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Conserved domains on  [gi|1804891971|ref|NP_001365159|]
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tryptophan--tRNA ligase, mitochondrial isoform 6 [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
 1-266 1.17e-118

tryptophanyl-tRNA synthetase; Reviewed


The actual alignment was detected with superfamily member PRK00927:

Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 342.45  E-value: 1.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKST 80
Cdd:PRK00927   61 LAADYLACGIDPEKSTIFVQSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRK 159
Cdd:PRK00927  141 LVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 160 AVTDFT--SEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKD 235
Cdd:PRK00927  221 AVTDSErlREIRYDLPNKPEVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPA 300

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1804891971 236 HLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:PRK00927  301 YLDEILAEGAEKARAVASKTLKEVREAMGLL 331
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 1-266 1.17e-118

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 342.45  E-value: 1.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKST 80
Cdd:PRK00927   61 LAADYLACGIDPEKSTIFVQSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRK 159
Cdd:PRK00927  141 LVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 160 AVTDFT--SEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKD 235
Cdd:PRK00927  221 AVTDSErlREIRYDLPNKPEVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPA 300

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1804891971 236 HLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:PRK00927  301 YLDEILAEGAEKARAVASKTLKEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-266 1.20e-112

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: 327.01  E-value: 1.20e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKS 79
Cdd:COG0180    63 VAADYLAAGLDPEKSTIFVQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  80 THVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFR 158
Cdd:COG0180   143 DLVPVGEDQKQHLELTRDIARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIK 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 159 KAVTDfTSEVTYDPAGRAGVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKD 235
Cdd:COG0180   219 SAVTD-SERLRYDDPGKPEVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPA 297

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1804891971 236 HLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:COG0180   298 ELDEILAEGAEKARAIAAKTLAEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 1-218 5.53e-98

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: 288.33  E-value: 5.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKST 80
Cdd:cd00806    61 NAKDYLACGLDPEKSTIFFQSDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKAC 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKA 160
Cdd:cd00806   140 LVPVGIDQDPHLELTRDIARRFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKA 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804891971 161 VTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 218
Cdd:cd00806   218 ATDGGRTEHRRDGGGPGVSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 1-265 2.47e-71

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: 221.82  E-value: 2.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKST 80
Cdd:TIGR00233  63 LAADYLAVGLDPEKTFIFLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRK 159
Cdd:TIGR00233 141 LVPVGIDQDQHLELTRDLAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRK 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 160 AVTDFTSEVTYDPAGRAGVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKL 232
Cdd:TIGR00233 217 AATDGGRVTLFEHREKPGVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EI 294

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1804891971 233 DKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGF 265
Cdd:TIGR00233 295 AEEILDKILEPGAKKARETANKTLADVYKAMGL 327
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
5-221 6.81e-47

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 157.82  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   5 LLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHV 82
Cdd:pfam00579  75 QLACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQ 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  83 PVGEDQVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVT 162
Cdd:pfam00579 155 PGGSDQWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYT 226

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891971 163 DFTSEVTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 221
Cdd:pfam00579 227 DPDREVRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 1-266 1.17e-118

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 342.45  E-value: 1.17e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKST 80
Cdd:PRK00927   61 LAADYLACGIDPEKSTIFVQSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRK 159
Cdd:PRK00927  141 LVPVGEDQKQHLELTRDIARRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 160 AVTDFT--SEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKD 235
Cdd:PRK00927  221 AVTDSErlREIRYDLPNKPEVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPA 300

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1804891971 236 HLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:PRK00927  301 YLDEILAEGAEKARAVASKTLKEVREAMGLL 331
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-266 1.20e-112

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: 327.01  E-value: 1.20e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKS 79
Cdd:COG0180    63 VAADYLAAGLDPEKSTIFVQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  80 THVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFR 158
Cdd:COG0180   143 DLVPVGEDQKQHLELTRDIARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIK 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 159 KAVTDfTSEVTYDPAGRAGVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKD 235
Cdd:COG0180   219 SAVTD-SERLRYDDPGKPEVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPA 297

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1804891971 236 HLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:COG0180   298 ELDEILAEGAEKARAIAAKTLAEVREAMGLL 328
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 1-218 5.53e-98

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: 288.33  E-value: 5.53e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKST 80
Cdd:cd00806    61 NAKDYLACGLDPEKSTIFFQSDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKAC 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKA 160
Cdd:cd00806   140 LVPVGIDQDPHLELTRDIARRFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKA 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804891971 161 VTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 218
Cdd:cd00806   218 ATDGGRTEHRRDGGGPGVSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
PLN02886 PLN02886
aminoacyl-tRNA ligase
 1-266 9.81e-75

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 232.78  E-value: 9.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQ-KHDGTVGLLTYPVLQAADILLYKS 79
Cdd:PLN02886  106 TAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  80 THVPVGEDQVQHMELVQDLAQGFNKKYG------------EFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDKLATVRI 146
Cdd:PLN02886  186 DLVPVGEDQKQHLELTRDIAERVNNLYGgrkwkklggrggSVFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 147 TDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKRE 226
Cdd:PLN02886  266 LDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVR 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1804891971 227 IEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 266
Cdd:PLN02886  346 YEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFV 385
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 1-265 2.47e-71

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: 221.82  E-value: 2.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKST 80
Cdd:TIGR00233  63 LAADYLAVGLDPEKTFIFLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  81 HVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRK 159
Cdd:TIGR00233 141 LVPVGIDQDQHLELTRDLAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRK 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 160 AVTDFTSEVTYDPAGRAGVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKL 232
Cdd:TIGR00233 217 AATDGGRVTLFEHREKPGVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EI 294

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1804891971 233 DKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGF 265
Cdd:TIGR00233 295 AEEILDKILEPGAKKARETANKTLADVYKAMGL 327
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 6-264 3.33e-52

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 172.73  E-value: 3.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   6 LACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtKQKHDG---TVGLLTYPVLQAADILLYKSTHV 82
Cdd:PRK12282   68 LAVGIDPAKSTIFIQSQIPELAELTMYYMNLVTVARLERNPTVKTEI-AQKGFGrsiPAGFLTYPVSQAADITAFKATLV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  83 PVGEDQVQHMELVQDLAQGFNKKYG-EFFPVPESILTSMKKVKSLrDPSAKMSKSDPDKLAtvrITDSPEEIVQKFRKAV 161
Cdd:PRK12282  147 PVGDDQLPMIEQTREIVRRFNSLYGtDVLVEPEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMY 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 162 TDfTSEVTYDPAGRAGVSNIVAVHAAV--TGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHL 237
Cdd:PRK12282  223 TD-PNHIRVEDPGKVEGNVVFTYLDAFdpDKAEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYV 301

                         250       260
                  ....*....|....*....|....*..
gi 1804891971 238 EKVLQIGSAKAKELAYTVCQEVKKLVG 264
Cdd:PRK12282  302 LEILKAGSEKAREVAAQTLSEVKDAMG 328
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
5-221 6.81e-47

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 157.82  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   5 LLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHV 82
Cdd:pfam00579  75 QLACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQ 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  83 PVGEDQVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVT 162
Cdd:pfam00579 155 PGGSDQWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYT 226

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891971 163 DFTSEVTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 221
Cdd:pfam00579 227 DPDREVRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
 3-265 8.72e-46

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 156.42  E-value: 8.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   3 AVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADIL 75
Cdd:PRK12556   67 ATWLSLGLDPEDVIFYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEAGldldagvNMGLYTYPILMAADIL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  76 LYKSTHVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDpSAKMSKSDPDklaTVRITDSPEEIVQ 155
Cdd:PRK12556  147 LFQATHVPVGKDQIQHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD-GRKMSKSYGN---VIPLFAEQEKLRK 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 156 KFRKAVTDFT-SEVTYDPAGragvSNIVAVHAA-VTGLSVEEV-VRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKL 232
Cdd:PRK12556  223 LIFKIKTDSSlPNEPKDPET----SALFTIYKEfATEEEVQSMrEKYETGIGWGDVKKELFRVVDRELAGPREKYAMYMN 298

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1804891971 233 DKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGF 265
Cdd:PRK12556  299 EPSLLDEALEKGAERAREIAKPNLAEIKKAIGF 331
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
 3-264 1.79e-34

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 128.58  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   3 AVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADIL 75
Cdd:PRK12284   66 ATWLAAGLDPERVTFYRQSDIPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADIL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  76 LYKSTHVPVGEDQVQHMELVQDLAQGFNKKYG-EFFPVPESILTsmKKVKSL-----RdpsaKMSKSDPDklaTVRITDS 149
Cdd:PRK12284  146 MFNAHKVPVGRDQIQHIEMARDIAQRFNHLYGgEFFVLPEAVIE--ESVATLpgldgR----KMSKSYDN---TIPLFAP 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 150 PEEIVQKFRKAVTDftSEVTYDPAGRAGvSNIVAVHAAVTGLSVEEVVRRS--AGMNTARYKLAVADAVIEKFAPIKREI 227
Cdd:PRK12284  217 REELKKAIFSIVTD--SRAPGEPKDTEG-SALFQLYQAFATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERY 293

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1804891971 228 EKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVG 264
Cdd:PRK12284  294 EALIARPADIEDILLAGAAKARRIATPFLAELREAVG 330
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 6-264 1.87e-33

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 125.06  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   6 LACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD--GTVGLLTYPVLQAADILLYKSTHVP 83
Cdd:PRK12283   68 LAAGVDPAQATLFIQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVP 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  84 VGEDQVQHMELVQDLAQGFNKKYG-------------------------------------------------------- 107
Cdd:PRK12283  148 VGEDQVPHVEMTREIARRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqarallqeqqnlsmg 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 108 --------------EFFPVPESILTSMKKVKSLrDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFTSEVTYDPa 173
Cdd:PRK12283  228 drerlfgylegagkIILPEPQALLTEASKMPGL-D-GQKMSKSYGN---TIGLREDPESVTKKIRTMPTDPARVRRTDP- 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971 174 GRAGVSNIVAVHAAVTGLSVEEVVR---RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKE 250
Cdd:PRK12283  302 GDPEKCPVWQLHQVYSDEETKEWVQkgcRSAGIGCLECKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARK 381

                         330
                  ....*....|....
gi 1804891971 251 LAYTVCQEVKKLVG 264
Cdd:PRK12283  382 VARETMRDVREAMG 395
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 1-218 1.27e-21

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: 91.21  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGI--NPEKSILFQQSQV---SEHTQLSWILSCMVRLPRLQHLHQWKAKTtkqKHDGTVGLLTYPVLQAADIL 75
Cdd:cd00395    70 IAAQYLAVGIfeDPTQATLFNNSDWpgpLAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  76 LYKSTH----VPVGEDQVQHMELVQDLAQGFNkkygeFFPVPESILTSMkkVKSLRDPsaKMSKSDPDKLATVRITDSPE 151
Cdd:cd00395   147 LLNTTEgcdiQPGGSDQWGNITLGRELARRFN-----GFTIAEGLTIPL--VTKLDGP--KFGKSESGPKWLDTEKTSPY 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804891971 152 EIVQKFRKAVtdftsevtydpagragVSNIVAVHAAVTGLSVEEVVRRSAGMNTAR----YKLAVADAVIE 218
Cdd:cd00395   218 EFYQFWINAV----------------DSDVINILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 5-162 1.40e-18

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 84.15  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   5 LLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTkqkhdgtVGLLTYPVLQAADILL------YK 78
Cdd:PRK12285  131 LIALGFDPDKTEIYFQSENIKVYDLAFELAKKVNFSELKAIYGFTGETN-------IGHIFYPATQAADILHpqleegPK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  79 STHVPVGEDQVQHMELVQDLAQGFNKKYGefFPVPESILtsMKKVKSLRdpSAKMSKSDPDklATVRITDSPEEIVQKFR 158
Cdd:PRK12285  204 PTLVPVGIDQDPHIRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKMSSSKPE--SAIYLTDDPETVKKKIM 275


                  ....
gi 1804891971 159 KAVT 162
Cdd:PRK12285  276 KALT 279
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 1-160 5.02e-09

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 56.03  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKS--IL---FQQSqvSEHTQLSWILSCMVRLPRLQHlhqwkAKT--TKQKHDGTVGLLTYPVLQAAD 73
Cdd:PRK08560   91 NKKVFEALGLDPDKTefVLgseFQLD--KEYWLLVLKLAKNTTLARARR-----SMTimGRRMEEPDVSKLVYPLMQVAD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  74 ILlYKSTHVPV-GEDQVQ-HMeLVQDLAQGFNkkygefFPVPESILTSMkkVKSLRDPSAKMSKSDPDklATVRITDSPE 151
Cdd:PRK08560  164 IF-YLDVDIAVgGMDQRKiHM-LAREVLPKLG------YKKPVCIHTPL--LTGLDGGGIKMSKSKPG--SAIFVHDSPE 231


                  ....*....
gi 1804891971 152 EIVQKFRKA 160
Cdd:PRK08560  232 EIRRKIKKA 240
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 1-173 1.30e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 49.13  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   1 MTAVLLACGINPEKSI-LFQQSQVSEHTQLSWILscMVRLPRLQHLHQWKAKTT---KQKHDGTVGLLTYPVLQAADILL 76
Cdd:PTZ00348   96 LIEVWKAAGMDMDKVLfLWSSEEITNHANTYWRT--VLDIGRQNTIARIKKCCTimgKTEGTLTAAQVLYPLMQCADIFF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  77 YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpvpESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQK 156
Cdd:PTZ00348  174 LKADICQLGLDQRKVNMLAREYCDLIGRKL-------KPVILSHHMLAGLKQGQAKMSKSDPD--SAIFMEDTEEDVARK 244

                         170       180
                  ....*....|....*....|.
gi 1804891971 157 FRKA----VTDFTSEVTYDPA 173
Cdd:PTZ00348  245 IRQAycprVKQSASEITDDGA 265
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 64-160 5.17e-06

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 46.99  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  64 LTYPVLQAADILLYKSTHVPVGEDQVQhmelVQDLAqgfnKKYGEFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDklA 142
Cdd:PTZ00126  196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLA----REYCDKKKIKKKpIILSHHMLPGLLEGQEKMSKSDPN--S 265

                          90
                  ....*....|....*...
gi 1804891971 143 TVRITDSPEEIVQKFRKA 160
Cdd:PTZ00126  266 AIFMEDSEEDVNRKIKKA 283
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 64-160 1.04e-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: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  64 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKK--YGEFFPvpesILTSMKkvkslrdpSAKMSKSDPDK 140
Cdd:cd00805   137 FIYPLLQAYDFVyLDVDLQLG-GSDQRGNITLGRDLIRKLGYKkvVGLTTP----LLTGLD--------GGKMSKSEGNA 203

                          90       100
                  ....*....|....*....|
gi 1804891971 141 lATVRITDSPEEIVQKFRKA 160
Cdd:cd00805   204 -IWDPVLDSPYDVYQKIRNA 222
PLN02486 PLN02486
aminoacyl-tRNA ligase
 5-159 5.15e-04

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 40.88  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971   5 LLACGINPEKSILFQQSQ-VSehtqlSWILSCMVRLprlqhlhqWKAKTTKQKH-----DGT--VGLLTYPVLQAA---- 72
Cdd:PLN02486  140 IIACGFDVERTFIFSDFDyVG-----GAFYKNMVKI--------AKCVTLNQVRgifgfSGEdnIGKISFPAVQAApsfp 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  73 ---DILLYKSTH----VPVGEDQVQHMELVQDLAQ--GFNKK---YGEFFPvpesiltsmkkvkSLRDPSAKMSKSDPDk 140
Cdd:PLN02486  207 ssfPHLFGGKDKlrclIPCAIDQDPYFRMTRDVAPrlGYYKPaliESRFFP-------------ALQGESGKMSASDPN- 272

                         170
                  ....*....|....*....
gi 1804891971 141 lATVRITDSPEEIVQKFRK 159
Cdd:PLN02486  273 -SAIYVTDTPKEIKNKINK 290
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 64-168 2.25e-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: 38.92  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891971  64 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKKYGEFFPVPesILTSMKKVKSLRDPSAKMSkSDPDKLA 142
Cdd:TIGR00234 164 FIYPLLQAYDFVyLNVDLQLG-GSDQWFNIRKGRDLARENLPSLQFGLTVP--LLTPADGEKMGKSLGGAVS-LDEGKYD 239

                          90       100
                  ....*....|....*....|....*..
gi 1804891971 143 T-VRITDSPEEIVQKFRKAVTDFTSEV 168
Cdd:TIGR00234 240 FyQKVINTPDELVKKYLKLFTFLGLEE 266
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 66-137 4.44e-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: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804891971  66 YPVLQAADILL---YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpVPESILTSMKKVKSLRdpsaKMSKSD 137
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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