|
Name |
Accession |
Description |
Interval |
E-value |
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
2-456 |
0e+00 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 812.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 2 MNRTLVKHVLDSEVEMPDVLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVAG 81
Cdd:PRK03932 1 MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 82 QGR-QRWELRAASLELVGAVPDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPII 160
Cdd:PRK03932 81 PRAgQGYELQATKIEVIGEDPEDYPIQKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 161 TASDCEGAGEMFRVTTLDVgdaasrDASRDFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMV 240
Cdd:PRK03932 161 TASDCEGAGELFRVTTLDL------DFSKDFFGKEAYLTVSGQLYAEAYAMALGKVYTFGPTFRAENSNTRRHLAEFWMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 241 EPEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDILLKSGKTFDYP 320
Cdd:PRK03932 235 EPEMAFADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPRITYTEAIEILQKSGKKFEFP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 321 VSWGINLQSEHERFLTEEHFKCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRM 400
Cdd:PRK03932 315 VEWGDDLGSEHERYLAEEHFKKPVFVTNYPKDIKAFYMRLNPDGKTVAAMDLLAPGIGEIIGGSQREERLDVLEARIKEL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1554508772 401 GMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFARTPRNCEF 456
Cdd:PRK03932 395 GLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRAEF 450
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-455 |
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: 689.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 3 NRTLVKHVLDSEVEmPDVLIQGWVRTRRDSKTFSFLEVNDGSSVasLQVVADEG-IPGYERIGEMATGSAVSIRGALVAG 81
Cdd:COG0017 1 KRTYIKDLLPEHVG-QEVTVAGWVRTKRDSGGISFLILRDGSGF--IQVVVKKDkLENFEEAKKLTTESSVEVTGTVVES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 82 QGR-QRWELRAASLELVGAVPDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPII 160
Cdd:COG0017 78 PRApQGVELQAEEIEVLGEADEPYPLQPKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 161 TASDCEGAGEMFRVttldvgdaasrdasrDFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMV 240
Cdd:COG0017 158 TASATEGGGELFPV---------------DYFGKEAYLTQSGQLYKEALAMALEKVYTFGPTFRAEKSNTRRHLAEFWMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 241 EPEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTRFVdkglrERLEHVKETPFVRCSYTEAVDILLKSGKtfdyP 320
Cdd:COG0017 223 EPEMAFADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGRDV-----ERLEKVPESPFPRITYTEAIEILKKSGE----K 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 321 VSWGINLQSEHERFLTEEHFKCPVIVYNYPKEIKPFYMRLN-EDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRR 399
Cdd:COG0017 294 VEWGDDLGTEHERYLGEEFFKKPVFVTDYPKEIKAFYMKPNpDDPKTVAAFDLLAPGIGEIIGGSQREHRYDVLVERIKE 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1554508772 400 MGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFARTPRNCE 455
Cdd:COG0017 374 KGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLT 429
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
20-456 |
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: 650.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYE--RIGEMATGSAVSIRGALVAGQGR-QRWELRAASLEL 96
Cdd:TIGR00457 19 VTVSGWVRTKRSSKKIIFLELNDGSSLGPIQAVINGEDNPYLfqLLKSLTTGSSVSVTGKVVESPGKgQPVELQVKKIEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 97 VG-AVPDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVT 175
Cdd:TIGR00457 99 VGeAEPDDYPLQKKEHSLEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 176 TLDVgdaasrDASRDFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMVEPEMAFCDLYGDMDM 255
Cdd:TIGR00457 179 TGNI------DFSQDFFGKEAYLTVSGQLYLETYALALSKVYTFGPTFRAEKSNTSRHLSEFWMIEPEMAFANLNDLLQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 256 AEEFVRFLVGDALANSSEEVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDILLKSGKTFDYPVSWGINLQSEHERFL 335
Cdd:TIGR00457 253 AETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFARITYTDAIEILKESDKNFEYEDFWGDDLQTEHERFL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 336 TEEHFKCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRR 415
Cdd:TIGR00457 333 AEEYFKPPVFVTNYPKDIKAFYMKLNDDGKTVAAMDLLAPGIGEIIGGSEREDDLDKLENRMKEMGLDTDALNWYLDLRK 412
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1554508772 416 YGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFARTPRNCEF 456
Cdd:TIGR00457 413 YGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
20-456 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 586.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERI--GEMATGSAVSIRGALVAGQG-RQRWELRAASLEL 96
Cdd:PLN02603 110 LNVMGWVRTLRAQSSVTFIEVNDGSCLSNMQCVMTPDAEGYDQVesGLITTGASVLVQGTVVSSQGgKQKVELKVSKIVV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 97 VGAVPDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVTT 176
Cdd:PLN02603 190 VGKSDPSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 177 L-----DVGDAASR----------DASRDFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMVE 241
Cdd:PLN02603 270 LipnsaENGGSLVDdipktkdgliDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 242 PEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDILLKSGKTFDYPV 321
Cdd:PLN02603 350 PELAFADLNDDMACATAYLQYVVKYILENCKEDMEFFNTWIEKGIIDRLSDVVEKNFVQLSYTDAIELLLKAKKKFEFPV 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 322 SWGINLQSEHERFLTEEHF-KCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRM 400
Cdd:PLN02603 430 KWGLDLQSEHERYITEEAFgGRPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVPRVGELIGGSQREERLEYLEARLDEL 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1554508772 401 GMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFARTPRNCEF 456
Cdd:PLN02603 510 KLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSAEF 565
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
3-451 |
0e+00 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 529.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 3 NRTLVKHVLDSevemPD---------VLIQGWVRTRRDS--KTFSFLEVNDGSSVASLQVVADEGIPGYERIgeMATGSA 71
Cdd:PLN02221 31 DRVLIRSILDR----PDggaglagqkVRIGGWVKTGREQgkGTFAFLEVNDGSCPANLQVMVDSSLYDLSTL--VATGTC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 72 VSIRGALVA---GQG-RQRWELRAASLELVGAV-PDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRF 146
Cdd:PLN02221 105 VTVDGVLKVppeGKGtKQKIELSVEKVIDVGTVdPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 147 FQERDFSWVSTPIITASDCEGAGEMFRVTTL--------------------DV----------GDA--------ASRDA- 187
Cdd:PLN02221 185 FQEHSFLYIHTPIITTSDCEGAGEMFQVTTLinyterleqdlidnpppteaDVeaarlivkerGEVvaqlkaakASKEEi 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 188 ------------------------------------SRDFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTT 231
Cdd:PLN02221 265 taavaelkiakeslahieersklkpglpkkdgkidySKDFFGRQAFLTVSGQLQVETYACALSSVYTFGPTFRAENSHTS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 232 RHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDIL- 310
Cdd:PLN02221 345 RHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCKWLLDKCFDDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLe 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 311 --LKSGKTFDYPVSWGINLQSEHERFLTEEHFKCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREE 388
Cdd:PLN02221 425 eaVAKGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREE 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1554508772 389 RLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFARTP 451
Cdd:PLN02221 505 RYDVIKQRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYP 567
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
20-456 |
1.60e-163 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 473.74 E-value: 1.60e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSK--TFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVAG--QGRQRWELRAASLE 95
Cdd:PTZ00425 84 ITVCGWSKAVRKQGggRFCFVNLNDGSCHLNLQIIVDQSIENYEKLLKCGVGCCFRFTGKLIISpvQNENKKGLLKENVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 96 LV--------------GAVPDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIIT 161
Cdd:PTZ00425 164 LAlkdnsihnfeiygeNLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNALAIATHLFFQSRGFLYIHTPLIT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 162 ASDCEGAGEMFRVTTL--------------------------------DVGDAASR----------------DASRDFFG 193
Cdd:PTZ00425 244 TSDCEGGGEMFTVTTLlgedadyraiprvnkknkkgekredilntcnaNNNNGNSSssnavsspaypdqyliDYKKDFFS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 194 KAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVGDALANSSE 273
Cdd:PTZ00425 324 KQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAESYIKYCIGYVLNNNFD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 274 EVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDILLKSGKTFDYPVSWGINLQSEHERFLTEEHFKCPVIVYNYPKEI 353
Cdd:PTZ00425 404 DIYYFEENVETGLISRLKNILDEDFAKITYTNVIDLLQPYSDSFEVPVKWGMDLQSEHERFVAEQIFKKPVIVYNYPKDL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 354 KPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLM 433
Cdd:PTZ00425 484 KAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWWYRQLRKFGSHPHAGFGLGFERLIM 563
|
490 500
....*....|....*....|...
gi 1554508772 434 FVTGVTNIRDVLPFARTPRNCEF 456
Cdd:PTZ00425 564 LVTGVDNIKDTIPFPRYPGHAEF 586
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
16-450 |
7.22e-152 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 445.85 E-value: 7.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 16 EMPDVLIQGWVRTRRDSktfSFLEVNDGSSVASLQVVADEGIPGYERIgeMATGSAVSIRGAL---VAGQGRQRWELRAA 92
Cdd:PLN02532 119 EKTEIAIQKSAPPPPSV---AYLLISDGSCVASLQVVVDSALAPLTQL--MATGTCILAEGVLklpLPAQGKHVIELEVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 93 SLELVGAV-PDSYPLQKKGHTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEM 171
Cdd:PLN02532 194 KILHIGTVdPEKYPLSKKRLPLDMLRDFSHFRPRTTTVASVTRVRSALTHATHTFFQDHGFLYVQVPIITTTDATGFGEM 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 172 FRVTTL---------------------DVGDAASRDASR----------------------------------------- 189
Cdd:PLN02532 274 FRVTTLlgksddkeekkpvhetegislEAVKAAIKEKTNlveelkrsesnrealvaaeqdlrktnqlasqleakeklktg 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 190 ------------DFFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMVEPEMAFCDLYGDMDMAE 257
Cdd:PLN02532 354 tsvkadklsfskDFFSRPTYLTVSGRLHLESYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSELEDAMNCAE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 258 EFVRFLVGDALANSSEEVEFLTRFVDKGLRERLEHVKETPFVRCSYTEAVDILLK-SGKTFDYPVSWGINLQSEHERFLT 336
Cdd:PLN02532 434 DYFKFLCKWVLENCSEDMKFVSKRIDKTISTRLEAIISSSLQRISYTEAVDLLKQaTDKKFETKPEWGIALTTEHLSYLA 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 337 EEHFKCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRY 416
Cdd:PLN02532 514 DEIYKKPVIIYNYPKELKPFYVRLNDDGKTVAAFDLVVPKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRRH 593
|
490 500 510
....*....|....*....|....*....|....
gi 1554508772 417 GTVPHAGFGAGFERLLMFVTGVTNIRDVLPFART 450
Cdd:PLN02532 594 GTVKHSGFSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
111-452 |
3.03e-149 |
|
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: 427.37 E-value: 3.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 111 HTPEFLRSIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVttldvgdaasrdasrD 190
Cdd:cd00776 2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKV---------------S 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 191 FFGKAAYLTVSGQLEGEAFACALSNIYTFGPTFRAENSNTTRHAAEFWMVEPEMAFCDLYGD-MDMAEEFVRFLVGDALA 269
Cdd:cd00776 67 YFGKPAYLAQSPQLYKEMLIAALERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEvMDLIEELIKYIFKRVLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 270 NSSEEVEFLTRFvdkglrERLEHVKETPFVRCSYTEAVDILLKSGKTfdYPVSWGINLQSEHERFLTEEHFKCPVIVYNY 349
Cdd:cd00776 147 RCAKELELVNQL------NRELLKPLEPFPRITYDEAIELLREKGVE--EEVKWGEDLSTEHERLLGEIVKGDPVFVTDY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 350 PKEIKPFYMRLNED-GKTVTAMDVLVPGIGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGF 428
Cdd:cd00776 219 PKEIKPFYMKPDDDnPETVESFDLLMPGVGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGL 298
|
330 340
....*....|....*....|....
gi 1554508772 429 ERLLMFVTGVTNIRDVLPFARTPR 452
Cdd:cd00776 299 ERLVMWLLGLDNIREAILFPRDPK 322
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-449 |
2.03e-85 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 268.60 E-value: 2.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 1 MMNRTLVKHVLDsEVEMPDVLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVA 80
Cdd:PRK05159 1 MMKRHLTSELTP-ELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTVKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 81 -GQGRQRWELRAASLELVGAVPDSYPLQKKGHTPEFL------RSIAHLRPRTNlfgAVFRMRSRLAFAIHRFFQERDFS 153
Cdd:PRK05159 80 nPKAPGGVEVIPEEIEVLNKAEEPLPLDISGKVLAELdtrldnRFLDLRRPRVR---AIFKIRSEVLRAFREFLYENGFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 154 WVSTPIITASDCEGAGEMFRVttldvgdaasrdasrDFFGKAAYLTVSGQLEGEAFACA-LSNIYTFGPTFRAENSNTTR 232
Cdd:PRK05159 157 EIFTPKIVASGTEGGAELFPI---------------DYFEKEAYLAQSPQLYKQMMVGAgFERVFEIGPVFRAEEHNTSR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 233 HAAEFWMVEPEMAFCDLYGD-MDMAEEFVRFLVGDALANSSEEVEfltrfvdkglreRLEH---VKETPFVRCSYTEAVD 308
Cdd:PRK05159 222 HLNEYTSIDVEMGFIDDHEDvMDLLENLLRYMYEDVAENCEKELE------------LLGIelpVPETPIPRITYDEAIE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 309 ILLKSGktfdYPVSWGINLQSEHERFL----TEEHFKCPVIVYNYPKEIKPFY-MRLNEDGKTVTAMDVLVPGIgEIVGG 383
Cdd:PRK05159 290 ILKSKG----NEISWGDDLDTEGERLLgeyvKEEYGSDFYFITDYPSEKRPFYtMPDEDDPEISKSFDLLFRGL-EITSG 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1554508772 384 SQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPFAR 449
Cdd:PRK05159 365 GQRIHRYDMLVESIKEKGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPR 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
121-451 |
4.20e-77 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 243.24 E-value: 4.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 121 HLRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVttldvgdaASRdASRDFFgkaaYLTV 200
Cdd:pfam00152 10 YLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLV--------PSR-ALGKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 201 SGQLEGEAFACA-LSNIYTFGPTFRAENSNTTRHAaEFWMVEPEMAFCDLYGDMDMAEEFVRFLVgdalanssEEVEFLT 279
Cdd:pfam00152 77 SPQLYKQLLMVAgFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVDYEDVMDLTEELIKEIF--------KEVEGIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 280 RFVDKGLRERLEhvkeTPFVRCSYTEAVDILLKsgktfDYPVSWGINLQSEHERFLTE----EHFKCPVIVYNYPKEIKP 355
Cdd:pfam00152 148 KELEGGTLLDLK----KPFPRITYAEAIEKLNG-----KDVEELGYGSDKPDLRFLLElvidKNKFNPLWVTDFPAEHHP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 356 FYMRLNEDGKTVT-AMDVLVPGIgEIVGGSQREERLDILEENMRRMGMNAEAYR----WYADLRRYGTVPHAGFGAGFER 430
Cdd:pfam00152 219 FTMPKDEDDPALAeAFDLVLNGV-EIGGGSIRIHDPELQEERFEEQGLDPEEAEekfgFYLDALKYGAPPHGGLGIGLDR 297
|
330 340
....*....|....*....|.
gi 1554508772 431 LLMFVTGVTNIRDVLPFARTP 451
Cdd:pfam00152 298 LVMLLTGLESIREVIAFPKTR 318
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
132-451 |
4.32e-61 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 202.17 E-value: 4.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 132 VFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGemfrvttlDVGDAASRDASRDFFGKAAYLTVSGQLEGEAFAC 211
Cdd:PRK06462 29 VLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMG--------LGSDLPVKQISIDFYGVEYYLADSMILHKQLALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 212 ALSNIYTFGPTFRAEN--SNTTRHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTRfvdkglreR 289
Cdd:PRK06462 101 MLGKIFYLSPNFRLEPvdKDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGR--------D 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 290 LEHVKeTPFVRCSYTEAVDILLKSGKTFDyPVSwgiNLQSEHERFLtEEHFKCPVIVYNYPKEIKPFYMR--LNEDGKTV 367
Cdd:PRK06462 173 LPHLK-RPFKRITHKEAVEILNEEGCRGI-DLE---ELGSEGEKSL-SEHFEEPFWIIDIPKGSREFYDRedPERPGVLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 368 tAMDVLVP-GIGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLP 446
Cdd:PRK06462 247 -NYDLLLPeGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQP 325
|
....*
gi 1554508772 447 FARTP 451
Cdd:PRK06462 326 FPRVP 330
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
125-454 |
6.57e-37 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 141.77 E-value: 6.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 125 RTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVttldvgdaasrdasrDFFGKAAYLTVSGQL 204
Cdd:PLN02850 217 RTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRL---------------DYKGQPACLAQSPQL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 205 EGEAFACA-LSNIYTFGPTFRAENSNTTRHAAEFWMVEPEMAFCDLYGD-MDMAEEFvrflvgdalansseeveFLTRFv 282
Cdd:PLN02850 282 HKQMAICGdFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEvLDVVDEL-----------------FVAIF- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 283 dKGLRER----LEHVKET-PF---------VRCSYTEAVDILLKSGKTFDyPVSwgiNLQSEHERFL---TEEHFKCPV- 344
Cdd:PLN02850 344 -DGLNERckkeLEAIREQyPFeplkylpktLRLTFAEGIQMLKEAGVEVD-PLG---DLNTESERKLgqlVKEKYGTDFy 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 345 IVYNYPKEIKPFY-MRLNEDGKTVTAMDVLVPGiGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAG 423
Cdd:PLN02850 419 ILHRYPLAVRPFYtMPCPDDPKYSNSFDVFIRG-EEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGG 497
|
330 340 350
....*....|....*....|....*....|.
gi 1554508772 424 FGAGFERLLMFVTGVTNIRDVLPFARTPRNC 454
Cdd:PLN02850 498 FGVGLERVVMLFCGLNNIRKTSLFPRDPQRL 528
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
133-452 |
3.14e-36 |
|
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: 134.53 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 133 FRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEMFRVTTLDVGdaasrdasrdffgKAAYLTVSGQLEGEAF-AC 211
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALG-------------LDYYLRISPQLFKKRLmVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 212 ALSNIYTFGPTFRAEnSNTTRHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVGDALANSSEEVEFLTrfVDKGLrerle 291
Cdd:cd00669 68 GLDRVFEINRNFRNE-DLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYGFEL--EDFGL----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 292 hvketPFVRCSYTEAVDILLKsgktfdypvswginlqseherflteehfkcPVIVYNYPKEIKPFYMRLNEDGKTVT-AM 370
Cdd:cd00669 140 -----PFPRLTYREALERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIAdAF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 371 DVLVPGIgEIVGGSQREERLDILEENMRRMGMNAEAYR----WYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLP 446
Cdd:cd00669 185 DLFINGV-EVGNGSSRLHDPDIQAEVFQEQGINKEAGMeyfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIA 263
|
....*.
gi 1554508772 447 FARTPR 452
Cdd:cd00669 264 FPKMRR 269
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
20-452 |
4.38e-33 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 131.27 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPG--YERIGEMATGSAVSIRGAL------VAGQGRQRWELRA 91
Cdd:PTZ00401 81 VLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKemIDFIGQIPTESIVDVEATVckveqpITSTSHSDIELKV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 92 ASLELVGAVPDSYPL---------QKKGHTPEFLRSIAH--LRPRTNLFGAVFRMRSRLAFAIHRFFQERDFSWVSTPII 160
Cdd:PTZ00401 161 KKIHTVTESLRTLPFtledasrkeSDEGAKVNFDTRLNSrwMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 161 TASDCEGAGEMFRVttldvgdaasrdasrDFFGKAAYLTVSGQLEGE-AFACALSNIYTFGPTFRAENSNTTRHAAEFWM 239
Cdd:PTZ00401 241 INAPSEGGANVFKL---------------EYFNRFAYLAQSPQLYKQmVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 240 VEPEMAFCDLYGD-MDMAEEFVRFLVgDALANSSEEVEFLTR------FVDKGLRERLE--------------------- 291
Cdd:PTZ00401 306 LDVEMRINEHYYEvLDLAESLFNYIF-ERLATHTKELKAVCQqypfepLVWKLTPERMKelgvgvisegveptdkyqarv 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 292 HVKETPFVRCSYTEAVDILlksGKTFDYPVSWGINLQSEHERF---LTEEHFKCPVIVYN-YPKEIKPFY-MRLNEDGKT 366
Cdd:PTZ00401 385 HNMDSRMLRINYMHCIELL---NTVLEEKMAPTDDINTTNEKLlgkLVKERYGTDFFISDrFPSSARPFYtMECKDDERF 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 367 VTAMDVLVPGiGEIVGGSQREERLDILEENMRRMGMNAEAYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLP 446
Cdd:PTZ00401 462 TNSYDMFIRG-EEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASL 540
|
....*.
gi 1554508772 447 FARTPR 452
Cdd:PTZ00401 541 FPRDPQ 546
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
19-98 |
7.75e-30 |
|
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: 111.12 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 19 DVLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVAGQGR-QRWELRAASLELV 97
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELNDGSCLKNLQVVVDKELTNFKEILKLSTGSSIRVEGVLVKSPGAkQPFELQAEKIEVL 80
|
.
gi 1554508772 98 G 98
Cdd:cd04318 81 G 81
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
133-450 |
1.41e-19 |
|
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: 88.40 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 133 FRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGAGEmFRVttldvgdaasrdASRDFFGKAAYLTVSGQLegeaF--- 209
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARD-FLV------------PSRLHPGKFYALPQSPQL----Fkql 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 210 --ACALSNIYTFGPTFRAENSNTTRHAaEFWMVEPEMAFCDLYGDMDMAEEFVRFLVgdalansseevefltrfvdkglR 287
Cdd:cd00777 64 lmVSGFDRYFQIARCFRDEDLRADRQP-EFTQIDIEMSFVDQEDIMSLIEGLLKYVF----------------------K 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 288 ERLEHVKETPFVRCSYTEAVDillKSGKTFDYPVSWGINLQSEHERFLTEEHfkcpvivynypkeiKPFYM-------RL 360
Cdd:cd00777 121 EVLGVELTTPFPRMTYAEAME---RYGFKFLWIVDFPLFEWDEEEGRLVSAH--------------HPFTApkeedldLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 361 NEDGKTVTAM--DVLVPGIgEIVGGSQREERLDILEENMRRMGMN-AEAYRWYADLRR---YGTVPHAGFGAGFERLLMF 434
Cdd:cd00777 184 EKDPEDARAQayDLVLNGV-ELGGGSIRIHDPDIQEKVFEILGLSeEEAEEKFGFLLEafkYGAPPHGGIALGLDRLVML 262
|
330
....*....|....*.
gi 1554508772 435 VTGVTNIRDVLPFART 450
Cdd:cd00777 263 LTGSESIRDVIAFPKT 278
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
132-447 |
5.23e-15 |
|
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: 75.70 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 132 VFRMRSRLAFAIHRFFQERDFSWVSTPIitasdcegageMFRVTtldvGDAASR-------DASRDFFGKAA---YL--- 198
Cdd:cd00775 7 TFIVRSKIISYIRKFLDDRGFLEVETPM-----------LQPIA----GGAAARpfithhnALDMDLYLRIApelYLkrl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 199 TVSGqlegeafacaLSNIYTFGPTFRAENSNTTrHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVgDALaNSSEEVEFL 278
Cdd:cd00775 72 IVGG----------FERVYEIGRNFRNEGIDLT-HNPEFTMIEFYEAYADYNDMMDLTEDLFSGLV-KKI-NGKTKIEYG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 279 TRFVD-----------KGLRERL-----EHVKETPFvrcsytEAVDILLKS-GKTFDYPVSWGINLQSEHERFLtEEHFK 341
Cdd:cd00775 139 GKELDftppfkrvtmvDALKEKTgidfpELDLEQPE------ELAKLLAKLiKEKIEKPRTLGKLLDKLFEEFV-EPTLI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 342 CPVIVYNYPKEIKPFYMRLNEDgktvtamdvlvPGIGE----IVGG--------------SQREERLDILEEnmRRMGmN 403
Cdd:cd00775 212 QPTFIIDHPVEISPLAKRHRSN-----------PGLTErfelFICGkeianaytelndpfDQRERFEEQAKQ--KEAG-D 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1554508772 404 AEAYRWYADLRR---YGTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:cd00775 278 DEAMMMDEDFVTaleYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILF 324
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
20-98 |
1.96e-13 |
|
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: 65.66 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSvaSLQVVADEGIPG--YERIGEMATGSAVSIRGALVAGQGRQRW----ELRAAS 93
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSG--IVQVVVNKEELGefFEEAEKLRTESVVGVTGTVVKRPEGNLAtgeiELQAEE 79
|
....*
gi 1554508772 94 LELVG 98
Cdd:cd04100 80 LEVLS 84
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
19-447 |
1.49e-12 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 69.32 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 19 DVLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGY--ERIGEMATGSAVSIRGALVAgqgRQRWELRAASLEL 96
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVynDQFKKWDLGDIIGARGTLFK---TQTGELSIHCTEL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 97 VGAVPDSYPLQKKGH---------TPEFLRSIAHLRPRTNlfgavFRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEG 167
Cdd:PRK12445 144 RLLTKALRPLPDKFHglqdqevryRQRYLDLIANDKSRQT-----FVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 168 AGEMFRV--TTLDVgDAASRDASRDFFGKaayLTVSGqlegeafacaLSNIYTFGPTFRAENSnTTRHAAEFWMVEPEMA 245
Cdd:PRK12445 219 SARPFIThhNALDL-DMYLRIAPELYLKR---LVVGG----------FERVFEINRNFRNEGI-SVRHNPEFTMMELYMA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 246 FCDLYGDMDMAEEFVRFLVGDALANSS----EEV-EFLTRFVDKGLRERLE-HVKETPFVRCSYTEAVDILLKS-GKTFD 318
Cdd:PRK12445 284 YADYHDLIELTESLFRTLAQEVLGTTKvtygEHVfDFGKPFEKLTMREAIKkYRPETDMADLDNFDAAKALAESiGITVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 319 YpvSWGIN-LQSEHERFLTEEHFKCPVIVYNYPKEIKPFYMRLNEDGKTVTAMDVLV------PGIGEIVGGSQREERLD 391
Cdd:PRK12445 364 K--SWGLGrIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIggreigNGFSELNDAEDQAERFQ 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1554508772 392 ilEENMRRMGMNAEAYRW---YADLRRYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:PRK12445 442 --EQVNAKAAGDDEAMFYdedYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILF 498
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
132-447 |
2.44e-11 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 65.50 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 132 VFRMRSRLAFAIHRFFQERDFSWVSTPII-------TAsdcegagemfR--VT---TLDVgdaasrdasrDFFGKAA--- 196
Cdd:PRK00484 171 TFRKRSKIISAIRRFLDNRGFLEVETPMLqpiaggaAA----------RpfIThhnALDI----------DLYLRIApel 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 197 YL--TVSGQLEGeafacalsnIYTFGPTFRAENSNTtRHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLVGDALAnsSEE 274
Cdd:PRK00484 231 YLkrLIVGGFER---------VYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLG--TTK 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 275 VEFLTRFVDKGlrerlehvkeTPFVRCSYTEA------VDIL---------LKSGKTFDYPVSWG----INLQSEHerfL 335
Cdd:PRK00484 299 VTYQGTEIDFG----------PPFKRLTMVDAikeytgVDFDdmtdeearaLAKELGIEVEKSWGlgklINELFEE---F 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 336 TEEHFKCPVIVYNYPKEIKPFYMRLNEDgktvtamdvlvPGIGE----IVGGS--------------QREERLDILEEnm 397
Cdd:PRK00484 366 VEPKLIQPTFITDYPVEISPLAKRHRED-----------PGLTErfelFIGGReianafselndpidQRERFEAQVEA-- 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1554508772 398 RRMGmNAEAYRWYAD-LR--RYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:PRK00484 433 KEAG-DDEAMFMDEDfLRalEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILF 484
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
20-450 |
2.56e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 62.50 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALvagqgRQRW------------ 87
Cdd:PLN02903 75 VTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTV-----RSRPqespnkkmktgs 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 88 -ELRAASLELVGAVPDSYPL------QKKGHTPEFLR-SIAHLRPRTNLFGAVFRMRSRLAFAIHRFFQER-DFSWVSTP 158
Cdd:PLN02903 150 vEVVAESVDILNVVTKSLPFlvttadEQKDSIKEEVRlRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDVhGFVEIETP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 159 IITASDCEGAGEMFRVTTLDVGDAASRDASRDFFGKAayLTVSGqlegeafacaLSNIYTFGPTFRAENSNTTRHaAEFW 238
Cdd:PLN02903 230 ILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQM--LMVSG----------FDRYYQIARCFRDEDLRADRQ-PEFT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 239 MVEPEMAFCDLYGDMDMAEEFVR--FL--VGDALANSSEEV---EFLTRF-VDK-GLRERLEHVKETP-FVRCS---YTE 305
Cdd:PLN02903 297 QLDMELAFTPLEDMLKLNEDLIRqvFKeiKGVQLPNPFPRLtyaEAMSKYgSDKpDLRYGLELVDVSDvFAESSfkvFAG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 306 AVD-------------------ILLKSGKTFDYPVSWGI----------------------NLQSEH-ERFLTE------ 337
Cdd:PLN02903 377 ALEsggvvkaicvpdgkkisnnTALKKGDIYNEAIKSGAkglaflkvlddgelegikalveSLSPEQaEQLLAAcgagpg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 338 ----------------------------------EH-------FkcPVIVYNyPKEIK------PFYMRLNEDGKTVT-- 368
Cdd:PLN02903 457 dlilfaagptssvnktldrlrqfiaktldlidpsRHsilwvtdF--PMFEWN-EDEQRlealhhPFTAPNPEDMGDLSsa 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 369 ---AMDVLVPGIgEIVGGSQREERLDILEENMRRMGMNAE----AYRWYADLRRYGTVPHAGFGAGFERLLMFVTGVTNI 441
Cdd:PLN02903 534 ralAYDMVYNGV-EIGGGSLRIYRRDVQQKVLEAIGLSPEeaesKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSI 612
|
....*....
gi 1554508772 442 RDVLPFART 450
Cdd:PLN02903 613 RDVIAFPKT 621
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
379-447 |
3.13e-09 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 58.93 E-value: 3.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1554508772 379 EIVGGSQREERLDILEENMRRMGMNAEAyrwyADLR--------RYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:PRK00476 483 ELGGGSIRIHRPEIQEKVFEILGISEEE----AEEKfgflldalKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAF 555
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
379-447 |
6.53e-08 |
|
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: 55.00 E-value: 6.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1554508772 379 EIVGGSQREERLDILEENMRRMGMNAEAyrwyADLR--------RYGTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:COG0173 482 ELGGGSIRIHDPELQEKVFELLGISEEE----AEEKfgflleafKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
131-447 |
2.72e-07 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 53.09 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 131 AVFRMRSRLAFAIHRFFQERDFSWVSTPIITasdcegagemfrvttLDVGDAASR-------DASRDFfgkaaYLTVSGQ 203
Cdd:PTZ00417 251 STFITRTKIINYLRNFLNDRGFIEVETPTMN---------------LVAGGANARpfithhnDLDLDL-----YLRIATE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 204 LEGEAFACA-LSNIYTFGPTFRAENSNTTrHAAEFWMVEPEMAFCDLYGDMDMAEEFVRFLV------------GDALAN 270
Cdd:PTZ00417 311 LPLKMLIVGgIDKVYEIGKVFRNEGIDNT-HNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVmhlfgtykilynKDGPEK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 271 SSEEVEFLTRFVDKGLRERLEHVKET----PFVRCSYTEAVDILLKSGKT-FDYPVSWGINLQSEHERFLTEEHFKCPVI 345
Cdd:PTZ00417 390 DPIEIDFTPPYPKVSIVEELEKLTNTkleqPFDSPETINKMINLIKENKIeMPNPPTAAKLLDQLASHFIENKYPNKPFF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 346 VYNYPKEIKPF--YMR----LNEDGKTVTAMDVLVPGIGEIVGGSQREERLDiLEENMRRMGmNAEAYRW---YADLRRY 416
Cdd:PTZ00417 470 IIEHPQIMSPLakYHRskpgLTERLEMFICGKEVLNAYTELNDPFKQKECFS-AQQKDREKG-DAEAFQFdaaFCTSLEY 547
|
330 340 350
....*....|....*....|....*....|.
gi 1554508772 417 GTVPHAGFGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:PTZ00417 548 GLPPTGGLGLGIDRITMFLTNKNCIKDVILF 578
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
14-447 |
4.74e-07 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 51.92 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 14 EVEMPDVLIQGWVRTRRDSKTFSFLEVNDGSsvASLQVVAD-----EGIPGYERI-GEMATGSAVSIRGALvagqGR-QR 86
Cdd:PLN02502 105 ELEDVSVSVAGRIMAKRAFGKLAFYDLRDDG--GKIQLYADkkrldLDEEEFEKLhSLVDRGDIVGVTGTP----GKtKK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 87 WELRAASLELVGAVPDSYPLQKKGH---------TPEFLRSIAHLRPRTnlfgaVFRMRSRLAFAIHRFFQERDFSWVST 157
Cdd:PLN02502 179 GELSIFPTSFEVLTKCLLMLPDKYHgltdqetryRQRYLDLIANPEVRD-----IFRTRAKIISYIRRFLDDRGFLEVET 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 158 PIItasdcEGAGemfrvttldvGDAASR-------DASRDFFGKAA---YLT--VSGQLEgeafacalsNIYTFGPTFRA 225
Cdd:PLN02502 254 PML-----NMIA----------GGAAARpfvthhnDLNMDLYLRIAtelHLKrlVVGGFE---------RVYEIGRQFRN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 226 ENSNTtRHAAEFWMVEPEMAFCDlYGD-MDMAEEFVRFLV-----GDALANSSEEVEFLTRFVDKGLRERLEHVKETPFV 299
Cdd:PLN02502 310 EGIST-RHNPEFTTCEFYQAYAD-YNDmMELTEEMVSGMVkeltgSYKIKYHGIEIDFTPPFRRISMISLVEEATGIDFP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 300 R-CSYTEAVDILLKSGKTFDypvswgINLQSEHE--RFLTE--EHF---KC--PVIVYNYPKEIKPF--YMRLNedgktv 367
Cdd:PLN02502 388 AdLKSDEANAYLIAACEKFD------VKCPPPQTtgRLLNElfEEFleeTLvqPTFVLDHPVEMSPLakPHRSK------ 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 368 tamdvlvPGIGE-----IVGGS-------------QREErldiLEENMRRMGMNaEAYRWYAD------LrRYGTVPHAG 423
Cdd:PLN02502 456 -------PGLTErfelfINGRElanafseltdpvdQRER----FEEQVKQHNAG-DDEAMALDedfctaL-EYGLPPTGG 522
|
490 500
....*....|....*....|....
gi 1554508772 424 FGAGFERLLMFVTGVTNIRDVLPF 447
Cdd:PLN02502 523 WGLGIDRLVMLLTDSASIRDVIAF 546
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
20-97 |
9.45e-07 |
|
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: 46.07 E-value: 9.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1554508772 20 VLIQGWV-RTRRDSKTFSFLEVNDGSsvASLQVVADEGiPGYERIGEMATGSAVSIRGALVAGQGRqRWELRAASLELV 97
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGT--GSIQVVVFKE-EAEKLAKKLKEGDVVRVTGKVKKRKGG-ELELVVEEIELL 75
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
136-246 |
2.33e-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: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 136 RSRLAFAIHRFFQERDFSWVSTPIIT-ASDCEGAGEMFRVttldvgdaasRDASRDFFGKAAYLTVSGQL-EGEAFACAL 213
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVErEPLLEKAGHEPKD----------LLPVGAENEEDLYLRPTLEPgLVRLFVSHI 71
|
90 100 110
....*....|....*....|....*....|....*...
gi 1554508772 214 SN----IYTFGPTFRAENSNT-TRHAAEFWMVEPEMAF 246
Cdd:cd00768 72 RKlplrLAEIGPAFRNEGGRRgLRRVREFTQLEGEVFG 109
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
20-98 |
2.96e-06 |
|
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: 45.30 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVasLQ-VVADEGIPGYERIGEMATGSAVSIRGALV----AGQGRQRWELRAASL 94
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGF--LQcVLSKKLVTEFYDAKSLTQESSVEVTGEVKedprAKQAPGGYELQVDYL 79
|
....
gi 1554508772 95 ELVG 98
Cdd:cd04323 80 EIIG 83
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
20-168 |
2.12e-05 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 46.98 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVAslQVVADEGIPGYERIGEMATGSAVSIRGALVA------------GQgrqrW 87
Cdd:PRK00476 20 VTLCGWVHRRRDHGGLIFIDLRDREGIV--QVVFDPDAEAFEVAESLRSEYVIQVTGTVRArpegtvnpnlptGE----I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 88 ELRAASLELVG-AVPDSYPLQKKGHTPEFLRsiahL--------RPRT--NLfgavfRMRSRLAFAIHRFFQERDFSWVS 156
Cdd:PRK00476 94 EVLASELEVLNkSKTLPFPIDDEEDVSEELR----LkyryldlrRPEMqkNL-----KLRSKVTSAIRNFLDDNGFLEIE 164
|
170
....*....|..
gi 1554508772 157 TPIITASDCEGA 168
Cdd:PRK00476 165 TPILTKSTPEGA 176
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
20-122 |
2.63e-05 |
|
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: 42.90 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1554508772 20 VLIQGWVRTRRDSKTFSFLEVNDGSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVAG-QGRQRWELRAASLELVG 98
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKADpRAPGGAEVHGEKLEIIQ 81
|
90 100
....*....|....*....|....
gi 1554508772 99 AVpDSYPLQKKGhTPEFLRSIAHL 122
Cdd:cd04319 82 NV-EFFPITEDA-SDEFLLDVRHL 103
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| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
133-168 |
3.78e-04 |
|
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: 42.68 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1554508772 133 FRMRSRLAFAIHRFFQERDFSWVSTPIITASDCEGA 168
Cdd:COG0173 142 LILRHKVTKAIRNYLDENGFLEIETPILTKSTPEGA 177
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
19-89 |
1.34e-03 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal 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. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 37.68 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1554508772 19 DVLIQGWVRTRRD-SKTFSFLEVNDgSSVASLQVVADEGIPGYERIGEMATGSAVSIRGALVAGQGR-----QRWEL 89
Cdd:cd04321 1 KVTLNGWIDRKPRiVKKLSFADLRD-PNGDIIQLVSTAKKDAFSLLKSITAESPVQVRGKLQLKEAKsseknDEWEL 76
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
416-447 |
5.75e-03 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 39.18 E-value: 5.75e-03
10 20 30
....*....|....*....|....*....|..
gi 1554508772 416 YGTVPHAGFGAGFERLLMFVTGvTNIRDVLPF 447
Cdd:PRK02983 1057 YAMPPTGGLGMGVDRLVMLLTG-RSIRETLPF 1087
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