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Conserved domains on  [gi|491478351|ref|WP_005336092|]
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MULTISPECIES: Cys-tRNA(Pro) deacylase [Aeromonas]

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 ...
 1-151 1.01e-77

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: 227.33  E-value: 1.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   1 MTPAINLLKKLKIPHKLYPYECEAHDDFGKHAATQLGLPEAQVFKTLVAHHDKQA-VVAIVPSSGMCSLKQLAKATGLKK 79
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGlVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491478351  80 VEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-151 1.01e-77

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: 227.33  E-value: 1.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   1 MTPAINLLKKLKIPHKLYPYECEAHDDFGKHAATQLGLPEAQVFKTLVAHHDKQA-VVAIVPSSGMCSLKQLAKATGLKK 79
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGlVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491478351  80 VEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-151 2.63e-59

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: 180.89  E-value: 2.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351    2 TPAINLLKKLKIPHKLYPYECEAHDDFGKHAATQLGLPEAQVFKTLVAHHDKQA-VVAIVPSSGMCSLKQLAKATGLKKV 80
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLDGESAAEKLGVDPHRVFKTLVAEGDKKGpVVAVIPGDEELDLKKLAKASGGKKA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491478351   81 EMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:TIGR00011  81 EMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADI 151
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-154 3.75e-58

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: 177.97  E-value: 3.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   2 TPAINLLKKLKIPHKLYPYECEAHDdfGKHAATQLGLPEAQVFKTLVAHHDKQAVVAIVPSSGMCSLKQLAKATGLKKVE 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAAT--AEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKVE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491478351  82 MMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPIGEE 154
Cdd:COG2606   79 MADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-151 7.57e-49

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 154.52  E-value: 7.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   1 MTPAINLLKKLKIPHKLYPYECEAHD-DFGKHAATQLGLPEAQVFKTL---VAHHDKQAVVAIVPSSGMCSLKQLAKATG 76
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAEtNFGDEVVRKLGLNADQVYKTLlvaVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491478351  77 LKKVEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-143 2.48e-23

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: 88.43  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   32 AATQLGLPEAQVFKTLVAHHDK-QAVVAIVPSSGMCSLKQLAKATGLKKVEMMKPAEAEKLTGYKVGGISPLA-QKKLLP 109
Cdd:pfam04073  10 LAAALGVPPGRIAKTLVLKDKKgKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGVP 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 491478351  110 TVLDESALQFDEILVSGGKRGLSVGVAPQDMLTL 143
Cdd:pfam04073  90 VLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
 
Name Accession Description Interval E-value
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 1-151 1.01e-77

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: 227.33  E-value: 1.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   1 MTPAINLLKKLKIPHKLYPYECEAHDDFGKHAATQLGLPEAQVFKTLVAHHDKQA-VVAIVPSSGMCSLKQLAKATGLKK 79
Cdd:cd00002    1 KTPAIRLLDKAKIPYELHEYEHDEDASDGLEAAEKLGLDPEQVFKTLVVEGDKKGlVVAVVPVDEELDLKKLAKALGAKK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491478351  80 VEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:cd00002   81 VEMAPPKDAERLTGYIRGGISPLGQKKRLPTVIDESALDLDTIYVSAGKRGLQIELAPQDLAKLTGAKFADI 152
YbaK_EbsC TIGR00011
Cys-tRNA(Pro) deacylase; This model represents the YbaK family, bacterial proteins whose full ...
 2-151 2.63e-59

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: 180.89  E-value: 2.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351    2 TPAINLLKKLKIPHKLYPYECEAHDDFGKHAATQLGLPEAQVFKTLVAHHDKQA-VVAIVPSSGMCSLKQLAKATGLKKV 80
Cdd:TIGR00011   1 TNAIRLLDKAKIEYEVHEYEVDPDHLDGESAAEKLGVDPHRVFKTLVAEGDKKGpVVAVIPGDEELDLKKLAKASGGKKA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491478351   81 EMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:TIGR00011  81 EMADPKDAEKVTGYIRGGISPIGQKKKFPTYIDESAKQLETIYVSGGKRGLQIELAPDDLIRLLDGTFADI 151
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 2-154 3.75e-58

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: 177.97  E-value: 3.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   2 TPAINLLKKLKIPHKLYPYECEAHDdfGKHAATQLGLPEAQVFKTLVAHHDKQAVVAIVPSSGMCSLKQLAKATGLKKVE 81
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPEPAAT--AEEAAEALGVPPEQIAKTLVFRGDGGPVLAVVPGDRRLDLKKLAAALGAKKVE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491478351  82 MMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPIGEE 154
Cdd:COG2606   79 MADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEFDEVYVSAGDRGLLVELAPADLARLTGATVADIARP 151
PRK10670 PRK10670
Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
1-151 7.57e-49

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


Pssm-ID: 182634  Cd Length: 159  Bit Score: 154.52  E-value: 7.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   1 MTPAINLLKKLKIPHKLYPYECEAHD-DFGKHAATQLGLPEAQVFKTL---VAHHDKQAVVAIVPSSGMCSLKQLAKATG 76
Cdd:PRK10670   1 MTPAVKLLEKNKISFTLHTYEHDPAEtNFGDEVVRKLGLNADQVYKTLlvaVNGDMKHLAVAVTPVAGQLDLKKVAKALG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491478351  77 LKKVEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:PRK10670  81 AKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTVIDAPAQEFATIYVSGGKRGLDIELAAGDLAKLLDAKFADI 155
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 19-145 2.93e-36

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: 121.88  E-value: 2.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351  19 PYECEAHDD---FGKHAATQLGLPEAQVFKTLVAHHDK-QAVVAIVPSSGMCSLKQLAKATGLKKVEMMKPAEAEKLTGY 94
Cdd:cd04332    1 EYLEYEHTPgakTIEEAAEALGVPPGQIAKTLVLKDDKgGLVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTGC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491478351  95 KVGGISPLAQKKLLPTVLDESALQFDEILVSGGKRGLSVGVAPQDMLTLMK 145
Cdd:cd04332   81 EPGGVGPFGLKKGVPVVVDESLLELEDVYVGAGERGADLHLSPADLLRLLG 131
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 32-143 2.48e-23

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: 88.43  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   32 AATQLGLPEAQVFKTLVAHHDK-QAVVAIVPSSGMCSLKQLAKATGLKKVEMMKPAEAEKLTGYKVGGISPLA-QKKLLP 109
Cdd:pfam04073  10 LAAALGVPPGRIAKTLVLKDKKgKYVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVTPFGlKAKGVP 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 491478351  110 TVLDESALQFDEILVSGGKRGLSVGVAPQDMLTL 143
Cdd:pfam04073  90 VLVDESLKDLPDVVVGAGENGATLRLSNADLRKL 123
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 32-143 1.02e-14

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: 66.76  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351  32 AATQLGLPEAQVFKTLVAHHDKQAVVAIVPSSGMCSLKQLAKATGlKKVEMMKPAEAEKLTGYKVGGISPLAQKKLLPTV 111
Cdd:cd04333   30 AAEALGCEPGQIAKSLVFRVDDEPVLVVTSGDARVDNKKFKALFG-EKLKMADAEEVRELTGFAIGGVCPFGHPEPLPVY 108

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491478351 112 LDESALQFDEILVSGGKRGLSVGVAPQDMLTL 143
Cdd:cd04333  109 LDESLKRFDEVWAAAGTPNAAFRLTPDELERL 140
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 5-151 3.13e-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: 63.13  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351   5 INLLKKLKIPHKLYPYECEAHDDfgkHAATQLGLPEAQVFKTL---VAHHDKQAVVAIVPSSGMCSLKQLAKATGLKKVE 81
Cdd:cd04336    5 QELLNTNGARFRVLDHPPEGTSE---EVAAIRGTELGQGAKALlckVKDGSRRFVLAVLPADKKLDLKAVAAAVGGKKAD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491478351  82 MMKPAEAEKLTGYKVGGISPLAQKKLLPTVLDESAL-QFDEILVSGGKRGLSVGVAPQDMLTLMKWIAAPI 151
Cdd:cd04336   82 LASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLdRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQF 152
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 33-116 1.55e-07

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 49.31  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351  33 ATQLGLPEAQVFKTLVAHHDKQAVVAIVPSSGMCSLKQLAKATGLKKVEMMKPAEAEKLTGYKVGGISPLAQKKLLPTVL 112
Cdd:PRK09194 265 AEFLNVPAEKTVKTLLVKADGELVAVLVRGDHELNEVKLENLLGAAPLELATEEEIRAALGAVPGFLGPVGLPKDVPIIA 344


                 ....
gi 491478351 113 DESA 116
Cdd:PRK09194 345 DRSV 348
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 33-116 9.34e-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: 42.88  E-value: 9.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491478351  33 ATQLGLPEAQVFKTLV--AHHDKQAVVAIVPSSGMCSLKQLAKATGLKKVEMMKPAEAEKLTGYKVGGISPLAQKKlLPT 110
Cdd:cd04334   42 AEFLGVPPSQTVKTLLvkADGEEELVAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPGFIGPVGLKK-IPI 120


                 ....*.
gi 491478351 111 VLDESA 116
Cdd:cd04334  121 IADRSV 126
 
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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