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Conserved domains on  [gi|550714082|ref|WP_022646971|]
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MULTISPECIES: YbaK/EbsC family protein [Enterobacter]

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 1.07e-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: 194.26  E-value: 1.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   3 LQSVQQFFAEHAPDIEIIELNQSTATVALAAAAHNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550714082  83 SCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDV 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 1.07e-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: 194.26  E-value: 1.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   3 LQSVQQFFAEHAPDIEIIELNQSTATVALAAAAHNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550714082  83 SCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDV 150
Cdd:cd04333   81 DAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 4-151 1.57e-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: 150.63  E-value: 1.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   4 QSVQQFFAEHAPDIEIIELNQSTATVALAAAAHNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGA-KARML 82
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAkKVEMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714082  83 SCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDVC 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 ...
 37-142 1.30e-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: 86.50  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   37 NVEPGQIAKTLSLKI-KNDVILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGL-ENPLSVYCDI 113
Cdd:pfam04073  15 GVPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKrLRLASEEELLELTGVEPGGVTPFGLkAKGVPVLVDE 94

                          90       100
                  ....*....|....*....|....*....
gi 550714082  114 TLKQYAEVLPAAGAIHSAVRISPDRMAEL 142
Cdd:pfam04073  95 SLKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 37-151 1.35e-12

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: 61.09  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   37 NVEPGQIAKTLSLKI-KNDVILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:TIGR00011  36 GVDPHRVFKTLVAEGdKKGPVVAVIPGDEELDLKKLAKASGGKkAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDES 115

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 550714082  115 LKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDVC 151
Cdd:TIGR00011 116 AKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 36-116 1.78e-07

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 48.93  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  36 HNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGAKA-RMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:PRK09194 268 LNVPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPlELATEEEIRAALGAVPGFLGPVGLPKDVPIIADRS 347


                 ..
gi 550714082 115 LK 116
Cdd:PRK09194 348 VA 349
 
Name Accession Description Interval E-value
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 3-150 1.07e-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: 194.26  E-value: 1.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   3 LQSVQQFFAEHAPDIEIIELNQSTATVALAAAAHNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGAKARML 82
Cdd:cd04333    1 VERVRAFLAARGLDLEVIELPESTRTAALAAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFGEKLKMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550714082  83 SCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDV 150
Cdd:cd04333   81 DAEEVRELTGFAIGGVCPFGHPEPLPVYLDESLKRFDEVWAAAGTPNAAFRLTPDELERLTGAEWVDV 148
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 4-151 1.57e-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: 150.63  E-value: 1.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   4 QSVQQFFAEHAPDIEIIELNQSTATVALAAAAHNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGA-KARML 82
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAATAEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAkKVEMA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714082  83 SCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDVC 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 ...
 37-148 1.24e-29

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: 104.93  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  37 NVEPGQIAKTLSLKIKND-VILVVAKGDARLDNKKLKETFGA-KARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:cd04332   22 GVPPGQIAKTLVLKDDKGgLVLVVVPGDHELDLKKLAKALGAkKLRLASEEELEELTGCEPGGVGPFGLKKGVPVVVDES 101

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 550714082 115 LKQYAEVLPAAGAIHSAVRISPDRMAELTA-AKWV 148
Cdd:cd04332  102 LLELEDVYVGAGERGADLHLSPADLLRLLGeAEVA 136
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 37-142 1.30e-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: 86.50  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   37 NVEPGQIAKTLSLKI-KNDVILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGL-ENPLSVYCDI 113
Cdd:pfam04073  15 GVPPGRIAKTLVLKDkKGKYVLVVVPGDREVDLKKLAKLLGVKrLRLASEEELLELTGVEPGGVTPFGLkAKGVPVLVDE 94

                          90       100
                  ....*....|....*....|....*....
gi 550714082  114 TLKQYAEVLPAAGAIHSAVRISPDRMAEL 142
Cdd:pfam04073  95 SLKDLPDVVVGAGENGATLRLSNADLRKL 123
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 37-150 4.50e-15

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: 67.86  E-value: 4.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  37 NVEPGQIAKTLSLKI-KNDVILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:cd00002   37 GLDPEQVFKTLVVEGdKKGLVVAVVPVDEELDLKKLAKALGAKkVEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDES 116

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 550714082 115 LKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDV 150
Cdd:cd00002  117 ALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 37-151 1.35e-12

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: 61.09  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082   37 NVEPGQIAKTLSLKI-KNDVILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:TIGR00011  36 GVDPHRVFKTLVAEGdKKGPVVAVIPGDEELDLKKLAKASGGKkAEMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDES 115

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 550714082  115 LKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDVC 151
Cdd:TIGR00011 116 AKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADIA 152
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 38-126 3.88e-08

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: 49.27  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  38 VEPGQIAKTLSLKIKNDV---ILVVAKGDARLDNKKLKETFGA-KARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDI 113
Cdd:cd04336   35 TELGQGAKALLCKVKDGSrrfVLAVLPADKKLDLKAVAAAVGGkKADLASPEEAEELTGCVIGAVPPFSFDPKLKLIADP 114

                         90
                 ....*....|....
gi 550714082 114 TL-KQYAEVLPAAG 126
Cdd:cd04336  115 SLlDRGDEIAFNAG 128
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 36-116 1.78e-07

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 48.93  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  36 HNVEPGQIAKTLSLKIKNDVILVVAKGDARLDNKKLKETFGAKA-RMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDIT 114
Cdd:PRK09194 268 LNVPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPlELATEEEIRAALGAVPGFLGPVGLPKDVPIIADRS 347


                 ..
gi 550714082 115 LK 116
Cdd:PRK09194 348 VA 349
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 37-117 2.05e-05

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: 42.11  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  37 NVEPGQIAKTLSLKIKND--VILVVAKGDARLDNKKLKETFGAKA-RMLSCDEVVTLTGHPVGGVCPFGLENpLSVYCDI 113
Cdd:cd04334   46 GVPPSQTVKTLLVKADGEeeLVAVLLRGDHELNEVKLENLLGAAPlELASEEEIEAATGAPPGFIGPVGLKK-IPIIADR 124


                 ....
gi 550714082 114 TLKQ 117
Cdd:cd04334  125 SVAD 128
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
37-150 4.00e-04

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 38.57  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  37 NVEPGQIAKTLSLKIKND---VILVVAKGDARLDNKKLKETFGAK-ARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCD 112
Cdd:PRK10670  38 GLNADQVYKTLLVAVNGDmkhLAVAVTPVAGQLDLKKVAKALGAKkVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVID 117

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 550714082 113 ITLKQYAEVLPAAGAIHSAVRISPDRMAELTAAKWVDV 150
Cdd:PRK10670 118 APAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 40-121 5.62e-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: 37.88  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  40 PGQIAKTLSLK-IKNDVILVVAKGDARLDNKKLKETFGAKA-RMLSCDEVVTLTGHPVGGVCPFGL----ENPLSVYCDI 113
Cdd:cd04335   37 PGAHTKNLFLKdKKGRLYLVTALHDKKVDLKALSKQLGASRlSFASEERLEEKLGVTPGSVTPFALindkENDVQVVLDK 116


                 ....*...
gi 550714082 114 TLKQYAEV 121
Cdd:cd04335  117 DLLEEERV 124
PA2301 cd04939
PA2301 is an uncharacterized Pseudomonas aeruginosa protein with a YbaK-like domain of unknown ...
 58-145 1.04e-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: 36.94  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714082  58 VVAKGDARLD-NKKLKETFGA-KARMLSCDEVVTLTGHPVGGVCPFGLENPLSVYCDITLKQYAEVLPAAGAIHSAVRIS 135
Cdd:cd04939   47 CVVLATTRADvNGVVKRRLGArKASFAPMETAVELTGMEYGGITPVGLPAGWPILVDSAVAERPAVVIGSGVRRSKLLLP 126

                         90
                 ....*....|
gi 550714082 136 PDRMAELTAA 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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