|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
24-579 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 799.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 24 GEMVSKSELKKRIKQRQVEAKKAAKKAAAQPKPASKKK-------TDLFADLDPSQYFETRSRQIQELRKTHEpNPYPHK 96
Cdd:PLN02502 5 GEPLSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAAKgrsrksaAADDETMDPTQYRANRLKKVEALRAKGV-EPYPYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 97 FHVSISNPEFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQLQDY-CDPDSYEKDHDLLK 175
Cdd:PLN02502 84 FDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFEKLHSLVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 176 RGDIVGVEGYVGRTqpKKGgegEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIR 255
Cdd:PLN02502 163 RGDIVGVTGTPGKT--KKG---ELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 256 YIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHN 335
Cdd:PLN02502 238 YIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 336 PEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHPdpadpakeLELNFSRPWKRINMIEELEKVFNVKFPSG 415
Cdd:PLN02502 318 PEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHG--------IEIDFTPPFRRISMISLVEEATGIDFPAD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 416 dqLHTAETGEFLKKILVDNKLECPPPLTNARMLDKLVGE-LEDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVA 494
Cdd:PLN02502 390 --LKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEfLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFIN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 495 TKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PLN02502 468 GRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
....*
gi 135139 575 TLKPD 579
Cdd:PLN02502 548 AMKPQ 552
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
69-580 |
0e+00 |
|
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273107 [Multi-domain] Cd Length: 493 Bit Score: 778.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 69 DPSQYFETRSRQIQELRKTHEpNPYPHKFHVSISNPEFLAKYAHLKKGE-TLPEEKVSIAGRIHAKReSGSKLKFYVLHG 147
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGN-NPYLHKFERTHSAQEFQEKYADLSNEElKEKELKVSIAGRIKAIR-SMGKATFITLQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 148 DGVEVQLMSQLQDYCDpDSYEKDHDLLKRGDIVGVEGYvgrtqPKKGGEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQE 227
Cdd:TIGR00499 79 ESGQIQLYVNKNKLPE-DFYEFDEYLLDLGDIIGVTGY-----PFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 228 TRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFL 307
Cdd:TIGR00499 153 TRYRQRYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 308 KQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYhpdpadpaKEL 387
Cdd:TIGR00499 233 KRLIVGGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY--------NDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 388 ELNFSRPWKRINMIEELEKVFNVkfpSGDQLHTAETGEFLKKILVDNKLECppPLTNARMLDKLVGE-LEDTCINPTFIF 466
Cdd:TIGR00499 305 EIDLKPPWKRITMVDALEMVTGI---DFDILKDDETAKALAKEHGIEVAED--SLTLGHILNKFFEQfLEHTLIQPTFIT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 467 GHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPP 546
Cdd:TIGR00499 380 HYPAEISPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPP 459
|
490 500 510
....*....|....*....|....*....|....
gi 135139 547 TGGWGCGIDRLAMFLTDSNTIREVLLFPTLKPDV 580
Cdd:TIGR00499 460 TGGLGIGIDRLVMLLTDAPSIRDVLLFPQLRPQK 493
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
69-578 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 676.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 69 DPSQYFETRSRQIQELRKTHEpNPYPHKFHVSISNPEFLAKYAHLKKGETLP-EEKVSIAGRIHAKRESGsKLKFYVLHG 147
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGI-DPYPNKFERTHTAAELRAKYDDKEKEELEElEIEVSVAGRVMLKRVMG-KASFATLQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 148 DGVEVQLMSQLQDYCDpDSYE--KDHDLlkrGDIVGVEGYVGRTQpkkggEGEVSVFVSRVQLLTPCLHMLPADHFGFKD 225
Cdd:PRK00484 80 GSGRIQLYVSKDDVGE-EALEafKKLDL---GDIIGVEGTLFKTK-----TGELSVKATELTLLTKSLRPLPDKFHGLTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 226 QETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPEL 305
Cdd:PRK00484 151 VETRYRQRYVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 306 FLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHpdpadpak 385
Cdd:PRK00484 231 YLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQ-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 386 ELELNFSRPWKRINMIEELEKVFNVKFpsgdqlhTAETGEFLKKILVDNKLECPPPLTNARMLDKLVGEL-EDTCINPTF 464
Cdd:PRK00484 303 GTEIDFGPPFKRLTMVDAIKEYTGVDF-------DDMTDEEARALAKELGIEVEKSWGLGKLINELFEEFvEPKLIQPTF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 465 IFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGL 544
Cdd:PRK00484 376 ITDYPVEISPLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGM 455
|
490 500 510
....*....|....*....|....*....|....
gi 135139 545 PPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKP 578
Cdd:PRK00484 456 PPTGGLGIGIDRLVMLLTDSPSIRDVILFPLMRP 489
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
69-578 |
0e+00 |
|
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: 675.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 69 DPSQYFETRSRQIQELRKTHEpNPYPHKFHVSISNPEFLAKYAHLKKGETLPEEkVSIAGRIHAKRESGsKLKFYVLHGD 148
Cdd:COG1190 6 DLNEQIRVRREKLEELREAGI-DPYPNKFPRTHTAAEIREKYDELEAEEETGDE-VSVAGRIMAKRDMG-KASFADLQDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 149 GVEVQLMSQLQDYCDpDSYE--KDHDLlkrGDIVGVEGYVGRTQpkkggEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQ 226
Cdd:COG1190 83 SGRIQLYLRRDELGE-EAYElfKLLDL---GDIVGVEGTVFRTK-----TGELSVKVEELTLLSKSLRPLPEKFHGLTDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 227 ETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELF 306
Cdd:COG1190 154 ETRYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 307 LKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYhpdpadpaKE 386
Cdd:COG1190 234 LKRLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY--------QG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 387 LELNFSRPWKRINMIEELEKVFNVKFpsgDQLHTAETgefLKKILVDNKLECPPPLTNARMLDKLVGEL-EDTCINPTFI 465
Cdd:COG1190 306 QEIDLSPPWRRITMVEAIKEATGIDV---TPLTDDEE---LRALAKELGIEVDPGWGRGKLIDELFEELvEPKLIQPTFV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 466 FGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLP 545
Cdd:COG1190 380 TDYPVEVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMP 459
|
490 500 510
....*....|....*....|....*....|...
gi 135139 546 PTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKP 578
Cdd:COG1190 460 PTGGLGIGIDRLVMLLTDSPSIRDVILFPLMRP 492
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
240-578 |
0e+00 |
|
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: 597.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 240 NKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVY 319
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 320 EIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYhpdpadpaKELELNFSRPWKRIN 399
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY--------GGKELDFTPPFKRVT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 400 MIEELEKVFNVKFPSGDQLHTAETgefLKKILVDNKLECPPPLTNARMLDKLVGE-LEDTCINPTFIFGHPQMMSPLAKY 478
Cdd:cd00775 153 MVDALKEKTGIDFPELDLEQPEEL---AKLLAKLIKEKIEKPRTLGKLLDKLFEEfVEPTLIQPTFIIDHPVEISPLAKR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 479 SRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLA 558
Cdd:cd00775 230 HRSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLV 309
|
330 340
....*....|....*....|
gi 135139 559 MFLTDSNTIREVLLFPTLKP 578
Cdd:cd00775 310 MLLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
60-578 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 576.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 60 KKTDLFADLDPSQYFETRSRQIQElRKTHEPNPYPHKFHVSISNPEFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGSK 139
Cdd:PTZ00417 72 KKKEEEAEVDPRLYYENRSKFIQE-QKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 140 LKFYVLHGDGVEVQLMSQ--LQDYcDPDSYEKDHDLLKRGDIVGVEGYvgrtqPKKGGEGEVSVFVSRVQLLTPCLHMLP 217
Cdd:PTZ00417 151 LRFFDLVGDGAKIQVLANfaFHDH-TKSNFAECYDKIRRGDIVGIVGF-----PGKSKKGELSIFPKETIILSPCLHMLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 218 ADhFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDM 297
Cdd:PTZ00417 225 MK-YGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 298 YMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYH 377
Cdd:PTZ00417 304 YLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYN 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 378 PDpaDPAKE-LELNFSRPWKRINMIEELEKVFNVKFPSgdQLHTAETGEFLKKILVDNKLECPPPLTNARMLDKLVGELE 456
Cdd:PTZ00417 384 KD--GPEKDpIEIDFTPPYPKVSIVEELEKLTNTKLEQ--PFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFI 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 457 DTCIN--PTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDE 534
Cdd:PTZ00417 460 ENKYPnkPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDA 539
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 135139 535 TFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKP 578
Cdd:PTZ00417 540 AFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
105-587 |
2.18e-142 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 427.53 E-value: 2.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 105 EFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIVGVEG 184
Cdd:PTZ00385 91 EVRERYGYLASGDRAAQATVRVAGRVTSVRDIG-KIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIGADG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 185 YVGRTQpkkggEGEVSVFVSRVQLLTPCL---HMLPADHFGF---KDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIR 258
Cdd:PTZ00385 170 VPCRMQ-----RGELSVAASRMLILSPYVctdQVVCPNLRGFtvlQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 259 RFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEF 338
Cdd:PTZ00385 245 DYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 339 TTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHPDPADpAKELELNFSRPWKRINMIEELEKVFNVKFPSGDQL 418
Cdd:PTZ00385 325 TSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAH-GNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNEL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 419 HTAETGEFLKKILVDNKLECPPPLTNARMLDKLVG-ELEDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKE 497
Cdd:PTZ00385 404 NTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDfFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 498 ICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLK 577
Cdd:PTZ00385 484 YCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
490
....*....|
gi 135139 578 PDVLREEVKK 587
Cdd:PTZ00385 564 QDIRSHDSKR 573
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
117-579 |
2.05e-130 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 408.58 E-value: 2.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 117 ETLPEEKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQlQDYCDPDSYEKDHDLLKRGDIVGVEGYVGRTQpkkggE 196
Cdd:PRK02983 647 DAPTGEEVSVSGRVLRIRDYG-GVLFADLRDWSGELQVLLD-ASRLEQGSLADFRAAVDLGDLVEVTGTMGTSR-----N 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 197 GEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNV 276
Cdd:PRK02983 720 GTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLLRARSAVVRAVRETLVARGFLEVETPILQQ 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 277 IAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADvYDLM-D 355
Cdd:PRK02983 800 VHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTLLEAYQAHAD-YDTMrD 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 356 MTELMFSEMVKEITGSYIIkyhPDPADPAKELELNFSRPWKRINMIEEL-EKVfnvkfpsGDQLhTAETG-EFLKKILVD 433
Cdd:PRK02983 879 LTRELIQNAAQAAHGAPVV---MRPDGDGVLEPVDISGPWPVVTVHDAVsEAL-------GEEI-DPDTPlAELRKLCDA 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 434 NKLECPPPLTNARMLDKLVGEL-EDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQR 512
Cdd:PRK02983 948 AGIPYRTDWDAGAVVLELYEHLvEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELGTAYSELTDPVEQR 1027
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 135139 513 ARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTdSNTIREVLLFPTLKPD 579
Cdd:PRK02983 1028 RRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPLVKPR 1093
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
123-578 |
6.45e-116 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 353.98 E-value: 6.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 123 KVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQlQDYCDPDSYEKDHDLLKRGDIVGVEGYVGRTQpkkggEGEVSVF 202
Cdd:PRK12445 67 EVSVAGRMMTRRIMG-KASFVTLQDVGGRIQLYVA-RDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQ-----TGELSIH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 203 VSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGAT 282
Cdd:PRK12445 140 CTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGAS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 283 AKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFS 362
Cdd:PRK12445 220 ARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 363 EMVKEITGSYIIKYhpdpadpaKELELNFSRPWKRINMIEELEKvfnvKFPSGDqLHTAETGEFLKKILVDNKLECPPPL 442
Cdd:PRK12445 300 TLAQEVLGTTKVTY--------GEHVFDFGKPFEKLTMREAIKK----YRPETD-MADLDNFDAAKALAESIGITVEKSW 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 443 TNARMLDKLVGEL-EDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQ 521
Cdd:PRK12445 367 GLGRIVTEIFDEVaEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 135139 522 KDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKP 578
Cdd:PRK12445 447 KAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRP 503
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
225-577 |
3.23e-109 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 330.30 E-value: 3.23e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 225 DQETRYRKRYLDLiMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPE 304
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 305 LFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHPDpadpa 384
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGGT----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 385 kelELNFSRPWKRINMIEELEKVfnvkfpsgdqlhtAETGEFLKKILVDNKLEcpppltnaRMLDKLVGELEDtcINPTF 464
Cdd:pfam00152 155 ---LLDLKKPFPRITYAEAIEKL-------------NGKDVEELGYGSDKPDL--------RFLLELVIDKNK--FNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 465 IFGHPQMMSPLAKYSR-DQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKdqgdDEAQLVDETFCNALEYG 543
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDeDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 135139 544 LPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLK 577
Cdd:pfam00152 285 APPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
247-578 |
5.34e-89 |
|
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: 276.28 E-value: 5.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 247 FITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFR 326
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 327 NEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYhpdpadpaKELELNFSRPWKRINMIEELEK 406
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY--------GFELEDFGLPFPRLTYREALER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 407 VfnvkfpsgdqlhtaetgeflkkilvdnklecpppltnarmldklvgeledtcINPTFIFGHP-QMMSPLAKYSRDQPGL 485
Cdd:cd00669 153 Y----------------------------------------------------GQPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 486 CERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEaqlvDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSN 565
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 135139 566 TIREVLLFPTLKP 578
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
260-571 |
1.69e-52 |
|
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]
Pssm-ID: 273090 [Multi-domain] Cd Length: 290 Bit Score: 181.21 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 260 FLDQRKFIEVETPMMnvIAGGATA---KPFITH---HNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMT 333
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPVTDphlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 334 HNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITgsyiikyhpdpadpakelelnfsRPWKRINMIEELEKVFNVkfp 413
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPF-----------------------APAERLSYQEAFLRYAGI--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 414 sgdQLHTAETGEfLKKILVDNKLECPPPLTNARMLDKLVGELEDTCIN---PTFIFGHPQMMSPLAKYSRDQPGLCERFE 490
Cdd:TIGR00462 133 ---DPLTASLAE-LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHLGfgrPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 491 VFVATKEICNAYTELNDPFDQRARFE-EQARQKDQGDDEAQLvDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIRE 569
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEaDNALRKALGLPRYPL-DERFLAALEAGLPECSGVALGVDRLLMLALGADSIDD 287
|
..
gi 135139 570 VL 571
Cdd:TIGR00462 288 VL 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
250-571 |
3.11e-52 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 181.07 E-value: 3.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 250 RSEIIRYIRRFLDQRKFIEVETPMMnVIAGGATA--KPFIT---HHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQ 324
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPAL-SVAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 325 FRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTElmfsEMVKEItgsyiikyhpdpadpakeLELNFSRPWKRINMIEEL 404
Cdd:COG2269 88 FRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVE----ALLQLV------------------LGAAGFAPAERLSYQEAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 405 EKVFNVkfpsgDqLHTAETGEfLKKILVDNKLECPPPLTNARMLDKLVGEledtCI-------NPTFIFGHPQMMSPLAK 477
Cdd:COG2269 146 LRYLGI-----D-PLTADLDE-LAAAAAAAGLRVADDDDRDDLLDLLLSE----RVepqlgrdRPTFLYDYPASQAALAR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 478 YSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRL 557
Cdd:COG2269 215 ISPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRL 294
|
330
....*....|....
gi 135139 558 AMFLTDSNTIREVL 571
Cdd:COG2269 295 LMLALGAERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
123-237 |
3.03e-44 |
|
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b 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. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs, both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role, human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific 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.
Pssm-ID: 239817 [Multi-domain] Cd Length: 108 Bit Score: 152.63 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 123 KVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQLQDYcDPDSYEKDHDLLKRGDIVGVEGYVGRTQPkkggeGEVSVF 202
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKT-----GELSIF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 135139 203 VSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDL 237
Cdd:cd04322 74 VKEFTLLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
247-570 |
1.71e-40 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 149.31 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 247 FITRSEIIRYIRRFLDQRKFIEVETPMM---------------NVIAGGATAKpfithhndldMDMYMRIAPELFLKQLV 311
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPILsqatvtdihlvpfetRFVGPGASQG----------KTLWLMTSPEYHMKRLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 312 VGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKeitgsyiikyhpdpadpakelelnf 391
Cdd:PRK09350 75 AAGSGPIFQICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 392 SRPWKRINMIEELEKVFNVKFPSGDQlhtaetgEFLKKILvdNKLECPPPLTNARMLDKLVGELEDTCI-------NPTF 464
Cdd:PRK09350 130 CEPAESLSYQQAFLRYLGIDPLSADK-------TQLREVA--AKLGLSNIADEEEDRDTLLQLLFTFGVepnigkeKPTF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 465 IFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGL 544
Cdd:PRK09350 201 VYHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGL 280
|
330 340
....*....|....*....|....*.
gi 135139 545 PPTGGWGCGIDRLAMFLTDSNTIREV 570
Cdd:PRK09350 281 PDCSGVALGVDRLIMLALGAESISEV 306
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
119-574 |
3.08e-30 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 123.38 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 119 LPEEKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMsqLQDYCDPDSYEKdHDLLKRGDIVGVEGYVGRTQPKKGGege 198
Cdd:PRK05159 14 LDGEEVTLAGWVHEIRDLG-GIAFLILRDRSGIIQVV--VKKKVDEELFET-IKKLKRESVVSVTGTVKANPKAPGG--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 199 VSVFVSRVQLLTPCLHMLPADHFGFKDQE--TRYRKRYLDLiMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPmmNV 276
Cdd:PRK05159 87 VEVIPEEIEVLNKAEEPLPLDISGKVLAEldTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 277 IA----GGATAKPfITHhndLDMDMYMRIAPELFlKQLVVG-GLDRVYEIGRQFRNEGIDMT-HNPEFTTCEFYQAYADV 350
Cdd:PRK05159 164 VAsgteGGAELFP-IDY---FEKEAYLAQSPQLY-KQMMVGaGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 351 Y-DLMDMTELMFSEMVKEITGSYiikyhpdpadpAKELEL---NFSRP---WKRINMIEELEKVFN--VKFPSGDQLHTA 421
Cdd:PRK05159 239 HeDVMDLLENLLRYMYEDVAENC-----------EKELELlgiELPVPetpIPRITYDEAIEILKSkgNEISWGDDLDTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 422 EtgeflkkilvdnklecpppltnarmlDKLVGE--LEDTCINPTFIFGHPQMMSPL-AKYSRDQPGLCERFEVFVATKEI 498
Cdd:PRK05159 308 G--------------------------ERLLGEyvKEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSFDLLFRGLEI 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 135139 499 CNAYTELNDPFDQRARFeeqarqKDQGDDEAQLvdETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PRK05159 362 TSGGQRIHRYDMLVESI------KEKGLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
225-574 |
1.88e-27 |
|
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: 113.04 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 225 DQETRYRKRYLDLimnkdaRNRFIT-----RSEIIRYIRRFLDQRKFIEVETPMMNVIA--GGATAKPFithhNDLDMDM 297
Cdd:cd00776 3 NLETLLDNRHLDL------RTPKVQaifriRSEVLRAFREFLRENGFTEVHTPKITSTDteGGAELFKV----SYFGKPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 298 YMRIAPELFlKQLVVGGLDRVYEIGRQFRNEGIDMT-HNPEFTTCEFYQAYADVY-DLMDMTELMFSEMVKEITgsyiik 375
Cdd:cd00776 73 YLAQSPQLY-KEMLIAALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIEDYnEVMDLIEELIKYIFKRVL------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 376 yhpdpADPAKELELnfsrpwkrINMIEELEKVFNVKFPsgdQLHTAETGEFLKKilvdNKLECPPPLT---NARMLDKLV 452
Cdd:cd00776 146 -----ERCAKELEL--------VNQLNRELLKPLEPFP---RITYDEAIELLRE----KGVEEEVKWGedlSTEHERLLG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 453 GELEDTcinPTFIFGHPQMMSPL-AKYSRDQPGLCERFEVFV-ATKEICNAYTELNDPfdqrarfEE-QARQKDQGDDEA 529
Cdd:cd00776 206 EIVKGD---PVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMpGVGEIVGGSQRIHDY-------DElEERIKEHGLDPE 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 135139 530 QLvdETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:cd00776 276 SF--EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
122-574 |
1.79e-26 |
|
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: 112.22 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 122 EKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQLQDYcdPDSYEKDHDLLKRGDIVGVEGYVGRTQPKKGGEGEVSV 201
Cdd:TIGR00458 13 QEVTFMGWVHEIRDLG-GLIFVLLRDREGLIQITAPAKKV--SKNLFKWAKKLNLESVVAVRGIVKIKEKAPGGFEIIPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 202 FVSRVQLLTPCLHMLPADHFGfKDQETRYRKRYLDLimnKDARNR--FITRSEIIRYIRRFLDQRKFIEVETPMMNVIA- 278
Cdd:TIGR00458 90 KIEVINEAKEPLPLDPTEKVP-AELDTRLDYRFLDL---RRPTVQaiFRIRSGVLESVREFLAEEGFIEVHTPKLVASAt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 279 -GGATAKPfITHhndLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMT-HNPEFTTCEFYQAYADVYDLMDM 356
Cdd:TIGR00458 166 eGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 357 TELMFSEMVKEITGSYIIKYhpdpadPAKELELNFSR-PWKRINMIEELEKVF--NVKFPSGDQLHTAEtgeflkkilvd 433
Cdd:TIGR00458 242 LEELVVRVFEDVPERCAHQL------ETLEFKLEKPEgKFVRLTYDEAIEMANakGVEIGWGEDLSTEA----------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 434 nklecpppltnarmlDKLVGELEDTCInptFIFGHPQMMSPL-AKYSRDQPGLCERFEVFVATKEICNAYTELNDpFDQR 512
Cdd:TIGR00458 305 ---------------EKALGEEMDGLY---FITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSGAQRIHL-HDLL 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 135139 513 arfeeQARQKDQGDDEAQLvdETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:TIGR00458 366 -----VERIKAKGLNPEGF--KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
122-574 |
7.89e-26 |
|
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: 110.14 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 122 EKVSIAGRIHAKRESGsKLKFYVLH-GDGV--------EVQLMSQLQDycdpdsyekdhdlLKRGDIVGVEGYVGRTQPK 192
Cdd:COG0017 15 QEVTVAGWVRTKRDSG-GISFLILRdGSGFiqvvvkkdKLENFEEAKK-------------LTTESSVEVTGTVVESPRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 193 KGGegeVSVFVSRVQLLTPCLHMLP---ADHfgfkDQETRYRKRYLDLimnkdaRNR-----FITRSEIIRYIRRFLDQR 264
Cdd:COG0017 81 PQG---VELQAEEIEVLGEADEPYPlqpKRH----SLEFLLDNRHLRL------RTNrfgaiFRIRSELARAIREFFQER 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 265 KFIEVETPMMnvIA----GGATAKP---FithhndlDMDMYMRIAPELFlKQLVVGGLDRVYEIGRQFRNEGIDMT-HNP 336
Cdd:COG0017 148 GFVEVHTPII--TAsateGGGELFPvdyF-------GKEAYLTQSGQLY-KEALAMALEKVYTFGPTFRAEKSNTRrHLA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 337 EFTTCEFYQAYADVYDLMDMTElmfsEMVKEITgSYIIKYHPDpadpakELELnFSRpwkrinMIEELEKVFNVKFPsgd 416
Cdd:COG0017 218 EFWMIEPEMAFADLEDVMDLAE----EMLKYII-KYVLENCPE------ELEF-LGR------DVERLEKVPESPFP--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 417 QLHTAETGEFLKKIlvDNKLECPPPLTNA--RML-DKLVGEledtcinPTFIFGHPqmMSPLAKYSR---DQPGLCERFE 490
Cdd:COG0017 277 RITYTEAIEILKKS--GEKVEWGDDLGTEheRYLgEEFFKK-------PVFVTDYP--KEIKAFYMKpnpDDPKTVAAFD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 491 VfvatkeICNAYTEL-------NDPFDQRARFEEQarqkdqGDDEAQLvdETFCNALEYGLPPTGGWGCGIDRLAMFLTD 563
Cdd:COG0017 346 L------LAPGIGEIiggsqreHRYDVLVERIKEK------GLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTG 411
|
490
....*....|.
gi 135139 564 SNTIREVLLFP 574
Cdd:COG0017 412 LENIREVIPFP 422
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
162-574 |
1.76e-20 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 95.13 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 162 CDPDS--YEKDHDLlKRGDIVGVEGYVGR----TQPKKGGEGEVSVFVSRVQLLTPClHMLPADHFGFKD--QETRYRKR 233
Cdd:PRK00476 51 FDPDAeaFEVAESL-RSEYVIQVTGTVRArpegTVNPNLPTGEIEVLASELEVLNKS-KTLPFPIDDEEDvsEELRLKYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 234 YLDL---IMnkdaRNRFITRSEIIRYIRRFLDQRKFIEVETPMMnviaGGAT---AKPFI----THHNDLdmdmYmriA- 302
Cdd:PRK00476 129 YLDLrrpEM----QKNLKLRSKVTSAIRNFLDDNGFLEIETPIL----TKSTpegARDYLvpsrVHPGKF----Y---Al 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 303 ---PELFlKQ-LVVGGLDRVYEIGRQFRNEgiDMTHN--PEFTT--CEFyqAYADVYDLMDMTELMFSEMVKEITGsyii 374
Cdd:PRK00476 194 pqsPQLF-KQlLMVAGFDRYYQIARCFRDE--DLRADrqPEFTQidIEM--SFVTQEDVMALMEGLIRHVFKEVLG---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 375 kyhpdpadpaKELELNFSR-PWK-------------RINM-IEELEKVF-NVKFP--SGdqlhTAETGEFLKKILVdnkl 436
Cdd:PRK00476 265 ----------VDLPTPFPRmTYAeamrrygsdkpdlRFGLeLVDVTDLFkDSGFKvfAG----AANDGGRVKAIRV---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 437 ecppPLTNARMLDKLVGELEDtcinptF--IFGHPQMM----------SPLAK-YSRDQ-PGLCERFEV-------FVA- 494
Cdd:PRK00476 327 ----PGGAAQLSRKQIDELTE------FakIYGAKGLAyikvnedglkGPIAKfLSEEElAALLERTGAkdgdlifFGAd 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 495 TKEICNAY---------TELN-------------D------------------PF-----DQRARFEEQ------ARQKD 523
Cdd:PRK00476 397 KAKVVNDAlgalrlklgKELGlidedkfaflwvvDfpmfeydeeegrwvaahhPFtmpkdEDLDELETTdpgkarAYAYD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 524 --------------------Q---------GDDEAQlvdETF---CNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVL 571
Cdd:PRK00476 477 lvlngyelgggsirihrpeiQekvfeilgiSEEEAE---EKFgflLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVI 553
|
...
gi 135139 572 LFP 574
Cdd:PRK00476 554 AFP 556
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
158-574 |
2.44e-20 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 95.24 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 158 LQDYCDPDSYEKDHDLLKRGD---IVGVEGYVgRTQP-----KKGGEGEVSVFVSRVQLLTPCLHMLP-----ADhfGFK 224
Cdd:PLN02903 102 VQVVTLPDEFPEAHRTANRLRneyVVAVEGTV-RSRPqespnKKMKTGSVEVVAESVDILNVVTKSLPflvttAD--EQK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 225 D---QETRYRKRYLDLIMNKDARNRFItRSEIIRYIRRFL-DQRKFIEVETPMMN---------------VIAGGATAKP 285
Cdd:PLN02903 179 DsikEEVRLRYRVLDLRRPQMNANLRL-RHRVVKLIRRYLeDVHGFVEIETPILSrstpegardylvpsrVQPGTFYALP 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 286 fithhndldmdmymrIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMV 365
Cdd:PLN02903 258 ---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVF 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 366 KEITG----------SY---IIKYHPDPADPAKELELN-----FSRPWKRI--NMIEELEKVFNVKFPSGDQLHTAET-- 423
Cdd:PLN02903 323 KEIKGvqlpnpfprlTYaeaMSKYGSDKPDLRYGLELVdvsdvFAESSFKVfaGALESGGVVKAICVPDGKKISNNTAlk 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 424 -----GEFLK---------KILVDNKLECPP-------PLTNARMLDK---------LVGELEDTCINPTF-----IFGH 468
Cdd:PLN02903 403 kgdiyNEAIKsgakglaflKVLDDGELEGIKalveslsPEQAEQLLAAcgagpgdliLFAAGPTSSVNKTLdrlrqFIAK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 469 PQMMSPLAKYS----RDQPglceRFEVfvatKEICNAYTELNDPFD----------QRAR-------------------- 514
Cdd:PLN02903 483 TLDLIDPSRHSilwvTDFP----MFEW----NEDEQRLEALHHPFTapnpedmgdlSSARalaydmvyngveigggslri 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 135139 515 FEEQARQK-----DQGDDEAQlvdETF---CNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PLN02903 555 YRRDVQQKvleaiGLSPEEAE---SKFgylLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFP 619
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
116-574 |
2.40e-19 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 91.69 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 116 GETLPEEKVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIVGVEGYVGR-TQPKKG 194
Cdd:PLN02850 76 GEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESVVDVEGVVSVpKKPVKG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 195 GEGEVSVFVSRVQLLTPCLHMLP-------------------ADHFGFKDQETRYRKRYLDLimnKDARNRFITR--SEI 253
Cdd:PLN02850 155 TTQQVEIQVRKIYCVSKALATLPfnvedaarseseiekalqtGEQLVRVGQDTRLNNRVLDL---RTPANQAIFRiqSQV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 254 IRYIRRFLDQRKFIEVETPmmNVIAGGAT--AKPFithhnDLDmdmYMRI------APELFlKQLVV-GGLDRVYEIGRQ 324
Cdd:PLN02850 232 CNLFREFLLSKGFVEIHTP--KLIAGASEggSAVF-----RLD---YKGQpaclaqSPQLH-KQMAIcGDFRRVFEIGPV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 325 FRNEGiDMTHNP--EFTTCEFYQAYADVYD-LMDMTELMFSEMVKEITGSYiikyhpdpadpAKELElnfsrpwkRINMI 401
Cdd:PLN02850 301 FRAED-SFTHRHlcEFTGLDLEMEIKEHYSeVLDVVDELFVAIFDGLNERC-----------KKELE--------AIREQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 402 EELEKVfnvKF-PSGDQLHTAETGEFLKK--ILVDnklecppPL-----TNARMLDKLVGELEDTcinpTFIFGH--PQM 471
Cdd:PLN02850 361 YPFEPL---KYlPKTLRLTFAEGIQMLKEagVEVD-------PLgdlntESERKLGQLVKEKYGT----DFYILHryPLA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 472 MSPLakYSR---DQPGLCERFEVFVATKEICNAYTELNDPfdqrARFEEQARQKdqGDDEAQLvdETFCNALEYGLPPTG 548
Cdd:PLN02850 427 VRPF--YTMpcpDDPKYSNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEEC--GIDVKTI--STYIDSFRYGAPPHG 496
|
490 500
....*....|....*....|....*.
gi 135139 549 GWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PLN02850 497 GFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
247-574 |
3.63e-18 |
|
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: 84.93 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 247 FITRSEIIRYIRRFLDQRKFIEVETPMMnviaGGAT---AKPFI----THHND---LDMdmymriAPELFlKQ-LVVGGL 315
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL----TKSTpegARDFLvpsrLHPGKfyaLPQ------SPQLF-KQlLMVSGF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 316 DRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGsyiikyhpdpadpaKELELNFsrpw 395
Cdd:cd00777 70 DRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG--------------VELTTPF---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 396 KRINMIEELEK-----VFNVKFP---------SGDQLH---TAETGEFLKKiLVDNKLECpppltnarmldklVGELEDT 458
Cdd:cd00777 132 PRMTYAEAMERygfkfLWIVDFPlfewdeeegRLVSAHhpfTAPKEEDLDL-LEKDPEDA-------------RAQAYDL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 459 CINptfifGHpqmmsplakysrdqpglcerfevfvatkEICNAYTELNDPFDQRARFEeqarqkDQGDDEAQLVDE--TF 536
Cdd:cd00777 198 VLN-----GV----------------------------ELGGGSIRIHDPDIQEKVFE------ILGLSEEEAEEKfgFL 238
|
330 340 350
....*....|....*....|....*....|....*...
gi 135139 537 CNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:cd00777 239 LEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
197-370 |
4.20e-17 |
|
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: 84.66 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 197 GEVSVFVSRVQLLTPClHMLPADHFGFKD--QETRYRKRYLDLiMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMM 274
Cdd:COG0173 92 GEIEVLASELEILNKA-KTPPFQIDDDTDvsEELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPIL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 275 nviaGGAT---AKPFI----THHNDLdmdmYmriA----PELFlKQ-LVVGGLDRVYEIGRQFRNEgiDMTHN--PEFTT 340
Cdd:COG0173 170 ----TKSTpegARDYLvpsrVHPGKF----Y---AlpqsPQLF-KQlLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQ 235
|
170 180 190
....*....|....*....|....*....|..
gi 135139 341 --CEFyqAYADVYDLMDMTELMFSEMVKEITG 370
Cdd:COG0173 236 ldIEM--SFVDQEDVFELMEGLIRHLFKEVLG 265
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
117-574 |
2.50e-15 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 78.88 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 117 ETLPEEKVSIAGRIHAKRESGsKLKFYVLHgDGVE-VQLMSQLQDYCdPDSYEKDHDLLKRGDIVGVEGYV-GRTQP-KK 193
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLR-DGSDsVQAMAAVEGDV-PKEMIDFIGQIPTESIVDVEATVcKVEQPiTS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 194 GGEGEVSVFVSRVQLLTPCLHMLP---ADHFGFKDQE-------TRYRKRYLDLimNKDARNR-FITRSEIIRYIRRFLD 262
Cdd:PTZ00401 151 TSHSDIELKVKKIHTVTESLRTLPftlEDASRKESDEgakvnfdTRLNSRWMDL--RTPASGAiFRLQSRVCQYFRQFLI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 263 QRKFIEVETPMMNVIAGGATAKPFITHHndLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDM-THNPEFTTC 341
Cdd:PTZ00401 229 DSDFCEIHSPKIINAPSEGGANVFKLEY--FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFVGL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 342 EFYQAYAD-VYDLMDMTELMFS-------------------------------EMVKEItGSYIIKYHPDPADPAKELEL 389
Cdd:PTZ00401 307 DVEMRINEhYYEVLDLAESLFNyiferlathtkelkavcqqypfeplvwkltpERMKEL-GVGVISEGVEPTDKYQARVH 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 390 NFSRPWKRINM---IEELEKVFNVKFPSGDQLHTaetgeflkkilvdnklecppplTNARMLDKLVGEL--EDTCINPTF 464
Cdd:PTZ00401 386 NMDSRMLRINYmhcIELLNTVLEEKMAPTDDINT----------------------TNEKLLGKLVKERygTDFFISDRF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 465 ifghPQMMSPLAKYS-RDQPGLCERFEVFVATKEICNAYTELNDP--FDQRArfeeqarqKDQGDDEAQLVDetFCNALE 541
Cdd:PTZ00401 444 ----PSSARPFYTMEcKDDERFTNSYDMFIRGEEISSGAQRIHDPdlLLARA--------KMLNVDLTPIKE--YVDSFR 509
|
490 500 510
....*....|....*....|....*....|...
gi 135139 542 YGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PTZ00401 510 LGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
123-211 |
4.93e-15 |
|
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: 70.29 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 123 KVSIAGRIHAKRESGsKLKFYVLHGDGVEVQLMsqlqdyCDPDSYEKDHDL---LKRGDIVGVEGYVGRTQPKKGGEGEV 199
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVV------VNKEELGEFFEEaekLRTESVVGVTGTVVKRPEGNLATGEI 73
|
90
....*....|..
gi 135139 200 SVFVSRVQLLTP 211
Cdd:cd04100 74 ELQAEELEVLSK 85
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
123-405 |
1.88e-14 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 76.56 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 123 KVSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMSQlqDYCDPDSYEKDHDLlkRGDI-VGVEGYVGRTQPKKGG----EG 197
Cdd:PRK12820 20 EVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSP--EAAPADVYELAASL--RAEFcVALQGEVQKRLEETENphieTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 198 EVSVFVSRVQLLTPCLhMLP----------------ADHFgfkDQETRYRKRYLDlIMNKDARNRFITRSEIIRYIRRFL 261
Cdd:PRK12820 96 DIEVFVRELSILAASE-ALPfaisdkamtagagsagADAV---NEDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 262 DQRKFIEVETPMMNvIAGGATAKPFITHHNDLDMDMY-MRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTT 340
Cdd:PRK12820 171 DSRGFLEIETPILT-KSTPEGARDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQ 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 135139 341 CEFYQAYADVYDLMDMTELMFSEMVkEITGsyiikyhpdpadpakeleLNFSRPWKRINMIEELE 405
Cdd:PRK12820 250 LDIEASFIDEEFIFELIEELTARMF-AIGG------------------IALPRPFPRMPYAEAMD 295
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
250-574 |
3.46e-14 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 73.90 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 250 RSEIIRYIRRFLDQRKFIEVETPMMNVI----AGGATAKPFithhNDLDMDMY---MRIAPEL-FLKQLVVGGLDRVYEI 321
Cdd:PRK06462 33 QSSILRYTREFLDGRGFVEVLPPIISPStdplMGLGSDLPV----KQISIDFYgveYYLADSMiLHKQLALRMLGKIFYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 322 GRQFRNEG---IDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEitgsyIIKYHPDPADpAKELELN-FSRPWKR 397
Cdd:PRK06462 109 SPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKE-----LLEEHEDELE-FFGRDLPhLKRPFKR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 398 INMiEELEKVFNVKFPSGDQLhtAETGEFLKKILVdNKLEcpppltnarmldklvgeledtciNPTFIFGHPQMMSPLak 477
Cdd:PRK06462 183 ITH-KEAVEILNEEGCRGIDL--EELGSEGEKSLS-EHFE-----------------------EPFWIIDIPKGSREF-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 478 YSRDQPG-----------LCERFEVFVATKEICNAYTELndpfdqrarfeeQARQKDQGDDEAQLvdETFCNALEYGLPP 546
Cdd:PRK06462 234 YDREDPErpgvlrnydllLPEGYGEAVSGGEREYEYEEI------------VERIREHGVDPEKY--KWYLEMAKEGPLP 299
|
330 340
....*....|....*....|....*...
gi 135139 547 TGGWGCGIDRLAMFLTDSNTIREVLLFP 574
Cdd:PRK06462 300 SAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
249-360 |
5.31e-14 |
|
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: 71.38 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 249 TRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATA----KPFITHHNDLDMDMYMRIAPELFLKQLVVGGL----DRVYE 320
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAghepKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 135139 321 IGRQFRNEGI--DMTHNPEFTTCEFYQAYADVYDLMDMTELM 360
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDGEEASEFEELI 122
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
124-209 |
1.18e-13 |
|
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: 66.10 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 124 VSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMsqlqdyCDPDSYEKDHDLLKRGDIVGVEGYVGRTQpkkggEGEVSVFV 203
Cdd:pfam01336 1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQVV------VFKEEAEKLAKKLKEGDVVRVTGKVKKRK-----GGELELVV 69
|
....*.
gi 135139 204 SRVQLL 209
Cdd:pfam01336 70 EEIELL 75
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
250-413 |
3.93e-05 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 46.25 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 250 RSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDmymriaPELFLKQ--LVVGG----------LDR 317
Cdd:PRK03932 136 RNTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTTLDLDFS------KDFFGKEayLTVSGqlyaeayamaLGK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 318 VYEIGRQFRNEGIDMT-HNPEFTTCEFYQAYADVYDLMDMTElmfsEMVKeitgsYIIKY----HPDpadpakelELNFS 392
Cdd:PRK03932 210 VYTFGPTFRAENSNTRrHLAEFWMIEPEMAFADLEDNMDLAE----EMLK-----YVVKYvlenCPD--------DLEFL 272
|
170 180
....*....|....*....|.
gi 135139 393 RPWKRINMIEELEKVFNVKFP 413
Cdd:PRK03932 273 NRRVDKGDIERLENFIESPFP 293
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
123-209 |
4.63e-04 |
|
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: 39.22 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 123 KVSIAGRIHAKRESGSKLKFYVL---HGDgvEVQLMSqlqdycdpDSYEKDHDLLKR---GDIVGVEGYVGRTQPKKGGE 196
Cdd:cd04321 1 KVTLNGWIDRKPRIVKKLSFADLrdpNGD--IIQLVS--------TAKKDAFSLLKSitaESPVQVRGKLQLKEAKSSEK 70
|
90
....*....|....
gi 135139 197 G-EVSVFVSRVQLL 209
Cdd:cd04321 71 NdEWELVVDDIQTL 84
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
122-237 |
1.02e-03 |
|
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: 39.43 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 135139 122 EKVSIAGRIHAKRESGsKLKFYVLhGD--GVeVQLMsqlqdyCDPDSYE--KDHDLLKRGDIVGVEGYV-GRTQP---KK 193
Cdd:cd04317 15 QEVTLCGWVQRRRDHG-GLIFIDL-RDryGI-VQVV------FDPEEAPefELAEKLRNESVIQVTGKVrARPEGtvnPK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 135139 194 GGEGEVSVFVSRVQLLTPC--LHMLPADHFGfKDQETRYRKRYLDL 237
Cdd:cd04317 86 LPTGEIEVVASELEVLNKAktLPFEIDDDVN-VSEELRLKYRYLDL 130
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
314-369 |
2.55e-03 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 39.45 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 135139 314 GLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADV--YDLMDMTELMFSEMVKEIT 369
Cdd:cd00496 79 PPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLtfADLKGTLEEFAKELFGPIT 136
|
|
| |
