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Conserved domains on  [gi|1720405111|ref|XP_030108675|]
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tryptophan--tRNA ligase, mitochondrial isoform X3 [Mus musculus]

Protein Classification

tryptophan--tRNA ligase( domain architecture ID 1000926)

tryptophan--tRNA ligase is a class I tRNA synthetase and aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA

EC:  6.1.1.2
Gene Ontology:  GO:0006436|GO:0004830|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00927 super family cl35130
tryptophanyl-tRNA synthetase; Reviewed
 1-231 1.01e-90

tryptophanyl-tRNA synthetase; Reviewed


The actual alignment was detected with superfamily member PRK00927:

Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 270.04  E-value: 1.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKS 80
Cdd:PRK00927   96 ITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  81 ILTSMK-KVKSLRDPSSKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYEPDSRAGVSNMVAIHAAVSGLS 157
Cdd:PRK00927  176 LIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEVSNLLTIYSALSGES 255

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405111 158 VEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:PRK00927  256 IEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTLKEVREAMGLL 331
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 1-231 1.01e-90

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 270.04  E-value: 1.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKS 80
Cdd:PRK00927   96 ITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  81 ILTSMK-KVKSLRDPSSKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYEPDSRAGVSNMVAIHAAVSGLS 157
Cdd:PRK00927  176 LIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEVSNLLTIYSALSGES 255

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405111 158 VEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:PRK00927  256 IEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTLKEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-231 2.04e-86

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


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 258.82  E-value: 2.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDG-TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPK 79
Cdd:COG0180    98 LTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRFNHRYGEVFPEPE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  80 SILT-SMKKVKSLrDPSSKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYEPDSRAGVSNMVAIHAAVSG-LS 157
Cdd:COG0180   178 ALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPEVCNLFTIYSAFSGkEE 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405111 158 VEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:COG0180   253 VEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKTLAEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 1-183 1.09e-71

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 219.76  E-value: 1.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDgTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKS 80
Cdd:cd00806    96 VVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARRFNKLYGEIFPKPAA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  81 ILTSMKKVKSLRDPSSKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSNMVAIHAAVSGLSVEE 160
Cdd:cd00806   175 LLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSNLVEIYSAFFNDDDEE 252

                         170       180
                  ....*....|....*....|....*..
gi 1720405111 161 VVRS----SAGLDTARYKLLVADAVIE 183
Cdd:cd00806   253 LEEIdeyrSGGLGYGECKKLLAEAIQE 279
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 6-229 7.48e-50

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 165.20  E-value: 7.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   6 RLQHLHQWKAKaaKQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKSILT-S 84
Cdd:TIGR00233 103 ELKRMTQFKDK--SQAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAERFNKKFKNFFPKPESLISkF 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  85 MKKVKSLRDpsSKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSNMVAIHAAVS-----GLSVE 159
Cdd:TIGR00233 181 FPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPNLLVIYQYLSfflidDDKLK 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720405111 160 EVVRS--SAGLDTARYKLLVADAVIEKFAPIRKEIEKLkmDKDHLRKVLLVGSAKAKELASPVFEEVKKLVG 229
Cdd:TIGR00233 257 EIYEAykSGKLGYGECKKALIEVLQEFLKEIQERRAEI--AEEILDKILEPGAKKARETANKTLADVYKAMG 326
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
2-186 1.87e-31

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 116.61  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   2 VRLPRLQHLHQWKAKAAKQKHDG--TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKygeFFPLPK 79
Cdd:pfam00579 107 GKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRFNKK---IFKKPV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  80 SILTsmkKVKSLRDPSSKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSN-MVAIHAAVSGLSV 158
Cdd:pfam00579 184 GLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDREVRKDLKLFTFLSNeEIEILEAELGKSP 258

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720405111 159 ---------EEVVRSSAGLDtarYKLLVADAVIEKFA 186
Cdd:pfam00579 259 yreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 1-231 1.01e-90

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 270.04  E-value: 1.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKS 80
Cdd:PRK00927   96 ITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  81 ILTSMK-KVKSLRDPSSKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYEPDSRAGVSNMVAIHAAVSGLS 157
Cdd:PRK00927  176 LIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEVSNLLTIYSALSGES 255

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405111 158 VEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:PRK00927  256 IEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTLKEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-231 2.04e-86

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


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 258.82  E-value: 2.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDG-TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPK 79
Cdd:COG0180    98 LTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRFNHRYGEVFPEPE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  80 SILT-SMKKVKSLrDPSSKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYEPDSRAGVSNMVAIHAAVSG-LS 157
Cdd:COG0180   178 ALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPEVCNLFTIYSAFSGkEE 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405111 158 VEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:COG0180   253 VEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKTLAEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 1-183 1.09e-71

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 219.76  E-value: 1.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   1 MVRLPRLQHLHQWKAKAAKQKHDgTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKS 80
Cdd:cd00806    96 VVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARRFNKLYGEIFPKPAA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  81 ILTSMKKVKSLRDPSSKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSNMVAIHAAVSGLSVEE 160
Cdd:cd00806   175 LLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSNLVEIYSAFFNDDDEE 252

                         170       180
                  ....*....|....*....|....*..
gi 1720405111 161 VVRS----SAGLDTARYKLLVADAVIE 183
Cdd:cd00806   253 LEEIdeyrSGGLGYGECKKLLAEAIQE 279
PLN02886 PLN02886
aminoacyl-tRNA ligase
 7-231 2.80e-52

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 173.46  E-value: 2.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   7 LQHLHQWKAKAAKQ-KHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYG------------E 73
Cdd:PLN02886  147 LNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNNLYGgrkwkklggrggS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  74 FFPLPKS-ILTSMKKVKSLRDPSSKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSNMVAIHAA 152
Cdd:PLN02886  227 VFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQL 306

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405111 153 VSGLSVEEVVRSSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGIL 231
Cdd:PLN02886  307 VTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFV 385
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 6-229 7.48e-50

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 165.20  E-value: 7.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   6 RLQHLHQWKAKaaKQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKSILT-S 84
Cdd:TIGR00233 103 ELKRMTQFKDK--SQAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAERFNKKFKNFFPKPESLISkF 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  85 MKKVKSLRDpsSKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSNMVAIHAAVS-----GLSVE 159
Cdd:TIGR00233 181 FPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPNLLVIYQYLSfflidDDKLK 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720405111 160 EVVRS--SAGLDTARYKLLVADAVIEKFAPIRKEIEKLkmDKDHLRKVLLVGSAKAKELASPVFEEVKKLVG 229
Cdd:TIGR00233 257 EIYEAykSGKLGYGECKKALIEVLQEFLKEIQERRAEI--AEEILDKILEPGAKKARETANKTLADVYKAMG 326
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 2-230 3.83e-39

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 137.68  E-value: 3.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   2 VRLPRLQHLHQWKAKAAkQKHDG---TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYG-EFFPL 77
Cdd:PRK12282   99 VTVARLERNPTVKTEIA-QKGFGrsiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQTREIVRRFNSLYGtDVLVE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  78 PKSILTSMKKVKSLrDPSSKMSKSDPDKLAtvrITDSPEEIVQKFRKAVTDfTSEVTYEPDSRAGVSNMVAIHAAVSG-- 155
Cdd:PRK12282  178 PEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMYTD-PNHIRVEDPGKVEGNVVFTYLDAFDPdk 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720405111 156 LSVEEVVR--SSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGI 230
Cdd:PRK12282  253 AEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKAREVAAQTLSEVKDAMGL 329
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
 11-230 4.66e-34

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 124.45  E-value: 4.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  11 HQWKAKAAKQKHDG-------TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYGEFFPLPKSILT 83
Cdd:PRK12556  110 HAYKAKVDQNKEAGldldagvNMGLYTYPILMAADILLFQATHVPVGKDQIQHIEIARDIATYFNHTFGDTFTLPEYVIQ 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  84 SMKKVKSLRDpSSKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFT-SEVTYEPDSragvSNMVAIHAAVSGLS-VEEV 161
Cdd:PRK12556  190 EEGAILPGLD-GRKMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSSlPNEPKDPET----SALFTIYKEFATEEeVQSM 261

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111 162 -VRSSAGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGI 230
Cdd:PRK12556  262 rEKYETGIGWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKGAERAREIAKPNLAEIKKAIGF 331
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
2-186 1.87e-31

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 116.61  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111   2 VRLPRLQHLHQWKAKAAKQKHDG--TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKygeFFPLPK 79
Cdd:pfam00579 107 GKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRFNKK---IFKKPV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  80 SILTsmkKVKSLRDPSSKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSEVTYEPDSRAGVSN-MVAIHAAVSGLSV 158
Cdd:pfam00579 184 GLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDREVRKDLKLFTFLSNeEIEILEAELGKSP 258

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720405111 159 ---------EEVVRSSAGLDtarYKLLVADAVIEKFA 186
Cdd:pfam00579 259 yreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
 11-230 2.07e-26

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 105.47  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  11 HQWKAKAAKQKHDG-------TVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYG-EFFPLPKSIL 82
Cdd:PRK12284  109 HAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEMARDIAQRFNHLYGgEFFVLPEAVI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  83 TsmKKVKSLrdP---SSKMSKSDPDklaTVRITDSPEEIvqkfRKAVtdfTSEVTyepDSRA-GV------SNMVAIHAA 152
Cdd:PRK12284  189 E--ESVATL--PgldGRKMSKSYDN---TIPLFAPREEL----KKAI---FSIVT---DSRApGEpkdtegSALFQLYQA 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111 153 VSGLSVEEVVRSS--AGLDTARYKLLVADAVIEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGI 230
Cdd:PRK12284  252 FATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAGAAKARRIATPFLAELREAVGL 331
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 19-230 3.67e-22

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 93.48  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  19 KQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQKYG-------------------------- 72
Cdd:PRK12283  118 KEKDLSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIARRFNHLYGrepgfeekaeaaikklgkkraklyhe 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  73 --------------------------------------------EFFPLPKSILTSMKKVKSLrdPSSKMSKSDPDklaT 108
Cdd:PRK12283  198 lrnayqeegddealeqarallqeqqnlsmgdrerlfgylegagkIILPEPQALLTEASKMPGL--DGQKMSKSYGN---T 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111 109 VRITDSPEEIVQKFRKAVTDfTSEV----TYEPDsRAGVSNMvaiHAAVSGLSVEEVVR---SSAGLDTARYKLLVADAV 181
Cdd:PRK12283  273 IGLREDPESVTKKIRTMPTD-PARVrrtdPGDPE-KCPVWQL---HQVYSDEETKEWVQkgcRSAGIGCLECKQPVIDAI 347

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720405111 182 IEKFAPIRKEIEKLKMDKDHLRKVLLVGSAKAKELASPVFEEVKKLVGI 230
Cdd:PRK12283  348 LREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREAMGL 396
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 19-183 3.99e-17

catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173893 [Multi-domain]  Cd Length: 273  Bit Score: 78.11  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  19 KQKHDGTVGLLTYPVLQAADILCYKSTH----VPVGEDQVQHMELVQDLARSFNqkyGEFFPLPKSIltsmKKVKSLRDP 94
Cdd:cd00395   125 RSEEGISATEFTYPPLQAADFLLLNTTEgcdiQPGGSDQWGNITLGRELARRFN---GFTIAEGLTI----PLVTKLDGP 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  95 ssKMSKSDPDKLATVRITDSPEEIVQKFRKAVtdftsevtyepdsragVSNMVAIHAAVSGLSVEEVVRSSAGLDTAR-- 172
Cdd:cd00395   198 --KFGKSESGPKWLDTEKTSPYEFYQFWINAV----------------DSDVINILKYFTFLSKEEIERLEQEQYEAPgy 259

                         170
                  ....*....|...
gi 1720405111 173 --YKLLVADAVIE 183
Cdd:cd00395   260 rvAQKTLAEEVTK 272
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 25-127 1.82e-16

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 77.21  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  25 TVGLLTYPVLQAADILC------YKSTHVPVGEDQVQHMELVQDLARSFNQKYGefFPLPKSILtsMKKVKSLRdpSSKM 98
Cdd:PRK12285  179 NIGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPHIRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKM 252

                          90       100
                  ....*....|....*....|....*....
gi 1720405111  99 SKSDPDklATVRITDSPEEIVQKFRKAVT 127
Cdd:PRK12285  253 SSSKPE--SAIYLTDDPETVKKKIMKALT 279
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 18-125 4.19e-09

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 55.64  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  18 AKQKHDGTVGLLTYPVLQAADILcYKSTHVPV-GEDQVQ-HMelvqdLARSFNQKYGefFPLPKSILTSMkkVKSLRDPS 95
Cdd:PRK08560  143 GRRMEEPDVSKLVYPLMQVADIF-YLDVDIAVgGMDQRKiHM-----LAREVLPKLG--YKKPVCIHTPL--LTGLDGGG 212

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720405111  96 SKMSKSDPDklATVRITDSPEEIVQKFRKA 125
Cdd:PRK08560  213 IKMSKSKPG--SAIFVHDSPEEIRRKIKKA 240
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 29-125 4.10e-07

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 49.69  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  29 LTYPVLQAADILCYKSTHVPVGEDQVQhmelVQDLARSFNQKYGEffpLPKSILTSMKKVKSLRDPSSKMSKSDPDklAT 108
Cdd:PTZ00126  196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLAREYCDKKKI---KKKPIILSHHMLPGLLEGQEKMSKSDPN--SA 266

                          90
                  ....*....|....*..
gi 1720405111 109 VRITDSPEEIVQKFRKA 125
Cdd:PTZ00126  267 IFMEDSEEDVNRKIKKA 283
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 19-125 7.14e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 46.43  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  19 KQKHDGTVGLLTYPVLQAADILCYKSTHVPVGEDQVQhmelVQDLARSFNQKYGEFFplpKSILTSMKKVKSLRDPSSKM 98
Cdd:PTZ00348  151 KTEGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRK----VNMLAREYCDLIGRKL---KPVILSHHMLAGLKQGQAKM 223

                          90       100
                  ....*....|....*....|....*..
gi 1720405111  99 SKSDPDklATVRITDSPEEIVQKFRKA 125
Cdd:PTZ00348  224 SKSDPD--SAIFMEDTEEDVARKIRQA 248
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 29-125 7.22e-06

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 45.67  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  29 LTYPVLQAADILCYKSTHVPVGEDQVQHMELVQDLARSFNQK--YGEFFPLpksiLTSMKkvkslrdpSSKMSKSDPDKl 106
Cdd:cd00805   137 FIYPLLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLGYKkvVGLTTPL----LTGLD--------GGKMSKSEGNA- 203

                          90
                  ....*....|....*....
gi 1720405111 107 ATVRITDSPEEIVQKFRKA 125
Cdd:cd00805   204 IWDPVLDSPYDVYQKIRNA 222
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 17-133 3.07e-04

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 41.23  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  17 AAKQKHDGTVGLLTYPVLQAADILC-YKSTHVPvGEDQVQHMELVQDLARSFNQKYGefFPLPKSILTSMKKVKSLRDPS 95
Cdd:TIGR00234 152 SSRFEENISLHEFIYPLLQAYDFVYlNVDLQLG-GSDQWFNIRKGRDLARENLPSLQ--FGLTVPLLTPADGEKMGKSLG 228

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720405111  96 SKMSkSDPDKLAT-VRITDSPEEIVQKFRKAVTDFTSEV 133
Cdd:TIGR00234 229 GAVS-LDEGKYDFyQKVINTPDELVKKYLKLFTFLGLEE 266
PLN02486 PLN02486
aminoacyl-tRNA ligase
 26-124 1.47e-03

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 38.96  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405111  26 VGLLTYPVLQAA---------------DILCYksthVPVGEDQVQHMELVQDLA-RSFNQK----YGEFFPlpksiltsm 85
Cdd:PLN02486  191 IGKISFPAVQAApsfpssfphlfggkdKLRCL----IPCAIDQDPYFRMTRDVApRLGYYKpaliESRFFP--------- 257

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720405111  86 kkvkSLRDPSSKMSKSDPDklATVRITDSPEEIVQKFRK 124
Cdd:PLN02486  258 ----ALQGESGKMSASDPN--SAIYVTDTPKEIKNKINK 290
 
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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