|
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: 902.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 1 MSVVPVADVLQGRVaVDSEVTVRGWVRTRRDSKaGISFLAVYDGSCFDPVQAVINNSlPNYNEDVLRLTTGCSVIVTGKV 80
Cdd:PRK03932 1 MMRVSIKDILKGKY-VGQEVTVRGWVRTKRDSG-KIAFLQLRDGSCFKQLQVVKDNG-EEYFEEIKKLTTGSSVIVTGTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 81 VASPGQGQQFEIQASKVEVAGWveDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWV 160
Cdd:PRK03932 78 VESPRAGQGYELQATKIEVIGE--DPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 161 STPLITASDTEGAGEMFRVSTLDLenlprndqgkvDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNT 240
Cdd:PRK03932 156 DTPIITASDCEGAGELFRVTTLDL-----------DFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 241 SRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAVTIL 320
Cdd:PRK03932 225 RRHLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 321 ENCGKKFENPVYWGVDLSSEHERYLAEEHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERL 400
Cdd:PRK03932 305 QKSGKKFEFPVEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1882436903 401 DVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNASF 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: 813.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 3 VVPVADVLQG-RVAVDSEVTVRGWVRTRRdSKAGISFLAVYDGSCFDPVQAVINNSLPNY-NEDVLRLTTGCSVIVTGKV 80
Cdd:TIGR00457 1 SAAIKDLLQQvYKFVGDEVTVSGWVRTKR-SSKKIIFLELNDGSSLGPIQAVINGEDNPYlFQLLKSLTTGSSVSVTGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 81 VASPGQGQQFEIQASKVEVAGWVEdPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWV 160
Cdd:TIGR00457 80 VESPGKGQPVELQVKKIEVVGEAE-PDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 161 STPLITASDTEGAGEMFRVSTldlenlprndqGKVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNT 240
Cdd:TIGR00457 159 SPPILTSNDCEGAGELFRVST-----------GNIDFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 241 SRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAVTIL 320
Cdd:TIGR00457 228 SRHLSEFWMIEPEMAFANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEIL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 321 ENCGKKFENPVYWGVDLSSEHERYLAEEHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERL 400
Cdd:TIGR00457 308 KESDKNFEYEDFWGDDLQTEHERFLAEEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1882436903 401 DVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNASF 466
Cdd:TIGR00457 388 DKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-465 |
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: 748.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 4 VPVADVLQGrvAVDSEVTVRGWVRTRRDSKaGISFLAVYDGSCFdpVQAVI-NNSLPNYnEDVLRLTTGCSVIVTGKVVA 82
Cdd:COG0017 3 TYIKDLLPE--HVGQEVTVAGWVRTKRDSG-GISFLILRDGSGF--IQVVVkKDKLENF-EEAKKLTTESSVEVTGTVVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 83 SPGQGQQFEIQASKVEVAGWVEDPdtYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVST 162
Cdd:COG0017 77 SPRAPQGVELQAEEIEVLGEADEP--YPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 163 PLITASDTEGAGEMFRVstldlenlprndqgkvdfdkDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTSR 242
Cdd:COG0017 155 PIITASATEGGGELFPV--------------------DYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 243 HLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDkdavsRLERFIEADFAQVDYTDAVTILEN 322
Cdd:COG0017 215 HLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDVE-----RLEKVPESPFPRITYTEAIEILKK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 323 CGKKFEnpvyWGVDLSSEHERYLAEEHFKAPVVVKNYPKDIKAFYMRLN-EDGKTVAAMDVLAPGIGEIIGGSQREERLD 401
Cdd:COG0017 290 SGEKVE----WGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNpDDPKTVAAFDLLAPGIGEIIGGSQREHRYD 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1882436903 402 VLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNAS 465
Cdd:COG0017 366 VLVERIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLT 429
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
6-466 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 614.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 6 VADVL----QGRVAVDSEVTVRGWVRTRRdSKAGISFLAVYDGSCFDPVQAVINNSLPNYNE-DVLRLTTGCSVIVTGKV 80
Cdd:PLN02603 92 IADVKggedEGLARVGKTLNVMGWVRTLR-AQSSVTFIEVNDGSCLSNMQCVMTPDAEGYDQvESGLITTGASVLVQGTV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 81 VASPGQGQQFEIQASKVEVAGwVEDPdTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWV 160
Cdd:PLN02603 171 VSSQGGKQKVELKVSKIVVVG-KSDP-SYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 161 STPLITASDTEGAGEMFRVSTL----------DLENLPRNDQGKVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFG 230
Cdd:PLN02603 249 SSPIITASDCEGAGEQFCVTTLipnsaenggsLVDDIPKTKDGLIDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 231 PTFRAENSNTSRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQ 310
Cdd:PLN02603 329 PTFRAENSNTSRHLAEFWMIEPELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVEKNFVQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 311 VDYTDAVTILENCGKKFENPVYWGVDLSSEHERYLAEEHFKA-PVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGE 389
Cdd:PLN02603 409 LSYTDAIELLLKAKKKFEFPVKWGLDLQSEHERYITEEAFGGrPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVPRVGE 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1882436903 390 IIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNASF 466
Cdd:PLN02603 489 LIGGSQREERLEYLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSAEF 565
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
20-464 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 533.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 20 VTVRGWVRTRRDS-KAGISFLAVYDGSCFDPVQAVINNSLpnynEDVLRLT-TGCSVIVTGKVVASP---GQGQQFEIQA 94
Cdd:PLN02221 53 VRIGGWVKTGREQgKGTFAFLEVNDGSCPANLQVMVDSSL----YDLSTLVaTGTCVTVDGVLKVPPegkGTKQKIELSV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 95 SKVEVAGWVeDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAG 174
Cdd:PLN02221 129 EKVIDVGTV-DPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 175 EMFRVSTL--------------------DLE------------------------------------------------- 185
Cdd:PLN02221 208 EMFQVTTLinyterleqdlidnpppteaDVEaarlivkergevvaqlkaakaskeeitaavaelkiakeslahieerskl 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 186 --NLPRNDqGKVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAFANLNDIA 263
Cdd:PLN02221 288 kpGLPKKD-GKIDYSKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDM 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 264 GLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAVTILENC---GKKFENPVYWGVDLSSE 340
Cdd:PLN02221 367 NCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAvakGKEFDNNVEWGIDLASE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 341 HERYLAEEHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDVLDERMLEMGLNKEDYWWY 420
Cdd:PLN02221 447 HERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWY 526
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1882436903 421 RDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNA 464
Cdd:PLN02221 527 LDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKA 570
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
16-466 |
0e+00 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 525.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 16 VDSEVTVRGWVRTRRDSKAG-ISFLAVYDGSCFDPVQAVINNSLPNYnEDVLRLTTGCSVIVTGKVVASPGQGQ------ 88
Cdd:PTZ00425 80 IDQIITVCGWSKAVRKQGGGrFCFVNLNDGSCHLNLQIIVDQSIENY-EKLLKCGVGCCFRFTGKLIISPVQNEnkkgll 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 89 ----QFEIQASKV---EVAGWVEDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVS 161
Cdd:PTZ00425 159 kenvELALKDNSIhnfEIYGENLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIH 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 162 TPLITASDTEGAGEMFRVSTL-----DLENLPR-------------------NDQGK-------------------VDFD 198
Cdd:PTZ00425 239 TPLITTSDCEGGGEMFTVTTLlgedaDYRAIPRvnkknkkgekredilntcnANNNNgnssssnavsspaypdqylIDYK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 199 KDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVL 278
Cdd:PTZ00425 319 KDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 279 EERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAVTILENCGKKFENPVYWGVDLSSEHERYLAEEHFKAPVVVKN 358
Cdd:PTZ00425 399 NNNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 359 YPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGF 438
Cdd:PTZ00425 479 YPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGF 558
|
490 500
....*....|....*....|....*...
gi 1882436903 439 ERLIAYVTGVQNVRDVIPFPRTPRNASF 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 |
4.86e-158 |
|
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: 450.09 E-value: 4.86e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 115 RHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGagemfrvstldlenlprndqGK 194
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG--------------------GA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 195 VDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAFAN-LNDIAGLAEAMLKYV 273
Cdd:cd00776 61 ELFKVSYFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEdYNEVMDLIEELIKYI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 274 FKAVLEERADDMKFFaervdkDAVSRLERFIEADFAQVDYTDAVTILENCGKkfENPVYWGVDLSSEHERYLAEEHFKAP 353
Cdd:cd00776 141 FKRVLERCAKELELV------NQLNRELLKPLEPFPRITYDEAIELLREKGV--EEEVKWGEDLSTEHERLLGEIVKGDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 354 VVVKNYPKDIKAFYMRLNED-GKTVAAMDVLAPGIGEIIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHS 432
Cdd:cd00776 213 VFVTDYPKEIKPFYMKPDDDnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHG 292
|
330 340 350
....*....|....*....|....*....|
gi 1882436903 433 GFGLGFERLIAYVTGVQNVRDVIPFPRTPR 462
Cdd:cd00776 293 GFGLGLERLVMWLLGLDNIREAILFPRDPK 322
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
1-460 |
2.99e-149 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 439.31 E-value: 2.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 1 MSVVP----VADVLQG-----RVAVDSEVTVRGWVRTRRdskaGISFLAVYDGSCFDPVQAVINNSLPNYNEdvlRLTTG 71
Cdd:PLN02532 95 QSRVPifrsIAKVLSGggstyPVREKTEIAIQKSAPPPP----SVAYLLISDGSCVASLQVVVDSALAPLTQ---LMATG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 72 CSVIVTGKV-VASPGQGQQ-FEIQASKVEVAGWVeDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALH 149
Cdd:PLN02532 168 TCILAEGVLkLPLPAQGKHvIELEVEKILHIGTV-DPEKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATH 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 150 RFFNEQGFFWVSTPLITASDTEGAGEMFRVSTL---------------------------------DLENLPRNDQG--- 193
Cdd:PLN02532 247 TFFQDHGFLYVQVPIITTTDATGFGEMFRVTTLlgksddkeekkpvhetegisleavkaaikektnLVEELKRSESNrea 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 194 ---------------------------------KVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNT 240
Cdd:PLN02532 327 lvaaeqdlrktnqlasqleakeklktgtsvkadKLSFSKDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDS 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 241 SRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAV-TI 319
Cdd:PLN02532 407 ARHLAEMWMVEVEMAFSELEDAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVdLL 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 320 LENCGKKFENPVYWGVDLSSEHERYLAEEHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREER 399
Cdd:PLN02532 487 KQATDKKFETKPEWGIALTTEHLSYLADEIYKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITGSQNEER 566
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1882436903 400 LDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRT 460
Cdd:PLN02532 567 MDILNARIEELGLPREQYEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
18-459 |
3.06e-83 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 263.20 E-value: 3.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 18 SEVTVRGWVRTRRDSKaGISFLAVYDGSCFdpVQAVI-NNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASK 96
Cdd:PRK05159 17 EEVTLAGWVHEIRDLG-GIAFLILRDRSGI--IQVVVkKKVDEELFETIKKLKRESVVSVTGTVKANPKAPGGVEVIPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 97 VEVAGWVEDP---DTYPMaaKRHSIEYLREVAHL---RPRTNligAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDT 170
Cdd:PRK05159 94 IEVLNKAEEPlplDISGK--VLAELDTRLDNRFLdlrRPRVR---AIFKIRSEVLRAFREFLYENGFTEIFTPKIVASGT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 171 EGAGEMFRVstldlenlprndqgkvdfdkDFFGKESFLTVSGQLngetY-----ACALSKIYTFGPTFRAENSNTSRHLA 245
Cdd:PRK05159 169 EGGAELFPI--------------------DYFEKEAYLAQSPQL----YkqmmvGAGFERVFEIGPVFRAEEHNTSRHLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 246 EFWMLEPEVAFANL-NDIAGLAEAMLKYVFKAVLEERADDMkffaERVDKDavsrLERfIEADFAQVDYTDAVTILENCG 324
Cdd:PRK05159 225 EYTSIDVEMGFIDDhEDVMDLLENLLRYMYEDVAENCEKEL----ELLGIE----LPV-PETPIPRITYDEAIEILKSKG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 325 KKFEnpvyWGVDLSSEHER----YLAEEHFKAPVVVKNYPKDIKAFY-MRLNEDGKTVAAMDVLAPGIgEIIGGSQREER 399
Cdd:PRK05159 296 NEIS----WGDDLDTEGERllgeYVKEEYGSDFYFITDYPSEKRPFYtMPDEDDPEISKSFDLLFRGL-EITSGGQRIHR 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 400 LDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPR 459
Cdd:PRK05159 371 YDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
117-461 |
3.07e-78 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 246.32 E-value: 3.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 117 SIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVstldlenlPRNDQGKvd 196
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLV--------PSRALGK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 197 fdkdFFgkesFLTVSGQLNGETYACA-LSKIYTFGPTFRAENSNTSRHLaEFWMLEPEVAFANLNDIAGLAEAMLKYVFK 275
Cdd:pfam00152 71 ----FY----ALPQSPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIFK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 276 AVLEERADDMKFFAERVDKDavsrlerfieadFAQVDYTDAVTILencgkKFENPVYWGVDLSSEHERYLAE----EHFK 351
Cdd:pfam00152 142 EVEGIAKELEGGTLLDLKKP------------FPRITYAEAIEKL-----NGKDVEELGYGSDKPDLRFLLElvidKNKF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 352 APVVVKNYPKDIKAFYMRLNEDGKTVA-AMDVLAPGIgEIIGGSQREERLDVLDERMLEMGLNKED----YWWYRDLRRY 426
Cdd:pfam00152 205 NPLWVTDFPAEHHPFTMPKDEDDPALAeAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEEaeekFGFYLDALKY 283
|
330 340 350
....*....|....*....|....*....|....*
gi 1882436903 427 GTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTP 461
Cdd:pfam00152 284 GAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
137-461 |
3.10e-61 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 202.94 E-value: 3.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 137 VARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGemfrvstldlenlPRNDQGKVDFDKDFFGKESFLTVSGQLNG 216
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMG-------------LGSDLPVKQISIDFYGVEYYLADSMILHK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 217 ETYACALSKIYTFGPTFRAEN--SNTSRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFaERvdk 294
Cdd:PRK06462 96 QLALRMLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFF-GR--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 295 dAVSRLERfieaDFAQVDYTDAVTILENCGKKfENPVYwgvDLSSEHERYLaEEHFKAPVVVKNYPKDIKAFYMRLNEDG 374
Cdd:PRK06462 172 -DLPHLKR----PFKRITHKEAVEILNEEGCR-GIDLE---ELGSEGEKSL-SEHFEEPFWIIDIPKGSREFYDREDPER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 375 KTVA-AMDVLAP-GIGEIIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVR 452
Cdd:PRK06462 242 PGVLrNYDLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIR 321
|
....*....
gi 1882436903 453 DVIPFPRTP 461
Cdd:PRK06462 322 EVQPFPRVP 330
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
19-462 |
4.66e-56 |
|
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: 191.96 E-value: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDsKAGISFLAVYDGSCFDPVQAVINNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASKVE 98
Cdd:TIGR00458 14 EVTFMGWVHEIRD-LGGLIFVLLRDREGLIQITAPAKKVSKNLFKWAKKLNLESVVAVRGIVKIKEKAPGGFEIIPTKIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 99 VAGwvEDPDTYPMAAKRHS---IEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGE 175
Cdd:TIGR00458 93 VIN--EAKEPLPLDPTEKVpaeLDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASATEGGTE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 176 MFRVStldlenlprndqgkvdfdkdFFGKESFLTVSGQLNGETY-ACALSKIYTFGPTFRAENSNTSRHLAEFWMLEPEV 254
Cdd:TIGR00458 171 LFPIT--------------------YFEREAFLGQSPQLYKQQLmAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 255 AFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDavsrlerfiEADFAQVDYTDAVTILENCGKkfenPVYWG 334
Cdd:TIGR00458 231 AFEDHHDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKP---------EGKFVRLTYDEAIEMANAKGV----EIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 335 VDLSSEHERYLAEEhFKAPVVVKNYPKDIKAFY-MRLNEDGKTVAAMDVLAPGIgEIIGGSQREERLDVLDERMLEMGLN 413
Cdd:TIGR00458 298 EDLSTEAEKALGEE-MDGLYFITDWPTEIRPFYtMPDEDNPEISKSFDLMYRDL-EISSGAQRIHLHDLLVERIKAKGLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1882436903 414 KEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPR 462
Cdd:TIGR00458 376 PEGFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRK 424
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
19-102 |
4.38e-36 |
|
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: 128.07 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDSKAgISFLAVYDGSCFDPVQAVINNSLPNYnEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASKVE 98
Cdd:cd04318 1 EVTVNGWVRSVRDSKK-ISFIELNDGSCLKNLQVVVDKELTNF-KEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKIE 78
|
....
gi 1882436903 99 VAGW 102
Cdd:cd04318 79 VLGE 82
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
4-462 |
1.74e-35 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 138.30 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 4 VPVADVlqGRVAVDSEVTVRGWVRTRRdSKAGISFLAVYDgSCFDpVQAVINNSLPNYNEDVLRLTTGCS----VIVTGk 79
Cdd:PLN02850 70 TDVSDL--GEELAGSEVLIRGRVHTIR-GKGKSAFLVLRQ-SGFT-VQCVVFVSEVTVSKGMVKYAKQLSresvVDVEG- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 80 VVASP-----GQGQQFEIQASKV--------EVAGWVED---PDTYPMAAKRHSIEYLREVAHLRP-------RTNLIGA 136
Cdd:PLN02850 144 VVSVPkkpvkGTTQQVEIQVRKIycvskalaTLPFNVEDaarSESEIEKALQTGEQLVRVGQDTRLnnrvldlRTPANQA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 137 VARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVstldlenlprndqgkvdfdkDFFGKESFLTVSGQLNG 216
Cdd:PLN02850 224 IFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRL--------------------DYKGQPACLAQSPQLHK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 217 ETYACA-LSKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAF-ANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDK 294
Cdd:PLN02850 284 QMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIkEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 295 DAVSRLERFIEADFAQvdytdAVTILENCGKKFENpvyWGvDLSSEHERYLAE---EHFKAPV-VVKNYPKDIKAFY-MR 369
Cdd:PLN02850 364 EPLKYLPKTLRLTFAE-----GIQMLKEAGVEVDP---LG-DLNTESERKLGQlvkEKYGTDFyILHRYPLAVRPFYtMP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 370 LNEDGKTVAAMDVLAPGiGEIIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQ 449
Cdd:PLN02850 435 CPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLN 513
|
490
....*....|...
gi 1882436903 450 NVRDVIPFPRTPR 462
Cdd:PLN02850 514 NIRKTSLFPRDPQ 526
|
|
| 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 |
7.35e-34 |
|
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: 128.36 E-value: 7.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 139 RVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVSTLDLenlprndqgkvdfdkdffGKESFLTVSGQLNGET 218
Cdd:cd00669 2 KVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNAL------------------GLDYYLRISPQLFKKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 219 Y-ACALSKIYTFGPTFRAEnSNTSRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKdav 297
Cdd:cd00669 64 LmVGGLDRVFEINRNFRNE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFELEDFGL--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 298 srlerfieaDFAQVDYTDAVtilencgkkfenpvywgvdlssehERYLaeehfkAPVVVKNYPKDIKAFYMRLNEDGKTV 377
Cdd:cd00669 140 ---------PFPRLTYREAL------------------------ERYG------QPLFLTDYPAEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 378 A-AMDVLAPGIgEIIGGSQREERLDVLDERMLEMGLNKED----YWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVR 452
Cdd:cd00669 181 AdAFDLFINGV-EVGNGSSRLHDPDIQAEVFQEQGINKEAgmeyFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIR 259
|
330
....*....|
gi 1882436903 453 DVIPFPRTPR 462
Cdd:cd00669 260 EVIAFPKMRR 269
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
4-465 |
3.13e-28 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 117.40 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 4 VPVADVLQGRVaVDSEVTVRGWVRTRRdSKAGISFLAVYDGScfDPVQAV--INNSLPNYNEDVL-RLTTGCSVIVTGKV 80
Cdd:PTZ00401 66 IPVAVLSKPEL-VDKTVLIRARVSTTR-KKGKMAFMVLRDGS--DSVQAMaaVEGDVPKEMIDFIgQIPTESIVDVEATV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 81 --VASP---GQGQQFEIQASKVEVAgwVEDPDTYPM----AAKRHSIEYLR-------EVAHLRPRTNLIGAVARVRHTL 144
Cdd:PTZ00401 142 ckVEQPitsTSHSDIELKVKKIHTV--TESLRTLPFtledASRKESDEGAKvnfdtrlNSRWMDLRTPASGAIFRLQSRV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 145 AQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVstldlenlprndqgkvdfdkDFFGKESFLTVSGQLNGE-TYACAL 223
Cdd:PTZ00401 220 CQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKL--------------------EYFNRFAYLAQSPQLYKQmVLQGDV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 224 SKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAF-ANLNDIAGLAEAMLKYVF----------KAVLEE----------RA 282
Cdd:PTZ00401 280 PRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRInEHYYEVLDLAESLFNYIFerlathtkelKAVCQQypfeplvwklTP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 283 DDMKFFAERVDKDAVSRLERF------IEADFAQVDYTDAVTILENCGKKFENPVYwgvDLSSEHERYLA---EEHFKAP 353
Cdd:PTZ00401 360 ERMKELGVGVISEGVEPTDKYqarvhnMDSRMLRINYMHCIELLNTVLEEKMAPTD---DINTTNEKLLGklvKERYGTD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 354 VVVKN-YPKDIKAFY-MRLNEDGKTVAAMDVLAPGiGEIIGGSQREERLDVLDERMLEMGLNKEDYWWYRDLRRYGTVPH 431
Cdd:PTZ00401 437 FFISDrFPSSARPFYtMECKDDERFTNSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPH 515
|
490 500 510
....*....|....*....|....*....|....
gi 1882436903 432 SGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNAS 465
Cdd:PTZ00401 516 GGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTT 549
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
139-460 |
1.92e-25 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 105.35 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 139 RVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEmFRVSTldlenlpRNDQGKvdfdkdFFG--------KEsFLTV 210
Cdd:cd00777 2 RLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARD-FLVPS-------RLHPGK------FYAlpqspqlfKQ-LLMV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 211 SGqlngetyacaLSKIYTFGPTFRAENSNTSRHlAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERaddmkffae 290
Cdd:cd00777 67 SG----------FDRYFQIARCFRDEDLRADRQ-PEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVE--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 291 rvdkdavsrlerfIEADFAQVDYTDAvtiLENCGKKFenpvYWGVD-----LSSEHERYLAEEH-FKAPVvvknyPKDIK 364
Cdd:cd00777 127 -------------LTTPFPRMTYAEA---MERYGFKF----LWIVDfplfeWDEEEGRLVSAHHpFTAPK-----EEDLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 365 AFYmrlNEDGKTVA-AMDVLAPGIgEIIGGSQREERLDvLDERMLE-MGLNKEDYW-----WYRDLrRYGTVPHSGFGLG 437
Cdd:cd00777 182 LLE---KDPEDARAqAYDLVLNGV-ELGGGSIRIHDPD-IQEKVFEiLGLSEEEAEekfgfLLEAF-KYGAPPHGGIALG 255
|
330 340
....*....|....*....|...
gi 1882436903 438 FERLIAYVTGVQNVRDVIPFPRT 460
Cdd:cd00777 256 LDRLVMLLTGSESIRDVIAFPKT 278
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
19-99 |
7.62e-19 |
|
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: 80.69 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDSKaGISFLAVYDGScfDPVQAVIN-NSLPNYNEDVLRLTTGCSVIVTGKVVASPG---QGQQFEIQA 94
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGS--GIVQVVVNkEELGEFFEEAEKLRTESVVGVTGTVVKRPEgnlATGEIELQA 77
|
....*
gi 1882436903 95 SKVEV 99
Cdd:cd04100 78 EELEV 82
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
16-460 |
5.78e-16 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 80.60 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 16 VDSEVTVRGWVRTRRDsKAGISFLAVYDGSCFDPVqAVINNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQ------- 88
Cdd:PLN02903 71 VGSRVTLCGWVDLHRD-MGGLTFLDVRDHTGIVQV-VTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQESPnkkmktg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 89 QFEIQASKVEVAGWVEDPDTYPMAAKRHSIEYLREVAHLRPR----------TNLigavaRVRHTLAQALHRFFNE-QGF 157
Cdd:PLN02903 149 SVEVVAESVDILNVVTKSLPFLVTTADEQKDSIKEEVRLRYRvldlrrpqmnANL-----RLRHRVVKLIRRYLEDvHGF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 158 FWVSTPLITASDTEGAGEMF---RVSTLDLENLPRNDQgkvdfdkdFFgkESFLTVSGqlngetyacaLSKIYTFGPTFR 234
Cdd:PLN02903 224 VEIETPILSRSTPEGARDYLvpsRVQPGTFYALPQSPQ--------LF--KQMLMVSG----------FDRYYQIARCFR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 235 AENSNTSRHlAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVL---------------------EERAD---DMKF--- 287
Cdd:PLN02903 284 DEDLRADRQ-PEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKgvqlpnpfprltyaeamskygSDKPDlryGLELvdv 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 288 ---FAE---RVDKDAV--------------------SRLER---FIEA--------DFAQV----------------DYT 314
Cdd:PLN02903 363 sdvFAEssfKVFAGALesggvvkaicvpdgkkisnnTALKKgdiYNEAiksgakglAFLKVlddgelegikalveslSPE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 315 DAVTILENCG-----------------------------------KKFENPVYWGVDL-----SSEHERYLAEEH-FKAP 353
Cdd:PLN02903 443 QAEQLLAACGagpgdlilfaagptssvnktldrlrqfiaktldliDPSRHSILWVTDFpmfewNEDEQRLEALHHpFTAP 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 354 VvvknyPKDIKAFymrlneDGKTVAAMDVLAPGIgEIIGGSQREERLDVlDERMLE-MGLNKED----YWWYRDLRRYGT 428
Cdd:PLN02903 523 N-----PEDMGDL------SSARALAYDMVYNGV-EIGGGSLRIYRRDV-QQKVLEaIGLSPEEaeskFGYLLEALDMGA 589
|
570 580 590
....*....|....*....|....*....|..
gi 1882436903 429 VPHSGFGLGFERLIAYVTGVQNVRDVIPFPRT 460
Cdd:PLN02903 590 PPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKT 621
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
16-460 |
8.67e-15 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 76.64 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 16 VDSEVTVRGWVRTRRDsKAGISFLAVYDGSCFdpVQAVINNSLPNY-------NEDVLRlttgcsviVTGKVVASPgQGQ 88
Cdd:PRK00476 16 VGQTVTLCGWVHRRRD-HGGLIFIDLRDREGI--VQVVFDPDAEAFevaeslrSEYVIQ--------VTGTVRARP-EGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 89 --------QFEIQASKVEVAGWVEDPdTYPMAAKRHSIE-------YL---REvahlRPRTNLIgavarVRHTLAQALHR 150
Cdd:PRK00476 84 vnpnlptgEIEVLASELEVLNKSKTL-PFPIDDEEDVSEelrlkyrYLdlrRP----EMQKNLK-----LRSKVTSAIRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 151 FFNEQGFFWVSTPLITASDTEGAGEmFRVstldlenlP-RNDQGKvdfdkdFFG--------KEsFLTVSGqlngetyac 221
Cdd:PRK00476 154 FLDDNGFLEIETPILTKSTPEGARD-YLV--------PsRVHPGK------FYAlpqspqlfKQ-LLMVAG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 222 aLSKIYTFGPTFRAENSNTSRhLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEER----------ADDM------ 285
Cdd:PRK00476 209 -FDRYYQIARCFRDEDLRADR-QPEFTQIDIEMSFVTQEDVMALMEGLIRHVFKEVLGVDlptpfprmtyAEAMrrygsd 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 286 ----------------------KFFAERVDKDAV-------------SRleRFIEA--DFAQV----------------- 311
Cdd:PRK00476 287 kpdlrfglelvdvtdlfkdsgfKVFAGAANDGGRvkairvpggaaqlSR--KQIDEltEFAKIygakglayikvnedglk 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 312 -----DYTDAVT--ILENCGKK--------------------------------FENPVY---WGVD-----LSSEHERY 344
Cdd:PRK00476 365 gpiakFLSEEELaaLLERTGAKdgdliffgadkakvvndalgalrlklgkelglIDEDKFaflWVVDfpmfeYDEEEGRW 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 345 LAEEH-FKAPvvvknypKDIKAFYMRLNEDGKTVA-AMDVLAPGIgEIIGGSQREERLDVLdERMLE-MGLNKEDYwwyR 421
Cdd:PRK00476 445 VAAHHpFTMP-------KDEDLDELETTDPGKARAyAYDLVLNGY-ELGGGSIRIHRPEIQ-EKVFEiLGISEEEA---E 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1882436903 422 D-----LR--RYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRT 460
Cdd:PRK00476 513 EkfgflLDalKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPKT 558
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
223-458 |
2.01e-13 |
|
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: 71.08 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 223 LSKIYTFGPTFRAENSNTsRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVL-------EERADDMKFFAERV--- 292
Cdd:cd00775 76 FERVYEIGRNFRNEGIDL-THNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINgktkieyGGKELDFTPPFKRVtmv 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 293 ----DKDAVSRLERFIEADFaqvdytDAVTILE-NCGKKFENPVYWGV---DLSSEheryLAEEHFKAPVVVKNYPKDIK 364
Cdd:cd00775 155 dalkEKTGIDFPELDLEQPE------ELAKLLAkLIKEKIEKPRTLGKlldKLFEE----FVEPTLIQPTFIIDHPVEIS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 365 AFYMRLNEDgktvaamdvlaPGIGE----IIGGsqRE------ERLDVLD--ERMLEMGLNKE---------DYWWYRDL 423
Cdd:cd00775 225 PLAKRHRSN-----------PGLTErfelFICG--KEianaytELNDPFDqrERFEEQAKQKEagddeammmDEDFVTAL 291
|
250 260 270
....*....|....*....|....*....|....*
gi 1882436903 424 RrYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFP 458
Cdd:cd00775 292 E-YGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
20-99 |
1.46e-12 |
|
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: 62.64 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 20 VTVRGWVRTRRDSKAGISFLAVYDGScfDPVQAVINNSlpNYNEDVLRLTTGCSVIVTGKVVASPGQGqqFEIQASKVEV 99
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGT--GSIQVVVFKE--EAEKLAKKLKEGDVVRVTGKVKKRKGGE--LELVVEEIEL 74
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
16-460 |
2.79e-12 |
|
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: 68.87 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 16 VDSEVTVRGWVRTRRDsKAGISFLAVYDGSCFdpVQAVINnslPNYNEDVLRLTTGC---SVI-VTGKVVA-SPGQ---- 86
Cdd:COG0173 15 VGQEVTLSGWVHRRRD-HGGLIFIDLRDRYGI--TQVVFD---PDDSAEAFEKAEKLrseYVIaVTGKVRArPEGTvnpk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 87 ---GQqFEIQASKVEVAGWVEDPdtyPMAAKRHsIEY------------LRevahlRPR--TNLIgavarVRHTLAQALH 149
Cdd:COG0173 89 lptGE-IEVLASELEILNKAKTP---PFQIDDD-TDVseelrlkyryldLR-----RPEmqKNLI-----LRHKVTKAIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 150 RFFNEQGFFWVSTPLITASDTEGAGEmFRVstldlenlP-RNDQGKvdfdkdFFG--------KEsFLTVSGqlngetya 220
Cdd:COG0173 154 NYLDENGFLEIETPILTKSTPEGARD-YLV--------PsRVHPGK------FYAlpqspqlfKQ-LLMVSG-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 221 caLSKIYTFGPTFRAENSNTSRHlAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEER----------ADDM----- 285
Cdd:COG0173 210 --FDRYFQIARCFRDEDLRADRQ-PEFTQLDIEMSFVDQEDVFELMEGLIRHLFKEVLGVElptpfprmtyAEAMerygs 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 286 -----------------------KFFAERVDKDAV------------SRleRFIEA--DFAQ-----------VD----- 312
Cdd:COG0173 287 dkpdlrfglelvdvtdifkdsgfKVFAGAAENGGRvkainvpggaslSR--KQIDEltEFAKqygakglayikVNedglk 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 313 ------YTDAVT--ILENCG-------------------------------------KKFeNPVyWGVD-----LSSEHE 342
Cdd:COG0173 365 spiakfLSEEELaaILERLGakpgdliffvadkpkvvnkalgalrlklgkelglideDEF-AFL-WVVDfplfeYDEEEG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 343 RYLAEEH-FKAPVvvknyPKDIKafymRLNED-GKTVA-AMDVLAPGIgEIIGGSQREERLDVLdERMLE-MGLNKEDYw 418
Cdd:COG0173 443 RWVAMHHpFTMPK-----DEDLD----LLETDpGKVRAkAYDLVLNGY-ELGGGSIRIHDPELQ-EKVFElLGISEEEA- 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1882436903 419 wyRD-----LR--RYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRT 460
Cdd:COG0173 511 --EEkfgflLEafKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKT 557
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
225-458 |
2.81e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 68.58 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 225 KIYTFGPTFRAENSNTsRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVL-------EERADDMKFFAERVD-KDA 296
Cdd:PRK00484 242 RVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLgttkvtyQGTEIDFGPPFKRLTmVDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 297 VSrleRFIEADFAQVDYTDAVTILENCGKKFENPVYWG--VDLSSEHeryLAEEHFKAPVVVKNYPKDIKAFYMRLNEDg 374
Cdd:PRK00484 321 IK---EYTGVDFDDMTDEEARALAKELGIEVEKSWGLGklINELFEE---FVEPKLIQPTFITDYPVEISPLAKRHRED- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 375 ktvaamdvlaPGIGE----IIGGsqRE------ERLDVLD--ERMLE------------MGLNkEDYwwyrdLR--RYGT 428
Cdd:PRK00484 394 ----------PGLTErfelFIGG--REianafsELNDPIDqrERFEAqveakeagddeaMFMD-EDF-----LRalEYGM 455
|
250 260 270
....*....|....*....|....*....|
gi 1882436903 429 VPHSGFGLGFERLIAYVTGVQNVRDVIPFP 458
Cdd:PRK00484 456 PPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
19-102 |
1.30e-11 |
|
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: 60.33 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDSKaGISFLAVYDGSCFdpVQAVINNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQQ---FEIQAS 95
Cdd:cd04323 1 RVKVFGWVHRLRSQK-KLMFLVLRDGTGF--LQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAKQApggYELQVD 77
|
....*..
gi 1882436903 96 KVEVAGW 102
Cdd:cd04323 78 YLEIIGE 84
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
115-458 |
4.15e-11 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 65.08 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 115 RHSIEYLREVAHLRPRTNLigavaRVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRV--STLDLENLPRndq 192
Cdd:PRK12445 166 RYRQRYLDLIANDKSRQTF-----VVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFIThhNALDLDMYLR--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 193 gkvdFDKDFFGKEsfLTVSGqlngetyacaLSKIYTFGPTFRAENSNTsRHLAEFWMLEPEVAFANLNDIAGLAEAMLKY 272
Cdd:PRK12445 238 ----IAPELYLKR--LVVGG----------FERVFEINRNFRNEGISV-RHNPEFTMMELYMAYADYHDLIELTESLFRT 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 273 VFKAVL--------EERADDMKFFAERVDKDAVSRLERfiEADFAQVDYTDAVTIL-ENCGKKFENPvyWGVD-LSSEHE 342
Cdd:PRK12445 301 LAQEVLgttkvtygEHVFDFGKPFEKLTMREAIKKYRP--ETDMADLDNFDAAKALaESIGITVEKS--WGLGrIVTEIF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 343 RYLAEEHFKAPVVVKNYPKDIKAFYMRLNEDGKTVAAMDV------LAPGIGEIIGGSQREERLDvlDERMLEMGLNKED 416
Cdd:PRK12445 377 DEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFfiggreIGNGFSELNDAEDQAERFQ--EQVNAKAAGDDEA 454
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1882436903 417 YWW---YRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFP 458
Cdd:PRK12445 455 MFYdedYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
19-127 |
1.94e-09 |
|
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: 54.84 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDSKAGIsFLAVYDGSCFdpVQAVI-NNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASKV 97
Cdd:cd04319 1 KVTLAGWVYRKREVGKKA-FIVLRDSTGI--VQAVFsKDLNEEAYREAKKVGIESSVIVEGAVKADPRAPGGAEVHGEKL 77
|
90 100 110
....*....|....*....|....*....|
gi 1882436903 98 EVAGWVEDpdtYPMaAKRHSIEYLREVAHL 127
Cdd:cd04319 78 EIIQNVEF---FPI-TEDASDEFLLDVRHL 103
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
146-269 |
7.34e-07 |
|
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: 49.81 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 146 QALHRFFNEQGFFWVSTPLIT-ASDTEGAGEMFRVStldlenlprnDQGKVDFDKDFFGKESFLTVSGQLNGETYACALS 224
Cdd:cd00768 7 QKLRRFMAELGFQEVETPIVErEPLLEKAGHEPKDL----------LPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1882436903 225 KIYTFGPTFRAENSNTS-RHLAEFWMLEPEVAFANLNDIAGLAEAM 269
Cdd:cd00768 77 RLAEIGPAFRNEGGRRGlRRVREFTQLEGEVFGEDGEEASEFEELI 122
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
16-99 |
1.92e-05 |
|
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: 44.05 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 16 VDSEVTVRGWVRTRRDSKaGISFLAVYDGSCFdpVQAVINNSLPNYNEDVLRLTTGCSVIVTGKVVASPgQGQ------- 88
Cdd:cd04317 13 VGQEVTLCGWVQRRRDHG-GLIFIDLRDRYGI--VQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARP-EGTvnpklpt 88
|
90
....*....|..
gi 1882436903 89 -QFEIQASKVEV 99
Cdd:cd04317 89 gEIEVVASELEV 100
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
19-99 |
2.38e-04 |
|
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: 40.38 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 19 EVTVRGWVRTRRDSkAGISFLAVYDGSCFdpVQAVINNSLPNYN--EDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASK 96
Cdd:cd04316 14 EVTVAGWVHEIRDL-GGIKFVILRDREGI--VQVTAPKKKVDKElfKTVRKLSRESVISVTGTVKAEPKAPNGVEIIPEE 90
|
...
gi 1882436903 97 VEV 99
Cdd:cd04316 91 IEV 93
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
379-459 |
6.55e-04 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 42.28 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1882436903 379 AMDVLAPGiGEIIGGSQREERLDVLDERMLEMGLNKED----YWWYRDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDV 454
Cdd:PRK12820 490 AYDLVVNG-EELGGGSIRINDKDIQLRIFAALGLSEEDiedkFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREV 568
|
....*
gi 1882436903 455 IPFPR 459
Cdd:PRK12820 569 IAFPK 573
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
426-458 |
7.30e-04 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 41.90 E-value: 7.30e-04
10 20 30
....*....|....*....|....*....|...
gi 1882436903 426 YGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFP 458
Cdd:PLN02502 515 YGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| |
