|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
1-466 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 877.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 1 MIVAPVVDVLQGRVaVGTEVTVQGWVRTRRDSnAGFSFLAVYDGSCFNPLQAIINNNlPNYNDEVLHLTTGCSVEVTGTV 80
Cdd:PRK03932 1 MMRVSIKDILKGKY-VGQEVTVRGWVRTKRDS-GKIAFLQLRDGSCFKQLQVVKDNG-EEYFEEIKKLTTGSSVIVTGTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 81 KESPGQGQSFELEATAVKVVGWveDPDTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWV 160
Cdd:PRK03932 78 VESPRAGQGYELQATKIEVIGE--DPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 161 STPVITASDTEGAGEMFRVSTLDynnlprddkgeVDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNT 240
Cdd:PRK03932 156 DTPIITASDCEGAGELFRVTTLD-----------LDFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 241 SRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKIL 320
Cdd:PRK03932 225 RRHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 321 ETCGQKFENPVYWGVDMSSEHERYLAEQHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERL 400
Cdd:PRK03932 305 QKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739086825 401 DMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPRNAAF 466
Cdd:PRK03932 385 DVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
3-466 |
0e+00 |
|
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273086 [Multi-domain] Cd Length: 453 Bit Score: 766.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 3 VAPVVDVLQG-RVAVGTEVTVQGWVRTRRdSNAGFSFLAVYDGSCFNPLQAIINNNLPNYNDE-VLHLTTGCSVEVTGTV 80
Cdd:TIGR00457 1 SAAIKDLLQQvYKFVGDEVTVSGWVRTKR-SSKKIIFLELNDGSSLGPIQAVINGEDNPYLFQlLKSLTTGSSVSVTGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 81 KESPGQGQSFELEATAVKVVGWVEdPDTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWV 160
Cdd:TIGR00457 80 VESPGKGQPVELQVKKIEVVGEAE-PDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 161 STPVITASDTEGAGEMFRVSTldynnlprddkGEVDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNT 240
Cdd:TIGR00457 159 SPPILTSNDCEGAGELFRVST-----------GNIDFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 241 SRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKIL 320
Cdd:TIGR00457 228 SRHLSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEIL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 321 ETCGQKFENPVYWGVDMSSEHERYLAEQHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERL 400
Cdd:TIGR00457 308 KESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739086825 401 DMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPRNAAF 466
Cdd:TIGR00457 388 DKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
16-464 |
0e+00 |
|
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl/asparaginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439788 [Multi-domain] Cd Length: 430 Bit Score: 732.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDSNaGFSFLAVYDGSCFnpLQAII-NNNLPNYnDEVLHLTTGCSVEVTGTVKESPGQGQSFELEA 94
Cdd:COG0017 13 VGQEVTVAGWVRTKRDSG-GISFLILRDGSGF--IQVVVkKDKLENF-EEAKKLTTESSVEVTGTVVESPRAPQGVELQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 95 TAVKVVGWVEDPdtYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAG 174
Cdd:COG0017 89 EEIEVLGEADEP--YPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPIITASATEGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 175 EMFRVstldynnlprddkgevdfseDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEV 254
Cdd:COG0017 167 ELFPV--------------------DYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMIEPEM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 255 AFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDkdvinRLESFVNSDFAQVDYTDAIKILETCGQKFEnpvyWG 334
Cdd:COG0017 227 AFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVE-----RLEKVPESPFPRITYTEAIEILKKSGEKVE----WG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 335 VDMSSEHERYLAEQHFKAPVVVKNYPKDIKAFYMRLN-EDGKTVAAMDVLAPGIGEIIGGSQREERLDMLDARLEEMGMN 413
Cdd:COG0017 298 DDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNpDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKEKGLD 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739086825 414 KEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPRNA 464
Cdd:COG0017 378 PEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRL 428
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
11-466 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 600.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 11 QGRVAVGTEVTVQGWVRTRRdSNAGFSFLAVYDGSCFNPLQAIINNNLPNYND-EVLHLTTGCSVEVTGTVKESPGQGQS 89
Cdd:PLN02603 101 EGLARVGKTLNVMGWVRTLR-AQSSVTFIEVNDGSCLSNMQCVMTPDAEGYDQvESGLITTGASVLVQGTVVSSQGGKQK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 90 FELEATAVKVVGwVEDPdTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASD 169
Cdd:PLN02603 180 VELKVSKIVVVG-KSDP-SYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 170 TEGAGEMFRVSTLDYNN----------LPRDDKGEVDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSN 239
Cdd:PLN02603 258 CEGAGEQFCVTTLIPNSaenggslvddIPKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 240 TSRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKI 319
Cdd:PLN02603 338 TSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVEKNFVQLSYTDAIEL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 320 LETCGQKFENPVYWGVDMSSEHERYLAEQHFKA-PVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREE 398
Cdd:PLN02603 418 LLKAKKKFEFPVKWGLDLQSEHERYITEEAFGGrPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVPRVGELIGGSQREE 497
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739086825 399 RLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPRNAAF 466
Cdd:PLN02603 498 RLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSAEF 565
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
17-464 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 524.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 17 GTEVTVQGWVRTRRDSNAG-FSFLAVYDGSCFNPLQAIINNNLPNYNDEVlhlTTGCSVEVTGTVK---ESPGQGQSFEL 92
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGKGtFAFLEVNDGSCPANLQVMVDSSLYDLSTLV---ATGTCVTVDGVLKvppEGKGTKQKIEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 93 EATAVKVVGWVeDPDTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEG 172
Cdd:PLN02221 127 SVEKVIDVGTV-DPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 173 AGEMFRVSTL-DYNN----------------------------------------------------------------- 186
Cdd:PLN02221 206 AGEMFQVTTLiNYTErleqdlidnpppteadveaarlivkergevvaqlkaakaskeeitaavaelkiakeslahieers 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 187 -----LPRDDkGEVDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFASLDD 261
Cdd:PLN02221 286 klkpgLPKKD-GKIDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLED 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 262 VAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKILETC---GQKFENPVYWGVDMS 338
Cdd:PLN02221 365 DMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAvakGKEFDNNVEWGIDLA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 339 SEHERYLAEQHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDMLDARLEEMGMNKEDYW 418
Cdd:PLN02221 445 SEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIEPYE 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 739086825 419 WYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPRNA 464
Cdd:PLN02221 525 WYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKA 570
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
16-466 |
7.34e-177 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 508.41 E-value: 7.34e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDSNAG-FSFLAVYDGSCFNPLQAIINNNLPNYnDEVLHLTTGCSVEVTGTVKESPGQGQS----- 89
Cdd:PTZ00425 80 IDQIITVCGWSKAVRKQGGGrFCFVNLNDGSCHLNLQIIVDQSIENY-EKLLKCGVGCCFRFTGKLIISPVQNENkkgll 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 90 -----FELEATAV---KVVGWVEDPDTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVS 161
Cdd:PTZ00425 159 kenveLALKDNSIhnfEIYGENLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIH 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 162 TPVITASDTEGAGEMFRVSTL-----DYNNLPR----DDKGE----------------------------------VDFS 198
Cdd:PTZ00425 239 TPLITTSDCEGGGEMFTVTTLlgedaDYRAIPRvnkkNKKGEkredilntcnannnngnssssnavsspaypdqylIDYK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 199 EDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAAL 278
Cdd:PTZ00425 319 KDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 279 EERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKILETCGQKFENPVYWGVDMSSEHERYLAEQHFKAPVVVKN 358
Cdd:PTZ00425 399 NNNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 359 YPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGF 438
Cdd:PTZ00425 479 YPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGF 558
|
490 500
....*....|....*....|....*...
gi 739086825 439 ERLVAYVTGVGNVREVIPFPRTPRNAAF 466
Cdd:PTZ00425 559 ERLIMLVTGVDNIKDTIPFPRYPGHAEF 586
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
115-462 |
1.69e-154 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 441.23 E-value: 1.69e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 115 RHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGagemfrvstldynnlprddkGE 194
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG--------------------GA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 195 VDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFA-SLDDVAGLAEKMLKFA 273
Cdd:cd00776 61 ELFKVSYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 274 FKAALEERRDDLEFFAQrvdkdvINRLESFVNSDFAQVDYTDAIKILETCGQkfENPVYWGVDMSSEHERYLAEQHFKAP 353
Cdd:cd00776 141 FKRVLERCAKELELVNQ------LNRELLKPLEPFPRITYDEAIELLREKGV--EEEVKWGEDLSTEHERLLGEIVKGDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 354 VVVKNYPKDIKAFYMRLNED-GKTVAAMDVLAPGIGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHS 432
Cdd:cd00776 213 VFVTDYPKEIKPFYMKPDDDnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHG 292
|
330 340 350
....*....|....*....|....*....|
gi 739086825 433 GFGLGFERLVAYVTGVGNVREVIPFPRTPR 462
Cdd:cd00776 293 GFGLGLERLVMWLLGLDNIREAILFPRDPK 322
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
18-460 |
3.10e-146 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 431.60 E-value: 3.10e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 18 TEVTVQGWVRTRRdsnaGFSFLAVYDGSCFNPLQAIINNNLPNYNDEvlhLTTGCSVEVTGTVKE-SPGQGQ-SFELEAT 95
Cdd:PLN02532 121 TEIAIQKSAPPPP----SVAYLLISDGSCVASLQVVVDSALAPLTQL---MATGTCILAEGVLKLpLPAQGKhVIELEVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 96 AVKVVGWVeDPDTYPMAAKRHSVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGE 175
Cdd:PLN02532 194 KILHIGTV-DPEKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 176 MFRVSTL------DYNNLPRDDKG-------------------------------------------------------- 193
Cdd:PLN02532 273 MFRVTTLlgksddKEEKKPVHETEgisleavkaaikektnlveelkrsesnrealvaaeqdlrktnqlasqleakeklkt 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 194 -------EVDFSEDFFGREAFLTVSGQLNGEAYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFASLDDVAGLA 266
Cdd:PLN02532 353 gtsvkadKLSFSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 267 EKMLKFAFKAALEERRDDLEFFAQRVDKDVINRLESFVNSDFAQVDYTDAIKIL-ETCGQKFENPVYWGVDMSSEHERYL 345
Cdd:PLN02532 433 EDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLkQATDKKFETKPEWGIALTTEHLSYL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 346 AEQHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRR 425
Cdd:PLN02532 513 ADEIYKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRR 592
|
490 500 510
....*....|....*....|....*....|....*
gi 739086825 426 YGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRT 460
Cdd:PLN02532 593 HGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
16-459 |
1.31e-81 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 258.97 E-value: 1.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDSnAGFSFLAVYDGSCFnpLQAII-NNNLPNYNDEVLHLTTGCSVEVTGTVKESPGQGQSFELEA 94
Cdd:PRK05159 15 DGEEVTLAGWVHEIRDL-GGIAFLILRDRSGI--IQVVVkKKVDEELFETIKKLKRESVVSVTGTVKANPKAPGGVEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 95 TAVKVVGWVEDP---DTYPMaaKRHSVEFLREAAHL---RPRTNligAVARVRHTLAQAIHRFFDEQGYFWVSTPVITAS 168
Cdd:PRK05159 92 EEIEVLNKAEEPlplDISGK--VLAELDTRLDNRFLdlrRPRVR---AIFKIRSEVLRAFREFLYENGFTEIFTPKIVAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 169 DTEGAGEMFRVstldynnlprddkgevdfseDFFGREAFLTVSGQLngeaY-----ATAISKVYTFGPTFRAENSNTSRH 243
Cdd:PRK05159 167 GTEGGAELFPI--------------------DYFEKEAYLAQSPQL----YkqmmvGAGFERVFEIGPVFRAEEHNTSRH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 244 LAEFWMVEPEVAFASLD-DVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKdvinrlesfVNSDFAQVDYTDAIKILET 322
Cdd:PRK05159 223 LNEYTSIDVEMGFIDDHeDVMDLLENLLRYMYEDVAENCEKELELLGIELPV---------PETPIPRITYDEAIEILKS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 323 CGQKFEnpvyWGVDMSSEHER----YLAEQHFKAPVVVKNYPKDIKAFY-MRLNEDGKTVAAMDVLAPGIgEIIGGSQRE 397
Cdd:PRK05159 294 KGNEIS----WGDDLDTEGERllgeYVKEEYGSDFYFITDYPSEKRPFYtMPDEDDPEISKSFDLLFRGL-EITSGGQRI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739086825 398 ERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPR 459
Cdd:PRK05159 369 HRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
117-461 |
1.39e-78 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 247.09 E-value: 1.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 117 SVEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGEMFRVSTLDYNnlprddkgevd 196
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALG----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 197 fseDFFgreaFLTVSGQLNGEAYATA-ISKVYTFGPTFRAENSNTSRHLaEFWMVEPEVAFASLDDVAGLAEKMLKFAFK 275
Cdd:pfam00152 70 ---KFY----ALPQSPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 276 AALEERRDDLEFFAQRVDKDvinrlesfvnsdFAQVDYTDAIKILetcgqKFENPVYWGVDMSSEHERYLAEQHFK---- 351
Cdd:pfam00152 142 EVEGIAKELEGGTLLDLKKP------------FPRITYAEAIEKL-----NGKDVEELGYGSDKPDLRFLLELVIDknkf 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 352 APVVVKNYPKDIKAFYMRLNEDGKTVA-AMDVLAPGIgEIIGGSQREERLDMLDARLEEMGMNKED----YWWYRDLRRY 426
Cdd:pfam00152 205 NPLWVTDFPAEHHPFTMPKDEDDPALAeAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEEaeekFGFYLDALKY 283
|
330 340 350
....*....|....*....|....*....|....*
gi 739086825 427 GTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTP 461
Cdd:pfam00152 284 GAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
137-461 |
7.40e-61 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 201.79 E-value: 7.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 137 VARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGemfrvstldynnlPRDDKGEVDFSEDFFGREAFLTVSGQLNG 216
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMG-------------LGSDLPVKQISIDFYGVEYYLADSMILHK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 217 EAYATAISKVYTFGPTFRAEN--SNTSRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVdk 294
Cdd:PRK06462 96 QLALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDL-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 295 dvinrleSFVNSDFAQVDYTDAIKILETCGqKFENPVYwgvDMSSEHERYLAEqHFKAPVVVKNYPKDIKAFYMRLNEDG 374
Cdd:PRK06462 174 -------PHLKRPFKRITHKEAVEILNEEG-CRGIDLE---ELGSEGEKSLSE-HFEEPFWIIDIPKGSREFYDREDPER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 375 KTVA-AMDVLAP-GIGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVR 452
Cdd:PRK06462 242 PGVLrNYDLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIR 321
|
....*....
gi 739086825 453 EVIPFPRTP 461
Cdd:PRK06462 322 EVQPFPRVP 330
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
17-462 |
3.47e-54 |
|
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273087 [Multi-domain] Cd Length: 428 Bit Score: 186.95 E-value: 3.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 17 GTEVTVQGWVRTRRDSnAGFSFLAVYDGSCFNPLQAIINNNLPNYNDEVLHLTTGCSVEVTGTVKESPGQGQSFELEATA 96
Cdd:TIGR00458 12 GQEVTFMGWVHEIRDL-GGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEKAPGGFEIIPTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 97 VKVVGwvEDPDTYPMAAKRHS---VEFLREAAHLRPRTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGA 173
Cdd:TIGR00458 91 IEVIN--EAKEPLPLDPTEKVpaeLDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 174 GEMFRVStldynnlprddkgevdfsedFFGREAFLTVSGQLNGEAY-ATAISKVYTFGPTFRAENSNTSRHLAEFWMVEP 252
Cdd:TIGR00458 169 TELFPIT--------------------YFEREAFLGQSPQLYKQQLmAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 253 EVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDvinrlesfvNSDFAQVDYTDAIKILETCGQkfenPVY 332
Cdd:TIGR00458 229 EMAFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKP---------EGKFVRLTYDEAIEMANAKGV----EIG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 333 WGVDMSSEHERYLAEQhFKAPVVVKNYPKDIKAFY-MRLNEDGKTVAAMDVLAPGIgEIIGGSQREERLDMLDARLEEMG 411
Cdd:TIGR00458 296 WGEDLSTEAEKALGEE-MDGLYFITDWPTEIRPFYtMPDEDNPEISKSFDLMYRDL-EISSGAQRIHLHDLLVERIKAKG 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739086825 412 MNKEDYWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRTPR 462
Cdd:TIGR00458 374 LNPEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRK 424
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
19-102 |
1.29e-35 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 126.91 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 19 EVTVQGWVRTRRDSNAgFSFLAVYDGSCFNPLQAIINNNLPNYnDEVLHLTTGCSVEVTGTVKESPGQGQSFELEATAVK 98
Cdd:cd04318 1 EVTVNGWVRSVRDSKK-ISFIELNDGSCLKNLQVVVDKELTNF-KEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIE 78
|
....
gi 739086825 99 VVGW 102
Cdd:cd04318 79 VLGE 82
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
139-462 |
1.86e-33 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 127.21 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 139 RVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGEMFRVStldYNNLprddkgevdfsedffGREAFLTVSGQLNGEA 218
Cdd:cd00669 2 KVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVK---YNAL---------------GLDYYLRISPQLFKKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 219 Y-ATAISKVYTFGPTFRAEnSNTSRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALEERRDDLEFFAQRVDKDvi 297
Cdd:cd00669 64 LmVGGLDRVFEINRNFRNE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGLP-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 298 nrlesfvnsdFAQVDYTDAIKILetcgqkfeNPVYWGVDMSSEHERYLAEQHFKAPVVVKNYPKDIKAFymrlnedgktv 377
Cdd:cd00669 141 ----------FPRLTYREALERY--------GQPLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGV----------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 378 aamdvlapgigEIIGGSQREERLDMLDARLEEMGMNKED----YWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVRE 453
Cdd:cd00669 192 -----------EVGNGSSRLHDPDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIRE 260
|
....*....
gi 739086825 454 VIPFPRTPR 462
Cdd:cd00669 261 VIAFPKMRR 269
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
130-462 |
8.66e-31 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 124.82 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 130 RTNLIGAVARVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGEMFRvstLDYnnlprddkgevdfsedfFGREAFLT 209
Cdd:PLN02850 217 RTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFR---LDY-----------------KGQPACLA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 210 VSGQLNGE-AYATAISKVYTFGPTFRAENSNTSRHLAEFWMVEPEVAFAS-LDDVAGLAEKMLKFAFKAaLEER-RDDLE 286
Cdd:PLN02850 277 QSPQLHKQmAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDG-LNERcKKELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 287 FFAQRVDKDVINRLESFVNSDFAQvdytdAIKILETCGQKFENpvyWGvDMSSEHERYLAEqhfkapvVVKN-------- 358
Cdd:PLN02850 356 AIREQYPFEPLKYLPKTLRLTFAE-----GIQMLKEAGVEVDP---LG-DLNTESERKLGQ-------LVKEkygtdfyi 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 359 ---YPKDIKAFY-MRLNEDGKTVAAMDVLAPGiGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGF 434
Cdd:PLN02850 420 lhrYPLAVRPFYtMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGF 498
|
330 340
....*....|....*....|....*...
gi 739086825 435 GLGFERLVAYVTGVGNVREVIPFPRTPR 462
Cdd:PLN02850 499 GVGLERVVMLFCGLNNIRKTSLFPRDPQ 526
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
7-462 |
7.95e-28 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 116.25 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 7 VDVLQGRVAVGTEVTVQGWVRTRRdSNAGFSFLAVYDGScfNPLQAI--INNNLPN-YNDEVLHLTTGCSVEVTGTV--K 81
Cdd:PTZ00401 68 VAVLSKPELVDKTVLIRARVSTTR-KKGKMAFMVLRDGS--DSVQAMaaVEGDVPKeMIDFIGQIPTESIVDVEATVckV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 82 ESP---GQGQSFELEATAVKVVgwVEDPDTYPM----AAKRHSVEFLR-------EAAHLRPRTNLIGAVARVRHTLAQA 147
Cdd:PTZ00401 145 EQPitsTSHSDIELKVKKIHTV--TESLRTLPFtledASRKESDEGAKvnfdtrlNSRWMDLRTPASGAIFRLQSRVCQY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 148 IHRFFDEQGYFWVSTPVITASDTEGAGEMFRVstldynnlprddkgevdfseDFFGREAFLTVSGQLNGE-AYATAISKV 226
Cdd:PTZ00401 223 FRQFLIDSDFCEIHSPKIINAPSEGGANVFKL--------------------EYFNRFAYLAQSPQLYKQmVLQGDVPRV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 227 YTFGPTFRAENSNTSRHLAEFWMVEPEVAF-ASLDDVAGLAEKMLKFAFK------AALEE--RRDDLEFFAQRVDKDVI 297
Cdd:PTZ00401 283 FEVGPVFRSENSNTHRHLTEFVGLDVEMRInEHYYEVLDLAESLFNYIFErlathtKELKAvcQQYPFEPLVWKLTPERM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 298 NRL------ESFVNSDFAQ------------VDYTDAIKILETCGQKFENPVYwgvDMSSEHERYLA----EQHFKAPVV 355
Cdd:PTZ00401 363 KELgvgvisEGVEPTDKYQarvhnmdsrmlrINYMHCIELLNTVLEEKMAPTD---DINTTNEKLLGklvkERYGTDFFI 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 356 VKNYPKDIKAFY-MRLNEDGKTVAAMDVLAPGiGEIIGGSQREERLDMLDARLEEMGMNKEDYWWYRDLRRYGTVPHSGF 434
Cdd:PTZ00401 440 SDRFPSSARPFYtMECKDDERFTNSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGF 518
|
490 500
....*....|....*....|....*...
gi 739086825 435 GLGFERLVAYVTGVGNVREVIPFPRTPR 462
Cdd:PTZ00401 519 GVGLERVVMLYLGLSNVRLASLFPRDPQ 546
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
19-101 |
8.31e-18 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 77.99 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 19 EVTVQGWVRTRRDSNaGFSFLAVYDGScfNPLQAIIN-NNLPNYNDEVLHLTTGCSVEVTGTVKESPG---QGQSFELEA 94
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGS--GIVQVVVNkEELGEFFEEAEKLRTESVVGVTGTVVKRPEgnlATGEIELQA 77
|
....*..
gi 739086825 95 TAVKVVG 101
Cdd:cd04100 78 EELEVLS 84
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
16-460 |
5.11e-15 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 77.52 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDsNAGFSFLAVYDGSCFnpLQAIIN-NNLPNYNDEVLHLTTGCSVEVTGTVKESPGQGQ------ 88
Cdd:PLN02903 71 VGSRVTLCGWVDLHRD-MGGLTFLDVRDHTGI--VQVVTLpDEFPEAHRTANRLRNEYVVAVEGTVRSRPQESPnkkmkt 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 89 -SFELEATAVKVVGWVEDPDTYPMAAKRHSVEFLREAAHLRPR----------TNLigavaRVRHTLAQAIHRFF-DEQG 156
Cdd:PLN02903 148 gSVEVVAESVDILNVVTKSLPFLVTTADEQKDSIKEEVRLRYRvldlrrpqmnANL-----RLRHRVVKLIRRYLeDVHG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 157 YFWVSTPVITASDTEGAGEMF---RVSTLDYNNLPRddkgevdfSEDFFgrEAFLTVSGqlngeayataISKVYTFGPTF 233
Cdd:PLN02903 223 FVEIETPILSRSTPEGARDYLvpsRVQPGTFYALPQ--------SPQLF--KQMLMVSG----------FDRYYQIARCF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 234 RAENSNTSRHlAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALE------------------------ERRDDLEF-- 287
Cdd:PLN02903 283 RDEDLRADRQ-PEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKGvqlpnpfprltyaeamskygsdkpDLRYGLELvd 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 288 ------------FAQRVDK------------------------DVINR--------LESFVNSDFAQVDYTDAIK----- 318
Cdd:PLN02903 362 vsdvfaessfkvFAGALESggvvkaicvpdgkkisnntalkkgDIYNEaiksgakgLAFLKVLDDGELEGIKALVeslsp 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 319 -----ILETCG-----------------------------------QKFENPVYWGVDM-----SSEHERYLAEQH-FKA 352
Cdd:PLN02903 442 eqaeqLLAACGagpgdlilfaagptssvnktldrlrqfiaktldliDPSRHSILWVTDFpmfewNEDEQRLEALHHpFTA 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 353 PVvvknyPKDIKAFymrlneDGKTVAAMDVLAPGIgEIIGGSQREERLDMLDARLEEMGMNKED----YWWYRDLRRYGT 428
Cdd:PLN02903 522 PN-----PEDMGDL------SSARALAYDMVYNGV-EIGGGSLRIYRRDVQQKVLEAIGLSPEEaeskFGYLLEALDMGA 589
|
570 580 590
....*....|....*....|....*....|..
gi 739086825 429 VPHSGFGLGFERLVAYVTGVGNVREVIPFPRT 460
Cdd:PLN02903 590 PPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKT 621
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
139-458 |
2.12e-14 |
|
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238398 [Multi-domain] Cd Length: 329 Bit Score: 74.16 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 139 RVRHTLAQAIHRFFDEQGYFWVSTPvITASDTEGAgeMFRVSTLDYNNLPRDdkgevdfsedFFGREA------FLTVSG 212
Cdd:cd00775 9 IVRSKIISYIRKFLDDRGFLEVETP-MLQPIAGGA--AARPFITHHNALDMD----------LYLRIApelylkRLIVGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 213 qlngeayataISKVYTFGPTFRAENSNTsRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAAL-------EERRDDL 285
Cdd:cd00775 76 ----------FERVYEIGRNFRNEGIDL-THNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINgktkieyGGKELDF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 286 EFFAQRVDkdVINRLESFVNSDF---AQVDYTDAIKILE-TCGQKFENPVYWGVDMSSEHERYLaEQHFKAPVVVKNYPK 361
Cdd:cd00775 145 TPPFKRVT--MVDALKEKTGIDFpelDLEQPEELAKLLAkLIKEKIEKPRTLGKLLDKLFEEFV-EPTLIQPTFIIDHPV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 362 DIKAFYMRLNEDgktvaamdvlaPGIGE----IIGGS--------------QRE---ERLDMLDARLEEMGMNKEDYwwy 420
Cdd:cd00775 222 EISPLAKRHRSN-----------PGLTErfelFICGKeianaytelndpfdQRErfeEQAKQKEAGDDEAMMMDEDF--- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 739086825 421 rdLR--RYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFP 458
Cdd:cd00775 288 --VTalEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
19-102 |
5.63e-14 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239818 [Multi-domain] Cd Length: 84 Bit Score: 67.26 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 19 EVTVQGWVRTRRDSNaGFSFLAVYDGSCFnpLQAIINNNLPNYNDEVLHLTTGCSVEVTGTVKESPGQGQS---FELEAT 95
Cdd:cd04323 1 RVKVFGWVHRLRSQK-KLMFLVLRDGTGF--LQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAKQApggYELQVD 77
|
....*..
gi 739086825 96 AVKVVGW 102
Cdd:cd04323 78 YLEIIGE 84
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
20-100 |
3.40e-10 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 56.09 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 20 VTVQGWVRTRRDSNAGFSFLAVYDGScfNPLQAIINNnlPNYNDEVLHLTTGCSVEVTGTVKESPGQGqsFELEATAVKV 99
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGT--GSIQVVVFK--EEAEKLAKKLKEGDVVRVTGKVKKRKGGE--LELVVEEIEL 74
|
.
gi 739086825 100 V 100
Cdd:pfam01336 75 L 75
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
137-458 |
4.83e-10 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 61.64 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 137 VARVRHTLAQAIHRFFDEQGYFWVSTPV-------------IT---ASDTEgageMF-RVSTLDYnnLPRddkgevdfse 199
Cdd:PRK00484 171 TFRKRSKIISAIRRFLDNRGFLEVETPMlqpiaggaaarpfIThhnALDID----LYlRIAPELY--LKR---------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 200 dffgreafLTVSGqlngeayataISKVYTFGPTFRAENSNTsRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAAL- 278
Cdd:PRK00484 235 --------LIVGG----------FERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLg 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 279 ------EERRDDL--EFfaQRVD-KDVINRlesFVNSDFAQVDYTDAIKILETCGQKFENPVYWG--VDMSSEHeryLAE 347
Cdd:PRK00484 296 ttkvtyQGTEIDFgpPF--KRLTmVDAIKE---YTGVDFDDMTDEEARALAKELGIEVEKSWGLGklINELFEE---FVE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 348 QHFKAPVVVKNYPKDIKAFYMRLNEDgktvaamdvlaPGIGE----IIGGS--------------QREERLDMLDAR--- 406
Cdd:PRK00484 368 PKLIQPTFITDYPVEISPLAKRHRED-----------PGLTErfelFIGGReianafselndpidQRERFEAQVEAKeag 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 739086825 407 -LEEMGMNkEDYwwyrdLR--RYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFP 458
Cdd:PRK00484 437 dDEAMFMD-EDF-----LRalEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
16-460 |
1.88e-09 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 59.70 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDsNAGFSFLAVYD--GSCfnplQAIINNNLPNYnDEVLHLTTGCSVEVTGTVKE-SPGQ------ 86
Cdd:PRK00476 16 VGQTVTLCGWVHRRRD-HGGLIFIDLRDreGIV----QVVFDPDAEAF-EVAESLRSEYVIQVTGTVRArPEGTvnpnlp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 87 -GQsFELEATAVKVVGWVEDPdTYPMAAKRHSVEFLReaahL--------RPR--TNLIgavarVRHTLAQAIHRFFDEQ 155
Cdd:PRK00476 90 tGE-IEVLASELEVLNKSKTL-PFPIDDEEDVSEELR----LkyryldlrRPEmqKNLK-----LRSKVTSAIRNFLDDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 156 GYFWVSTPVITASDTEGAgemfRvstlDYnnL-P-RDDKGEvdfsedFFgreA-------F---LTVSGqlngeayataI 223
Cdd:PRK00476 159 GFLEIETPILTKSTPEGA----R----DY--LvPsRVHPGK------FY---AlpqspqlFkqlLMVAG----------F 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 224 SKVYTFGPTFRAENSNTSRhLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAALE----------------ER------ 281
Cdd:PRK00476 210 DRYYQIARCFRDEDLRADR-QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGvdlptpfprmtyaeamRRygsdkp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 282 --RDDLEF--------------FAQRVDKD------------------VINRLESFVNSD------FAQVD--------- 312
Cdd:PRK00476 289 dlRFGLELvdvtdlfkdsgfkvFAGAANDGgrvkairvpggaaqlsrkQIDELTEFAKIYgakglaYIKVNedglkgpia 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 313 --YTDAI--KILETCGQK--------------------------------FENPVY---WGVD-----MSSEHERYLAEQ 348
Cdd:PRK00476 369 kfLSEEElaALLERTGAKdgdliffgadkakvvndalgalrlklgkelglIDEDKFaflWVVDfpmfeYDEEEGRWVAAH 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 349 H-FKAPvvvknypKDIKAFYMRLNEDGKTVA-AMDVLAPGIgEIIGGSQREERLDMLDARLEEMGMNKEDYwwyRD---- 422
Cdd:PRK00476 449 HpFTMP-------KDEDLDELETTDPGKARAyAYDLVLNGY-ELGGGSIRIHRPEIQEKVFEILGISEEEA---EEkfgf 517
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 739086825 423 -LR--RYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRT 460
Cdd:PRK00476 518 lLDalKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKT 558
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
139-458 |
9.25e-08 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 54.30 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 139 RVRHTLAQAIHRFFDEQGYFWVSTPVITASDtegAGEMFRVSTLDYNNLPRDDKGEVDfSEDFFGReafLTVSGqlngea 218
Cdd:PRK12445 185 VVRSKILAAIRQFMVARGFMEVETPMMQVIP---GGASARPFITHHNALDLDMYLRIA-PELYLKR---LVVGG------ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 219 yataISKVYTFGPTFRAENSNTsRHLAEFWMVEPEVAFASLDDVAGLAEKMLKFAFKAAL--------EERRDDLEFFAQ 290
Cdd:PRK12445 252 ----FERVFEINRNFRNEGISV-RHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLgttkvtygEHVFDFGKPFEK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 291 RVDKDVINRLESfvNSDFAQVDYTDAIKIL-ETCGQKFENPvyWGVD-MSSEHERYLAEQHFKAPVVVKNYPKDIKAFYM 368
Cdd:PRK12445 327 LTMREAIKKYRP--ETDMADLDNFDAAKALaESIGITVEKS--WGLGrIVTEIFDEVAEAHLIQPTFITEYPAEVSPLAR 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 369 RLNEDGKTVAAMDV------LAPGIGEIIGGSQREERL-DMLDARL---EEMGMNKEDYwwyRDLRRYGTVPHSGFGLGF 438
Cdd:PRK12445 403 RNDVNPEITDRFEFfiggreIGNGFSELNDAEDQAERFqEQVNAKAagdDEAMFYDEDY---VTALEYGLPPTAGLGIGI 479
|
330 340
....*....|....*....|
gi 739086825 439 ERLVAYVTGVGNVREVIPFP 458
Cdd:PRK12445 480 DRMIMLFTNSHTIRDVILFP 499
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
389-460 |
1.01e-07 |
|
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439943 [Multi-domain] Cd Length: 589 Bit Score: 54.23 E-value: 1.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739086825 389 EIIGGSQREERLDMLDARLEEMGMNKEDYwwyRD-----LR--RYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFPRT 460
Cdd:COG0173 482 ELGGGSIRIHDPELQEKVFELLGISEEEA---EEkfgflLEafKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKT 557
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
146-257 |
2.81e-06 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 48.27 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 146 QAIHRFFDEQGYFWVSTPVIT-ASDTEGAGEMFRVStldynnlprdDKGEVDFSEDFFGREAFLTVSGQLNGEAYATAIS 224
Cdd:cd00768 7 QKLRRFMAELGFQEVETPIVErEPLLEKAGHEPKDL----------LPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPL 76
|
90 100 110
....*....|....*....|....*....|....
gi 739086825 225 KVYTFGPTFRAENSNTS-RHLAEFWMVEPEVAFA 257
Cdd:cd00768 77 RLAEIGPAFRNEGGRRGlRRVREFTQLEGEVFGE 110
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
16-99 |
6.41e-06 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 45.59 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 16 VGTEVTVQGWVRTRRDsNAGFSFLAVYDGSCFnpLQAIINNNLPNYNDEVLHLTTGCSVEVTGTVKESPgQGQS------ 89
Cdd:cd04317 13 VGQEVTLCGWVQRRRD-HGGLIFIDLRDRYGI--VQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARP-EGTVnpklpt 88
|
90
....*....|..
gi 739086825 90 --FELEATAVKV 99
Cdd:cd04317 89 geIEVVASELEV 100
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
139-276 |
2.18e-04 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 43.87 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 139 RVRHTLAQAIHRFFDEQGYFWVSTPVItASDTEGAGEMFRVSTLDYNNLprddkgevdfsedffgrEAFLTVSGQLN-GE 217
Cdd:PTZ00385 234 KKRHVMLQALRDYFNERNFVEVETPVL-HTVASGANAKSFVTHHNANAM-----------------DLFLRVAPELHlKQ 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 218 AYATAISKVYTFGPTFRAENSNTSrHLAEFWMVEPEVAFASLDDVAGLAEKM-LKFAFKA 276
Cdd:PTZ00385 296 CIVGGMERIYEIGKVFRNEDADRS-HNPEFTSCEFYAAYHTYEDLMPMTEDIfRQLAMRV 354
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
379-465 |
3.28e-04 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 43.05 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 379 AMDVLAPGiGEIIGGSQREERLDMLDARLEEMGMNKED----YWWYRDLRRYGTVPHSGFGLGFERLVAYVTGVGNVREV 454
Cdd:PRK12820 490 AYDLVVNG-EELGGGSIRINDKDIQLRIFAALGLSEEDiedkFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREV 568
|
90
....*....|.
gi 739086825 455 IPFPRTpRNAA 465
Cdd:PRK12820 569 IAFPKN-RSAA 578
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
19-127 |
4.90e-04 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 39.43 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 19 EVTVQGWVRTRRDSNAGfSFLAVYDGSCFnpLQAIINNNL-PNYNDEVLHLTTGCSVEVTGTVKESPGQGQSFELEATAV 97
Cdd:cd04319 1 KVTLAGWVYRKREVGKK-AFIVLRDSTGI--VQAVFSKDLnEEAYREAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKL 77
|
90 100 110
....*....|....*....|....*....|
gi 739086825 98 KVVGWVEDpdtYPMaAKRHSVEFLREAAHL 127
Cdd:cd04319 78 EIIQNVEF---FPI-TEDASDEFLLDVRHL 103
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
139-458 |
8.91e-04 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 41.51 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 139 RVRHTLAQAIHRFFDEQGYFWVSTPVITASDTEGAGEMFRVstldYNNlprddkgevDFSEDFFGR---EAFL---TVSG 212
Cdd:PLN02502 230 RTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVT----HHN---------DLNMDLYLRiatELHLkrlVVGG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 213 qlngeayataISKVYTFGPTFRAENSNTsRHLAEFWMVEPEVAFASLDDVAGLAEKML-------KFAFKAALEERRDDL 285
Cdd:PLN02502 297 ----------FERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYADYNDMMELTEEMVsgmvkelTGSYKIKYHGIEIDF 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 286 EFFAQRVDkdVINRLESFVNSDFAQVDYTDA-----IKILETCGQKFENPVYWG--VDMSSEHeryLAEQHFKAPVVVKN 358
Cdd:PLN02502 366 TPPFRRIS--MISLVEEATGIDFPADLKSDEanaylIAACEKFDVKCPPPQTTGrlLNELFEE---FLEETLVQPTFVLD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 359 YPKDIK--AFYMRLNedgktvaamdvlaPGIGE----IIGG--------------SQREERLDMLDAR----LEEMGMnk 414
Cdd:PLN02502 441 HPVEMSplAKPHRSK-------------PGLTErfelFINGrelanafseltdpvDQRERFEEQVKQHnagdDEAMAL-- 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 739086825 415 eDYWWYRDLRrYGTVPHSGFGLGFERLVAYVTGVGNVREVIPFP 458
Cdd:PLN02502 506 -DEDFCTALE-YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
17-106 |
2.07e-03 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 37.68 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739086825 17 GTEVTVQGWVRTRRDSnAGFSFLAVYDGSCFnpLQAIINNNLPnyNDEVLHLTTGCSVE----VTGTVKESPGQGQSFEL 92
Cdd:cd04316 12 GEEVTVAGWVHEIRDL-GGIKFVILRDREGI--VQVTAPKKKV--DKELFKTVRKLSREsvisVTGTVKAEPKAPNGVEI 86
|
90
....*....|....
gi 739086825 93 EATAVKVVGWVEDP 106
Cdd:cd04316 87 IPEEIEVLSEAKTP 100
|
|
| |
