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Conserved domains on  [gi|2731280314|ref|WP_345384952|]
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aminoacyl--tRNA ligase-related protein, partial [Pseudonocardia yuanmonensis]

Protein Classification

proline--tRNA ligase( domain architecture ID 1001641)

proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)

EC:  6.1.1.15
Gene Ontology:  GO:0006433|GO:0004827|GO:0005524|GO:0005737
PubMed:  8274143|10704480

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09194 super family cl35782
prolyl-tRNA synthetase; Provisional
 1-166 4.19e-94

prolyl-tRNA synthetase; Provisional


The actual alignment was detected with superfamily member PRK09194:

Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 283.13  E-value: 4.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:PRK09194  141 DEIRPRFGLMRGREFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAEApgLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRG 160
Cdd:PRK09194  221 IVYSDESDYAANIEKAEA--LPPPRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE----LVAVLVRG 294


                  ....*.
gi 2731280314 161 DHELNE 166
Cdd:PRK09194  295 DHELNE 300
 
Name Accession Description Interval E-value
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 1-166 4.19e-94

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 283.13  E-value: 4.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:PRK09194  141 DEIRPRFGLMRGREFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAEApgLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRG 160
Cdd:PRK09194  221 IVYSDESDYAANIEKAEA--LPPPRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE----LVAVLVRG 294


                  ....*.
gi 2731280314 161 DHELNE 166
Cdd:PRK09194  295 DHELNE 300
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
 1-166 1.22e-85

Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440211 [Multi-domain]  Cd Length: 564  Bit Score: 261.63  E-value: 1.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:COG0442   141 DEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAEAPGLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRG 160
Cdd:COG0442   221 IVYCDACDYAANIEKAEALAPPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKADGE----LVAVLVRG 296


                  ....*.
gi 2731280314 161 DHELNE 166
Cdd:COG0442   297 DHELNE 302
proS_fam_II TIGR00409
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
 1-166 2.44e-62

prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273063 [Multi-domain]  Cd Length: 568  Bit Score: 201.20  E-value: 2.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:TIGR00409 141 DEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAE--APGlyaSRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDgEKGADIWLLLL 158
Cdd:TIGR00409 221 IVYSDESDYAANIELAEalAPG---ERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAV-DKSEPLVALLV 296


                  ....*...
gi 2731280314 159 RGDHELNE 166
Cdd:TIGR00409 297 RGDHELNE 304
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 1-75 8.95e-44

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 145.03  E-value: 8.95e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAE 75
Cdd:cd00779   125 DEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP 199
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 117-166 4.81e-08

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: 48.75  E-value: 4.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2731280314 117 TPGAAKCEDVAKLLGLPLERTIKSIVLATDGEKgadIWLLLLRGDHELNE 166
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK---YVLVVVPGDREVDL 47
 
Name Accession Description Interval E-value
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 1-166 4.19e-94

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 283.13  E-value: 4.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:PRK09194  141 DEIRPRFGLMRGREFIMKDAYSFHADEESLDETYDAMYQAYSRIFDRLGLDFRAVEADSGAIGGSASHEFMVLADSGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAEApgLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRG 160
Cdd:PRK09194  221 IVYSDESDYAANIEKAEA--LPPPRAAAEEALEKVDTPNAKTIEELAEFLNVPAEKTVKTLLVKADGE----LVAVLVRG 294


                  ....*.
gi 2731280314 161 DHELNE 166
Cdd:PRK09194  295 DHELNE 300
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
 1-166 1.22e-85

Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440211 [Multi-domain]  Cd Length: 564  Bit Score: 261.63  E-value: 1.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:COG0442   141 DEIRPRFGLLRTREFLMKDAYSFHATEEELDEEYQKMLDAYERIFERLGLPVRAVEADSGAIGGSESHEFMVLADSGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAEAPGLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRG 160
Cdd:COG0442   221 IVYCDACDYAANIEKAEALAPPAERAEPTKELEAVATPGAKTIEEVAEFLGVPAEKTVKTLVYKADGE----LVAVLVRG 296


                  ....*.
gi 2731280314 161 DHELNE 166
Cdd:COG0442   297 DHELNE 302
proS_fam_II TIGR00409
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
 1-166 2.44e-62

prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273063 [Multi-domain]  Cd Length: 568  Bit Score: 201.20  E-value: 2.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:TIGR00409 141 DEIRPRFGLMRGREFIMKDAYSFHSDEESLDATYQKMYQAYSNIFSRLGLDFRPVQADSGAIGGSASHEFMVLAESGEDT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  81 LVYNADSEYAANIELAE--APGlyaSRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDgEKGADIWLLLL 158
Cdd:TIGR00409 221 IVYSDESDYAANIELAEalAPG---ERNAPTAELDKVDTPNTKTIAELVECFNLPAEKVVKTLLVKAV-DKSEPLVALLV 296


                  ....*...
gi 2731280314 159 RGDHELNE 166
Cdd:TIGR00409 297 RGDHELNE 304
PRK12325 PRK12325
prolyl-tRNA synthetase; Provisional
 1-86 2.27e-44

prolyl-tRNA synthetase; Provisional


Pssm-ID: 237059 [Multi-domain]  Cd Length: 439  Bit Score: 151.17  E-value: 2.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAETGEDL 80
Cdd:PRK12325  141 DEIRPRFGVMRGREFLMKDAYSFDLDEEGARHSYNRMFVAYLRTFARLGLKAIPMRADTGPIGGDLSHEFIILAETGEST 220


                  ....*.
gi 2731280314  81 LVYNAD 86
Cdd:PRK12325  221 VFYDKD 226
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 1-75 8.95e-44

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 145.03  E-value: 8.95e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIGGTRSHEFQVIAE 75
Cdd:cd00779   125 DEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSP 199
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 86-166 8.72e-29

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: 103.75  E-value: 8.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314  86 DSEYAANIELAEAPGLYASRAEPAQAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEKGadIWLLLLRGDHELN 165
Cdd:cd04334     1 DCDYAANIEKAESLPPAAERPAPPKELEKVATPGQKTIEELAEFLGVPPSQTVKTLLVKADGEEE--LVAVLLRGDHELN 78


                  .
gi 2731280314 166 E 166
Cdd:cd04334    79 E 79
ProRS_core cd00772
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 1-80 4.56e-13

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.


Pssm-ID: 238395 [Multi-domain]  Cd Length: 264  Bit Score: 65.08  E-value: 4.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDNMYAAYMRIFGRLG-LEFRAVAADTGS--IGGTRSHEFQVIAETG 77
Cdd:cd00772   131 DEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNMLSAYAEIARDLAaIDFIEGEADEGAkfAGASKSREFEALMEDG 210


                  ...
gi 2731280314  78 EDL 80
Cdd:cd00772   211 KAK 213
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 110-166 1.47e-10

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: 56.01  E-value: 1.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2731280314 110 QAMAEVPTPGAAKCEDVAKLLGLPLERTIKSIVLATDGEKgadIWLLLLRGDHELNE 166
Cdd:cd04332     1 EYLEYEHTPGAKTIEEAAEALGVPPGQIAKTLVLKDDKGG---LVLVVVPGDHELDL 54
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 117-166 4.81e-08

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: 48.75  E-value: 4.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2731280314 117 TPGAAKCEDVAKLLGLPLERTIKSIVLATDGEKgadIWLLLLRGDHELNE 166
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK---YVLVVVPGDREVDL 47
Gly_His_Pro_Ser_Thr_tRS_core cd00670
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ...
 1-63 7.02e-07

Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238359 [Multi-domain]  Cd Length: 235  Bit Score: 47.39  E-value: 7.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731280314   1 DERRPRFGLMRGREFTMKDAYSFDRDEAgAQRSYDNMYAAYMRIFGRLGLEFRAVAADTGSIG 63
Cdd:cd00670   100 HEPSGRRGLMRVREFRQVEYVVFGEPEE-AEEERREWLELAEEIARELGLPVRVVVADDPFFG 161
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 8-75 2.15e-05

tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.


Pssm-ID: 395469 [Multi-domain]  Cd Length: 181  Bit Score: 42.78  E-value: 2.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731280314   8 GLMRGREFTMKDAYSFdRDEAGAQRSYDNMYAAYMRIFGRLGLEFRAVAADTG--SIGGTRSHEFQVIAE 75
Cdd:pfam00587  56 GLIRVRQFHQDDAHIF-HAPGQSPDELEDYIKLIDRVYSRLGLEVRVVRLSNSdgSAFYGPKLDFEVVFP 124
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 118-165 2.39e-03

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: 36.61  E-value: 2.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2731280314 118 PGAAKCEDVAKLLGLPLERTIKSIVLATDGEkgadIWLLLLRGDHELN 165
Cdd:COG2606    21 EPAATAEEAAEALGVPPEQIAKTLVFRGDGG----PVLAVVPGDRRLD 64
 
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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