|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
9-565 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 894.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 9 GDKLSKNELKRRMKAEKKAAEKEAKVKEQQEQKETNDK-PQQNAYGADEETLDPNQYFKIRSQAIQALKGTAEDPYPHKF 87
Cdd:PLN02502 5 GEPLSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAAKgRSRKSAAADDETMDPTQYRANRLKKVEALRAKGVEPYPYKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 88 HVDLSLTEFIERYNHLQPGDHLTDVVLNLSGRVHAKRASGaKLLFYDLRGEGVKLQVMANSRNYT-SEEAFVHINNKLRR 166
Cdd:PLN02502 85 DVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDlDEEEFEKLHSLVDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 167 GDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPHLHFGLKDKETRFRQRYLDLILNDFVRQKFVTRSKIITYLRSFL 246
Cdd:PLN02502 164 GDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 247 DQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTC 326
Cdd:PLN02502 244 DDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTC 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 327 EFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYHpdgpegqAYEIDFTPPFRRISMTQELEKELGVKFPPPdtYDSDE 406
Cdd:PLN02502 324 EFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRISMISLVEEATGIDFPAD--LKSDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 407 MRKFLDDLCVQKEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQIMSPLAKWHRSQKGLTERFELFVMKKEICNA 486
Cdd:PLN02502 395 ANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANA 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036551372 487 YTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKPED 565
Cdd:PLN02502 475 FSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
56-566 |
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: 685.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 56 EETLDPNQYFKIRSQAIQALKGTAEDPYPHKFHVDLSLTEFIERYNHLQPGDHLTDVVlNLSGRVHAKRASGaKLLFYDL 135
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEEETGDEV-SVAGRIMAKRDMG-KASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 136 RGEGVKLQVMAnSRNYTSEEAFVHINnKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPHLHFGLKDKETRF 215
Cdd:COG1190 80 QDGSGRIQLYL-RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 216 RQRYLDLILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKML 295
Cdd:COG1190 158 RQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 296 VVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhpdgpegQAYEIDF 375
Cdd:COG1190 238 IVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 376 TPPFRRISMTQELEKELGVKFpppDTYDSDEmrkFLDDLCVQKEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQ 455
Cdd:COG1190 311 SPPWRRITMVEAIKEATGIDV---TPLTDDE---ELRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 456 IMSPLAKWHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGW 535
Cdd:COG1190 385 EVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGL 464
|
490 500 510
....*....|....*....|....*....|.
gi 1036551372 536 GMGIDRLTMFLTDSNNIKEVLLFPAMKPEDN 566
Cdd:COG1190 465 GIGIDRLVMLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
60-565 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 681.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 60 DPNQYFKIRSQAIQALKGTAEDPYPHKFHVDLSLTEFIERYNHLQPGD-HLTDVVLNLSGRVHAKRASGaKLLFYDLRGE 138
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKRVMG-KASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 139 GVKLQVMAnSRNYTSEEAFVHINnKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPHLHFGLKDKETRFRQR 218
Cdd:PRK00484 81 SGRIQLYV-SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 219 YLDLILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVG 298
Cdd:PRK00484 159 YVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 299 GIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhpdgpegQAYEIDFTPP 378
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 379 FRRISMTQELEKELGVKFpppDTYDSDEMRKFLDDLcvqkEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQIMS 458
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDF---DDMTDEEARALAKEL----GIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 459 PLAKWHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMG 538
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 1036551372 539 IDRLTMFLTDSNNIKEVLLFPAMKPED 565
Cdd:PRK00484 465 IDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
39-563 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 651.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 39 EQKETNDKPQQNAYGADEETLDPNQYFKIRSQAIQALKGTAEDPYPHKFHVDLSLTEFIERYNHLQPGDHLTDVVLNLSG 118
Cdd:PTZ00417 60 EKKVRSVQASKDKKKEEEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 119 RVHAKRASGAKLLFYDLRGEGVKLQVMANSRNYTSEEA-FVHINNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPC 197
Cdd:PTZ00417 140 RIMRVSASGQKLRFFDLVGDGAKIQVLANFAFHDHTKSnFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPC 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 198 LHMLPhLHFGLKDKETRFRQRYLDLILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHND 277
Cdd:PTZ00417 220 LHMLP-MKYGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHND 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 278 LNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAY 357
Cdd:PTZ00417 299 LDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTY 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 358 KVTYHPDGPEGQAYEIDFTPPFRRISMTQELEKELGVKFPPPdtYDSDEMRKFLDDLCVQKEVECPPPRTTARLLDKLVG 437
Cdd:PTZ00417 379 KILYNKDGPEKDPIEIDFTPPYPKVSIVEELEKLTNTKLEQP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLAS 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 438 DFLEVKCIN-PTYICDHPQIMSPLAKWHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMF 516
Cdd:PTZ00417 457 HFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQ 536
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1036551372 517 IDETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKP 563
Cdd:PTZ00417 537 FDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
60-563 |
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: 620.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 60 DPNQYFKIRSQAIQALKGTAEDPYPHKFHVDLSLTEFIERYNHLQPGDH-LTDVVLNLSGRVHAKRaSGAKLLFYDLRGE 138
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkEKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 139 GVKLQVMANSRNYTseEAFVHINNK-LRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPHLHFGLKDKETRFRQ 217
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 218 RYLDLILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVV 297
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 298 GGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhpdgpegQAYEIDFTP 377
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 378 PFRRISMTQELEKELGVKFppPDTYDSDEMRKFLDDLCVQKeVECPPprTTARLLDKLVGDFLEVKCINPTYICDHPQIM 457
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDF--DILKDDETAKALAKEHGIEV-AEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 458 SPLAKWHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGM 537
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 1036551372 538 GIDRLTMFLTDSNNIKEVLLFPAMKP 563
Cdd:TIGR00499 466 GIDRLVMLLTDAPSIRDVLLFPQLRP 491
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
225-563 |
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: 614.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 225 NDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGIDRVY 304
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 305 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGaykvtyhPDGPEGQAYEIDFTPPFRRISM 384
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING-------KTKIEYGGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 385 TQELEKELGVKFPPPDTYDSDEMRKFLDDLCVqkeVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQIMSPLAKWH 464
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLIK---EKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 465 RSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRLTM 544
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 1036551372 545 FLTDSNNIKEVLLFPAMKP 563
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
70-562 |
1.37e-149 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 445.63 E-value: 1.37e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 70 QAIQALKGTAEDPYPHK-FHVDLSLTEFIERYNHLQPGDHLTDVVLNLSGRVHAKRASGaKLLFYDLRGEGVKLQVMANS 148
Cdd:PTZ00385 65 EASRAPRSKLDLPAAYSsFRGITPISEVRERYGYLASGDRAAQATVRVAGRVTSVRDIG-KIIFVTIRSNGNELQVVGQV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 149 RNYTSEEAFVHINNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSP--CLHML--PHLH-FG-LKDKETRFRQRYLDL 222
Cdd:PTZ00385 144 GEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 223 ILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGIDR 302
Cdd:PTZ00385 224 MTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMER 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 303 VYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYHPDGPEGQAYEIDFTPPFRRI 382
Cdd:PTZ00385 304 IYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 383 SMTQELEKELGVKFPPPDTYDSDEMRKFLDDLCVQKEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQIMSPLAK 462
Cdd:PTZ00385 384 SVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 463 WHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRL 542
Cdd:PTZ00385 464 EQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRA 543
|
490 500
....*....|....*....|
gi 1036551372 543 TMFLTDSNNIKEVLLFPAMK 562
Cdd:PTZ00385 544 LMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
81-565 |
3.54e-136 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 423.22 E-value: 3.54e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 81 DPYPhkfhVDLSLTEFIErynhlQPGDHLTDVVLNLSGRVHAKRASGaKLLFYDLRGEGVKLQVMAnSRNYTSEEAFVHI 160
Cdd:PRK02983 630 DPYP----VGVPPTHTVA-----EALDAPTGEEVSVSGRVLRIRDYG-GVLFADLRDWSGELQVLL-DASRLEQGSLADF 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 161 NNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPHLHFGLKDKETRFRQRYLDLILNDFVRQKFVTRSKIIT 240
Cdd:PRK02983 699 RAAVDLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLLRARSAVVR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 241 YLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHN 320
Cdd:PRK02983 779 AVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 321 PEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhpDGPEGQAYEIDFTPPFRRISMTQELEKELGVKFpPPD 400
Cdd:PRK02983 859 PEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEALGEEI-DPD 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 401 TyDSDEMRKflddLCVQKEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDHPQIMSPLAKWHRSQKGLTERFELFVMK 480
Cdd:PRK02983 936 T-PLAELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWG 1010
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 481 KEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRLTMFLTdSNNIKEVLLFPA 560
Cdd:PRK02983 1011 VELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPL 1089
|
....*
gi 1036551372 561 MKPED 565
Cdd:PRK02983 1090 VKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
48-564 |
4.48e-131 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 392.50 E-value: 4.48e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 48 QQNAYGADEeTLDPNQYFKIRSQAIQALK--GTAedpYPHKFHVDLSLTEFIERYNhLQPGDHLT--DVVLNLSGRVHAK 123
Cdd:PRK12445 3 EQETRGANE-AIDFNDELRNRREKLAALRqqGVA---FPNDFRRDHTSDQLHEEFD-AKDNQELEslNIEVSVAGRMMTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 124 RASGaKLLFYDLRGEGVKLQVMAnSRNYTSEEAFVHINNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLLSPCLHMLPH 203
Cdd:PRK12445 78 RIMG-KASFVTLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 204 LHFGLKDKETRFRQRYLDLILNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLY 283
Cdd:PRK12445 156 KFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 284 MRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhp 363
Cdd:PRK12445 236 LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 364 dgpegQAYEIDFTPPFRRISMTQELEKELgvkfPPPDTYDSDEM---RKFLDDLCVQKEVECPPPRTTARLLDKLVgdfl 440
Cdd:PRK12445 314 -----GEHVFDFGKPFEKLTMREAIKKYR----PETDMADLDNFdaaKALAESIGITVEKSWGLGRIVTEIFDEVA---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 441 EVKCINPTYICDHPQIMSPLAKWHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDET 520
Cdd:PRK12445 381 EAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDED 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1036551372 521 FCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKPE 564
Cdd:PRK12445 461 YVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
210-562 |
3.04e-119 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 355.33 E-value: 3.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 210 DKETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPE 289
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 290 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYHPdgpegq 369
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 370 aYEIDFTPPFRRISMTQELEKELGVKfPPPDTYDSDEmrkflDDLcvqkevecppprttaRLLDKLVGDFLEvkcINPTY 449
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKD-VEELGYGSDK-----PDL---------------RFLLELVIDKNK---FNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 450 ICDHPQIMSPLAKWHRSQ-KGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKaegdDEAMFIDETFCTALEYG 528
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 1036551372 529 LPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMK 562
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 ... |
232-563 |
5.20e-91 |
|
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: 280.90 E-value: 5.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 232 FVTRSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 311
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 312 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVTYhpdgpegQAYEIDFTPPFRRISMTQELEKE 391
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 392 LgvkfpppdtydsdemrkflddlcvqkevecppprttarlldklvgdflevkciNPTYICDHP-QIMSPLAKWHRSQKGL 470
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 471 TERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGddeaMFIDETFCTALEYGLPPTAGWGMGIDRLTMFLTDSN 550
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 1036551372 551 NIKEVLLFPAMKP 563
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
245-556 |
2.79e-53 |
|
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: 183.14 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 245 FLDQLGFLEIETPMmnLIPGG-------AVAKPFITYHNDlNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 317
Cdd:TIGR00462 1 FFAERGVLEVETPL--LSPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 318 THNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKhitgaykvtyhpdgpegqayeiDFTPPFRRISMTQELEKELGVKfp 397
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGID-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 398 PPDTYDSDemrkfLDDLCVQKEVECPPPRTTARLLDKLvgdFLEV-----KCINPTYICDHPQIMSPLAKWHRSQKGLTE 472
Cdd:TIGR00462 134 PLTASLAE-----LQAAAAAHGIRASEEDDRDDLLDLL---FSEKvephlGFGRPTFLYDYPASQAALARISPDDPRVAE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 473 RFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNI 552
Cdd:TIGR00462 206 RFELYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSI 285
|
....
gi 1036551372 553 KEVL 556
Cdd:TIGR00462 286 DDVL 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
235-556 |
6.34e-50 |
|
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: 174.91 E-value: 6.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 235 RSKIITYLRSFLDQLGFLEIETPMMNLIPGGAVA-KPFITY---HNDLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 310
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 311 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSgmvkhitgaykvtyhpdgpegQAYEIDFTPPFRRISMTQELEK 390
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 391 ELGVkfpPPDTYDSDEMRKFLDDLCVqkEVECPPPRTTarLLDKLvgdFLEvkCI-------NPTYICDHPQIMSPLAKW 463
Cdd:COG2269 148 YLGI---DPLTADLDELAAAAAAAGL--RVADDDDRDD--LLDLL---LSE--RVepqlgrdRPTFLYDYPASQAALARI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 464 HRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRLT 543
Cdd:COG2269 216 SPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLL 295
|
330
....*....|...
gi 1036551372 544 MFLTDSNNIKEVL 556
Cdd:COG2269 296 MLALGAERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
114-222 |
2.04e-49 |
|
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: 166.50 E-value: 2.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 114 LNLSGRVHAKRASGaKLLFYDLRGEGVKLQVMANSRNYtSEEAFVHINNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTL 193
Cdd:cd04322 2 VSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTL 79
|
90 100
....*....|....*....|....*....
gi 1036551372 194 LSPCLHMLPHLHFGLKDKETRFRQRYLDL 222
Cdd:cd04322 80 LSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
235-555 |
2.76e-40 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 148.54 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 235 RSKIITYLRSFLDQLGFLEIETPMM--------NLIPggaVAKPFITYHNDLNMNLYMRIAPElYH-KMLVVGGIDRVYE 305
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 306 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSgmvkhitgaykvtyhpdgpegqayEIDFTPPFRRISMT 385
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ------------------------QVLDCEPAESLSYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 386 QELEKELGVKFPPPDTYDSDEMRKFLDDLCVQKEVEcppPRTTarLLDKLVGDFLEVKcIN---PTYICDHPQIMSPLAK 462
Cdd:PRK09350 140 QAFLRYLGIDPLSADKTQLREVAAKLGLSNIADEEE---DRDT--LLQLLFTFGVEPN-IGkekPTFVYHFPASQAALAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 463 WHRSQKGLTERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFIDETFCTALEYGLPPTAGWGMGIDRL 542
Cdd:PRK09350 214 ISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDRL 293
|
330
....*....|...
gi 1036551372 543 TMFLTDSNNIKEV 555
Cdd:PRK09350 294 IMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
116-559 |
4.52e-39 |
|
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: 148.43 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGAkLLFYDLRGEGVKLQVMAnSRNYTSEEAFVHINnKLRRGDIIGVRGNPGKTKK--GELSIIPVEMTL 193
Cdd:TIGR00458 17 FMGWVHEIRDLGG-LIFVLLRDREGLIQITA-PAKKVSKNLFKWAK-KLNLESVVAVRGIVKIKEKapGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 194 LSPCLHMLPHLhfgLKDK-----ETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMMNLIP--GGA 266
Cdd:TIGR00458 94 INEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 267 VAKPfITYhndLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKL 345
Cdd:TIGR00458 170 ELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 346 LsgmvkhitgaykVTYHPDGPEGQAYEIDFtppfrrismtqelekeLGVKFPPPD------TYDsdEMRKFLDdlcvQKE 419
Cdd:TIGR00458 246 V------------VRVFEDVPERCAHQLET----------------LEFKLEKPEgkfvrlTYD--EAIEMAN----AKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 420 VECPPPRTTARLLDKLVGDFLEvkciNPTYICDHPQIMSPL-AKWHRSQKGLTERFELFVMKKEICNAYTElndpIRQRE 498
Cdd:TIGR00458 292 VEIGWGEDLSTEAEKALGEEMD----GLYFITDWPTEIRPFyTMPDEDNPEISKSFDLMYRDLEISSGAQR----IHLHD 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036551372 499 LFEQQAKAKAEGDDEAMFidetFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:TIGR00458 364 LLVERIKAKGLNPEGFKD----YLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
105-559 |
2.48e-32 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 129.54 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 105 PGDHLTDVVLnlSGRVHAKRASGaKLLFYDLRGEGVKLQVMAnsRNYTSEEAFVHINnKLRRGDIIGVRG----NPgKTK 180
Cdd:PRK05159 12 PELDGEEVTL--AGWVHEIRDLG-GIAFLILRDRSGIIQVVV--KKKVDEELFETIK-KLKRESVVSVTGtvkaNP-KAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 181 KGeLSIIPVEMTLLSPCLHMLPhlhFGLKDK-----ETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFLDQLGFLEIE 255
Cdd:PRK05159 85 GG-VEVIPEEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 256 TPMM---------NLIPggavakpfITYhndLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTT 325
Cdd:PRK05159 160 TPKIvasgteggaELFP--------IDY---FEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 326 CEFYMAYAD-YHDLMEITEKLLSGMVKHITGAYKvtyhpdgPEGQAYEIDF---TPPFRRISMT--QELEKELGVKFPPP 399
Cdd:PRK05159 229 IDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITYDeaIEILKSKGNEISWG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 400 dtydsdemrkflDDLCVQKEvecppprttarlldKLVGDFLEVKCINPTY-ICDHPQIMSPL-AKWHRSQKGLTERFELf 477
Cdd:PRK05159 302 ------------DDLDTEGE--------------RLLGEYVKEEYGSDFYfITDYPSEKRPFyTMPDEDDPEISKSFDL- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 478 vMKK--EICNAYTELNDpirqRELFEQQAKAKaeGDDEAMFidETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEV 555
Cdd:PRK05159 355 -LFRglEITSGGQRIHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREA 425
|
....
gi 1036551372 556 LLFP 559
Cdd:PRK05159 426 VLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
116-559 |
6.92e-29 |
|
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: 119.39 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGaKLLFYDLR-GEGVkLQVMANSrnyTSEEAFVHINnKLRRGDIIGVRG----NPGKtkKGELSIIPVE 190
Cdd:COG0017 19 VAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKK---DKLENFEEAK-KLTTESSVEVTGtvveSPRA--PQGVELQAEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 191 MTLLSPCLHMLPhlhFGLKDK--ETRFRQRYLDLILNDFvRQKFVTRSKIITYLRSFLDQLGFLEIETPMmnLIP----- 263
Cdd:COG0017 91 IEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTPI--ITAsateg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 264 GGAVakpF-ITYHNDlnmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEI 341
Cdd:COG0017 165 GGEL---FpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 342 TEKLLSGMVKHItgaykVTYHPDgpEGQAYEIDFT-------PPFRRISMTQELE--KELGVKFpppdtydsdemrKFLD 412
Cdd:COG0017 238 AEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITYTEAIEilKKSGEKV------------EWGD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 413 DLcvQKEVEcppprttaRLL-DKLVGDFLEV----KCINPTYICDHPQimsplakwhrsQKGLTERFELfvmkkeICNAY 487
Cdd:COG0017 299 DL--GTEHE--------RYLgEEFFKKPVFVtdypKEIKAFYMKPNPD-----------DPKTVAAFDL------LAPGI 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036551372 488 TELndpI--RQRE--LFEQQAKAKAEGDDEAMFidETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:COG0017 352 GEI---IggSQREhrYDVLVERIKEKGLDPEDY--EWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
212-559 |
1.03e-28 |
|
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: 116.51 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 212 ETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMM--NLIPGGAVAKPFITYHNDLnmnlYMRIAPE 289
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFKVSYFGKPA----YLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 290 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKLLSGMVKHITGAYK-----VTYH 362
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 363 PDGPEGqayeidFTPPFRRISMT--QELEKELGVKFPPPDTydsdemrkflDDLcvQKEVEcppprttaRLLDKLVGDfl 440
Cdd:cd00776 159 NRELLK------PLEPFPRITYDeaIELLREKGVEEEVKWG----------EDL--STEHE--------RLLGEIVKG-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 441 evkciNPTYICDHPQIMSPL-AKWHRSQKGLTERFELFVMKK-EICNAYTELNDPirqrELFEQQAKAKaeGDDEAMFid 518
Cdd:cd00776 211 -----DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF-- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1036551372 519 ETFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:cd00776 278 EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
232-559 |
5.13e-28 |
|
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: 113.44 E-value: 5.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 232 FVTRSKIITYLRSFLDQLGFLEIETPMMN-LIPGGavAKPFITyHNDLNMNLYMRI--APELYHKMLVVGGIDRVYEIGR 308
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEG--ARDFLV-PSRLHPGKFYALpqSPQLFKQLLMVSGFDRYFQIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 309 QFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGaykvtyhpdgpegqayeIDFTPPFRRIsmtqel 388
Cdd:cd00777 78 CFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRM------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 389 ekelgvkfpppdTYDsDEMRKFLDDLCvqkevecppprttarlldkLVGDFlevkcinptyicdhpqimsPLAKWHRSQK 468
Cdd:cd00777 135 ------------TYA-EAMERYGFKFL-------------------WIVDF-------------------PLFEWDEEEG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 469 GLTERFELFVMKKE--------------------ICNAYtEL-------NDPIRQRELFEQQAKAKAEGDDEAMFidetF 521
Cdd:cd00777 164 RLVSAHHPFTAPKEedldllekdpedaraqaydlVLNGV-ELgggsiriHDPDIQEKVFEILGLSEEEAEEKFGF----L 238
|
330 340 350
....*....|....*....|....*....|....*...
gi 1036551372 522 CTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:cd00777 239 LEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
116-559 |
6.13e-27 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 115.16 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGaKLLFYDLRG-EGVkLQVMANSrnytSEEAFvHINNKLRRGDIIGVRG----------NPgKTKKGEL 184
Cdd:PRK00476 22 LCGWVHRRRDHG-GLIFIDLRDrEGI-VQVVFDP----DAEAF-EVAESLRSEYVIQVTGtvrarpegtvNP-NLPTGEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 185 SIIPVEMTLLSPClHMLPhlhFGLKDK-----ETRFRQRYLDLilndfvR-----QKFVTRSKIITYLRSFLDQLGFLEI 254
Cdd:PRK00476 94 EVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL------RrpemqKNLKLRSKVTSAIRNFLDDNGFLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 255 ETPMmnLI---PGGAvakpfityhNDlnmnlYM---RI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLT 318
Cdd:PRK00476 164 ETPI--LTkstPEGA---------RD-----YLvpsRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE--DLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 319 HN--PEFTT--CEfyMAYADYHDLMEITEKLLSGMVKHITGaykvtyhpdgpegqayeIDFTPPFRRISMTQELEK---- 390
Cdd:PRK00476 226 ADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTYAEAMRRygsd 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 391 --------EL--------------------------GVKFPPPDTYDSdemRKFLDDL----------------CVQKEV 420
Cdd:PRK00476 287 kpdlrfglELvdvtdlfkdsgfkvfagaandggrvkAIRVPGGAAQLS---RKQIDELtefakiygakglayikVNEDGL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 421 ECP-----PPRTTARLLDKL---VGD--FLevkcinptyICDHPQIMSP--------LAKwhrsQKGLTER--------- 473
Cdd:PRK00476 364 KGPiakflSEEELAALLERTgakDGDliFF---------GADKAKVVNDalgalrlkLGK----ELGLIDEdkfaflwvv 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 474 ----FEL-------------FVMKKEICNAYTELNDP---------------------IR--QRELfeqQAKA-KAEG-- 510
Cdd:PRK00476 431 dfpmFEYdeeegrwvaahhpFTMPKDEDLDELETTDPgkarayaydlvlngyelgggsIRihRPEI---QEKVfEILGis 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1036551372 511 DDEAM-----FIDetfctALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:PRK00476 508 EEEAEekfgfLLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
116-383 |
6.52e-27 |
|
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: 115.10 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGAkLLFYDLRG-EGVkLQVMANSRNytSEEAFvHINNKLRRGDIIGVRG----------NPgKTKKGEL 184
Cdd:COG0173 21 LSGWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDPDD--SAEAF-EKAEKLRSEYVIAVTGkvrarpegtvNP-KLPTGEI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 185 SIIPVEMTLLSPClHMLPhlhFGLKDK-----ETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFLDQLGFLEIETPMm 259
Cdd:COG0173 95 EVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIETPI- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 260 nLI---PGGAvakpfityhNDlnmnlYM---RI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN--P 321
Cdd:COG0173 169 -LTkstPEGA---------RD-----YLvpsRVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADrqP 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036551372 322 EFTT--CEfyMAYADYHDLMEITEKLLSGMVKHITGaykvtyhpdgpegqayeIDFTPPFRRIS 383
Cdd:COG0173 232 EFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMT 276
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
116-390 |
2.25e-23 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 104.49 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGAkLLFYDLRGEGVKLQVMANSRnyTSEEAfVHINNKLRRGDIIGVRG----------NPgKTKKGELS 185
Cdd:PLN02903 77 LCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPD--EFPEA-HRTANRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 186 IIPVEMTLLSPCLHMLPHLHFGLKD------KETRFRQRYLDLilndfVRQKFVT----RSKIITYLRSFL-DQLGFLEI 254
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDL-----RRPQMNAnlrlRHRVVKLIRRYLeDVHGFVEI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 255 ETPMMN---------------LIPGGAVAKPfityhndlnmnlymrIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTH 319
Cdd:PLN02903 227 ETPILSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADR 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036551372 320 NPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGaykvtyhpdgpegqayeIDFTPPFRRISMTQELEK 390
Cdd:PLN02903 292 QPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLTYAEAMSK 345
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
116-559 |
1.32e-19 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 92.08 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGaKLLFYDLRGEGVKLQVMANSRNYTSEEAFVHINNKLRRG---DIIGVRGNPGKTKKG---ELSIIPV 189
Cdd:PLN02850 86 IRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSREsvvDVEGVVSVPKKPVKGttqQVEIQVR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 190 EMTLLSPCLHMLPhlhFGLKD----------------------KETRFRQRYLDLIL--NDFVrqkFVTRSKIITYLRSF 245
Cdd:PLN02850 165 KIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDLRTpaNQAI---FRIQSQVCNLFREF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 246 LDQLGFLEIETPmmNLIPG-----GAVakpFITYHNDLNMNLYMriAPELYHKMLVVGGIDRVYEIGRQFRNEGiDLTHN 320
Cdd:PLN02850 239 LLSKGFVEIHTP--KLIAGaseggSAV---FRLDYKGQPACLAQ--SPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 321 P--EFTTCEFYMAYAD-YHDLMEITEKLLSGMVKHITGAYK------VTYHPDGPegqayeIDFTPPFRRISMTQ--ELE 389
Cdd:PLN02850 311 HlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKkeleaiREQYPFEP------LKYLPKTLRLTFAEgiQML 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 390 KELGVKFPPpdtydsdemrkfLDDLCVQKEvecpppRTTARL-LDKLVGDFlevkcinptYICD-HPQIMSP---LAKWH 464
Cdd:PLN02850 385 KEAGVEVDP------------LGDLNTESE------RKLGQLvKEKYGTDF---------YILHrYPLAVRPfytMPCPD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 465 RSQkgLTERFELFVMKKEICNAYTELNDPirqrELFEQQAKAKA-EGDDEAMFIDetfctALEYGLPPTAGWGMGIDRLT 543
Cdd:PLN02850 438 DPK--YSNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEECGiDVKTISTYID-----SFRYGAPPHGGFGVGLERVV 506
|
490
....*....|....*.
gi 1036551372 544 MFLTDSNNIKEVLLFP 559
Cdd:PLN02850 507 MLFCGLNNIRKTSLFP 522
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
107-559 |
1.44e-17 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 85.81 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 107 DHLTDVVLNLSGRVHAKRASGaKLLFYDLRGEGVKLQVMANSRNYTSEEaFVHINNKLRRGDIIGVRGNPGK-------T 179
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEGDVPKE-MIDFIGQIPTESIVDVEATVCKveqpitsT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 180 KKGELSIIPVEMTLLSPCLHMLPhlhFGLKDK-------------ETRFRQRYLDLiLNDFVRQKFVTRSKIITYLRSFL 246
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 247 DQLGFLEIETPMMNLIPGGAVAKPF-ITYhndLNMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL-THNPEFT 324
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFkLEY---FNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 325 TCEFYMAYAD-YHDLMEITEKLLSGMVKHITGaykvtyHPDGPEGQAYEIDFTPPFRRisMTQELEKELGV-----KFPP 398
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLAT------HTKELKAVCQQYPFEPLVWK--LTPERMKELGVgviseGVEP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 399 PDTY-------DSDEMRKFLDDlCVQ-----KEVECPPPRTTARLLDKLVGDFLEVKCINPTYICDH-PQIMSPLAKWH- 464
Cdd:PTZ00401 377 TDKYqarvhnmDSRMLRINYMH-CIEllntvLEEKMAPTDDINTTNEKLLGKLVKERYGTDFFISDRfPSSARPFYTMEc 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 465 RSQKGLTERFELFVMKKEICNAYTELNDPirqrELFEQQAKakaegddeAMFIDET----FCTALEYGLPPTAGWGMGID 540
Cdd:PTZ00401 456 KDDERFTNSYDMFIRGEEISSGAQRIHDP----DLLLARAK--------MLNVDLTpikeYVDSFRLGAWPHGGFGVGLE 523
|
490
....*....|....*....
gi 1036551372 541 RLTMFLTDSNNIKEVLLFP 559
Cdd:PTZ00401 524 RVVMLYLGLSNVRLASLFP 542
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
102-559 |
4.24e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 85.04 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 102 HLQPgDHLTDVVLnLSGRVHAKRASGaKLLFYDLRGEGVKLQVMAnSRNYTSEEAFvHINNKLRRGDIIGVRG------- 174
Cdd:PRK12820 11 HLSL-DDTGREVC-LAGWVDAFRDHG-ELLFIHLRDRNGFIQAVF-SPEAAPADVY-ELAASLRAEFCVALQGevqkrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 175 ---NPgKTKKGELSIIPVEMTLLSPCLhMLPhlhFGLKDK----------------ETRFRQRYLDlILNDFVRQKFVTR 235
Cdd:PRK12820 86 eteNP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 236 SKIITYLRSFLDQLGFLEIETPMMNL-IPGGAvaKPFITYHNDLNMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNE 313
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 314 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKhITGAYKVTYHPDGPEGQAYE---------------IDFTPP 378
Cdd:PRK12820 238 DLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFA-IGGIALPRPFPRMPYAEAMDttgsdrpdlrfdlkfADATDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 379 FRRIS------------------------------MTQELEKELGVKFPPPDT-----------------YDSDE----M 407
Cdd:PRK12820 317 FENTRygifkqilqrggrikginikgqseklsknvLQNEYAKEIAPSFGAKGMtwmraeaggldsnivqfFSADEkealK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 408 RKFL----DDLCVQKEVECPPPRTTARLLDKLVGDFLEV---KCINPTYICDHPQIMS-----------PLAKWHRSQ-- 467
Cdd:PRK12820 397 RRFHaedgDVIIMIADASCAIVLSALGQLRLHLADRLGLipeGVFHPLWITDFPLFEAtddggvtsshhPFTAPDREDfd 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 468 ----KGL----TERFELFVMKKEICNAYTELNDPIRQRELFEQQAKAKAEGDDEAMFidetFCTALEYGLPPTAGWGMGI 539
Cdd:PRK12820 477 pgdiEELldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGF----FLRAFDFAAPPHGGIALGL 552
|
570 580
....*....|....*....|
gi 1036551372 540 DRLTMFLTDSNNIKEVLLFP 559
Cdd:PRK12820 553 DRVVSMILQTPSIREVIAFP 572
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
234-347 |
2.35e-16 |
|
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: 77.93 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 234 TRSKIITYLRSFLDQLGFLEIETPMMNLIPG----GAVAKPFITYHNDLNMNLYMRIAPELYHKMLVVGGI----DRVYE 305
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1036551372 306 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKLLS 347
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
116-196 |
3.96e-16 |
|
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: 73.37 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGaKLLFYDLRGEGVKLQVMANSRNytsEEAFVHINNKLRRGDIIGVRGNPGKT-----KKGELSIIPVE 190
Cdd:cd04100 4 LAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEE---LGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEE 79
|
....*.
gi 1036551372 191 MTLLSP 196
Cdd:cd04100 80 LEVLSK 85
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
235-559 |
8.45e-15 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 75.83 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 235 RSKIITYLRSFLDQLGFLEIETPMMN-----LIPGGAVAKPFityhnDLNMNLY---MRIAPEL-YHKMLVVGGIDRVYE 305
Cdd:PRK06462 33 QSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSDLPVK-----QISIDFYgveYYLADSMiLHKQLALRMLGKIFY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 306 IGRQFRNEG---IDLTHNPEFTTCEFYMAYADYHDLMEITEKLLSGMVKHITGAYKVT---YHPDGPEgqayeidFTPPF 379
Cdd:PRK06462 108 LSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDElefFGRDLPH-------LKRPF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 380 RRISMTQ--ELEKELGVKFPPPDTYDSDEMRkflddlcvqkevecppprttarlldklvgdFLEVKCINPTYICDHPQIM 457
Cdd:PRK06462 181 KRITHKEavEILNEEGCRGIDLEELGSEGEK------------------------------SLSEHFEEPFWIIDIPKGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 458 SPLakWHRSQKGLTER---FELFVMKK--EICNAyTElndpiRQRELFEQQAKAKAEGDDEAMFidETFCTALEYGLPPT 532
Cdd:PRK06462 231 REF--YDREDPERPGVlrnYDLLLPEGygEAVSG-GE-----REYEYEEIVERIREHGVDPEKY--KWYLEMAKEGPLPS 300
|
330 340
....*....|....*....|....*..
gi 1036551372 533 AGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:PRK06462 301 AGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
116-194 |
1.71e-12 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 63.02 E-value: 1.71e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036551372 116 LSGRVHAKRASGAKLLFYDLRGEGVKLQVMANSrnytseEAFVHINNKLRRGDIIGVRGNPGKTKKGELSIIPVEMTLL 194
Cdd:pfam01336 3 VAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFK------EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
116-222 |
8.00e-07 |
|
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: 48.67 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551372 116 LSGRVHAKRASGaKLLFYDLR-GEGVkLQVMANSRNYTSEEAFvhinNKLRRGDIIGVRG----------NPgKTKKGEL 184
Cdd:cd04317 19 LCGWVQRRRDHG-GLIFIDLRdRYGI-VQVVFDPEEAPEFELA----EKLRNESVIQVTGkvrarpegtvNP-KLPTGEI 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1036551372 185 SIIPVEMTLLSPClhmlPHLHFGLKDK-----ETRFRQRYLDL 222
Cdd:cd04317 92 EVVASELEVLNKA----KTLPFEIDDDvnvseELRLKYRYLDL 130
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
527-559 |
2.38e-04 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 43.94 E-value: 2.38e-04
10 20 30
....*....|....*....|....*....|...
gi 1036551372 527 YGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
118-181 |
9.18e-04 |
|
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: 38.70 E-value: 9.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036551372 118 GRVHAKRASGAKLLFYDLRGEGVKLQVMANSRNYTSEEAFVHINNKLRRGDIIGVRGNPGKTKK 181
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEE 69
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
526-559 |
1.84e-03 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 41.16 E-value: 1.84e-03
10 20 30
....*....|....*....|....*....|....
gi 1036551372 526 EYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
512-559 |
4.52e-03 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 39.96 E-value: 4.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1036551372 512 DEAMFIDETFCTALE---YGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFP 559
Cdd:PLN02603 507 DELKLNKESYWWYLDlrrYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| |
