|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
12-577 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 898.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 12 DGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNhttdnGVGPEEESVDPNQYYKIRSQAIHQLKVNG 91
Cdd:PLN02502 2 ESNGEPLSKNALKKRLKAKQAEEEKAAKEEAKAAAAAAAAKGRSRK-----SAAADDETMDPTQYRANRLKKVEALRAKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 92 EDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNY-KSEEEFI 170
Cdd:PLN02502 77 VEPYPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 171 HINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKI 250
Cdd:PLN02502 156 KLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 251 ITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT 330
Cdd:PLN02502 236 ISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 331 HNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHpdgpegqAYDVDFTPPFRRINMVEELEKALGMKLPE 410
Cdd:PLN02502 316 HNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRISMISLVEEATGIDFPA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 411 tnLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFV 490
Cdd:PLN02502 389 --DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 491 MKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLF 570
Cdd:PLN02502 467 NGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAF 546
|
....*..
gi 5031815 571 PAMKPED 577
Cdd:PLN02502 547 PAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
68-578 |
0e+00 |
|
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440803 [Multi-domain] Cd Length: 495 Bit Score: 703.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 68 EESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDhLTDITLKVAGRIHAKRaSGGKLIFYDL 147
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE-ETGDEVSVAGRIMAKR-DMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 148 RGEGVKLQVMAnSRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRY 227
Cdd:COG1190 80 QDGSGRIQLYL-RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 228 RQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKML 307
Cdd:COG1190 158 RQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 308 VVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDF 387
Cdd:COG1190 238 IVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 388 TPPFRRINMVEELEKALGmkLPETNLFETEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQ 467
Cdd:COG1190 311 SPPWRRITMVEAIKEATG--IDVTPLTDDEELRALAK----ELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 468 IMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGW 547
Cdd:COG1190 385 EVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGL 464
|
490 500 510
....*....|....*....|....*....|.
gi 5031815 548 GMGIDRVAMFLTDSNNIKEVLLFPAMKPEDK 578
Cdd:COG1190 465 GIGIDRLVMLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
72-577 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 696.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 72 DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGD-HLTDITLKVAGRIHAKRaSGGKLIFYDLRGE 150
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKR-VMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 151 GVKLQVMAnSRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQR 230
Cdd:PRK00484 81 SGRIQLYV-SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 231 YLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVG 310
Cdd:PRK00484 159 YVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 311 GIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPP 390
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 391 FRRINMVEELEKALGMKLPETNlfeTEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMS 470
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDFDDMT---DEEARALAK----ELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 471 PLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMG 550
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 5031815 551 IDRVAMFLTDSNNIKEVLLFPAMKPED 577
Cdd:PRK00484 465 IDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
67-575 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 640.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 67 EEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYD 146
Cdd:PTZ00417 76 EEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQKLRFFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 147 LRGEGVKLQVMAN-SRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPhLHFGLKDKET 225
Cdd:PTZ00417 156 LVGDGAKIQVLANfAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-MKYGLKDTEI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 226 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 305
Cdd:PTZ00417 235 RYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 306 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDV 385
Cdd:PTZ00417 315 MLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 386 DFTPPFRRINMVEELEKALGMKLPETnlFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCIN-PTFICD 464
Cdd:PTZ00417 395 DFTPPYPKVSIVEELEKLTNTKLEQP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 465 HPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPT 544
Cdd:PTZ00417 473 HPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPT 552
|
490 500 510
....*....|....*....|....*....|.
gi 5031815 545 AGWGMGIDRVAMFLTDSNNIKEVLLFPAMKP 575
Cdd:PTZ00417 553 GGLGLGIDRITMFLTNKNCIKDVILFPTMRP 583
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
72-575 |
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: 636.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 72 DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH-LTDITLKVAGRIHAKRaSGGKLIFYDLRGE 150
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkEKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 151 GVKLQVMANSRNYKseEEFIHINNK-LRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQ 229
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 230 RYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVV 309
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 310 GGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTP 389
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 390 PFRRINMVEELEKALGMKLpetNLFETEETRKILDDICVAKAVECPPprTTARLLDKLVGEFLEVTCINPTFICDHPQIM 469
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDF---DILKDDETAKALAKEHGIEVAEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 470 SPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGM 549
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 5031815 550 GIDRVAMFLTDSNNIKEVLLFPAMKP 575
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 ... |
237-575 |
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: 624.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 237 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVY 316
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 317 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINM 396
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 397 VEELEKALGMKLPETNLFETEETRKILDDICvakAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWH 476
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 477 RSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAM 556
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 5031815 557 FLTDSNNIKEVLLFPAMKP 575
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
104-581 |
1.11e-145 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 436.00 E-value: 1.11e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 104 SLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRaSGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIG 183
Cdd:PTZ00385 88 PISEVRERYGYLASGDRAAQATVRVAGRVTSVR-DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 184 VQGNPGKTKKGELSIIPYEITLLSP--CLHML--PHLH-FG-LKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSF 257
Cdd:PTZ00385 167 ADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 258 LDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTT 337
Cdd:PTZ00385 247 FNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 338 CEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETE 417
Cdd:PTZ00385 327 CEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTP 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 418 ETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICN 497
Cdd:PTZ00385 407 KGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 498 AYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPED 577
Cdd:PTZ00385 487 AYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDI 566
|
....
gi 5031815 578 KKEN 581
Cdd:PTZ00385 567 RSHD 570
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
87-577 |
7.70e-142 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 438.63 E-value: 7.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 87 LKVNGEDPYPhkfhVDISLTDFIQkyshlQPGDHLTDITLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANsrnyKSE 166
Cdd:PRK02983 624 LRAAGVDPYP----VGVPPTHTVA-----EALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLD----ASR 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 167 EEFIHINNKLR---RGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQK 243
Cdd:PRK02983 690 LEQGSLADFRAavdLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 244 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 323
Cdd:PRK02983 770 LRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFR 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 324 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpDGPEGQAYDVDFTPPFRRINMVEELEKA 403
Cdd:PRK02983 850 NEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEA 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 404 LGMKL-PETNLfetEETRKilddICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGL 482
Cdd:PRK02983 928 LGEEIdPDTPL---AELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGL 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 483 TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTdSN 562
Cdd:PRK02983 1001 AERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GR 1079
|
490
....*....|....*
gi 5031815 563 NIKEVLLFPAMKPED 577
Cdd:PRK02983 1080 SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
68-576 |
5.12e-135 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 403.29 E-value: 5.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 68 EESVDPNQYYKIRSQAIHQLKVNGEdPYPHKFHVDISlTDFIQKYSHLQPGDHLT--DITLKVAGRIHAKRASGgKLIFY 145
Cdd:PRK12445 10 NEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHT-SDQLHEEFDAKDNQELEslNIEVSVAGRMMTRRIMG-KASFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 146 DLRGEGVKLQVMAnSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKET 225
Cdd:PRK12445 87 TLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 226 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 305
Cdd:PRK12445 166 RYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 306 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDV 385
Cdd:PRK12445 246 RLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-------GEHVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 386 DFTPPFRRINMVEELEKalgmKLPETNLFEteetrkiLDDICVAKA------VECPPPRTTARLLDKLVGEFLEVTCINP 459
Cdd:PRK12445 319 DFGKPFEKLTMREAIKK----YRPETDMAD-------LDNFDAAKAlaesigITVEKSWGLGRIVTEIFDEVAEAHLIQP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 460 TFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEY 539
Cdd:PRK12445 388 TFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEY 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 5031815 540 GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPE 576
Cdd:PRK12445 468 GLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
222-574 |
1.07e-122 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 364.96 E-value: 1.07e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 222 DKETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPE 301
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 302 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPdgpegq 381
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 382 aYDVDFTPPFRRINMVEELEKALGMKLPETnlfeteetrkiLDDIcvakavecppPRTTARLLDKLVgefLEVTCINPTF 461
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVEEL-----------GYGS----------DKPDLRFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 462 ICDHPQIMSPLAKWHRSK-EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKaagdDEAMFIDENFCTALEYG 540
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 5031815 541 LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMK 574
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 ... |
244-575 |
5.88e-93 |
|
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: 286.68 E-value: 5.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 244 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 323
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 324 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEELEKA 403
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 404 LgmklpetnlfeteetrkilddicvakavecppprttarlldklvgeflevtciNPTFICDHP-QIMSPLAKWHRSKEGL 482
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 483 TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGddeaMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSN 562
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 5031815 563 NIKEVLLFPAMKP 575
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
257-568 |
1.02e-55 |
|
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: 190.07 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 257 FLDELGFLEIETPMMniIPGG-------AVAKPFITYHNElDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 329
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 330 THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhitgsykvtyhpdgpegqaydvDFTPPFRRINMVEELEKALGMKLP 409
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 410 ETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKEGLTERFE 487
Cdd:TIGR00462 136 TASLAE-------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 488 LFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEV 567
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 5031815 568 L 568
Cdd:TIGR00462 289 L 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
247-568 |
3.46e-53 |
|
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: 183.77 E-value: 3.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 247 RSKIITYIRSFLDELGFLEIETPMMNIIPGGAVA-KPFITY---HNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 322
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 323 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSgmvkhitgsykvtyhpdgpegQAYDVDFTPPFRRINMVEELEK 402
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 403 ALGMKLPETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKE 480
Cdd:COG2269 148 YLGIDPLTADLDE-------LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQlgRDRPTFLYDYPASQAALARISPDDP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 481 GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD 560
Cdd:COG2269 221 RVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALG 300
|
....*...
gi 5031815 561 SNNIKEVL 568
Cdd:COG2269 301 AERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
125-234 |
7.50e-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: 7.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYkSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEIT 204
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 5031815 205 LLSPCLHMLPHLHFGLKDKETRYRQRYLDL 234
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
247-567 |
5.35e-41 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 150.85 E-value: 5.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 247 RSKIITYIRSFLDELGFLEIETPMM--------NIIPggaVAKPFITYHNELDMNLYMRIAPElYH-KMLVVGGIDRVYE 317
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 318 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHpdgpegQAY----DVDFTPPfrr 393
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-CEPAESLSYQ------QAFlrylGIDPLSA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 394 inMVEELeKALGMKLPETNLFETEETRKILDDICVAKAVEcppprttarllDKLVGEflevtciNPTFICDHPQIMSPLA 473
Cdd:PRK09350 154 --DKTQL-REVAAKLGLSNIADEEEDRDTLLQLLFTFGVE-----------PNIGKE-------KPTFVYHFPASQAALA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 474 KWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDR 553
Cdd:PRK09350 213 KISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDR 292
|
330
....*....|....
gi 5031815 554 VAMFLTDSNNIKEV 567
Cdd:PRK09350 293 LIMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
128-571 |
1.94e-40 |
|
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: 152.29 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 128 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFIHINNKLRRGDIIGVQGNPGKTKK--GELSIIPYEITL 205
Cdd:TIGR00458 17 FMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAK--KVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 206 LSPCLHMLPHLhfgLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIP--GGA 278
Cdd:TIGR00458 94 INEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 279 VAKPfITYhneLDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKM 357
Cdd:TIGR00458 170 ELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 358 VsgmVKHITGSYKVTYHPDGPEGQAYDVDFTPpFRRINMVEELEkalgmklpetnlfeteetrkilddICVAKAVECPPP 437
Cdd:TIGR00458 246 V---VRVFEDVPERCAHQLETLEFKLEKPEGK-FVRLTYDEAIE------------------------MANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 438 RTTARLLDKLVGEFLEvtciNPTFICDHPQ------IMSPLAKWHRSKEglterFELFVMKKEICNAYTELNDpmrqRQL 511
Cdd:TIGR00458 298 EDLSTEAEKALGEEMD----GLYFITDWPTeirpfyTMPDEDNPEISKS-----FDLMYRDLEISSGAQRIHL----HDL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 512 FEEQAKAKAAGDDEAmfidENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:TIGR00458 365 LVERIKAKGLNPEGF----KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
125-571 |
7.71e-38 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 145.33 E-value: 7.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMAnsRNYKSEEEFIHINnKLRRGDIIGVQG----NPgKTKKGeLSIIP 200
Cdd:PRK05159 18 EVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVV--KKKVDEELFETIK-KLKRESVVSVTGtvkaNP-KAPGG-VEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 201 YEITLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPmmNIIP 275
Cdd:PRK05159 92 EEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 276 ----GGAVAKPfITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYAD-YHD 349
Cdd:PRK05159 166 sgteGGAELFP-IDYFEK---EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 350 LMEITEKMVSGMVKHITGSYKvtyhpdgPEGQAYDVDF---TPPFRRINMVEELE--KALGMKLPETNLFETEETRKILD 424
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITYDEAIEilKSKGNEISWGDDLDTEGERLLGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 425 DIcvakavecppprttarlLDKLVGEFLevtcinptFICDHPQIMSPL-AKWHRSKEGLTERFELfvMKK--EICNAYTE 501
Cdd:PRK05159 315 YV-----------------KEEYGSDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDL--LFRglEITSGGQR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 502 LNDpmrqRQLFEEQAKAKaaGDDEAMFidENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:PRK05159 368 IHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
125-571 |
1.79e-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: 120.93 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGgKLIFYDLR-GEGVkLQVMANSRNYKSEEEFihinNKLRRGDIIGVQG----NPGKtkKGELSII 199
Cdd:COG0017 16 EVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKDKLENFEEA----KKLTTESSVEVTGtvveSPRA--PQGVELQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 200 PYEITLLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLILNDFvRQKFIIRSKIITYIRSFLDELGFLEIETPmmnIIPGG 277
Cdd:COG0017 88 AEEIEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTP---IITAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 278 AV---AKPF-ITYHNEldmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLME 352
Cdd:COG0017 161 ATeggGELFpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 353 ITEKMVSGMVKHItgsykVTYHPDgpEGQAYDVDFT-------PPFRRINM---VEELEKAlGMKLPETNLFETEETRKI 422
Cdd:COG0017 237 LAEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITYteaIEILKKS-GEKVEWGDDLGTEHERYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 423 lddicvakavecppprtTARLLDKLVgeflevtcinptFICDHPQIMSPlakwhrskeglterfelFVMK-----KEICN 497
Cdd:COG0017 309 -----------------GEEFFKKPV------------FVTDYPKEIKA-----------------FYMKpnpddPKTVA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 498 A-------YTELndpmrQRqlfEEQ-----AKAKAAGDDEAMF---IDenfctALEYGLPPTAGWGMGIDRVAMFLTDSN 562
Cdd:COG0017 343 AfdllapgIGEIig-gsQR---EHRydvlvERIKEKGLDPEDYewyLD-----LRRYGSVPHAGFGLGLERLVMWLTGLE 413
|
....*....
gi 5031815 563 NIKEVLLFP 571
Cdd:COG0017 414 NIREVIPFP 422
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
125-571 |
2.97e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 122.48 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyksEEEFIHINNKLRRGDIIGVQG----------NPgKTKK 193
Cdd:PRK00476 19 TVTLCGWVHRRRDHGG-LIFIDLRDrEGI-VQVVFDP-----DAEAFEVAESLRSEYVIQVTGtvrarpegtvNP-NLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 194 GELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLilndfvR-----QKFIIRSKIITYIRSFLDELGF 263
Cdd:PRK00476 91 GEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL------RrpemqKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 264 LEIETPMMniI---PGGA----VakPfityhneldmnlyMRI----------APELYHKMLVVGGIDRVYEIGRQFRNEg 326
Cdd:PRK00476 161 LEIETPIL--TkstPEGArdylV--P-------------SRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 327 iDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK 402
Cdd:PRK00476 223 -DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTYAEAMRR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 403 --------ALGMKLPE-TNLFETEE--------------------------TRKILDD---------------ICV---- 428
Cdd:PRK00476 283 ygsdkpdlRFGLELVDvTDLFKDSGfkvfagaandggrvkairvpggaaqlSRKQIDEltefakiygakglayIKVnedg 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 429 -----------------AKAVECPP----------PRTTARLLDKL---VGEFLEVT---CINPTFICD----------- 464
Cdd:PRK00476 363 lkgpiakflseeelaalLERTGAKDgdliffgadkAKVVNDALGALrlkLGKELGLIdedKFAFLWVVDfpmfeydeeeg 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 465 ------HPQIMsPlakwhrsKEGLTERFELFVMKKEICNAY------TEL-------NDPMRQRQLF------EEQAKAK 519
Cdd:PRK00476 443 rwvaahHPFTM-P-------KDEDLDELETTDPGKARAYAYdlvlngYELgggsiriHRPEIQEKVFeilgisEEEAEEK 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 5031815 520 AAGddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:PRK00476 515 FGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
125-571 |
2.97e-28 |
|
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: 119.33 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyKSEEEFIHINNKLRRGDIIGVQG----------NPgKTKK 193
Cdd:COG0173 18 EVTLSGWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDP---DDSAEAFEKAEKLRSEYVIAVTGkvrarpegtvNP-KLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 194 GELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIET 268
Cdd:COG0173 92 GEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 269 PMMNI-IPGGA----VakPFityhneldmnlymRI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN- 332
Cdd:COG0173 167 PILTKsTPEGArdylV--PS-------------RVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 333 -PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK------- 402
Cdd:COG0173 230 qPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMTYAEAMERygsdkpd 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 403 -ALGMKLPE-TNLFETEE-------------------------TRKILDDIC------------------------VAKA 431
Cdd:COG0173 291 lRFGLELVDvTDIFKDSGfkvfagaaenggrvkainvpggaslSRKQIDELTefakqygakglayikvnedglkspIAKF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 432 VecpPPRTTARLLDKL---VGEFLevtcinpTFICDHPQIMSP--------LAKwhrsKEGLTER-------------FE 487
Cdd:COG0173 371 L---SEEELAAILERLgakPGDLI-------FFVADKPKVVNKalgalrlkLGK----ELGLIDEdefaflwvvdfplFE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 488 L-------------FVMKKE-------------ICNAY------TEL-------NDPMRQRQLF------EEQAKAKAAG 522
Cdd:COG0173 437 YdeeegrwvamhhpFTMPKDedldlletdpgkvRAKAYdlvlngYELgggsiriHDPELQEKVFellgisEEEAEEKFGF 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 5031815 523 ddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:COG0173 517 -----LLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
244-571 |
3.18e-27 |
|
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: 111.51 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 244 FIIRSKIITYIRSFLDELGFLEIETPMMN-IIPGGA----VakPFITYHNE---LDMnlymriAPELYHKMLVVGGIDRV 315
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGArdflV--PSRLHPGKfyaLPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 316 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRIN 395
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 396 MVEELEKaLGMKL------PetnLFE-TEETRKIlddicvaKAVECP---PPRTTARLLDKlvgeflevtciNPTFIcdh 465
Cdd:cd00777 136 YAEAMER-YGFKFlwivdfP---LFEwDEEEGRL-------VSAHHPftaPKEEDLDLLEK-----------DPEDA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 466 pqimsplakwhrskegLTERFELFVMKKEICNAYTELNDPMRQRQLFE------EQAKAKAAGddeamfidenFCTALEY 539
Cdd:cd00777 191 ----------------RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEilglseEEAEEKFGF----------LLEAFKY 244
|
330 340 350
....*....|....*....|....*....|..
gi 5031815 540 GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:cd00777 245 GAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
224-571 |
7.84e-27 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 111.12 E-value: 7.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 224 ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMM--NIIPGGAVAKPfITYHNEldmNLYMRIAPE 301
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFK-VSYFGK---PAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 302 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKMVSGMVKHITGSYK-----VTYH 374
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 375 PDGPEGqaydvdFTPPFRRInmveELEKALGMklpetnLFETEETRKILDDICVAKAVEcppprttaRLLDKLVGEflev 454
Cdd:cd00776 159 NRELLK------PLEPFPRI----TYDEAIEL------LREKGVEEEVKWGEDLSTEHE--------RLLGEIVKG---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 455 tciNPTFICDHPQIMSPL-AKWHRSKEGLTERFELFVMKK-EICNAYTELNDPmrqrQLFEEQAKAKaaGDDEAMFidEN 532
Cdd:cd00776 211 ---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF--EW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 5031815 533 FCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
128-402 |
1.64e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 108.34 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 128 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNYKSEEEFIhinNKLRRGDIIGVQG----------NPgKTKKGELS 197
Cdd:PLN02903 77 LCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDEFPEAHRTA---NRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 198 IIPYEITLLSPCLHMLPHLHFGLKD------KETRYRQRYLDLILNDFVRQkFIIRSKIITYIRSFL-DELGFLEIETPM 270
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLeDVHGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 271 MN---------------IIPGGAVAKPfityhneldmnlymrIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEF 335
Cdd:PLN02903 231 LSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031815 336 TTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK 402
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLTYAEAMSK 345
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
11-571 |
6.04e-19 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 90.15 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 11 VDGSEPKLSKNELKrrlKAEKKvAEKEAKQKELSEKQLSQataaatnhttdngvgPEEESVDPNQYYKIRSQAIhQLKVN 90
Cdd:PLN02850 6 VEESGEKISKKAAK---KAAAK-AEKLRREATAKAAAASL---------------EDEDDPLASNYGDVPLEEL-QSKVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 91 GedpyphKFHVDISltdfiqkyshlQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFI 170
Cdd:PLN02850 66 G------REWTDVS-----------DLGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 171 HINNKLRRG---DIIGVQGNPGKTKKG---ELSIIPYEITLLSPCLHMLPhlhFGLKD---------------------- 222
Cdd:PLN02850 128 KYAKQLSREsvvDVEGVVSVPKKPVKGttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 223 KETRYRQRYLDLIL--NDFVrqkFIIRSKIITYIRSFLDELGFLEIETPmmNIIPG-----GAVAKpfityhneLDmnlY 295
Cdd:PLN02850 205 QDTRLNNRVLDLRTpaNQAI---FRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGaseggSAVFR--------LD---Y 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 296 M------RIAPELYHKMLVVGGIDRVYEIGRQFRNEGiDLTHNP--EFTTCEFYMAYAD-YHDLMEITEKMVSGMVKHIT 366
Cdd:PLN02850 269 KgqpaclAQSPQLHKQMAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 367 GSYK------VTYHPDGPegqaydVDFTPPFRRINMVE--ELEKALGMKLPETNLFETEETRKiLDDICVAKAvecpppR 438
Cdd:PLN02850 348 ERCKkeleaiREQYPFEP------LKYLPKTLRLTFAEgiQMLKEAGVEVDPLGDLNTESERK-LGQLVKEKY------G 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 439 TTARLLDKL---VGEFLEVTCI-NPTFicdhpqimsplakwhrskeglTERFELFVMKKEICNAYTELNDPmrqrQLFEE 514
Cdd:PLN02850 415 TDFYILHRYplaVRPFYTMPCPdDPKY---------------------SNSFDVFIRGEEIISGAQRVHDP----ELLEK 469
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031815 515 QAKAKAAG-DDEAMFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:PLN02850 470 RAEECGIDvKTISTYID-----SFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
114-571 |
5.56e-18 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 87.73 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 114 HLQPGDHLTDITLkvAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNykSEEEFIHINNKLRRGDIIGVQG------- 186
Cdd:PRK12820 11 HLSLDDTGREVCL--AGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEA--APADVYELAASLRAEFCVALQGevqkrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 187 ---NPgKTKKGELSIIPYEITLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNDFVRQKFIIR 247
Cdd:PRK12820 86 eteNP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 248 SKIITYIRSFLDELGFLEIETPMMNI-IPGGAvaKPFITYHNELDMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNE 325
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 326 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHPDGPEGQAYD---------------VDFTPP 390
Cdd:PRK12820 238 DLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFA-IGGIALPRPFPRMPYAEAMDttgsdrpdlrfdlkfADATDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 391 FRR------------------INMVEELEK-------------------ALGM--------KLpETNL---FETEETRKI 422
Cdd:PRK12820 317 FENtrygifkqilqrggrikgINIKGQSEKlsknvlqneyakeiapsfgAKGMtwmraeagGL-DSNIvqfFSADEKEAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 423 L--------DDICVAKAVECPPPRTTARLLDKLVGEFLEVT---CINPTFICDHPQIMS-----------PLAKWHRSK- 479
Cdd:PRK12820 396 KrrfhaedgDVIIMIADASCAIVLSALGQLRLHLADRLGLIpegVFHPLWITDFPLFEAtddggvtsshhPFTAPDREDf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 480 -----EGL----TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFidenFCTALEYGLPPTAGWGMG 550
Cdd:PRK12820 476 dpgdiEELldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGF----FLRAFDFAAPPHGGIALG 551
|
570 580
....*....|....*....|.
gi 5031815 551 IDRVAMFLTDSNNIKEVLLFP 571
Cdd:PRK12820 552 LDRVVSMILQTPSIREVIAFP 572
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
246-359 |
8.40e-18 |
|
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: 82.17 E-value: 8.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 246 IRSKIITYIRSFLDELGFLEIETPMMNIIPG----GAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGI----DRVYE 317
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 5031815 318 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKMVS 359
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
119-571 |
9.07e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 86.59 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 119 DHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyKSEEEFIHINNKLRRGDIIGVQGNPGK-------T 191
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEG-DVPKEMIDFIGQIPTESIVDVEATVCKveqpitsT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 192 KKGELSIIPYEITLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFL 258
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 259 DELGFLEIETPMMNIIPGGAVAKPF-ITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL-THNPEFT 336
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFkLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 337 TCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSykvtyhpdgpEGQAYDVDFTPPFRRI--NMVEELEKALGMKLPETNL 413
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLATH----------TKELKAVCQQYPFEPLvwKLTPERMKELGVGVISEGV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 414 FETEETR-------------------KILDDICVAKAVECPPPRTT-ARLLDKLVGEFLEVTcinpTFICDH-PQIMSPL 472
Cdd:PTZ00401 375 EPTDKYQarvhnmdsrmlrinymhciELLNTVLEEKMAPTDDINTTnEKLLGKLVKERYGTD----FFISDRfPSSARPF 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 473 AKWH-RSKEGLTERFELFVMKKEICNAYTELNDPmrqrQLFeeQAKAKAAGDDEAMFIDenFCTALEYGLPPTAGWGMGI 551
Cdd:PTZ00401 451 YTMEcKDDERFTNSYDMFIRGEEISSGAQRIHDP----DLL--LARAKMLNVDLTPIKE--YVDSFRLGAWPHGGFGVGL 522
|
490 500
....*....|....*....|
gi 5031815 552 DRVAMFLTDSNNIKEVLLFP 571
Cdd:PTZ00401 523 ERVVMLYLGLSNVRLASLFP 542
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
125-208 |
1.14e-17 |
|
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.
Pssm-ID: 239766 [Multi-domain] Cd Length: 85 Bit Score: 77.99 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFIhinNKLRRGDIIGVQGNPGKT-----KKGELSII 199
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEELGEFFEEA---EKLRTESVVGVTGTVVKRpegnlATGEIELQ 76
|
....*....
gi 5031815 200 PYEITLLSP 208
Cdd:cd04100 77 AEELEVLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
127-206 |
7.97e-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: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 127 KVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSrnykseEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLL 206
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFK------EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
246-571 |
2.18e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.59 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 246 IRSKIITYIRSFLDELGFLEIETPMMN-----IIPGGA---VAKPFITYHNEldmnlYMRIAPEL-YHKMLVVGGIDRVY 316
Cdd:PRK06462 32 VQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSdlpVKQISIDFYGV-----EYYLADSMiLHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 317 EIGRQFRNEG---IDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHItgsykVTYHPDGPEGQAYDV-DFTPPFR 392
Cdd:PRK06462 107 YLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKEL-----LEEHEDELEFFGRDLpHLKRPFK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 393 RINMvEELEKALGMKLPETNLFEteetrKILDDicvakavecppprttarlldklvGE-FLEVTCINPTFICDHPQIMSP 471
Cdd:PRK06462 182 RITH-KEAVEILNEEGCRGIDLE-----ELGSE-----------------------GEkSLSEHFEEPFWIIDIPKGSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 472 LakWHRSKEG-----------LTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAK-----AKAagddeamfidenfct 535
Cdd:PRK06462 233 F--YDREDPErpgvlrnydllLPEGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKwylemAKE--------------- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 5031815 536 aleyGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:PRK06462 296 ----GPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
125-234 |
2.02e-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: 50.21 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGGkLIFYDLR-GEGVkLQVMANSRNYKSEEEFihinNKLRRGDIIGVQG----------NPgKTKK 193
Cdd:cd04317 16 EVTLCGWVQRRRDHGG-LIFIDLRdRYGI-VQVVFDPEEAPEFELA----EKLRNESVIQVTGkvrarpegtvNP-KLPT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 5031815 194 GELSIIPYEITLLSPClhmlPHLHFGLKDK-----ETRYRQRYLDL 234
Cdd:cd04317 89 GEIEVVASELEVLNKA----KTLPFEIDDDvnvseELRLKYRYLDL 130
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
125-207 |
5.61e-05 |
|
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: 42.69 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 125 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFIHINNKLRRGDIIGVQGNPGKTKK--GELSIIPYE 202
Cdd:cd04316 14 EVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPKK--KVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEE 90
|
....*
gi 5031815 203 ITLLS 207
Cdd:cd04316 91 IEVLS 95
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
130-193 |
1.29e-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: 38.31 E-value: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031815 130 GRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKK 193
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEE 69
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
539-571 |
1.78e-03 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 41.25 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|...
gi 5031815 539 YGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 571
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
254-340 |
3.25e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 40.21 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031815 254 IRSFLDELGFLEIETPMMniIPGGAVAKPFITYHNEL-------DMNLYMR--IAPELYHKMLVVGGI--D--RVYEIGR 320
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYNYLRKLDRIlpDpiKIFEIGP 290
|
90 100
....*....|....*....|
gi 5031815 321 QFRNEGIDLTHNPEFTTCEF 340
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNF 310
|
|
| |
