGGVGPFGLKKGVPVVVDESL 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 555036833 116 KQYAEVLPAAGAIHSAVRISPDRMAELT-SAKWV 148
Cdd:cd04332  103 LELEDVYVGAGERGADLHLSPADLLRLLgEAEVA 136
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 38-142 6.04e-22

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: 84.58  E-value: 6.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   38 VEPGQIAKTLSLKV-KNEVILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGL-ENPLAVYCDIS 114
Cdd:pfam04073  16 VPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKrLRLASEEELLELTGVEPGGVTPFGLkAKGVPVLVDES 95

                          90       100
                  ....*....|....*....|....*...
gi 555036833  115 LKQYAEVLPAAGAIHSAVRISPDRMAEL 142
Cdd:pfam04073  96 LKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 38-150 3.50e-16

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: 70.56  E-value: 3.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKV-KNEVILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISL 115
Cdd:cd00002   38 LDPEQVFKTLVVEGdKKGLVVAVVPVDEELDLKKLAKALGAKkVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESA 117

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 555036833 116 KQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDV 150
Cdd:cd00002  118 LDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 38-151 9.94e-13

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: 61.48  E-value: 9.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833   38 VEPGQIAKTLSLKV-KNEVILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISL 115
Cdd:TIGR00011  37 VDPHRVFKTLVAEGdKKGPVVAVIPGDEELDLKKLAKASGGKkAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESA 116

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 555036833  116 KQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDVC 151
Cdd:TIGR00011 117 KQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 38-126 2.18e-09

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: 52.73  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKVK---NEVILVVAKGDARLDNKKLKDTFGA-KARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDI 113
Cdd:cd04336   35 TELGQGAKALLCKVKdgsRRFVLAVLPADKKLDLKAVAAAVGGkKADLASPEEAEELTGCVIGAVPPFSFDPKLKLIADP 114

                         90
                 ....*....|....
gi 555036833 114 SL-KQYAEVLPAAG 126
Cdd:cd04336  115 SLlDRGDEIAFNAG 128
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 38-116 4.36e-08

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 50.85  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKVKNEVILVVAKGDARLDNKKLKDTFGAKA-RMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISLK 116
Cdd:PRK09194 270 VPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPlELATEEEIRAALGAVPGFLGPVGLPKDVPIIADRSVA 349
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 38-117 8.91e-06

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: 43.27  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  38 VEPGQIAKTLSLKVKN--EVILVVAKGDARLDNKKLKDTFGAKA-RMLSSDEVVTITGHPVGGVCPFGLENpLAVYCDIS 114
Cdd:cd04334   47 VPPSQTVKTLLVKADGeeELVAVLLRGDHELNEVKLENLLGAAPlELASEEEIEAATGAPPGFIGPVGLKK-IPIIADRS 125


                 ...
gi 555036833 115 LKQ 117
Cdd:cd04334  126 VAD 128
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 40-121 1.09e-04

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: 40.19  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  40 PGQIAKTLSLK-VKNEVILVVAKGDARLDNKKLKDTFGAKA-RMLSSDEVVTITGHPVGGVCPFGL----ENPLAVYCDI 113
Cdd:cd04335   37 PGAHTKNLFLKdKKGRLYLVTALHDKKVDLKALSKQLGASRlSFASEERLEEKLGVTPGSVTPFALindkENDVQVVLDK 116


                 ....*...
gi 555036833 114 SLKQYAEV 121
Cdd:cd04335  117 DLLEEERV 124
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
37-150 5.59e-04

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 38.19  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  37 RVEPGQIAKTLSLKVKNE---VILVVAKGDARLDNKKLKDTFGAK-ARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCD 112
Cdd:PRK10670  38 GLNADQVYKTLLVAVNGDmkhLAVAVTPVAGQLDLKKVAKALGAKkVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVID 117

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 555036833 113 ISLKQYAEVLPAAGAIHSAVRISPDRMAELTSAKWVDV 150
Cdd:PRK10670 118 APAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 58-145 7.07e-03

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: 34.63  E-value: 7.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555036833  58 VVAKGDARLD-NKKLKDTFGA-KARMLSSDEVVTITGHPVGGVCPFGLENPLAVYCDISLKQYAEVLPAAGAIHSAVRIS 135
Cdd:cd04939   47 CVVLATTRADvNGVVKRRLGArKASFAPMETAVELTGMEYGGITPVGLPAGWPILVDSAVAERPAVVIGSGVRRSKLLLP 126

                         90
                 ....*....|
gi 555036833 136 PDRMAELTSA 145
Cdd:cd04939  127 GAALAELPGA 136
 
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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