|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
49-531 |
0e+00 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 737.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 49 AEDHAAGRYGLSEMIQSKDKRSERNFVPVSELSGQVGKGLVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDV-IS 127
Cdd:PLN02850 44 EDDPLASNYGDVPLEELQSKVTGREWTDVSDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVFVSEVtVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 128 KQMVKFAGNIPKESIIDIQAKPVAVSSKIESCTeQSLELSVEQIFVISQAKAQLPLQIEDASRPE-----NADDAEGLnI 202
Cdd:PLN02850 124 KGMVKYAKQLSRESVVDVEGVVSVPKKPVKGTT-QQVEIQVRKIYCVSKALATLPFNVEDAARSEseiekALQTGEQL-V 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 203 RVNQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLAQSPQL 282
Cdd:PLN02850 202 RVGQDTRLNNRVLDLRTPANQAIFRIQSQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 283 YKQMAIAADFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQY 362
Cdd:PLN02850 282 HKQMAICGDFRRVFEIGPVFRAEDSFTHRHLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 363 KVDAFKFLEPPLILQFADGVAMLREAGVETGDEEDLSTPNEKLLGRLVKAKYDTDFYILDKFPLAIRPFYTMPDPNNPVY 442
Cdd:PLN02850 362 PFEPLKYLPKTLRLTFAEGIQMLKEAGVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 443 SNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMF 522
Cdd:PLN02850 442 SNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLF 521
|
....*....
gi 440214341 523 PRDPKRLTP 531
Cdd:PLN02850 522 PRDPQRLAP 530
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
203-527 |
6.90e-179 |
|
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: 505.56 E-value: 6.90e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 203 RVNQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLAQSPQL 282
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 283 YKQMAIAAdFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVgQQY 362
Cdd:cd00776 81 YKEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 363 KVDAFKFLEPPLILQFADGVAMLREAGVET--GDEEDLSTPNEKLLGRLVKakydTDFYILDKFPLAIRPFYTMPDPNNP 440
Cdd:cd00776 159 NRELLKPLEPFPRITYDEAIELLREKGVEEevKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 441 VYSNSYDMFMRG-EEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKT 519
Cdd:cd00776 235 ETVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREA 314
|
....*...
gi 440214341 520 SMFPRDPK 527
Cdd:cd00776 315 ILFPRDPK 322
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
57-531 |
2.04e-177 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 511.08 E-value: 2.04e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 57 YGLSEMIQSKDKRSeRNFVPVSELSGQ--VGKgLVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQMVKFA 134
Cdd:PTZ00401 49 FGAAPMVQSTTYKS-RTFIPVAVLSKPelVDK-TVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGDVPKEMIDFI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 135 GNIPKESIIDIQAKPVAVSSKIESCTEQSLELSVEQIFVISQAKAQLPLQIEDASRPEnadDAEGlnIRVNQDTRLDNRV 214
Cdd:PTZ00401 127 GQIPTESIVDVEATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLPFTLEDASRKE---SDEG--AKVNFDTRLNSRW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 215 LDLRTPANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLAQSPQLYKQMAIAADFDK 294
Cdd:PTZ00401 202 MDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 295 VYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKYHYHEVLHTIGNTFTSIFKGLRdKYAKEIESVGQQYKVDafkflepPL 374
Cdd:PTZ00401 282 VFEVGPVFRSENSNTHRHLTEFVGLDVEMRINEHYYEVLDLAESLFNYIFERLA-THTKELKAVCQQYPFE-------PL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 375 ILQFAD------GVAMLREaGVETGDE-----------------------------------EDLSTPNEKLLGRLVKAK 413
Cdd:PTZ00401 354 VWKLTPermkelGVGVISE-GVEPTDKyqarvhnmdsrmlrinymhciellntvleekmaptDDINTTNEKLLGKLVKER 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 414 YDTDFYILDKFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRYGC 493
Cdd:PTZ00401 433 YGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKEYVDSFRLGA 512
|
490 500 510
....*....|....*....|....*....|....*...
gi 440214341 494 PPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRLTP 531
Cdd:PTZ00401 513 WPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRTTP 550
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
89-531 |
4.44e-167 |
|
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: 480.09 E-value: 4.44e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQcILAVGDVISKQMVKFAGNIPKESIIDIQAKpvavsSKIESCTEQSLELSV 168
Cdd:TIGR00458 15 VTFMGWVHEIRDLGGLIFVLLRDREGLIQ-ITAPAKKVSKNLFKWAKKLNLESVVAVRGI-----VKIKEKAPGGFEIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 169 EQIFVISQAKAQLPLQIEDASRPEnaddaeglnirvnQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTEI 248
Cdd:TIGR00458 89 TKIEVINEAKEPLPLDPTEKVPAE-------------LDTRLDYRFLDLRRPTVQAIFRIRSGVLESVREFLAEEGFIEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 249 HTPKIISAASEGGANVFTVSYFKDSAYLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKYH 328
Cdd:TIGR00458 156 HTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHRHLNEATSIDIEMAFEDH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 329 yHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQYKVDAFKFLEppliLQFADGVAMLREAGVETGDEEDLSTPNEKLLGR 408
Cdd:TIGR00458 236 -HDVMDILEELVVRVFEDVPERCAHQLETLEFKLEKPEGKFVR----LTYDEAIEMANAKGVEIGWGEDLSTEAEKALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 409 lvkaKYDTDFYILDkFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIES 488
Cdd:TIGR00458 311 ----EMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLLVERIKAKGLNPEGFKDYLEA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 440214341 489 FRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRLTP 531
Cdd:TIGR00458 386 FSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
75-531 |
6.11e-160 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 461.97 E-value: 6.11e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 75 VPVSELSGQVGKGLVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVisKQMVKFAGNIPKESIIDIQAKPVAvss 154
Cdd:PRK05159 5 HLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVD--EELFETIKKLKRESVVSVTGTVKA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 155 kiESCTEQSLELSVEQIFVISQAKAQLPLQIedaSRPENADdaegLnirvnqDTRLDNRVLDLRTPANQAIFRLEAGVCR 234
Cdd:PRK05159 80 --NPKAPGGVEVIPEEIEVLNKAEEPLPLDI---SGKVLAE----L------DTRLDNRFLDLRRPRVRAIFKIRSEVLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 235 LFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRHLT 314
Cdd:PRK05159 145 AFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 315 EFVGLDLEMAFKYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQYKVDAFKFLEppliLQFADGVAMLREAGVETGD 394
Cdd:PRK05159 225 EYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIPR----ITYDEAIEILKSKGNEISW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 395 EEDLSTPNEKLLGRLVKAKYDTDFYILDKFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKH 474
Cdd:PRK05159 301 GDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYDMLVESIKE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 440214341 475 HGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRLTP 531
Cdd:PRK05159 381 KGLNPESFEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
75-531 |
5.67e-147 |
|
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: 428.70 E-value: 5.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 75 VPVSELSGQ-VGKgLVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQMVKfagNIPKESIIDIQAKPVAVS 153
Cdd:COG0017 3 TYIKDLLPEhVGQ-EVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAK---KLTTESSVEVTGTVVESP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 154 SKiesctEQSLELSVEQIFVISQAKAQLPLQIEDASrpenaddaeglnirvnQDTRLDNRVLDLRTPANQAIFRLEAGVC 233
Cdd:COG0017 79 RA-----PQGVELQAEEIEVLGEADEPYPLQPKRHS----------------LEFLLDNRHLRLRTNRFGAIFRIRSELA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 234 RLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLAQSPQLYKQMAIAAdFDKVYTVGAVFRAEDSNTHRHL 313
Cdd:COG0017 138 RAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 314 TEFVGLDLEMAFkYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQqyKVDAF-KFLEPPLI-LQFADGVAMLREAGVE 391
Cdd:COG0017 217 AEFWMIEPEMAF-ADLEDVMDLAEEMLKYIIKYVLENCPEELEFLGR--DVERLeKVPESPFPrITYTEAIEILKKSGEK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 392 TGDEEDLSTPNEKLLGrlvkAKYDTDFYILDKFPLAIRPFYTMPDPNNPVYSNSYDMFMRG-EEILSGAQRIHDPEYLIE 470
Cdd:COG0017 294 VEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHRYDVLVE 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440214341 471 RAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRLTP 531
Cdd:COG0017 370 RIKEKGLDPEDYEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
205-526 |
1.99e-98 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 300.25 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 205 NQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTV------SYFkdsaYLAQ 278
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 279 SPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRHLtEFVGLDLEMAFKyHYHEVLHTIGNTFTSIFKglrdkyakEIESV 358
Cdd:pfam00152 77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFV-DYEDVMDLTEELIKEIFK--------EVEGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 359 GQ-QYKVDAFKFLEPPLILQFADGVAMLREAGVETgDEEDLSTPNEKLLGRLVKAKYDTDFYILDKFPLAIRPFYTMPDP 437
Cdd:pfam00152 147 AKeLEGGTLLDLKKPFPRITYAEAIEKLNGKDVEE-LGYGSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 438 NNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAA----YIESFRYGCPPHAGGGIGMERVVMLYLGL 513
Cdd:pfam00152 226 DDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEkfgfYLDALKYGAPPHGGLGIGLDRLVMLLTGL 305
|
330
....*....|...
gi 440214341 514 DNIRKTSMFPRDP 526
Cdd:pfam00152 306 ESIREVIAFPKTR 318
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
73-531 |
1.95e-69 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 229.61 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 73 NFVPVSEL--SGQVGKgLVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQmvKFAGNIPKESIIDIQAKPV 150
Cdd:PRK03932 2 MRVSIKDIlkGKYVGQ-EVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYF--EEIKKLTTGSSVIVTGTVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 151 AVSSKiesctEQSLELSVEQIFVISQAKAQLPLQIEDASRpenaddaeglnirvnqDTRLDNRVLDLRTPANQAIFRLEA 230
Cdd:PRK03932 79 ESPRA-----GQGYELQATKIEVIGEDPEDYPIQKKRHSI----------------EFLREIAHLRPRTNKFGAVMRIRN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 231 GVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVS---------YFKDSAYLAQSPQLYKQMAIAAdFDKVYTVGAV 301
Cdd:PRK03932 138 TLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGPT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 302 FRAEDSNTHRHLTEFVGLDLEMAFkYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQYKVDAFKFLEPPLILQFA-- 379
Cdd:PRK03932 217 FRAENSNTRRHLAEFWMIEPEMAF-ADLEDNMDLAEEMLKYVVKYVLENCPDDLEFLNRRVDKGDIERLENFIESPFPri 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 380 ---DGVAMLREAG------VETGDeeDLSTPNEKLLgrlVKAKYDTDFYILDkFPLAIRPFYTMPDPNNPVYSnSYDMFM 450
Cdd:PRK03932 296 tytEAIEILQKSGkkfefpVEWGD--DLGSEHERYL---AEEHFKKPVFVTN-YPKDIKAFYMRLNPDGKTVA-AMDLLA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 451 RG-EEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRL 529
Cdd:PRK03932 369 PGiGEIIGGSQREERLDVLEARIKELGLNKEDYWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFPRTPGRA 448
|
..
gi 440214341 530 TP 531
Cdd:PRK03932 449 EF 450
|
|
| asnS |
TIGR00457 |
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
89-531 |
5.43e-67 |
|
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: 223.41 E-value: 5.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSS--TVQCIlaVGDVISKQMVKFAGNIPKESIIDIQAKPVAVSSKiesctEQSLEL 166
Cdd:TIGR00457 19 VTVSGWVRTKRSSKKIIFLELNDGSSlgPIQAV--INGEDNPYLFQLLKSLTTGSSVSVTGKVVESPGK-----GQPVEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 167 SVEQIFVISQA-KAQLPLQIEDASrpenaddaeglnirvnQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGF 245
Cdd:TIGR00457 92 QVKKIEVVGEAePDDYPLQKKEHS----------------LEFLRDIAHLRLRTNTLGAVMRVRNALSQAIHRYFQENGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 246 TEIHTPKIISAASEGGANVFTVS---------YFKDSAYLAQSPQLYKQmAIAADFDKVYTVGAVFRAEDSNTHRHLTEF 316
Cdd:TIGR00457 156 TWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLE-TYALALSKVYTFGPTFRAEKSNTSRHLSEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 317 VGLDLEMAFkYHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQYKVDAFKFLEPPLILQFA-----DGVAMLREAGVE 391
Cdd:TIGR00457 235 WMIEPEMAF-ANLNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIKRLENIINNKFAritytDAIEILKESDKN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 392 TGDEE----DLSTPNEKLLGRlvkaKYDTDFYILDKFPLAIRPFYTMP-DPNNPVysNSYDMFMRG-EEILSGAQRIHDP 465
Cdd:TIGR00457 314 FEYEDfwgdDLQTEHERFLAE----EYFKPPVFVTNYPKDIKAFYMKLnDDGKTV--AAMDLLAPGiGEIIGGSEREDDL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440214341 466 EYLIERAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKRLTP 531
Cdd:TIGR00457 388 DKLENRMKEMGLDTDALNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTPGNINF 453
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
226-525 |
2.13e-56 |
|
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: 189.61 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 226 FRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDS--AYLAQSPQLYKQMAIAADFDKVYTVGAVFR 303
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGldYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 304 AEDSNThRHLTEFVGLDLEMAFKyHYHEVLHTIGNTFTSIFKGLRDKYAKEIESVgqqykvdafkflepplilqfadgva 383
Cdd:cd00669 81 NEDLRA-RHQPEFTMMDLEMAFA-DYEDVIELTERLVRHLAREVLGVTAVTYGFE------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 384 mlreagvetgdEEDLSTPNEKLLGRLVKAKYDTDFYILDkFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIH 463
Cdd:cd00669 134 -----------LEDFGLPFPRLTYREALERYGQPLFLTD-YPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSRLH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440214341 464 DPEYLIERAKHHGIDTS----KIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRD 525
Cdd:cd00669 202 DPDIQAEVFQEQGINKEagmeYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
206-526 |
7.93e-51 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 177.13 E-value: 7.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 206 QDTRLDNRVLdLRTPANQAIFRLEAGVCRLFRDILTEQGFTEIHTPkIISA--------ASEGGANVFTVSYFKDSAYLA 277
Cdd:PRK06462 11 EEFLRMSWKH-ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPP-IISPstdplmglGSDLPVKQISIDFYGVEYYLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 278 QSPQLYKQMAIAAdFDKVYTVGAVFRAE--DSNTHRHLTEFVGLDLEMAfKYHYHEVLHTIGNTFTSIFKGLRDKYAKEI 355
Cdd:PRK06462 89 DSMILHKQLALRM-LGKIFYLSPNFRLEpvDKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 356 ESVGQQYKVDAFKFLepplILQFADGVAMLREAGVETGDEEDLSTPNEKLLgrlvKAKYDTDFYILDkFPLAIRPFYTMP 435
Cdd:PRK06462 167 EFFGRDLPHLKRPFK----RITHKEAVEILNEEGCRGIDLEELGSEGEKSL----SEHFEEPFWIID-IPKGSREFYDRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 436 DPNNPVYSNSYDMFMR---GEeILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLG 512
Cdd:PRK06462 238 DPERPGVLRNYDLLLPegyGE-AVSGGEREYEYEEIVERIREHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICG 316
|
330
....*....|....
gi 440214341 513 LDNIRKTSMFPRDP 526
Cdd:PRK06462 317 LRHIREVQPFPRVP 330
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
89-187 |
3.32e-45 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic 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 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.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 154.26 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKG-KQCFLILRQQSSTVQCILAVG-DVISKQMVKFAGNIPKESIIDIQAKPVAVSSKIESCTEQSLEL 166
Cdd:cd04320 2 VLIRARVHTSRAQGaKLAFLVLRQQGYTIQGVLAASaEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDVEL 81
|
90 100
....*....|....*....|.
gi 440214341 167 SVEQIFVISQAKAQLPLQIED 187
Cdd:cd04320 82 HIEKIYVVSEAAEPLPFQLED 102
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
93-523 |
6.10e-39 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 149.83 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 93 GRVHTSRAKGKQCFLILRQQSSTVQCilaVGDVISKQMVKfAGNIPKESIIDIQAKPVA-----VSSKIEScteQSLELS 167
Cdd:PRK00476 24 GWVHRRRDHGGLIFIDLRDREGIVQV---VFDPDAEAFEV-AESLRSEYVIQVTGTVRArpegtVNPNLPT---GEIEVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 168 VEQIFVISQAKaQLPLQIEDasrpenaddaeglNIRVNQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTE 247
Cdd:PRK00476 97 ASELEVLNKSK-TLPFPIDD-------------EEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 248 IHTPkIISAASEGGANVFTV-------SYFkdsAyLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRhLTEFVGLD 320
Cdd:PRK00476 163 IETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADR-QPEFTQID 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 321 LEMAF--------------KYHYHEVL-HTIGNTF----------------------------TSIF------------- 344
Cdd:PRK00476 237 IEMSFvtqedvmalmegliRHVFKEVLgVDLPTPFprmtyaeamrrygsdkpdlrfglelvdvTDLFkdsgfkvfagaan 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 345 -----KGLR-------------DKYAKEIESVGQ------QYKVDAF-----KFLEPPlilQFAdgvAMLREAGVETGD- 394
Cdd:PRK00476 317 dggrvKAIRvpggaaqlsrkqiDELTEFAKIYGAkglayiKVNEDGLkgpiaKFLSEE---ELA---ALLERTGAKDGDl 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 395 ------EEDLSTpneKLLGRL-VKAKYDTDFYILDK--------FPL------AIR------PFyTMPDP--------NN 439
Cdd:PRK00476 391 iffgadKAKVVN---DALGALrLKLGKELGLIDEDKfaflwvvdFPMfeydeeEGRwvaahhPF-TMPKDedldeletTD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 440 P--VYSNSYDMFMRGEEILSGAQRIHDPEyLIERA-KHHGIDT----SKIAAYIESFRYGCPPHAGGGIGMERVVMLYLG 512
Cdd:PRK00476 467 PgkARAYAYDLVLNGYELGGGSIRIHRPE-IQEKVfEILGISEeeaeEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAG 545
|
570
....*....|.
gi 440214341 513 LDNIRKTSMFP 523
Cdd:PRK00476 546 ADSIRDVIAFP 556
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
226-523 |
3.54e-37 |
|
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: 138.48 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 226 FRLEAGVCRLFRDILTEQGFTEIHTPkIISAASEGGANVFTVSY--FKDSAY-LAQSPQLYKQMAIAADFDKVYTVGAVF 302
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 303 RAEDSNTHRHlTEFVGLDLEMAFkYHYHEVLHTIGNTFTSIFKGL----------RDKYAKEIESVGqqykvdaFKFL-- 370
Cdd:cd00777 80 RDEDLRADRQ-PEFTQIDIEMSF-VDQEDIMSLIEGLLKYVFKEVlgvelttpfpRMTYAEAMERYG-------FKFLwi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 371 -EPPLilqFADgvamlreagvetgDEEDlstpnekllGRLVKAKY------DTDFYILDKFPLAIRpfytmpdpnnpvyS 443
Cdd:cd00777 151 vDFPL---FEW-------------DEEE---------GRLVSAHHpftapkEEDLDLLEKDPEDAR-------------A 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 444 NSYDMFMRGEEILSGAQRIHDPEyLIERA-KHHGID----TSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRK 518
Cdd:cd00777 193 QAYDLVLNGVELGGGSIRIHDPD-IQEKVfEILGLSeeeaEEKFGFLLEAFKYGAPPHGGIALGLDRLVMLLTGSESIRD 271
|
....*
gi 440214341 519 TSMFP 523
Cdd:cd00777 272 VIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
93-523 |
1.94e-35 |
|
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: 139.75 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 93 GRVHTSRAKGKQCFLILRQQSSTVQCIlaVGDVISKQMVKFAGNIPKESIIDIQAKPVA-----VSSKIESCTeqsLELS 167
Cdd:COG0173 23 GWVHRRRDHGGLIFIDLRDRYGITQVV--FDPDDSAEAFEKAEKLRSEYVIAVTGKVRArpegtVNPKLPTGE---IEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 168 VEQIFVISQAKaQLPLQIEDasrpenaddaeglNIRVNQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQGFTE 247
Cdd:COG0173 98 ASELEILNKAK-TPPFQIDD-------------DTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 248 IHTPkIISAASEGGANVFTV-------SYFkdsAyLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRHLtEFVGLD 320
Cdd:COG0173 164 IETP-ILTKSTPEGARDYLVpsrvhpgKFY---A-LPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-EFTQLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 321 LEMAF-------------------------------KYHYHEVLHTIGN------------TFTSIF------------- 344
Cdd:COG0173 238 IEMSFvdqedvfelmeglirhlfkevlgvelptpfpRMTYAEAMERYGSdkpdlrfglelvDVTDIFkdsgfkvfagaae 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 345 -----KGLR------------DKYAKEIESVGQQ---Y-KVDA-------FKFLePPLILQfadgvAMLREAGVETGD-- 394
Cdd:COG0173 318 nggrvKAINvpggaslsrkqiDELTEFAKQYGAKglaYiKVNEdglkspiAKFL-SEEELA-----AILERLGAKPGDli 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 395 -----EEDLSTpneKLLGRL-VK-AK----YDTDFY----ILDkFPL------AIR------PFyTMPDP-------NNP 440
Cdd:COG0173 392 ffvadKPKVVN---KALGALrLKlGKelglIDEDEFaflwVVD-FPLfeydeeEGRwvamhhPF-TMPKDedldlleTDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 441 --VYSNSYDMFMRGEEILSGAQRIHDPEyLIERA-KHHGID----TSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGL 513
Cdd:COG0173 467 gkVRAKAYDLVLNGYELGGGSIRIHDPE-LQEKVfELLGISeeeaEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGE 545
|
570
....*....|
gi 440214341 514 DNIRKTSMFP 523
Cdd:COG0173 546 DSIRDVIAFP 555
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
72-526 |
3.43e-32 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 130.09 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 72 RNFVPVSELSGQVGKGLVWV------RGRVHTSRAKGKQCFLILRQQS--STVQCIL---AVG-DVISKQMVKFAGNIPK 139
Cdd:PLN02603 87 RKKLRIADVKGGEDEGLARVgktlnvMGWVRTLRAQSSVTFIEVNDGSclSNMQCVMtpdAEGyDQVESGLITTGASVLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 140 ESIIdiqakpvaVSSKiesCTEQSLELSVEQIFVISQAKAQLPLQIEDASRpenaddaEGLNIRVNqdtrldnrvLDLRT 219
Cdd:PLN02603 167 QGTV--------VSSQ---GGKQKVELKVSKIVVVGKSDPSYPIQKKRVSR-------EFLRTKAH---------LRPRT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 220 PANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVS------------------------------Y 269
Cdd:PLN02603 220 NTFGAVARVRNALAYATHKFFQENGFVWVSSPIITASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 270 FKDSAYLAQSPQLYKQMAIAADFDkVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFK-----------YHYHEVLHTIGN 338
Cdd:PLN02603 300 FGKPAFLTVSGQLNGETYATALSD-VYTFGPTFRAENSNTSRHLAEFWMIEPELAFAdlnddmacataYLQYVVKYILEN 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 339 T------F-TSIFKGLRDKYAKEIESvgqqykvdafKFLEppliLQFADGVAMLREA----------GVETGDEEDLSTP 401
Cdd:PLN02603 379 CkedmefFnTWIEKGIIDRLSDVVEK----------NFVQ----LSYTDAIELLLKAkkkfefpvkwGLDLQSEHERYIT 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 402 NEKLLGRLVkakydtdfyILDKFPLAIRPFYtMPDPNNPVYSNSYDMFM-RGEEILSGAQRIHDPEYLIERAKHHGIDTS 480
Cdd:PLN02603 445 EEAFGGRPV---------IIRDYPKEIKAFY-MRENDDGKTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKE 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 440214341 481 KIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDP 526
Cdd:PLN02603 515 SYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVP 560
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
89-531 |
1.93e-27 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 116.62 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAvGDVISKQMVKFAGNIPKESIIDIQAK-----PVAVSSKIEScteQS 163
Cdd:PRK12820 21 VCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFS-PEAAPADVYELAASLRAEFCVALQGEvqkrlEETENPHIET---GD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 164 LELSVEQIFVISQAKAqLPLQIEDASRPENADDAEGLNirVNQDTRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTEQ 243
Cdd:PRK12820 97 IEVFVRELSILAASEA-LPFAISDKAMTAGAGSAGADA--VNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDFLDSR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 244 GFTEIHTPKIISAASEGGANVFTVSYFKDSAY--LAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNTHRHlTEFVGLDL 321
Cdd:PRK12820 174 GFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFTQLDI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 322 EMAF------------------------------KYHYHEVLHTIG--------------------NTFTSIFKG----- 346
Cdd:PRK12820 253 EASFideefifelieeltarmfaiggialprpfpRMPYAEAMDTTGsdrpdlrfdlkfadatdifeNTRYGIFKQilqrg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 347 -------------------LRDKYAKEI-ESVGQQ----YKVDAFKfLEPPLILQFA--DGVAMLREAGVETGD------ 394
Cdd:PRK12820 333 grikginikgqseklsknvLQNEYAKEIaPSFGAKgmtwMRAEAGG-LDSNIVQFFSadEKEALKRRFHAEDGDviimia 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 395 EEDLSTPNEKL------LGRLVKAKYDTDFYIL--DKFPL-----------AIRPFyTMP-----DPNN-----PVYSNS 445
Cdd:PRK12820 412 DASCAIVLSALgqlrlhLADRLGLIPEGVFHPLwiTDFPLfeatddggvtsSHHPF-TAPdredfDPGDieellDLRSRA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 446 YDMFMRGEEILSGAQRIHDPEYLIERAKHHGID----TSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSM 521
Cdd:PRK12820 491 YDLVVNGEELGGGSIRINDKDIQLRIFAALGLSeediEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMILQTPSIREVIA 570
|
570
....*....|
gi 440214341 522 FPRDPKRLTP 531
Cdd:PRK12820 571 FPKNRSAACP 580
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
57-524 |
5.31e-27 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 115.27 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 57 YGLSEMIQSKDKRSERNFVPVSELSGQVGKGLVWVR----GRVHTSRAKGKQCFLILRQQSSTVQCILAVGDviSKQMVK 132
Cdd:PLN02903 39 TVIPVVSAVDSMSSQLTWPSRSHLCGALSVNDVGSRvtlcGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDE--FPEAHR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 133 FAGNIPKESII----DIQAKPV-AVSSKIEScteQSLELSVEQIFVISQAKAQLPLQIEDAsrPENADDaeglnirVNQD 207
Cdd:PLN02903 117 TANRLRNEYVVavegTVRSRPQeSPNKKMKT---GSVEVVAESVDILNVVTKSLPFLVTTA--DEQKDS-------IKEE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 208 TRLDNRVLDLRTPANQAIFRLEAGVCRLFRDILTE-QGFTEIHTPKIISAASEGGANVFTVSYFKDSAYLA--QSPQLYK 284
Cdd:PLN02903 185 VRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLEDvHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYAlpQSPQLFK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 285 QMAIAADFDKVYTVGAVFRAEDSNTHRHlTEFVGLDLEMAF--------------------------------------- 325
Cdd:PLN02903 265 QMLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQLDMELAFtpledmlklnedlirqvfkeikgvqlpnpfprltyaeam 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 326 -KY-------HYHEVLHTIGNTFTS--------------IFKGLR----------------DKYAKEIES---------V 358
Cdd:PLN02903 344 sKYgsdkpdlRYGLELVDVSDVFAEssfkvfagalesggVVKAICvpdgkkisnntalkkgDIYNEAIKSgakglaflkV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 359 GQQYKVDAFKFLEPPLILQFADgvAMLREAGVETGD-----EEDLSTPNEKL----------LGRLVKAKYD----TDFY 419
Cdd:PLN02903 424 LDDGELEGIKALVESLSPEQAE--QLLAACGAGPGDlilfaAGPTSSVNKTLdrlrqfiaktLDLIDPSRHSilwvTDFP 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 420 ILDKFPLAIR------PFyTMPDPNNP-----VYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGID----TSKIAA 484
Cdd:PLN02903 502 MFEWNEDEQRlealhhPF-TAPNPEDMgdlssARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSpeeaESKFGY 580
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 440214341 485 YIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPR 524
Cdd:PLN02903 581 LLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPK 620
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
70-523 |
8.88e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 108.58 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 70 SERNFVPVSELS---GQVGKG------LVWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQMVK-FAGNIPK 139
Cdd:PTZ00385 82 SFRGITPISEVReryGYLASGdraaqaTVRVAGRVTSVRDIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKkLKVSLRV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 140 ESIIDIQAKPvavsskiesCTEQSLELSVeqifVISQAKAQLPLQIEDASRpenADDAEGLNIRVNQDTRLDNRVLDLRT 219
Cdd:PTZ00385 162 GDIIGADGVP---------CRMQRGELSV----AASRMLILSPYVCTDQVV---CPNLRGFTVLQDNDVKYRYRFTDMMT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 220 -PANQAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAASEGGANVFTVSYFKDSA--YLAQSPQLYKQMAIAADFDKVY 296
Cdd:PTZ00385 226 nPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMdlFLRVAPELHLKQCIVGGMERIY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 297 TVGAVFRAEDSNtHRHLTEFVGLDLEMAfkYHYHEVLHTIGNtftSIFK--GLRDKYAKEIE-----SVGQQYKVDAFKf 369
Cdd:PTZ00385 306 EIGKVFRNEDAD-RSHNPEFTSCEFYAA--YHTYEDLMPMTE---DIFRqlAMRVNGTTVVQiypenAHGNPVTVDLGK- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 370 lePPLILQFADGVAmlREAGVETGDEEDLSTPNEKLLGRLVKAKYD----------------TDFYILDKFplaIRPFYT 433
Cdd:PTZ00385 379 --PFRRVSVYDEIQ--RMSGVEFPPPNELNTPKGIAYMSVVMLRYNiplppvrtaakmfeklIDFFITDRV---VEPTFV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 434 MPDP-----------NNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSK--------IAAYIESFRYGCP 494
Cdd:PTZ00385 452 MDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGgdeeamplDETFLKSLQVGLP 531
|
490 500
....*....|....*....|....*....
gi 440214341 495 PHAGGGIGMERVVMLYLGLDNIRKTSMFP 523
Cdd:PTZ00385 532 PTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
243-526 |
8.16e-21 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 95.86 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 243 QGFTEIHTPKIISAASEGGANVFTVS------------------------------------------------------ 268
Cdd:PTZ00425 232 RGFLYIHTPLITTSDCEGGGEMFTVTtllgedadyraiprvnkknkkgekredilntcnannnngnssssnavsspaypd 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 269 ---------YFKDSAYLAQSPQLYKQmAIAADFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAF-------------- 325
Cdd:PTZ00425 312 qylidykkdFFSKQAFLTVSGQLSLE-NLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFadlydnmelaesyi 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 326 KY--------HYHEVLHTIGNTFTSIFKGLRDKYAKEIESVGQQYKVDafkfleppLILQFADGVamlrEAGVETGdeED 397
Cdd:PTZ00425 391 KYcigyvlnnNFDDIYYFEENVETGLISRLKNILDEDFAKITYTNVID--------LLQPYSDSF----EVPVKWG--MD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 398 LSTPNEKLLGRLVKAKYdtdfYILDKFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGI 477
Cdd:PTZ00425 457 LQSEHERFVAEQIFKKP----VIVYNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKL 532
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 440214341 478 DTSKIAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDP 526
Cdd:PTZ00425 533 NMESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
89-523 |
9.02e-21 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 95.51 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQmvkFAGNIPKESIIDIqakpVAVSSKIESCTEQSLELSV 168
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGV---YNDQFKKWDLGDI----IGARGTLFKTQTGELSIHC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 169 EQIFVISQAKAQLPlqiedasrpenaDDAEGLNirvNQDTRLDNRVLDL-RTPANQAIFRLEAGVCRLFRDILTEQGFTE 247
Cdd:PRK12445 141 TELRLLTKALRPLP------------DKFHGLQ---DQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFME 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 248 IHTPKIISAASEGGANVFTVSY--FKDSAYLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNThRHLTEFVGLDLEMAF 325
Cdd:PRK12445 206 VETPMMQVIPGGASARPFITHHnaLDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAY 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 326 KyHYHEVLHTIGNTFTSIFKGLRDK----YAKEIESVGQQYKV----DAFKFLEPPLIL----QFADGVAMLREAGVETG 393
Cdd:PRK12445 285 A-DYHDLIELTESLFRTLAQEVLGTtkvtYGEHVFDFGKPFEKltmrEAIKKYRPETDMadldNFDAAKALAESIGITVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 394 DEEDLSTPNEKLLGRLVKAKYDTDFYILDkFPLAIRPFYTMPDPNnPVYSNSYDMFMRGEEILSGAQRIHDPEYLIER-- 471
Cdd:PRK12445 364 KSWGLGRIVTEIFDEVAEAHLIQPTFITE-YPAEVSPLARRNDVN-PEITDRFEFFIGGREIGNGFSELNDAEDQAERfq 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 440214341 472 ----AKHHGIDTSKI--AAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFP 523
Cdd:PRK12445 442 eqvnAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
226-523 |
2.00e-20 |
|
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: 92.26 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 226 FRLEAGVCRLFRDILTEQGFTEIHTPKIISAAseGGANV--FTVSY--FKDSAYLAQSPQLYKQMAIAADFDKVYTVGAV 301
Cdd:cd00775 8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpFITHHnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 302 FRAEDSNThRHLTEFVGLDLEMAFKyHYHEVLhtignTFT-SIFKGLRDKYAKEIESVGQQYKVDafkfLEPPL-ILQFA 379
Cdd:cd00775 86 FRNEGIDL-THNPEFTMIEFYEAYA-DYNDMM-----DLTeDLFSGLVKKINGKTKIEYGGKELD----FTPPFkRVTMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 380 DGVAmlREAGVETGDEEDLSTPN-EKLLGRLVKAKYD---TDFYILDK------------------FPLAIRPFyTMPDP 437
Cdd:cd00775 155 DALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL-AKRHR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 438 NNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIER------AKHHGIDTSKI--AAYIESFRYGCPPHAGGGIGMERVVML 509
Cdd:cd00775 232 SNPGLTERFELFICGKEIANAYTELNDPFDQRERfeeqakQKEAGDDEAMMmdEDFVTALEYGMPPTGGLGIGIDRLVML 311
|
330
....*....|....
gi 440214341 510 YLGLDNIRKTSMFP 523
Cdd:cd00775 312 LTDSNSIRDVILFP 325
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
265-528 |
3.43e-20 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 93.91 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 265 FTVSYFKDSAYLAQSPQLYKQmAIAADFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKyHYHEVLHTIGNTFTSIF 344
Cdd:PLN02221 300 YSKDFFGRQAFLTVSGQLQVE-TYACALSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFA-DLEDDMNCAEAYVKYMC 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 345 KGLRDKYAKEIESVGQQYK---VDAFKFLE--PPLILQFADGVAMLREAgVETGDEE--------DLSTPNEKLLGRLVK 411
Cdd:PLN02221 378 KWLLDKCFDDMELMAKNFDsgcIDRLRMVAstPFGRITYTEAIELLEEA-VAKGKEFdnnvewgiDLASEHERYLTEVLF 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 412 AKYdtdfYILDKFPLAIRPFYTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFRY 491
Cdd:PLN02221 457 QKP----LIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKQRIEEMGLPIEPYEWYLDLRRY 532
|
250 260 270
....*....|....*....|....*....|....*..
gi 440214341 492 GCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPRDPKR 528
Cdd:PLN02221 533 GTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
89-523 |
6.45e-18 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 86.97 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQ--CILAVGDVISKQMVKFAGNIPKESIIDIQAKPvavsskieSCTEQSlEL 166
Cdd:PLN02502 111 VSVAGRIMAKRAFGKLAFYDLRDDGGKIQlyADKKRLDLDEEEFEKLHSLVDRGDIVGVTGTP--------GKTKKG-EL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 167 SveqIFVIS---QAKAQLPLqiedasrpenADDAEGLNirvNQDTRLDNRVLDL-RTPANQAIFRLEAGVCRLFRDILTE 242
Cdd:PLN02502 182 S---IFPTSfevLTKCLLML----------PDKYHGLT---DQETRYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 243 QGFTEIHTPKIISAAseGGANV--FtVSYFKD---SAYLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNThRHLTEFV 317
Cdd:PLN02502 246 RGFLEVETPMLNMIA--GGAAArpF-VTHHNDlnmDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGIST-RHNPEFT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 318 GLDLEMAFKyHYHEVLHTIGNTFTSIFKGLRDKY-----AKEIESVGQQYKVDAFKFLEPPLILQFADGV--AMLREAGV 390
Cdd:PLN02502 322 TCEFYQAYA-DYNDMMELTEEMVSGMVKELTGSYkikyhGIEIDFTPPFRRISMISLVEEATGIDFPADLksDEANAYLI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 391 ETGDEEDLSTPNEKLLGRLVkakyDTDF------------YILDkFPLAIRPFyTMPDPNNPVYSNSYDMFMRGEEILSG 458
Cdd:PLN02502 401 AACEKFDVKCPPPQTTGRLL----NELFeefleetlvqptFVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELANA 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440214341 459 AQRIHDP----EYLIERAKHHGIDTSKIAAYIESF----RYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFP 523
Cdd:PLN02502 475 FSELTDPvdqrERFEEQVKQHNAGDDEAMALDEDFctalEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
89-176 |
1.34e-17 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 77.61 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISkqMVKFAGNIPKESIIDIQAKPVAvsSKIESCTEQSLELSV 168
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGE--FFEEAEKLRTESVVGVTGTVVK--RPEGNLATGEIELQA 77
|
....*...
gi 440214341 169 EQIFVISQ 176
Cdd:cd04100 78 EELEVLSK 85
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
205-523 |
2.71e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 85.06 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 205 NQDTRLDNRVLDLRTPAN-QAIFRLEAGVCRLFRDILTEQGFTEIHTPKIISAAseGGANVFT-VSYFKD---SAYLAQS 279
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINEStRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVA--GGANARPfITHHNDldlDLYLRIA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 280 PQLYKQMAIAADFDKVYTVGAVFRAED-SNTHRhlTEFVGLDLEMAFKYHY-----------HEVLHTIGNTFTSIFKGL 347
Cdd:PTZ00417 309 TELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYADFYdlikwsedffsQLVMHLFGTYKILYNKDG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 348 RDKYAKEIESVGQQYKVDAFKFLEP---PLILQFADGVAMLrEAGVETGDEEDLSTPN----EKLLGRLvkakydTDFYI 420
Cdd:PTZ00417 387 PEKDPIEIDFTPPYPKVSIVEELEKltnTKLEQPFDSPETI-NKMINLIKENKIEMPNpptaAKLLDQL------ASHFI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 421 LDKFPlaIRPFYTMPDP-----------NNPVYSNSYDMFMRGEEILSGAQRIHDPEYLIERAKHHGIDTSK-------- 481
Cdd:PTZ00417 460 ENKYP--NKPFFIIEHPqimsplakyhrSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKgdaeafqf 537
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 440214341 482 IAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFP 523
Cdd:PTZ00417 538 DAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP 579
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
93-523 |
1.00e-13 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 73.58 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 93 GRVHTSRAKGKQCFLILRQQSSTVQCILAVgDVISKQMVKFAGNIpkeSIIDIqakpVAVSSKIesCTEQSLELSV--EQ 170
Cdd:PRK00484 61 GRVMLKRVMGKASFATLQDGSGRIQLYVSK-DDVGEEALEAFKKL---DLGDI----IGVEGTL--FKTKTGELSVkaTE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 171 IFVISqaKAQLPLqiedasrPENADdaeGLNirvNQDTRLDNRVLDLRT-PANQAIFRLEAGVCRLFRDILTEQGFTEIH 249
Cdd:PRK00484 131 LTLLT--KSLRPL-------PDKFH---GLT---DVETRYRQRYVDLIVnPESRETFRKRSKIISAIRRFLDNRGFLEVE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 250 TPKIISAAseGGANV--FT--VSYFKDSAYLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNThRHLTEFVGLDLEMAF 325
Cdd:PRK00484 196 TPMLQPIA--GGAAArpFIthHNALDIDLYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 326 K-YH---------YHEVLHTIGNTFTSIFKGlrdkyaKEIeSVGQQYK----VDAFKFL--EPPLILQFADGVAMLREAG 389
Cdd:PRK00484 273 AdYNdmmdlteelIRHLAQAVLGTTKVTYQG------TEI-DFGPPFKrltmVDAIKEYtgVDFDDMTDEEARALAKELG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 390 VETGDEEDLSTPNEKLLGRLVKAKYDTDFYILDkFPLAIRPFyTMPDPNNPVYSNSYDMFMRGEEILSGAQRIHDP---- 465
Cdd:PRK00484 346 IEVEKSWGLGKLINELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAFSELNDPidqr 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440214341 466 EYLIE--RAKH------HGIDtskiAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFP 523
Cdd:PRK00484 424 ERFEAqvEAKEagddeaMFMD----EDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
91-523 |
2.40e-13 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 72.37 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 91 VRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQMVKFA----GNIpkesiidIQAKPVAVSSKIEscteqslEL 166
Cdd:COG1190 61 VAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDELGEEAYELFKlldlGDI-------VGVEGTVFRTKTG-------EL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 167 SV--EQIFVISqaKAQLPLqiedasrPENADdaeGLNirvNQDTRLDNRVLDLRT-PANQAIFRLEAGVCRLFRDILTEQ 243
Cdd:COG1190 127 SVkvEELTLLS--KSLRPL-------PEKFH---GLT---DPETRYRQRYVDLIVnPEVRETFRKRSKIIRAIRRFLDER 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 244 GFTEIHTPKIISAAseGGANvftvsyfkdsA--------------YLAQSPQLYKQMAIAADFDKVYTVGAVFRAEDSNT 309
Cdd:COG1190 192 GFLEVETPMLQPIA--GGAA----------ArpfithhnaldmdlYLRIAPELYLKRLIVGGFERVFEIGRNFRNEGIDT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 310 hRHLTEFVGLDLEMAFKyHYHEVLHTIGNTFTSIFKGLRDKYakEIEsvGQQYKVDafkfLEPP--------LILQFAdG 381
Cdd:COG1190 260 -THNPEFTMLELYQAYA-DYNDMMDLTEELIREAAEAVLGTT--KVT--YQGQEID----LSPPwrritmveAIKEAT-G 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 382 V------------AMLREAGVETGDEEDLSTPNEKLLGRLVKAKYDTDFYILDkFPLAIRPFyTMPDPNNPVYSNSYDMF 449
Cdd:COG1190 329 IdvtpltddeelrALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTD-YPVEVSPL-AKRHRDDPGLTERFELF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 450 MRGEEILSGAQRIHDP--------EYLIERAK----HHGIDtskiAAYIESFRYGCPPHAGGGIGMERVVMLYLGLDNIR 517
Cdd:COG1190 407 IAGREIANAFSELNDPidqrerfeEQLELKAAgddeAMPMD----EDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIR 482
|
....*.
gi 440214341 518 KTSMFP 523
Cdd:COG1190 483 DVILFP 488
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
265-524 |
3.09e-12 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 69.13 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 265 FTVSYFKDSAYLAQSPQLYKQmAIAADFDKVYTVGAVFRAEDSNTHRHLTEFVGLDLEMAFKyHYHEVLHTIGNTFTSIF 344
Cdd:PLN02532 363 FSKDFFSRPTYLTVSGRLHLE-SYACALGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFS-ELEDAMNCAEDYFKFLC 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 345 KGLRDKYAKEIESVGQQYKVDAFKFLE-----PPLILQFADGVAMLREA---GVETGDEEDLSTPNEKLlgrlvkaKYDT 416
Cdd:PLN02532 441 KWVLENCSEDMKFVSKRIDKTISTRLEaiissSLQRISYTEAVDLLKQAtdkKFETKPEWGIALTTEHL-------SYLA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 417 D-FY----ILDKFPLAIRPFYTMPDPNNPVYSnSYDMFM-RGEEILSGAQRIHDPEYLIERAKHHGIDTSKIAAYIESFR 490
Cdd:PLN02532 514 DeIYkkpvIIYNYPKELKPFYVRLNDDGKTVA-AFDLVVpKVGTVITGSQNEERMDILNARIEELGLPREQYEWYLDLRR 592
|
250 260 270
....*....|....*....|....*....|....
gi 440214341 491 YGCPPHAGGGIGMERVVMLYLGLDNIRKTSMFPR 524
Cdd:PLN02532 593 HGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
89-523 |
1.55e-11 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 67.30 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDVISKQMVKFAGNIPKESIIDIQAKPVAvsSKiescteqSLELSV 168
Cdd:PRK02983 654 VSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLADFRAAVDLGDLVEVTGTMGT--SR-------NGTLSL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 169 eqiFVIS---QAKAQLPLqiedasrPenaDDAEGLNirvNQDTRLDNRVLDLRT-PANQAIFRLEAGVCRLFRDILTEQG 244
Cdd:PRK02983 725 ---LVTSwrlAGKCLRPL-------P---DKWKGLT---DPEARVRQRYLDLAVnPEARDLLRARSAVVRAVRETLVARG 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 245 FTEIHTPkiISAASEGGANV--FTV---SYFKDsAYLAQSPQLY-KQMAIAAdFDKVYTVGAVFRAE------------- 305
Cdd:PRK02983 789 FLEVETP--ILQQVHGGANArpFVThinAYDMD-LYLRIAPELYlKRLCVGG-VERVFELGRNFRNEgvdathnpeftll 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 306 -------DSNTHRHLTEfvGLDLEMAFKYHYHEVL----HTIGNTFTSI-----FKGLRDKYAkeiESVGQQYKVDAfkf 369
Cdd:PRK02983 865 eayqahaDYDTMRDLTR--ELIQNAAQAAHGAPVVmrpdGDGVLEPVDIsgpwpVVTVHDAVS---EALGEEIDPDT--- 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 370 lepplilqfadGVAMLRE----AGVETGDEEDLSTPNEKLLGRLVKAKydTD---FYIldKFPLAIRPFyTMPDPNNPVY 442
Cdd:PRK02983 937 -----------PLAELRKlcdaAGIPYRTDWDAGAVVLELYEHLVEDR--TTfptFYT--DFPTSVSPL-TRPHRSDPGL 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 443 SNSYDMFMRGEEILSGAQRIHDPeyLIERAKHHgiDTSKIAA------------YIESFRYGCPPHAGGGIGMERVVMLY 510
Cdd:PRK02983 1001 AERWDLVAWGVELGTAYSELTDP--VEQRRRLT--EQSLLAAggdpeameldedFLQALEYAMPPTGGLGMGVDRLVMLL 1076
|
490
....*....|...
gi 440214341 511 LGLdNIRKTSMFP 523
Cdd:PRK02983 1077 TGR-SIRETLPFP 1088
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
234-505 |
1.32e-10 |
|
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: 60.98 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 234 RLFRDILTEQGFTEIHTPKIISAASEGGAN------VFTVSYFKDSAYLAQSPQLYKQMA----IAADFDKVYTVGAVFR 303
Cdd:cd00768 7 QKLRRFMAELGFQEVETPIVEREPLLEKAGhepkdlLPVGAENEEDLYLRPTLEPGLVRLfvshIRKLPLRLAEIGPAFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 304 AEDSNTH-RHLTEFVGLDLEMAFKY--HYHEVLHTIGNTFtsifkglrdkyakeiesvgqqykvdafkflepplilqfad 380
Cdd:cd00768 87 NEGGRRGlRRVREFTQLEGEVFGEDgeEASEFEELIELTE---------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 381 gvAMLREAGVETGDEEDLSTPNEKLLGrlvKAKYDTDFyildkfplairpFYTMPDPnnpvysnsydmfmRGEEILSGAQ 460
Cdd:cd00768 127 --ELLRALGIKLDIVFVEKTPGEFSPG---GAGPGFEI------------EVDHPEG-------------RGLEIGSGGY 176
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 440214341 461 RIHDPEYLIERAKhhgidtskiaaYIESFRYGCPPHAGGGIGMER 505
Cdd:cd00768 177 RQDEQARAADLYF-----------LDEALEYRYPPTIGFGLGLER 210
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
89-183 |
6.90e-09 |
|
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: 53.47 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQcILAVGDVISKQMVKFAGNIPKESIIDIQAKpVAVSSKIEScteqSLELSV 168
Cdd:cd04316 15 VTVAGWVHEIRDLGGIKFVILRDREGIVQ-VTAPKKKVDKELFKTVRKLSRESVISVTGT-VKAEPKAPN----GVEIIP 88
|
90
....*....|....*
gi 440214341 169 EQIFVISQAKAQLPL 183
Cdd:cd04316 89 EEIEVLSEAKTPLPL 103
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
93-220 |
3.17e-08 |
|
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: 52.52 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 93 GRVHTSRAKGKQCFLILRQQSSTVQCILavgDVISKQMVKFAGNIPKESIIDIQAKpvaVSSKIESCTEQSL-----ELS 167
Cdd:cd04317 21 GWVQRRRDHGGLIFIDLRDRYGIVQVVF---DPEEAPEFELAEKLRNESVIQVTGK---VRARPEGTVNPKLptgeiEVV 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 440214341 168 VEQIFVISQAKaQLPLQIEDasrpenaddaeglNIRVNQDTRLDNRVLDLRTP 220
Cdd:cd04317 95 ASELEVLNKAK-TLPFEIDD-------------DVNVSEELRLKYRYLDLRRP 133
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
89-174 |
1.36e-06 |
|
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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440214341 89 VWVRGRVHT-SRAKGKQCFLILRQQSSTVQCILAvgdviSKQMVKFAGNIPKESIIDIQAKPVAVsskiescTEQSLELS 167
Cdd:pfam01336 1 VTVAGRVTSiRRSGGKLLFLTLRDGTGSIQVVVF-----KEEAEKLAKKLKEGDVVRVTGKVKKR-------KGGELELV 68
|
....*..
gi 440214341 168 VEQIFVI 174
Cdd:pfam01336 69 VEEIELL 75
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
89-125 |
4.39e-04 |
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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: 39.14 E-value: 4.39e-04
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gi 440214341 89 VWVRGRVHTSRAKGKQCFLILRQQSSTVQCILAVGDV 125
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLV 38
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