|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
1-560 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 868.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 1 MAAASGELSKNELKRRLKAEQKAKEKAEKAAAAPAENTAG----KKKSSAAEEEEISPNEYFKLRSAAVQELkRSPATDP 76
Cdd:PLN02502 1 AESNGEPLSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAakgrSRKSAAADDETMDPTQYRANRLKKVEAL-RAKGVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 77 YPHKFHVSSSLEDFIAKYEnSLKEGETLENVKLSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSY-KSEADFEID 155
Cdd:PLN02502 80 YPYKFDVTHTAPELQEKYG-SLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFEKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 156 TSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNNNVREKFQIRAKIIS 235
Cdd:PLN02502 158 HSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 236 YVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHN 315
Cdd:PLN02502 238 YIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 316 PEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHPEgpegpeqELDFTPPFKRVSMIKTLEEKLQVKFPAAd 395
Cdd:PLN02502 318 PEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYHGI-------EIDFTPPFRRISMISLVEEATGIDFPAD- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 396 tFNSPETNQFLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEFCVNPTFICEHPQIMSPLAKYHRSIPGLTERFELFVAK 475
Cdd:PLN02502 390 -LKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFING 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 476 KEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPA 555
Cdd:PLN02502 469 RELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPA 548
|
....*
gi 259677401 556 MKPED 560
Cdd:PLN02502 549 MKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
49-560 |
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: 696.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 49 EEEISPNEYFKLRSAAVQELKRSpATDPYPHKFHVSSSLEDFIAKYENslKEGETLENVKLSVAGRVHAIRESGaKLIFY 128
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREA-GIDPYPNKFPRTHTAAEIREKYDE--LEAEEETGDEVSVAGRIMAKRDMG-KASFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 129 DLRGEGVKVQVMASaKSYKSEADFEIdTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKET 208
Cdd:COG1190 78 DLQDGSGRIQLYLR-RDELGEEAYEL-FKLLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 209 RYRQRYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHK 288
Cdd:COG1190 156 RYRQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 289 MLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHpegpegpEQEL 368
Cdd:COG1190 236 RLIVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTYQ-------GQEI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 369 DFTPPFKRVSMIKTLEEKLQVKFpaaDTFNSPETnqfLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEFCVNPTFICEH 448
Cdd:COG1190 309 DLSPPWRRITMVEAIKEATGIDV---TPLTDDEE---LRALAKELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 449 PQIMSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTG 528
Cdd:COG1190 383 PVEVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTG 462
|
490 500 510
....*....|....*....|....*....|..
gi 259677401 529 GFGMGIDRLAMFLTDSNNIKEVLLFPAMKPED 560
Cdd:COG1190 463 GLGIGIDRLVMLLTDSPSIRDVILFPLMRPEK 494
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
55-560 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 694.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 55 NEYFKLRSAAVQELkRSPATDPYPHKFHVSSSLEDFIAKYENSLKEGETLENVKLSVAGRVHAIRESGaKLIFYDLRGEG 134
Cdd:PRK00484 4 NEQIAVRREKLAEL-REQGIDPYPNKFERTHTAAELRAKYDDKEKEELEELEIEVSVAGRVMLKRVMG-KASFATLQDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 135 VKVQVMASAKSYKSEADFEIdtSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKETRYRQRY 214
Cdd:PRK00484 82 GRIQLYVSKDDVGEEALEAF--KKLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 215 LDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGG 294
Cdd:PRK00484 160 VDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 295 LDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHpegpegpEQELDFTPPF 374
Cdd:PRK00484 240 FERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTYQ-------GTEIDFGPPF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 375 KRVSMIKTLEEKLQVKFPAADTfnspetnQFLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEFCVNPTFICEHPQIMSP 454
Cdd:PRK00484 313 KRLTMVDAIKEYTGVDFDDMTD-------EEARALAKELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 455 LAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGI 534
Cdd:PRK00484 386 LAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGI 465
|
490 500
....*....|....*....|....*.
gi 259677401 535 DRLAMFLTDSNNIKEVLLFPAMKPED 560
Cdd:PRK00484 466 DRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
53-558 |
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: 637.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 53 SPNEYFKLRSAAVQELKRSpATDPYPHKFHVSSSLEDFIAKYENSLKEGETLENVKLSVAGRVHAIReSGAKLIFYDLRG 132
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQT-GNNPYLHKFERTHSAQEFQEKYADLSNEELKEKELKVSIAGRIKAIR-SMGKATFITLQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 133 EGVKVQVMASAKSYkSEADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKETRYRQ 212
Cdd:TIGR00499 79 ESGQIQLYVNKNKL-PEDFYEFDEYLLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 213 RYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVV 292
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 293 GGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHpegpegpEQELDFTP 372
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINYN-------DLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 373 PFKRVSMIktleEKLQVKFPAadTFNSPETNQFLSQLCAKHQVECPAPR-TTARLLDKLVGEFIEEFCVNPTFICEHPQI 451
Cdd:TIGR00499 311 PWKRITMV----DALEMVTGI--DFDILKDDETAKALAKEHGIEVAEDSlTLGHILNKFFEQFLEHTLIQPTFITHYPAE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 452 MSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFG 531
Cdd:TIGR00499 385 ISPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLG 464
|
490 500
....*....|....*....|....*..
gi 259677401 532 MGIDRLAMFLTDSNNIKEVLLFPAMKP 558
Cdd:TIGR00499 465 IGIDRLVMLLTDAPSIRDVLLFPQLRP 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
41-558 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 634.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 41 KKKSsaaEEEEISPNEYFKLRSAAVQElKRSPATDPYPHKFHVSSSLEDFIAKYENsLKEGETLENVKLSVAGRVHAIRE 120
Cdd:PTZ00417 72 KKKE---EEAEVDPRLYYENRSKFIQE-QKAKGINPYPHKFERTITVPEFVEKYQD-LASGEHLEDTILNVTGRIMRVSA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 121 SGAKLIFYDLRGEGVKVQVMASAKSYKSE-ADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPhL 199
Cdd:PTZ00417 147 SGQKLRFFDLVGDGAKIQVLANFAFHDHTkSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-M 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 200 HFGLKDKETRYRQRYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFM 279
Cdd:PTZ00417 226 KYGLKDTEIRYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 280 RIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHPE 359
Cdd:PTZ00417 306 RIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 360 GPEGPEQELDFTPPFKRVSMIKTLEEKLQVKFpaADTFNSPETNQFLSQLCAKHQVECPAPRTTARLLDKLVGEFIE-EF 438
Cdd:PTZ00417 386 GPEKDPIEIDFTPPYPKVSIVEELEKLTNTKL--EQPFDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIEnKY 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 439 CVNPTFICEHPQIMSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCT 518
Cdd:PTZ00417 464 PNKPFFIIEHPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCT 543
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 259677401 519 SLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPAMKP 558
Cdd:PTZ00417 544 SLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
220-558 |
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: 613.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 220 NNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVY 299
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 300 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGsykviyhPEGPEGPEQELDFTPPFKRVSM 379
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING-------KTKIEYGGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 380 IKTLEEKLQVKFPAADTFNSPETNQFLSQLCAKHqveCPAPRTTARLLDKLVGEFIEEFCVNPTFICEHPQIMSPLAKYH 459
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLIKEK---IEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 460 RSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAM 539
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 259677401 540 FLTDSNNIKEVLLFPAMKP 558
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
43-557 |
4.31e-151 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 449.10 E-value: 4.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 43 KSSAAEEEEISPNEYFKLRSAA------VQELKRSPATDP-YP---HKFHVSSSLEDFIAKYeNSLKEGETLENVKLSVA 112
Cdd:PTZ00385 35 RQVASLSSSRSPLELKKPISKAsatktvTQEASRAPRSKLdLPaaySSFRGITPISEVRERY-GYLASGDRAAQATVRVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 113 GRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSYKSEADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSP- 191
Cdd:PTZ00385 114 GRVTSVRDIG-KIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIGADGVPCRMQRGELSVAASRMLILSPy 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 192 -CLHML--PHLH-FG-LKDKETRYRQRYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPF 266
Cdd:PTZ00385 193 vCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 267 VTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVK 346
Cdd:PTZ00385 273 VTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 347 AIRGSYKVIYHPEGPEGPEQELDFTPPFKRVSMIKTLEEKLQVKFPAADTFNSPETNQFLSQLCAKHQVECPAPRTTARL 426
Cdd:PTZ00385 353 RVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 427 LDKLVGEFIEEFCVNPTFICEHPQIMSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGD 506
Cdd:PTZ00385 433 FEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGD 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 259677401 507 DEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPAMK 557
Cdd:PTZ00385 513 EEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
70-560 |
1.30e-147 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 452.88 E-value: 1.30e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 70 RSPATDPYPHKFHVSSSLEDFIAkyensLKEGETLenvklSVAGRVHAIRESGaKLIFYDLRGEGVKVQVM--ASAKSYK 147
Cdd:PRK02983 625 RAAGVDPYPVGVPPTHTVAEALD-----APTGEEV-----SVSGRVLRIRDYG-GVLFADLRDWSGELQVLldASRLEQG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 148 SEADF--EIDtsklrRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNNNVRE 225
Cdd:PRK02983 694 SLADFraAVD-----LGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARD 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 226 KFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQF 305
Cdd:PRK02983 769 LLRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNF 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 306 RNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSyKVIYHPeGPEGPEQELDFTPPFKRVSMIKTLEE 385
Cdd:PRK02983 849 RNEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGA-PVVMRP-DGDGVLEPVDISGPWPVVTVHDAVSE 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 386 KLQVKFpaadtfnSPETN-QFLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEFCVNPTFICEHPQIMSPLAKYHRSIPG 464
Cdd:PRK02983 927 ALGEEI-------DPDTPlAELRKLCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPG 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 465 LTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAMFLTdS 544
Cdd:PRK02983 1000 LAERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-G 1078
|
490
....*....|....*.
gi 259677401 545 NNIKEVLLFPAMKPED 560
Cdd:PRK02983 1079 RSIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
42-559 |
2.84e-129 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 387.88 E-value: 2.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 42 KKSSAAEEEEISPNEYFKLRSAAVQELKRSPATdpYPHKF---HVSSSL-EDFIAKYENSLkegETLeNVKLSVAGRVHA 117
Cdd:PRK12445 3 EQETRGANEAIDFNDELRNRREKLAALRQQGVA--FPNDFrrdHTSDQLhEEFDAKDNQEL---ESL-NIEVSVAGRMMT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 118 IRESGaKLIFYDLRGEGVKVQVMAsAKSYKSEADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLLSPCLHMLP 197
Cdd:PRK12445 77 RRIMG-KASFVTLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 198 HLHFGLKDKETRYRQRYLDLILNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDL 277
Cdd:PRK12445 155 DKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 278 FMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYH 357
Cdd:PRK12445 235 YLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 358 pegpegpEQELDFTPPFKRVSMIKTLEE-KLQVKFPAADTFNSPETnqflsqLCAKHQVECPAPRTTARLLDKLVGEFIE 436
Cdd:PRK12445 315 -------EHVFDFGKPFEKLTMREAIKKyRPETDMADLDNFDAAKA------LAESIGITVEKSWGLGRIVTEIFDEVAE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 437 EFCVNPTFICEHPQIMSPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENF 516
Cdd:PRK12445 382 AHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 259677401 517 CTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPAMKPE 559
Cdd:PRK12445 462 VTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
205-557 |
3.38e-118 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 352.64 E-value: 3.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 205 DKETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPE 284
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 285 LYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHPegpegp 364
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 365 eQELDFTPPFKRVSMIKTLEEKLQVKFPaadtfnspetnqflsqlcaKHQVECPAPRTtaRLLDKLVgefIEEFCVNPTF 444
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVE-------------------ELGYGSDKPDL--RFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 445 ICEHPQIMSPLAKYHRS-IPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKaagdDEAQLVDENFCTSLEYG 523
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEdDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 259677401 524 LPPTGGFGMGIDRLAMFLTDSNNIKEVLLFPAMK 557
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 ... |
227-558 |
2.69e-96 |
|
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: 294.77 E-value: 2.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 227 FQIRAKIISYVRQFLDRLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFR 306
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 307 NEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVIYHpegpegpEQELDFTPPFKRVSMIKTLEEK 386
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTYG-------FELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 387 LQvkfpaadtfnspetnqflsqlcakhqvecpaprttarlldklvgefieefcvnPTFICEHP-QIMSPLAKYHRSIPGL 465
Cdd:cd00669 154 GQ-----------------------------------------------------PLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 466 TERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEaqlvDENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSN 545
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEY----FEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 259677401 546 NIKEVLLFPAMKP 558
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
224-551 |
9.57e-54 |
|
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: 184.92 E-value: 9.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 224 REKFQIRAKIISYVRQFLDRLGFLEIETPMMNmIAGGATA--KPFVT---HHNDLKMDLFMRIAPELYHKMLVVGGLDRV 298
Cdd:COG2269 3 REALRARARLLAAIRAFFAERGVLEVETPALS-VAPGTDPhlDSFATefiGPDGGGRPLYLHTSPEFAMKRLLAAGSGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 299 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRgsykviyhpegpegpeqeldfTPPFKRVS 378
Cdd:COG2269 82 YQIAKVFRNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQLVLGAAG---------------------FAPAERLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 379 MIKTLEEKLQVKFPAADTfnspetnQFLSQLCAKHQVECPAPRTTARLLDKLVGEFIE-EFCVN-PTFICEHPQIMSPLA 456
Cdd:COG2269 141 YQEAFLRYLGIDPLTADL-------DELAAAAAAAGLRVADDDDRDDLLDLLLSERVEpQLGRDrPTFLYDYPASQAALA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 457 KYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDR 536
Cdd:COG2269 214 RISPDDPRVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDR 293
|
330
....*....|....*
gi 259677401 537 LAMFLTDSNNIKEVL 551
Cdd:COG2269 294 LLMLALGAERIDDVL 308
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
240-551 |
3.40e-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: 182.75 E-value: 3.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 240 FLDRLGFLEIETPMMnmIAGGATA---KPFVTH---HNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLT 313
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPVTDphlDAFATEfvgPDGQGRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 314 HNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGSYKVI-YhpegpegpeQELdftppFKRVSMIKTLEEKLQVkfp 392
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFAPAERLsY---------QEA-----FLRYAGIDPLTASLAE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 393 aadtfnspetnqfLSQLCAKHQVECPAPRTTARLLDKLVGEFIEEF--CVNPTFICEHPQIMSPLAKYHRSIPGLTERFE 470
Cdd:TIGR00462 142 -------------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 471 LFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEV 550
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 259677401 551 L 551
Cdd:TIGR00462 289 L 289
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
108-217 |
5.79e-53 |
|
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: 175.74 E-value: 5.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSYkSEADFEIDTSKLRRGDIIGVVGHPGKTKKGELSVMPSEIK 187
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 259677401 188 LLSPCLHMLPHLHFGLKDKETRYRQRYLDL 217
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
94-554 |
3.68e-41 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 154.19 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 94 YENSLKEGETLENVKlsVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKsyKSEADFEiDTSKLRRGDIIGVVGHPGK 173
Cdd:PRK05159 6 LTSELTPELDGEEVT--LAGWVHEIRDLG-GIAFLILRDRSGIIQVVVKKK--VDEELFE-TIKKLKRESVVSVTGTVKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 174 TKK--GELSVMPSEIKLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGF 246
Cdd:PRK05159 80 NPKapGGVEVIPEEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 247 LEIETPmmNMIA----GGAtakpfvthhNDLKMDLFMRIA-----PELYHKMLVVGGLDRVYEIGRQFRNEGIDLT-HNP 316
Cdd:PRK05159 156 TEIFTP--KIVAsgteGGA---------ELFPIDYFEKEAylaqsPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 317 EFTTCEFYMAYAD-YADIMDITEQLVSGMVKAIRGSYKviyhPE----GPEGPEQELdftpPFKRVsmikTLEEKLQVkf 391
Cdd:PRK05159 225 EYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCE----KElellGIELPVPET----PIPRI----TYDEAIEI-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 392 pAADTFNSPETNQFLSqlcAKHQvecpaprttarlldKLVGEFI-EEFCVNPTFICEHPQIMSPL-AKYHRSIPGLTERF 469
Cdd:PRK05159 291 -LKSKGNEISWGDDLD---TEGE--------------RLLGEYVkEEYGSDFYFITDYPSEKRPFyTMPDEDDPEISKSF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 470 ELFVAKKEICNAYTELNDPVVQRERFEQQASDKaagddeaqlvdENFCTSLE---YGLPPTGGFGMGIDRLAMFLTDSNN 546
Cdd:PRK05159 353 DLLFRGLEITSGGQRIHRYDMLVESIKEKGLNP-----------ESFEFYLEafkYGMPPHGGFGLGLERLTMKLLGLEN 421
|
....*...
gi 259677401 547 IKEVLLFP 554
Cdd:PRK05159 422 IREAVLFP 429
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
230-550 |
1.67e-38 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 143.53 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 230 RAKIISYVRQFLDRLGFLEIETPMMNMiaggATA-----KPFVTH----HNDLKMDLFMRIAPElYH-KMLVVGGLDRVY 299
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILSQ----ATVtdihlVPFETRfvgpGASQGKTLWLMTSPE-YHmKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 300 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVsgmvkairgsykviyhpegpegpeQELDFTPPFKRVSM 379
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLL------------------------QQVLDCEPAESLSY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 380 IKTLEEKLQVKFPAADtfnspetNQFLSQLCAKHQVECPAPRTTAR--LLDKLVGEFIE-----EfcvNPTFICEHPQIM 452
Cdd:PRK09350 139 QQAFLRYLGIDPLSAD-------KTQLREVAAKLGLSNIADEEEDRdtLLQLLFTFGVEpnigkE---KPTFVYHFPASQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 453 SPLAKYHRSIPGLTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDEAQLVDENFCTSLEYGLPPTGGFGM 532
Cdd:PRK09350 209 AALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVAL 288
|
330
....*....|....*...
gi 259677401 533 GIDRLAMFLTDSNNIKEV 550
Cdd:PRK09350 289 GVDRLIMLALGAESISEV 306
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
111-554 |
4.89e-36 |
|
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: 139.80 E-value: 4.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 111 VAGRVHAIRESGaKLIFYDLR-GEGVkVQVMASAKSyksEADFEiDTSKLRRGDIIGVVG--HPGKTKKGELSVMPSEIK 187
Cdd:COG0017 19 VAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKDK---LENFE-EAKKLTTESSVEVTGtvVESPRAPQGVELQAEEIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 188 LLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMnmIAGGA--TA 263
Cdd:COG0017 93 VLGEADEPYP---LQPKRHslEFLLDNRHLRL-RTNRFGAIFRIRSELARAIREFFQERGFVEVHTPII--TASATegGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 264 KPFvthhndlKMDLFMRIA-----PELYHKMLVvGGLDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYADIMDIT 337
Cdd:COG0017 167 ELF-------PVDYFGKEAyltqsGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 338 EQLVSGMVKAIRgsykviyhpegpEGPEQELDF------------TPPFKRVSM---IKTLEEK-LQVKFPaaDTFNSPE 401
Cdd:COG0017 239 EEMLKYIIKYVL------------ENCPEELEFlgrdverlekvpESPFPRITYteaIEILKKSgEKVEWG--DDLGTEH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 402 tNQFLSqlcakhqvecpaprttarlldklvgefiEEFCVNPTFICEHPqiMSPLAKYHR---SIPGLTERFELfvakkeI 478
Cdd:COG0017 305 -ERYLG----------------------------EEFFKKPVFVTDYP--KEIKAFYMKpnpDDPKTVAAFDL------L 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 479 CNAYTEL-------NDPVVQRERFEQQASDKaagddeaqlvdENFCTSLE---YGLPPTGGFGMGIDRLAMFLTDSNNIK 548
Cdd:COG0017 348 APGIGEIiggsqreHRYDVLVERIKEKGLDP-----------EDYEWYLDlrrYGSVPHAGFGLGLERLVMWLTGLENIR 416
|
....*.
gi 259677401 549 EVLLFP 554
Cdd:COG0017 417 EVIPFP 422
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
207-554 |
4.20e-31 |
|
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: 123.45 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 207 ETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGFLEIETPMMnmIAGGA--TAKPFvthhndlKMDLFMRIA-- 282
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKI--TSTDTegGAELF-------KVSYFGKPAyl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 283 ---PELYHKMLVvGGLDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYADIMDITEQLVSGMVKAIRGSYK---- 353
Cdd:cd00776 75 aqsPQLYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkele 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 354 -VIYHPEGPEGPEqeldftPPFKRVSM---IKTLEEK-LQVKFPAADTFNSPEtnqflsqlcakhqvecpaprttarllD 428
Cdd:cd00776 154 lVNQLNRELLKPL------EPFPRITYdeaIELLREKgVEEEVKWGEDLSTEH--------------------------E 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 429 KLVGEFIEEfcvNPTFICEHPQIMSPL-AKYHRSIPGLTERFELFVAKK-EICNAYTELNDPVVQRERFeqqasdKAAGD 506
Cdd:cd00776 202 RLLGEIVKG---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDYDELEERI------KEHGL 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 259677401 507 DEAQLvdENFCTSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:cd00776 273 DPESF--EWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
105-554 |
2.85e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 122.10 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 105 ENVKLSvaGRVHAIRESGaKLIFYDLRG-EGVkVQVMASaksyKSEADFEIdTSKLRRGDIIGVVGH----PGKT----- 174
Cdd:PRK00476 18 QTVTLC--GWVHRRRDHG-GLIFIDLRDrEGI-VQVVFD----PDAEAFEV-AESLRSEYVIQVTGTvrarPEGTvnpnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 175 KKGELSVMPSEIKLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGFLEI 249
Cdd:PRK00476 89 PTGEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL-RRPEMQKNLKLRSKVTSAIRNFLDDNGFLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 250 ETPMMnmiaGGAT---AKPFV----THHNDlkmdlFMRI--APELYHKMLVVGGLDRVYEIGRQFRNEgiDLTHN--PEF 318
Cdd:PRK00476 164 ETPIL----TKSTpegARDYLvpsrVHPGK-----FYALpqSPQLFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 319 TT--CEfyMAYADYADIMDITEQLVSGMVKAIRGsykviyhpegpegpeqeLDFTPPFKRVS----MIKTLEEKLQVKFP 392
Cdd:PRK00476 233 TQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTyaeaMRRYGSDKPDLRFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 393 -----AADTFNSPETNQFLSQLCAKHQVEC-PAPRTTARL----LDKLvGEFIEEF--------CVNPtficehPQIMSP 454
Cdd:PRK00476 294 lelvdVTDLFKDSGFKVFAGAANDGGRVKAiRVPGGAAQLsrkqIDEL-TEFAKIYgakglayiKVNE------DGLKGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 455 LAKY--HRSIPGLTERFE-------LFVA-KKEICN-------------------------------------------- 480
Cdd:PRK00476 367 IAKFlsEEELAALLERTGakdgdliFFGAdKAKVVNdalgalrlklgkelglidedkfaflwvvdfpmfeydeeegrwva 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 481 ---------------------------AY------TEL-------NDPVVQRERFEqqasdkAAG--DDEAQ-----LVD 513
Cdd:PRK00476 447 ahhpftmpkdedldelettdpgkarayAYdlvlngYELgggsiriHRPEIQEKVFE------ILGisEEEAEekfgfLLD 520
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 259677401 514 enfctSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:PRK00476 521 -----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
39-565 |
2.40e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 115.96 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 39 AGKKKSSAAEEEEispneyfKLRSAAVQELKRSPATDPYPHKFHvSSSLEDFIAKYENSL-----KEGETLENVKLSVAG 113
Cdd:PLN02850 17 AAKKAAAKAEKLR-------REATAKAAAASLEDEDDPLASNYG-DVPLEELQSKVTGREwtdvsDLGEELAGSEVLIRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 114 RVHAIRESGaKLIFYDLRGEGVKVQVMASAKSYKSEADFEIDTSKLRRG---DIIGVVGHPGKTKKG-----ELSVmpSE 185
Cdd:PLN02850 89 RVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSREsvvDVEGVVSVPKKPVKGttqqvEIQV--RK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 186 IKLLSPCLHMLPhlhFGLKD----------------------KETRYRQRYLDLIL--NNNVrekFQIRAKIISYVRQFL 241
Cdd:PLN02850 166 IYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDLRTpaNQAI---FRIQSQVCNLFREFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 242 DRLGFLEIETPmmNMIAGGATAKPFVthhndLKMDLFMRIA-----PELYHKMLVVGGLDRVYEIGRQFRNEGiDLTHNP 316
Cdd:PLN02850 240 LSKGFVEIHTP--KLIAGASEGGSAV-----FRLDYKGQPAclaqsPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHRH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 317 --EFTTCEFYMAYAD-YADIMDITEQLVSGMVKAIRGSYKviyhPEgPEGPEQELDFTPPfkrvsmiKTLEEKLQVKFpa 393
Cdd:PLN02850 312 lcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCK----KE-LEAIREQYPFEPL-------KYLPKTLRLTF-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 394 adtfnsPETNQFLSQlcAKHQVECPAPRTTA--RLLDKLVGE-FIEEFcvnptFIcehpqimspLAKYHRSI-------- 462
Cdd:PLN02850 378 ------AEGIQMLKE--AGVEVDPLGDLNTEseRKLGQLVKEkYGTDF-----YI---------LHRYPLAVrpfytmpc 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 463 ---PGLTERFELFVAKKEICNAYTELNDPvvqrERFEQQAsdKAAGDDEAQLvdENFCTSLEYGLPPTGGFGMGIDRLAM 539
Cdd:PLN02850 436 pddPKYSNSFDVFIRGEEIISGAQRVHDP----ELLEKRA--EECGIDVKTI--STYIDSFRYGAPPHGGFGVGLERVVM 507
|
570 580
....*....|....*....|....*.
gi 259677401 540 FLTDSNNIKEVLLFpamkPEDANRTA 565
Cdd:PLN02850 508 LFCGLNNIRKTSLF----PRDPQRLA 529
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
105-554 |
7.06e-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: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 105 ENVKLSvaGRVHAIRESGAkLIFYDLRG-EGVkVQVMASAKSykSEADFEIdTSKLRRGDIIGVVGH----PGKTKK--- 176
Cdd:COG0173 17 QEVTLS--GWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDPDD--SAEAFEK-AEKLRSEYVIAVTGKvrarPEGTVNpkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 177 --GELSVMPSEIKLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNNNVREKFQIRAKIISYVRQFLDRLGFLEI 249
Cdd:COG0173 90 ptGEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 250 ETPMMnmiaGGAT---AKPFV----THHNDlkmdlFMRI--APELYHKMLVVGGLDRVYEIGRQFRNEgiDLTHN--PEF 318
Cdd:COG0173 165 ETPIL----TKSTpegARDYLvpsrVHPGK-----FYALpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADrqPEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 319 TT--CEfyMAYADYADIMDITEQLVSGMVKAIRGsykviyhpegpegpeqeLDFTPPFKRVS----MIKTLEEKLQVKFP 392
Cdd:COG0173 234 TQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMTyaeaMERYGSDKPDLRFG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 393 -----AADTFNSPETNQFLSQLCAKHQVEC-PAPrTTARL----LDKLVgEFIEEF--------CVNPTficehpQIMSP 454
Cdd:COG0173 295 lelvdVTDIFKDSGFKVFAGAAENGGRVKAiNVP-GGASLsrkqIDELT-EFAKQYgakglayiKVNED------GLKSP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 455 LAKYH--RSIPGLTERFE-------LFVA-KKEICN-------------------------------------------- 480
Cdd:COG0173 367 IAKFLseEELAAILERLGakpgdliFFVAdKPKVVNkalgalrlklgkelglidedefaflwvvdfplfeydeeegrwva 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 481 --------------------------AY------TEL-------NDPVVQRERFEqqasdkAAG--DDEAQ-----LVDe 514
Cdd:COG0173 447 mhhpftmpkdedldlletdpgkvrakAYdlvlngYELgggsiriHDPELQEKVFE------LLGisEEEAEekfgfLLE- 519
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 259677401 515 nfctSLEYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:COG0173 520 ----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
227-554 |
4.21e-25 |
|
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.
Pssm-ID: 238400 [Multi-domain] Cd Length: 280 Bit Score: 104.96 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 227 FQIRAKIISYVRQFLDRLGFLEIETPMMnmiaGGAT---AKPFV----THHNdlkmdLFMRI--APELYHKMLVVGGLDR 297
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPIL----TKSTpegARDFLvpsrLHPG-----KFYALpqSPQLFKQLLMVSGFDR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 298 VYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGsykviyhpegpegpeqeLDFTPPFKRV 377
Cdd:cd00777 72 YFQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 378 smikTLEEKLQ---------VKFPAADTfnSPETNQFLSqlcAKHQVECPAPrttarlldklvgEFIEEFCVNPTFIceh 448
Cdd:cd00777 135 ----TYAEAMErygfkflwiVDFPLFEW--DEEEGRLVS---AHHPFTAPKE------------EDLDLLEKDPEDA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 449 pqimsplakyhrsipgLTERFELFVAKKEICNAYTELNDPVVQRERFEQqasdkaAGDDEAQLVDE--NFCTSLEYGLPP 526
Cdd:cd00777 191 ----------------RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEI------LGLSEEEAEEKfgFLLEAFKYGAPP 248
|
330 340
....*....|....*....|....*...
gi 259677401 527 TGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:cd00777 249 HGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
108-378 |
1.28e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 99.09 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGAkLIFYDLRGEGVKVQVMASAKSYKseaDFEIDTSKLRRGDIIGVVG----HPG-----KTKKGE 178
Cdd:PLN02903 74 RVTLCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDEFP---EAHRTANRLRNEYVVAVEGtvrsRPQespnkKMKTGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 179 LSVMPSEIKLLSPCLHMLPHLHFGLKD------KETRYRQRYLDL---ILNNNVRekfqIRAKIISYVRQFL-DRLGFLE 248
Cdd:PLN02903 150 VEVVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLrrpQMNANLR----LRHRVVKLIRRYLeDVHGFVE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 249 IETPMMN---------------MIAGGATAKPfvthhndlkmdlfmrIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLT 313
Cdd:PLN02903 226 IETPILSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRAD 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259677401 314 HNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRGsykviyhpegpegpeqeLDFTPPFKRVS 378
Cdd:PLN02903 291 RQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLT 338
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
108-566 |
1.21e-19 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 93.13 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSykSEADFEIDTSKLRRGDIIGVVGHPGK---------TKKGE 178
Cdd:PRK12820 20 EVCLAGWVDAFRDHG-ELLFIHLRDRNGFIQAVFSPEA--APADVYELAASLRAEFCVALQGEVQKrleetenphIETGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 179 LSVMPSEIKLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNNNVREKFQIRAKIISYVRQFLD 242
Cdd:PRK12820 97 IEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKRHRIIKCARDFLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 243 RLGFLEIETPMMNMIAGGATAKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGLDRVYEIGRQFRNEGIDLTHNPEFTTCE 322
Cdd:PRK12820 172 SRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEFTQLD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 323 FYMAYADYADIMDITEQLVSGM--VKAI-------RGSYKVIYHPEGPEGPEQELDF-----TPPFKRVSM--------- 379
Cdd:PRK12820 252 IEASFIDEEFIFELIEELTARMfaIGGIalprpfpRMPYAEAMDTTGSDRPDLRFDLkfadaTDIFENTRYgifkqilqr 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 380 --------IKTLEEKLQ-----------------------------------VKFPAAD-------TFNSPETNQFLSQL 409
Cdd:PRK12820 332 ggrikginIKGQSEKLSknvlqneyakeiapsfgakgmtwmraeaggldsniVQFFSADekealkrRFHAEDGDVIIMIA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 410 CAKHQVECPA-PRTTARLLDKLvgEFIEEFCVNPTFICEHPQIMS-----------PLAKYHRS------IPGL----TE 467
Cdd:PRK12820 412 DASCAIVLSAlGQLRLHLADRL--GLIPEGVFHPLWITDFPLFEAtddggvtsshhPFTAPDREdfdpgdIEELldlrSR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 468 RFELFVAKKEICNAYTELNDPVVQRERFeqqasdKAAGDDEAQLVDE--NFCTSLEYGLPPTGGFGMGIDRLAMFLTDSN 545
Cdd:PRK12820 490 AYDLVVNGEELGGGSIRINDKDIQLRIF------AALGLSEEDIEDKfgFFLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
|
570 580
....*....|....*....|.
gi 259677401 546 NIKEVLLFPamkpedANRTAA 566
Cdd:PRK12820 564 SIREVIAFP------KNRSAA 578
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
109-564 |
5.92e-19 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 90.44 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 109 LSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSY--KSEADF--EIDTSKLR--RGDIIGVVGHPGKTKKGELSVM 182
Cdd:PTZ00401 81 VLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEGDvpKEMIDFigQIPTESIVdvEATVCKVEQPITSTSHSDIELK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 183 PSEIKLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDL--ILNNNVrekFQIRAKIISYVRQFLDRLGFL 247
Cdd:PTZ00401 160 VKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDLrtPASGAI---FRLQSRVCQYFRQFLIDSDFC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 248 EIETPMMNMIA--GGAtakpfvthhNDLKMDLFMRIA-----PELYHKMLVVGGLDRVYEIGRQFRNEGIDL-THNPEFT 319
Cdd:PTZ00401 234 EIHSPKIINAPseGGA---------NVFKLEYFNRFAylaqsPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 320 TCEFYMAYAD-YADIMDITEQLVSGMVKAIRGsykviyHPEGPEGPEQELDFTPPFKRVSMIKTLE-------------E 385
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLAT------HTKELKAVCQQYPFEPLVWKLTPERMKElgvgvisegveptD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 386 KLQVKFPAADT----FNSPETNQFLSQLCAKHQVECPAPRTT-ARLLDKLVGE-FIEEFCVNPTFicehPQIMSPLakYH 459
Cdd:PTZ00401 379 KYQARVHNMDSrmlrINYMHCIELLNTVLEEKMAPTDDINTTnEKLLGKLVKErYGTDFFISDRF----PSSARPF--YT 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 460 RSIPG---LTERFELFVAKKEICNAYTELNDPVVQRERFEQQASDKAAGDDeaqlvdenFCTSLEYGLPPTGGFGMGIDR 536
Cdd:PTZ00401 453 MECKDderFTNSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE--------YVDSFRLGAWPHGGFGVGLER 524
|
490 500
....*....|....*....|....*...
gi 259677401 537 LAMFLTDSNNIKEVLLFpamkPEDANRT 564
Cdd:PTZ00401 525 VVMLYLGLSNVRLASLF----PRDPQRT 548
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
108-191 |
7.19e-18 |
|
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: 78.38 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSYKSEADFeidTSKLRRGDIIGVVGHPGKT-----KKGELSVM 182
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEELGEFFEE---AEKLRTESVVGVTGTVVKRpegnlATGEIELQ 76
|
....*....
gi 259677401 183 PSEIKLLSP 191
Cdd:cd04100 77 AEELEVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
229-342 |
6.24e-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: 76.77 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 229 IRAKIISYVRQFLDRLGFLEIETP-MMNMIAGGAT---AKPFVTHHNDLKMDLFMRIAPELYHKMLVVGGL----DRVYE 300
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPiVEREPLLEKAghePKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 259677401 301 IGRQFRNEGI--DLTHNPEFTTCEFYMAYADYADiMDITEQLVS 342
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDGEE-ASEFEELIE 123
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
206-554 |
2.26e-15 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 77.37 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 206 KETRYRQRYLDLILNNNV-------REKFQIRAKIISYVRQFLDRLGFLEIETPMMNMI----AGGATAKPFvthhNDLK 274
Cdd:PRK06462 2 DLERYPKEYEEFLRMSWKhissekyRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPStdplMGLGSDLPV----KQIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 275 MDLF---MRIAPEL-YHKMLVVGGLDRVYEIGRQFRNEG---IDLTHNPEFTTCEFYMAYADYADIMDITEQLVSGMVKA 347
Cdd:PRK06462 78 IDFYgveYYLADSMiLHKQLALRMLGKIFYLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 348 IRGSYKVIYHPEGPEGPEqeldFTPPFKRVSM--IKTLEEKLQVKFPAADTFNSpETNQFLSqlcakhqvecpaprttar 425
Cdd:PRK06462 158 LLEEHEDELEFFGRDLPH----LKRPFKRITHkeAVEILNEEGCRGIDLEELGS-EGEKSLS------------------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 426 lldklvgEFIEEfcvnPTFICEHPQIMSPLakYHRSIPG-----------LTERFELFVAKKEICNAYTELndpvvqrer 494
Cdd:PRK06462 215 -------EHFEE----PFWIIDIPKGSREF--YDREDPErpgvlrnydllLPEGYGEAVSGGEREYEYEEI--------- 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259677401 495 feqQASDKAAGDDEaqlvdENFCTSLEY---GLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:PRK06462 273 ---VERIREHGVDP-----EKYKWYLEMakeGPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
110-189 |
6.80e-15 |
|
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: 69.57 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 110 SVAGRVHAIRESGAKLIFYDLRGEGVKVQVMASAKSYKSEADfeidtsKLRRGDIIGVVGHPGKTKKGELSVMPSEIKLL 189
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFKEEAEKLAK------KLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
105-217 |
2.70e-08 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 52.52 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 105 ENVKLsvAGRVHAIRESGaKLIFYDLR-GEGVkVQVMASAKSYKSEADFEidtsKLRRGDIIGVVGH----PGKTKK--- 176
Cdd:cd04317 15 QEVTL--CGWVQRRRDHG-GLIFIDLRdRYGI-VQVVFDPEEAPEFELAE----KLRNESVIQVTGKvrarPEGTVNpkl 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 259677401 177 --GELSVMPSEIKLLSPClhmlPHLHFGLKDK-----ETRYRQRYLDL 217
Cdd:cd04317 87 ptGEIEVVASELEVLNKA----KTLPFEIDDDvnvseELRLKYRYLDL 130
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
108-554 |
1.33e-05 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 47.80 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGaKLIFYDLR-GEGVK-VQVMASaksyKSEADFEiDTSKLRRGDIIGVVGH----PGKTKKGELSV 181
Cdd:PRK03932 18 EVTVRGWVRTKRDSG-KIAFLQLRdGSCFKqLQVVKD----NGEEYFE-EIKKLTTGSSVIVTGTvvesPRAGQGYELQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 182 mpSEIKLLSPC---------------LHMLPHLhfglkdketryRQRyldlilNNNVREKFQIRAKIISYVRQFLDRLGF 246
Cdd:PRK03932 92 --TKIEVIGEDpedypiqkkrhsiefLREIAHL-----------RPR------TNKFGAVMRIRNTLAQAIHEFFNENGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 247 LEIETPMMNMIAGGATAKPF--VTHHNDLKMDLFMRIApelyhkMLVVGG----------LDRVYEIGRQFRNEGIDLT- 313
Cdd:PRK03932 153 VWVDTPIITASDCEGAGELFrvTTLDLDFSKDFFGKEA------YLTVSGqlyaeayamaLGKVYTFGPTFRAENSNTRr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 314 HNPEFTTCEFYMAYADYADIMDITEQLVSGMVKAIRgsykviyhpegpEGPEQELDF-----------------TPPFKR 376
Cdd:PRK03932 227 HLAEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYVL------------ENCPDDLEFlnrrvdkgdierlenfiESPFPR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 377 VS---MIKTLEEK-LQVKFPAA--DTFNSPEtNQFLSqlcakhqvecpaprttarlldklvgefiEEFCVNPTFICEHPq 450
Cdd:PRK03932 295 ITyteAIEILQKSgKKFEFPVEwgDDLGSEH-ERYLA----------------------------EEHFKKPVFVTNYP- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 451 imsplakyhrsipglterfelfvakKEICNAYTELNDP--VV-----------------QRErfeqqasdkaagDDEAQL 511
Cdd:PRK03932 345 -------------------------KDIKAFYMRLNPDgkTVaamdllapgigeiiggsQRE------------ERLDVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 259677401 512 VD--ENFCTSLE----------YGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:PRK03932 388 EAriKELGLNKEdywwyldlrrYGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
108-190 |
1.67e-04 |
|
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.
Pssm-ID: 239811 [Multi-domain] Cd Length: 108 Bit Score: 41.15 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 108 KLSVAGRVHAIRESGaKLIFYDLRGEGVKVQVMASAKSYKSEAdFEIdTSKLRRGDII---GVVGHPGKTKKGeLSVMPS 184
Cdd:cd04316 14 EVTVAGWVHEIRDLG-GIKFVILRDREGIVQVTAPKKKVDKEL-FKT-VRKLSRESVIsvtGTVKAEPKAPNG-VEIIPE 89
|
....*.
gi 259677401 185 EIKLLS 190
Cdd:cd04316 90 EIEVLS 95
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
507-554 |
4.34e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 43.04 E-value: 4.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 259677401 507 DEAQLVDENFCTSLE---YGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:PLN02603 507 DELKLNKESYWWYLDlrrYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFP 557
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
521-554 |
1.46e-03 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 41.55 E-value: 1.46e-03
10 20 30
....*....|....*....|....*....|....
gi 259677401 521 EYGLPPTGGFGMGIDRLAMFLTDSNNIKEVLLFP 554
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
113-197 |
2.39e-03 |
|
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: 37.54 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259677401 113 GRVHAIRESGAKLIFYDLRGEGVKVQVMASAKSYKSEADFEIDTSKLRRG---DIIGVVGHPGKTKKG------ELSVmp 183
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKEsivDVEGTVKKPEEPIKSctqqdvELHI-- 83
|
90
....*....|....
gi 259677401 184 SEIKLLSPCLHMLP 197
Cdd:cd04320 84 EKIYVVSEAAEPLP 97
|
|
| |
