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Conserved domains on  [gi|364023817|ref|NP_059100|]
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large ribosomal subunit protein mL39 isoform 1 [Mus musculus]

Protein Classification

threonine--tRNA ligase family protein( domain architecture ID 1000183)

threonine--tRNA ligase family protein such as threonine--tRNA ligase ThrRS, also termed cytoplasmic threonine--tRNA ligase, a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation, and such as the large ribosomal subunit protein mL39.

Gene Ontology:  GO:0000166

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02908 super family cl31949
threonyl-tRNA synthetase
 27-270 9.94e-29

threonyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02908:

Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 116.79  E-value: 9.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  27 SPAAELSPteLTEMRNDLFNREKSRQLSltpRTEKIEVKHVGKTDP-GTVFVMNKNISTPYSCAMHLSEWYCSKSILALV 105
Cdd:PLN02908  17 SDEEYLSA--VIKKRIELFEKIQARQLA---RLESAGGDPIKVTLPdGAVKDGKKWVTTPMDIAKEISKGLANSALIAQV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 106 DGQPWDMYKPLTKSCEIKFLTFKDPDPKEVnkaYWRSCAMMLGCVIERAfkddYVVSLVRAPEVPVIAGaFCYDVTLDKR 185
Cdd:PLN02908  92 DGVLWDMTRPLEGDCKLKLFKFDDDEGRDT---FWHSSAHILGEALELE----YGCKLCIGPCTTRGEG-FYYDAFYGDR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 186 -LDEwmptkENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQHNKYKVDFIEEKasqnPE-RIVKLHRIGDFIDVSEG 263
Cdd:PLN02908 164 tLNE-----EDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDL----PEdATITVYRCGPLVDLCRG 234


                 ....*..
gi 364023817 264 PLIPRTS 270
Cdd:PLN02908 235 PHIPNTS 241
 
Name Accession Description Interval E-value
PLN02908 PLN02908
threonyl-tRNA synthetase
 27-270 9.94e-29

threonyl-tRNA synthetase


Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 116.79  E-value: 9.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  27 SPAAELSPteLTEMRNDLFNREKSRQLSltpRTEKIEVKHVGKTDP-GTVFVMNKNISTPYSCAMHLSEWYCSKSILALV 105
Cdd:PLN02908  17 SDEEYLSA--VIKKRIELFEKIQARQLA---RLESAGGDPIKVTLPdGAVKDGKKWVTTPMDIAKEISKGLANSALIAQV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 106 DGQPWDMYKPLTKSCEIKFLTFKDPDPKEVnkaYWRSCAMMLGCVIERAfkddYVVSLVRAPEVPVIAGaFCYDVTLDKR 185
Cdd:PLN02908  92 DGVLWDMTRPLEGDCKLKLFKFDDDEGRDT---FWHSSAHILGEALELE----YGCKLCIGPCTTRGEG-FYYDAFYGDR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 186 -LDEwmptkENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQHNKYKVDFIEEKasqnPE-RIVKLHRIGDFIDVSEG 263
Cdd:PLN02908 164 tLNE-----EDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDL----PEdATITVYRCGPLVDLCRG 234


                 ....*..
gi 364023817 264 PLIPRTS 270
Cdd:PLN02908 235 PHIPNTS 241
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 63-125 4.96e-24

TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role.


Pssm-ID: 340455 [Multi-domain]  Cd Length: 61  Bit Score: 93.05  E-value: 4.96e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364023817  63 EVKHVGKTdPGTVFVMNKnISTPYSCAMHLSEWYCSKSILALVDGQPWDMYKPLTKSCEIKFL 125
Cdd:cd01616    1 EVFTVGKT-PGTVFVMNK-GATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKFL 61
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 99-272 3.43e-20

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


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 91.25  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  99 KSILALVDGQPWDMYKPLTKSCEIKFLTFKDPDPKEVnkaYWRSCAMMLGCVIERAFkddyvvslvraPEV-----PVIA 173
Cdd:COG0441   34 AAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEI---LRHSAAHLLAQAVKRLY-----------PDAkltigPVIE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 174 GAFCYDVTLDKRLdewmpTKENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQ--HNKYKVDFIEEKASqnpERIVKL 251
Cdd:COG0441  100 NGFYYDFDLERPF-----TPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVELIEDIPE---DEEISL 171

                        170       180
                 ....*....|....*....|.
gi 364023817 252 HRIGDFIDVSEGPLIPRTSVC 272
Cdd:COG0441  172 YRQGEFVDLCRGPHVPSTGKI 192
 
Name Accession Description Interval E-value
PLN02908 PLN02908
threonyl-tRNA synthetase
 27-270 9.94e-29

threonyl-tRNA synthetase


Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 116.79  E-value: 9.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  27 SPAAELSPteLTEMRNDLFNREKSRQLSltpRTEKIEVKHVGKTDP-GTVFVMNKNISTPYSCAMHLSEWYCSKSILALV 105
Cdd:PLN02908  17 SDEEYLSA--VIKKRIELFEKIQARQLA---RLESAGGDPIKVTLPdGAVKDGKKWVTTPMDIAKEISKGLANSALIAQV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 106 DGQPWDMYKPLTKSCEIKFLTFKDPDPKEVnkaYWRSCAMMLGCVIERAfkddYVVSLVRAPEVPVIAGaFCYDVTLDKR 185
Cdd:PLN02908  92 DGVLWDMTRPLEGDCKLKLFKFDDDEGRDT---FWHSSAHILGEALELE----YGCKLCIGPCTTRGEG-FYYDAFYGDR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 186 -LDEwmptkENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQHNKYKVDFIEEKasqnPE-RIVKLHRIGDFIDVSEG 263
Cdd:PLN02908 164 tLNE-----EDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDL----PEdATITVYRCGPLVDLCRG 234


                 ....*..
gi 364023817 264 PLIPRTS 270
Cdd:PLN02908 235 PHIPNTS 241
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
 63-125 4.96e-24

TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role.


Pssm-ID: 340455 [Multi-domain]  Cd Length: 61  Bit Score: 93.05  E-value: 4.96e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364023817  63 EVKHVGKTdPGTVFVMNKnISTPYSCAMHLSEWYCSKSILALVDGQPWDMYKPLTKSCEIKFL 125
Cdd:cd01616    1 EVFTVGKT-PGTVFVMNK-GATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKFL 61
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 99-272 3.43e-20

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


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 91.25  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  99 KSILALVDGQPWDMYKPLTKSCEIKFLTFKDPDPKEVnkaYWRSCAMMLGCVIERAFkddyvvslvraPEV-----PVIA 173
Cdd:COG0441   34 AAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEI---LRHSAAHLLAQAVKRLY-----------PDAkltigPVIE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 174 GAFCYDVTLDKRLdewmpTKENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQ--HNKYKVDFIEEKASqnpERIVKL 251
Cdd:COG0441  100 NGFYYDFDLERPF-----TPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVELIEDIPE---DEEISL 171

                        170       180
                 ....*....|....*....|.
gi 364023817 252 HRIGDFIDVSEGPLIPRTSVC 272
Cdd:COG0441  172 YRQGEFVDLCRGPHVPSTGKI 192
TGS_ThrRS cd01667
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ...
 73-131 1.67e-19

TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340458 [Multi-domain]  Cd Length: 65  Bit Score: 80.99  E-value: 1.67e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 364023817  73 GTVFVMNKNIsTPYSCAMHLSEWYCSKSILALVDGQPWDMYKPLTKSCEIKFLTFKDPD 131
Cdd:cd01667    8 GSVKEFPKGT-TPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 99-269 5.22e-10

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 60.53  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817  99 KSILALVDGQPWDMYKPLTKSCEIKFLTFkdpDPKEVNKAYWRSCAMMLGCVIERAFKDdyvVSLVRAPevpVIAGAFCY 178
Cdd:PRK12444  38 KAVAGKVNDKLYDLRRNLEEDAEVEIITI---DSNEGVEIARHSAAHILAQAVKRLYGD---VNLGVGP---VIENGFYY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364023817 179 DVTLDKRLdewmpTKENLRSFTKDAHALIYRDLPFETLDVDARVALEIFQ--HNKYKVDFIEEKASqnpERIVKLHRIGD 256
Cdd:PRK12444 109 DMDLPSSV-----NVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQemNDRLKLELLEAIPS---GESITLYKQGE 180

                        170
                 ....*....|...
gi 364023817 257 FIDVSEGPLIPRT 269
Cdd:PRK12444 181 FVDLCRGPHLPST 193
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 64-124 1.75e-06

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 45.01  E-value: 1.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364023817  64 VKHVGKTDPGTVFVMNKNiSTPYSCAMHLSEWY--CSKSILALVDGQPWDMYKP-----LTKSCEIKF 124
Cdd:cd00196    1 VKVETPSLKKIVVAVPPS-TTLRQVLEKVAKRIglPPDVIRLLFNGQVLDDLMTakqvgLEPGEELHF 67
 
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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