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Conserved domains on  [gi|1804891998|ref|NP_001365158|]
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tryptophan--tRNA ligase, mitochondrial isoform 5 [Homo sapiens]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK00927 super family cl35130
tryptophanyl-tRNA synthetase; Reviewed
 30-274 1.23e-102

tryptophanyl-tRNA synthetase; Reviewed


The actual alignment was detected with superfamily member PRK00927:

Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 302.01  E-value: 1.23e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:PRK00927   82 HVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRAGV 186
Cdd:PRK00927  162 FNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEV 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 187 SNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVC 264
Cdd:PRK00927  242 SNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTL 321

                         250
                  ....*....|
gi 1804891998 265 QEVKKLVGFL 274
Cdd:PRK00927  322 KEVREAMGLL 331
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 30-274 1.23e-102

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 302.01  E-value: 1.23e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:PRK00927   82 HVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRAGV 186
Cdd:PRK00927  162 FNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEV 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 187 SNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVC 264
Cdd:PRK00927  242 SNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTL 321

                         250
                  ....*....|
gi 1804891998 265 QEVKKLVGFL 274
Cdd:PRK00927  322 KEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 30-274 8.59e-97

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: 287.33  E-value: 8.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 108
Cdd:COG0180    84 DVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 109 GFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRAGVS 187
Cdd:COG0180   164 RFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPEVC 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 188 NIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVC 264
Cdd:COG0180   239 NLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKTL 318

                         250
                  ....*....|
gi 1804891998 265 QEVKKLVGFL 274
Cdd:COG0180   319 AEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 30-226 3.21e-84

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: 253.66  E-value: 3.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:cd00806    82 DVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNI 189
Cdd:cd00806   161 FNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSNL 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1804891998 190 VAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 226
Cdd:cd00806   239 VEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 29-273 5.56e-60

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: 192.93  E-value: 5.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  29 LQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 108
Cdd:TIGR00233  83 SDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 109 GFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVS 187
Cdd:TIGR00233 161 RFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVP 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 188 NIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAKELA 260
Cdd:TIGR00233 237 NLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKARETA 314

                         250
                  ....*....|...
gi 1804891998 261 YTVCQEVKKLVGF 273
Cdd:TIGR00233 315 NKTLADVYKAMGL 327
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
33-229 6.49e-38

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 135.10  E-value: 6.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  33 EHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGF 110
Cdd:pfam00579  95 EHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 111 NKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN-I 189
Cdd:pfam00579 175 NKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDREVRKDLKLFTFLSNeE 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1804891998 190 VAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 229
Cdd:pfam00579 247 IEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 30-274 1.23e-102

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 302.01  E-value: 1.23e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:PRK00927   82 HVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRAGV 186
Cdd:PRK00927  162 FNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPEV 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 187 SNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVC 264
Cdd:PRK00927  242 SNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKTL 321

                         250
                  ....*....|
gi 1804891998 265 QEVKKLVGFL 274
Cdd:PRK00927  322 KEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 30-274 8.59e-97

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: 287.33  E-value: 8.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 108
Cdd:COG0180    84 DVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 109 GFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRAGVS 187
Cdd:COG0180   164 RFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPEVC 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 188 NIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVC 264
Cdd:COG0180   239 NLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKTL 318

                         250
                  ....*....|
gi 1804891998 265 QEVKKLVGFL 274
Cdd:COG0180   319 AEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 30-226 3.21e-84

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: 253.66  E-value: 3.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:cd00806    82 DVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNI 189
Cdd:cd00806   161 FNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSNL 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1804891998 190 VAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 226
Cdd:cd00806   239 VEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
PLN02886 PLN02886
aminoacyl-tRNA ligase
 31-274 2.15e-63

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 203.89  E-value: 2.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  31 VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQ-KHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQG 109
Cdd:PLN02886  128 VPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAER 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNKKYG------------EFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFTSEV 176
Cdd:PLN02886  208 VNNLYGgrkwkklggrggSVFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGL 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 177 TYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKA 256
Cdd:PLN02886  288 EFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAA 367

                         250
                  ....*....|....*...
gi 1804891998 257 KELAYTVCQEVKKLVGFL 274
Cdd:PLN02886  368 AEIADRTLANVYQAMGFV 385
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 29-273 5.56e-60

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: 192.93  E-value: 5.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  29 LQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 108
Cdd:TIGR00233  83 SDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 109 GFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVS 187
Cdd:TIGR00233 161 RFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVP 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 188 NIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAKELA 260
Cdd:TIGR00233 237 NLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKARETA 314

                         250
                  ....*....|...
gi 1804891998 261 YTVCQEVKKLVGF 273
Cdd:TIGR00233 315 NKTLADVYKAMGL 327
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 30-272 1.13e-41

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 145.77  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtKQKHDG---TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 106
Cdd:PRK12282   84 QIPELAELTMYYMNLVTVARLERNPTVKTEI-AQKGFGrsiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQTREI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 107 AQGFNKKYG-EFFPVPESILTSMKKVKSLrDPSAKMSKSDPDKLAtvrITDSPEEIVQKFRKAVTDfTSEVTYDPAGRAG 185
Cdd:PRK12282  163 VRRFNSLYGtDVLVEPEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMYTD-PNHIRVEDPGKVE 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 186 VSNIVAVHAAV--TGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAY 261
Cdd:PRK12282  238 GNVVFTYLDAFdpDKAEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKAREVAA 317

                         250
                  ....*....|.
gi 1804891998 262 TVCQEVKKLVG 272
Cdd:PRK12282  318 QTLSEVKDAMG 328
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
33-229 6.49e-38

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 135.10  E-value: 6.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  33 EHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGF 110
Cdd:pfam00579  95 EHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 111 NKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN-I 189
Cdd:pfam00579 175 NKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDREVRKDLKLFTFLSNeE 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1804891998 190 VAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 229
Cdd:pfam00579 247 IEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
 2-273 2.77e-36

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 131.77  E-value: 2.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998   2 ALHSMRKARERWSFIRalhkgSAAAPAL---------------QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD 66
Cdd:PRK12556   48 ALNAVHDPEQFRSYTR-----EVAATWLslgldpedvifyrqsDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  67 G-------TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDpSA 139
Cdd:PRK12556  123 GldldagvNMGLYTYPILMAADILLFQATHVPVGKDQIQHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD-GR 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 140 KMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFT-SEVTYDPAGragvSNIVAVHAA-VTGLSVEEV-VRRSAGMNTARY 216
Cdd:PRK12556  202 KMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSSlPNEPKDPET----SALFTIYKEfATEEEVQSMrEKYETGIGWGDV 274

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1804891998 217 KLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGF 273
Cdd:PRK12556  275 KKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKGAERAREIAKPNLAEIKKAIGF 331
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
 31-272 3.72e-26

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 106.24  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  31 VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELV 103
Cdd:PRK12284   86 IPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEMA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 104 QDLAQGFNKKYG-EFFPVPESILTsmKKVKSL-----RdpsaKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDftSEVT 177
Cdd:PRK12284  166 RDIAQRFNHLYGgEFFVLPEAVIE--ESVATLpgldgR----KMSKSYDN---TIPLFAPREELKKAIFSIVTD--SRAP 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 178 YDPAGRAGvSNIVAVHAAVTGLSVEEVVRRS--AGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAK 255
Cdd:PRK12284  235 GEPKDTEG-SALFQLYQAFATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAGAAK 313

                         250
                  ....*....|....*..
gi 1804891998 256 AKELAYTVCQEVKKLVG 272
Cdd:PRK12284  314 ARRIATPFLAELREAVG 330
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 30-272 3.44e-23

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 97.33  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  30 QVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD--GTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLA 107
Cdd:PRK12283   84 KVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 108 QGFNKKYG----------------------------------------------------------------------EF 117
Cdd:PRK12283  164 RRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqarallqeqqnlsmgdrerlfgylegagkII 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 118 FPVPESILTSMKKVKSLrdPSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFTSEVTYDPaGRAGVSNIVAVHAAVT 197
Cdd:PRK12283  244 LPEPQALLTEASKMPGL--DGQKMSKSYGN---TIGLREDPESVTKKIRTMPTDPARVRRTDP-GDPEKCPVWQLHQVYS 317

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891998 198 GLSVEEVVR---RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVG 272
Cdd:PRK12283  318 DEETKEWVQkgcRSAGIGCLECKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREAMG 395
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 34-226 3.77e-20

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: 87.36  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  34 HTQLSWILSCMVRLPRLQHLHQWKAKTtkqKHDGTVGLLTYPVLQAADILLYKSTH----VPVGEDQVQHMELVQDLAQG 109
Cdd:cd00395   100 HIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQPGGSDQWGNITLGRELARR 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998 110 FNkkygeFFPVPESILTSMkkVKSLRDPsaKMSKSDPDKLATVRITDSPEEIVQKFRKAVtdftsevtydpagragVSNI 189
Cdd:cd00395   177 FN-----GFTIAEGLTIPL--VTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV----------------DSDV 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1804891998 190 VAVHAAVTGLSVEEVVRRSAGMNTAR----YKLAVADAVIE 226
Cdd:cd00395   232 INILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 68-170 4.49e-16

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 76.83  E-value: 4.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  68 TVGLLTYPVLQAADILL------YKSTHVPVGEDQVQHMELVQDLAQGFNKKYGefFPVPESILtsMKKVKSLRdpSAKM 141
Cdd:PRK12285  179 NIGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPHIRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKM 252

                          90       100
                  ....*....|....*....|....*....
gi 1804891998 142 SKSDPDklATVRITDSPEEIVQKFRKAVT 170
Cdd:PRK12285  253 SSSKPE--SAIYLTDDPETVKKKIMKALT 279
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 66-168 7.44e-09

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 55.64  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  66 DGTVGLLTYPVLQAADILlYKSTHVPV-GEDQVQ-HMeLVQDLAQGFNkkygefFPVPESILTSMkkVKSLRDPSAKMSK 143
Cdd:PRK08560  148 EPDVSKLVYPLMQVADIF-YLDVDIAVgGMDQRKiHM-LAREVLPKLG------YKKPVCIHTPL--LTGLDGGGIKMSK 217

                          90       100
                  ....*....|....*....|....*
gi 1804891998 144 SDPDklATVRITDSPEEIVQKFRKA 168
Cdd:PRK08560  218 SKPG--SAIFVHDSPEEIRRKIKKA 240
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 72-168 5.27e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 46.99  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  72 LTYPVLQAADILLYKSTHVPVGEDQVQhmelVQDLAqgfnKKYGEFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDklA 150
Cdd:PTZ00126  196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLA----REYCDKKKIKKKpIILSHHMLPGLLEGQEKMSKSDPN--S 265

                          90
                  ....*....|....*...
gi 1804891998 151 TVRITDSPEEIVQKFRKA 168
Cdd:PTZ00126  266 AIFMEDSEEDVNRKIKKA 283
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 62-181 1.05e-05

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 46.43  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  62 KQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpvpESILTSMKKVKSLRDPSAKM 141
Cdd:PTZ00348  151 KTEGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKL-------KPVILSHHMLAGLKQGQAKM 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1804891998 142 SKSDPDklATVRITDSPEEIVQKFRKA----VTDFTSEVTYDPA 181
Cdd:PTZ00348  224 SKSDPD--SAIFMEDTEEDVARKIRQAycprVKQSASEITDDGA 265
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 72-168 1.19e-04

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: 42.59  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  72 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKK--YGEFFPvpesILTSMKkvkslrdpSAKMSKSDPDK 148
Cdd:cd00805   137 FIYPLLQAYDFVyLDVDLQLG-GSDQRGNITLGRDLIRKLGYKkvVGLTTP----LLTGLD--------GGKMSKSEGNA 203

                          90       100
                  ....*....|....*....|
gi 1804891998 149 lATVRITDSPEEIVQKFRKA 168
Cdd:cd00805   204 -IWDPVLDSPYDVYQKIRNA 222
PLN02486 PLN02486
aminoacyl-tRNA ligase
 69-167 1.27e-03

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 39.73  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  69 VGLLTYPVLQAA-------DILLYKSTH----VPVGEDQVQHMELVQDLAQ--GFNKK---YGEFFPvpesiltsmkkvk 132
Cdd:PLN02486  191 IGKISFPAVQAApsfpssfPHLFGGKDKlrclIPCAIDQDPYFRMTRDVAPrlGYYKPaliESRFFP------------- 257

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1804891998 133 SLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRK 167
Cdd:PLN02486  258 ALQGESGKMSASDPN--SAIYVTDTPKEIKNKINK 290
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 72-207 1.89e-03

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: 39.30  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891998  72 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKKYGEFFPVPesILTSMKKVKSLRDPSAKMSkSDPDKLA 150
Cdd:TIGR00234 164 FIYPLLQAYDFVyLNVDLQLG-GSDQWFNIRKGRDLARENLPSLQFGLTVP--LLTPADGEKMGKSLGGAVS-LDEGKYD 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891998 151 T-VRITDSPEEIVQKFRKAVTDFTSEVTYDpagragVSNIVAVHA-AVTGLSVEEVVRR 207
Cdd:TIGR00234 240 FyQKVINTPDELVKKYLKLFTFLGLEEIEQ------LVELKGPNPrEVKENLALEITKY 292
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 74-145 4.62e-03

catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers 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 characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 36.69  E-value: 4.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804891998  74 YPVLQAADILL---YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpVPESILTSMKKVKSLRdpsaKMSKSD 145
Cdd:cd00802    78 YMFLQAADFLLlyeTECDIHLGGSDQLGHIELGLELLKKAGGPA-----RPFGLTFGRVMGADGT----KMSKSK 143
 
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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