|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
13-577 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 903.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 13 GEPkLSKNELKRRLKAEKKLAEKEAKQKELSEKQlnqttaAAATNHTADNGVGAEEETLDPNQYYKIRSQAVQQLKVSGE 92
Cdd:PLN02502 5 GEP-LSKNALKKRLKAKQAEEEKAAKEEAKAAAA------AAAAKGRSRKSAAADDETMDPTQYRANRLKKVEALRAKGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 93 DPYPHKFHVDISLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNY-KSEEEFVH 171
Cdd:PLN02502 78 EPYPYKFDVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFEK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 172 INNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKII 251
Cdd:PLN02502 157 LHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 252 TYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTH 331
Cdd:PLN02502 237 SYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 332 NPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHpdgpegqAYEIDFTPPFRRISMVEELEKVLGVKLPEt 411
Cdd:PLN02502 317 NPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRISMISLVEEATGIDFPA- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 412 sLFETEETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGLTERFELFVM 491
Cdd:PLN02502 389 -DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFIN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 492 KKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PLN02502 468 GRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
....*.
gi 2172664195 572 AMKPED 577
Cdd:PLN02502 548 AMKPQD 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: 702.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 68 EETLDPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDhLTDITLKVAGRIHAKRaSGGKLIFYDL 147
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE-ETGDEVSVAGRIMAKR-DMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 148 RGEGVKLQVMAnSRNYKSEEEFVHINnKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRY 227
Cdd:COG1190 80 QDGSGRIQLYL-RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 228 RQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKML 307
Cdd:COG1190 158 RQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 308 VVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDF 387
Cdd:COG1190 238 IVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 388 TPPFRRISMVEELEKVLGVklPETSLFETEETRKILDdicvARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQ 467
Cdd:COG1190 311 SPPWRRITMVEAIKEATGI--DVTPLTDDEELRALAK----ELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 468 IMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGW 547
Cdd:COG1190 385 EVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGL 464
|
490 500 510
....*....|....*....|....*....|.
gi 2172664195 548 GMGIDRVTMFLTDSNNIKEVLLFPAMKPEDK 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: 697.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 72 DPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGD-HLTDITLKVAGRIHAKRaSGGKLIFYDLRGE 150
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKR-VMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 151 GVKLQVMAnSRNYKSEEEFVHINnKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQR 230
Cdd:PRK00484 81 SGRIQLYV-SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 231 YLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVG 310
Cdd:PRK00484 159 YVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 311 GIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPP 390
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 391 FRRISMVEELEKVLGVKLPETSlfeTEETRKILDdicvARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMS 470
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDFDDMT---DEEARALAK----ELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 471 PLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMG 550
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 2172664195 551 IDRVTMFLTDSNNIKEVLLFPAMKPED 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: 641.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 67 EEETLDPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYD 146
Cdd:PTZ00417 76 EEAEVDPRLYYENRSKFIQEQKAKGINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQKLRFFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 147 LRGEGVKLQVMAN-SRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPhLHFGLKDKET 225
Cdd:PTZ00417 156 LVGDGAKIQVLANfAFHDHTKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-MKYGLKDTEI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 226 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 305
Cdd:PTZ00417 235 RYRQRYLDLMINESTRSTFITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 306 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPDGPEGQAYEI 385
Cdd:PTZ00417 315 MLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 386 DFTPPFRRISMVEELEKVLGVKLPETslFETEETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCIS-PTFICD 464
Cdd:PTZ00417 395 DFTPPYPKVSIVEELEKLTNTKLEQP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 465 HPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPT 544
Cdd:PTZ00417 473 HPQIMSPLAKYHRSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPT 552
|
490 500 510
....*....|....*....|....*....|.
gi 2172664195 545 AGWGMGIDRVTMFLTDSNNIKEVLLFPAMKP 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: 632.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 72 DPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDH-LTDITLKVAGRIHAKRaSGGKLIFYDLRGE 150
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkEKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 151 GVKLQVMANSRNYKseEEFVHINNK-LRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQ 229
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 230 RYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVV 309
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 310 GGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTP 389
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 390 PFRRISMVEELEKVLGVKLpetSLFETEETRKILDDICVARAVECPPprTTARLLDKLVGEFLEVTCISPTFICDHPQIM 469
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDF---DILKDDETAKALAKEHGIEVAEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 470 SPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGM 549
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 2172664195 550 GIDRVTMFLTDSNNIKEVLLFPAMKP 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: 619.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 237 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVY 316
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 317 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPPFRRISM 396
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 397 VEELEKVLGVKLPETSLFETEETRKILDDICvarAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWH 476
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 477 RCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTM 556
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 2172664195 557 FLTDSNNIKEVLLFPAMKP 575
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
104-574 |
2.75e-146 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 437.54 E-value: 2.75e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 104 SLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRaSGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIG 183
Cdd:PTZ00385 88 PISEVRERYGYLASGDRAAQATVRVAGRVTSVR-DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 184 VEGNPGKTKKGELSIVPREMTLLSP--CLHML--PHLH-FG-LKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSF 257
Cdd:PTZ00385 167 ADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 258 LDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTT 337
Cdd:PTZ00385 247 FNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 338 CEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPDGPEGQAYEIDFTPPFRRISMVEELEKVLGVKLPETSLFETE 417
Cdd:PTZ00385 327 CEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTP 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 418 ETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICN 497
Cdd:PTZ00385 407 KGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCN 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172664195 498 AYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMK 574
Cdd:PTZ00385 487 AYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLR 563
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
87-577 |
5.58e-143 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 441.71 E-value: 5.58e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 87 LKVSGEDPYPhkfhVDISLTQFIQEyshlqPGDHLTDITLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANsrnyKSE 166
Cdd:PRK02983 624 LRAAGVDPYP----VGVPPTHTVAE-----ALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLD----ASR 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 167 EEFVHINNKLR---RGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQK 243
Cdd:PRK02983 690 LEQGSLADFRAavdLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 244 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 323
Cdd:PRK02983 770 LRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFR 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 324 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpDGPEGQAYEIDFTPPFRRISMVEELEKV 403
Cdd:PRK02983 850 NEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEA 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 404 LGVKL-PETSLfetEETRKilddICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGL 482
Cdd:PRK02983 928 LGEEIdPDTPL---AELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGL 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 483 TERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTdSN 562
Cdd:PRK02983 1001 AERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GR 1079
|
490
....*....|....*
gi 2172664195 563 NIKEVLLFPAMKPED 577
Cdd:PRK02983 1080 SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
68-576 |
1.16e-134 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 402.52 E-value: 1.16e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 68 EETLDPNQYYKIRSQAVQQLKVSGEdPYPHKFHVDISLTQFIQEYShLQPGDHLT--DITLKVAGRIHAKRASGgKLIFY 145
Cdd:PRK12445 10 NEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHTSDQLHEEFD-AKDNQELEslNIEVSVAGRMMTRRIMG-KASFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 146 DLRGEGVKLQVMAnSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKET 225
Cdd:PRK12445 87 TLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 226 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 305
Cdd:PRK12445 166 RYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 306 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEI 385
Cdd:PRK12445 246 RLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-------GEHVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 386 DFTPPFRRISMVEELEKvlgvKLPETSLFEteetrkiLDDICVARA------VECPPPRTTARLLDKLVGEFLEVTCISP 459
Cdd:PRK12445 319 DFGKPFEKLTMREAIKK----YRPETDMAD-------LDNFDAAKAlaesigITVEKSWGLGRIVTEIFDEVAEAHLIQP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 460 TFICDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEY 539
Cdd:PRK12445 388 TFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEY 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 2172664195 540 GLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMKPE 576
Cdd:PRK12445 468 GLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
222-574 |
4.99e-121 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 360.73 E-value: 4.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 222 DKETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPE 301
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 302 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPdgpegq 381
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 382 aYEIDFTPPFRRISMVEELEKVLGVKLPETslfeteetrkiLDDIcvaravecppPRTTARLLDKLVgefLEVTCISPTF 461
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVEEL-----------GYGS----------DKPDLRFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 462 ICDHPQIMSPLAKWHRCK-EGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKaagdDEAMFIDENFCTALEYG 540
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 2172664195 541 LPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMK 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 |
7.90e-92 |
|
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: 283.60 E-value: 7.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 244 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 323
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 324 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYhpdgpegQAYEIDFTPPFRRISMVEELEKV 403
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 404 LgvklpetslfeteetrkilddicvaravecppprttarlldklvgeflevtciSPTFICDHP-QIMSPLAKWHRCKEGL 482
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 483 TERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGddeaMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSN 562
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 2172664195 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 |
1.17e-56 |
|
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: 192.38 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 257 FLDELGFLEIETPMMniIPGG-------AVAKPFITYHNElDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 329
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 330 THNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRsitgsykityhpdgpegqayeiDFTPPFRRISMVEELEKVLGVKLP 409
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 410 ETSLFEteetrkiLDDICVARAVECPPPRTTARLLDKLVGEFLEVT--CISPTFICDHPQIMSPLAKWHRCKEGLTERFE 487
Cdd:TIGR00462 136 TASLAE-------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 488 LFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEV 567
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 2172664195 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 |
6.32e-55 |
|
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: 188.39 E-value: 6.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 247 RSKIITYIRSFLDELGFLEIETPMMNIIPGGAVA-KPFITY---HNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 322
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 323 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSgmvrsitgsykityhpdgpegQAYEIDFTPPFRRISMVEELEK 402
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 403 VLGVKLPETSLFEteetrkiLDDICVARAVECPPPRTTARLLDKLVGEFLEVT--CISPTFICDHPQIMSPLAKwhRCKE 480
Cdd:COG2269 148 YLGIDPLTADLDE-------LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQlgRDRPTFLYDYPASQAALAR--ISPD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 481 G--LTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFL 558
Cdd:COG2269 219 DprVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLA 298
|
330
....*....|
gi 2172664195 559 TDSNNIKEVL 568
Cdd:COG2269 299 LGAERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
125-234 |
5.96e-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: 176.13 E-value: 5.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYkSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMT 204
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 2172664195 205 LLSPCLHMLPHLHFGLKDKETRYRQRYLDL 234
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
247-567 |
3.57e-41 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 151.23 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 247 RSKIITYIRSFLDELGFLEIETPMM--------NIIPggaVAKPFITYHNELDMNLYMRIAPElYH-KMLVVGGIDRVYE 317
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 318 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSgmvrsitgsykityhpdgpegqayEIDFTPPFRRISMV 397
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQ------------------------QVLDCEPAESLSYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 398 EELEKVLGV---------------KLPETSLFETEETRKILDDICVARAVEcppprttarllDKLVGEflevtciSPTFI 462
Cdd:PRK09350 140 QAFLRYLGIdplsadktqlrevaaKLGLSNIADEEEDRDTLLQLLFTFGVE-----------PNIGKE-------KPTFV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 463 CDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLP 542
Cdd:PRK09350 202 YHFPASQAALAKISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLP 281
|
330 340
....*....|....*....|....*
gi 2172664195 543 PTAGWGMGIDRVTMFLTDSNNIKEV 567
Cdd:PRK09350 282 DCSGVALGVDRLIMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
128-571 |
1.37e-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: 153.06 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 128 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFVHINNKLRRGDIIGVEGNPGKTKK--GELSIVPREMTL 205
Cdd:TIGR00458 17 FMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAK--KVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 206 LSPCLHMLPHLhfgLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIP--GGA 278
Cdd:TIGR00458 94 INEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 279 VAKPfITYhneLDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKM 357
Cdd:TIGR00458 170 ELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 358 LsgmVRSITGSYKITYHPDGPEGQAYEIDFTPpFRRISMVEELEkvlgvklpetslfeteetrkilddICVARAVECPPP 437
Cdd:TIGR00458 246 V---VRVFEDVPERCAHQLETLEFKLEKPEGK-FVRLTYDEAIE------------------------MANAKGVEIGWG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 438 RTTARLLDKLVGEFLEvtciSPTFICDHPQ------IMSPLAKWHRCKEglterFELFVMKKEICNAYTElndpVRQRQL 511
Cdd:TIGR00458 298 EDLSTEAEKALGEEMD----GLYFITDWPTeirpfyTMPDEDNPEISKS-----FDLMYRDLEISSGAQR----IHLHDL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 512 FEEQAKAKAAGDDEAmfidENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:TIGR00458 365 LVERIKAKGLNPEGF----KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
125-571 |
9.35e-37 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 142.25 E-value: 9.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMAnsRNYKSEEEFVHINnKLRRGDIIGVEG----NPgKTKKGeLSIVP 200
Cdd:PRK05159 18 EVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVV--KKKVDEELFETIK-KLKRESVVSVTGtvkaNP-KAPGG-VEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 201 REMTLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPmmNIIP 275
Cdd:PRK05159 92 EEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 276 ----GGAVAKPfITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYAD-YHD 349
Cdd:PRK05159 166 sgteGGAELFP-IDYFEK---EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 350 LMEITEKMLSGMVRSITGSYKityhpdgPEGQAYEIDF---TPPFRRISMVEELEKV--LGVKLPETSLFETEETRKILD 424
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITYDEAIEILksKGNEISWGDDLDTEGERLLGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 425 DIcvaravecppprttarlLDKLVGEFLevtcisptFICDHPQIMSPL-AKWHRCKEGLTERFELfvMKK--EICNAYTE 501
Cdd:PRK05159 315 YV-----------------KEEYGSDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDL--LFRglEITSGGQR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 502 LNDpvrqRQLFEEQAKAKaaGDDEAMFidENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PRK05159 368 IHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
125-571 |
3.19e-30 |
|
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: 123.24 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGgKLIFYDLR-GEGVkLQVMANSRNYKSEEEFvhinNKLRRGDIIGVEG----NPGKtkKGELSIV 199
Cdd:COG0017 16 EVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKDKLENFEEA----KKLTTESSVEVTGtvveSPRA--PQGVELQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 200 PREMTLLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLILNDFvRQKFIIRSKIITYIRSFLDELGFLEIETPmmnIIPGG 277
Cdd:COG0017 88 AEEIEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTP---IITAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 278 AV---AKPF-ITYHNEldmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLME 352
Cdd:COG0017 161 ATeggGELFpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 353 ITEKMLSGMVRSItgsykITYHPDgpEGQAYEIDFT-------PPFRRISM---VEELEKvLGVKLPETSLFETEETRKI 422
Cdd:COG0017 237 LAEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITYteaIEILKK-SGEKVEWGDDLGTEHERYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 423 lddicvaravecppprtTARLLDKLVgeflevtcisptFICDHPqimsplakwhrckeglterfelfvmkKEICNAYTEL 502
Cdd:COG0017 309 -----------------GEEFFKKPV------------FVTDYP--------------------------KEIKAFYMKP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 503 N--DP--VR----------------QRqlfEEQ-----AKAKAAGDDEAMF---IDenfctALEYGLPPTAGWGMGIDRV 554
Cdd:COG0017 334 NpdDPktVAafdllapgigeiiggsQR---EHRydvlvERIKEKGLDPEDYewyLD-----LRRYGSVPHAGFGLGLERL 405
|
490
....*....|....*..
gi 2172664195 555 TMFLTDSNNIKEVLLFP 571
Cdd:COG0017 406 VMWLTGLENIREVIPFP 422
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
125-571 |
1.50e-28 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 120.17 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyksEEEFVHINNKLRRGDIIGVEG----------NPgKTKK 193
Cdd:PRK00476 19 TVTLCGWVHRRRDHGG-LIFIDLRDrEGI-VQVVFDP-----DAEAFEVAESLRSEYVIQVTGtvrarpegtvNP-NLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 194 GELSIVPREMTLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLilndfvR-----QKFIIRSKIITYIRSFLDELGF 263
Cdd:PRK00476 91 GEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL------RrpemqKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 264 LEIETPMMniI---PGGA----VakPfityhneldmnlyMRI----------APELYHKMLVVGGIDRVYEIGRQFRNEg 326
Cdd:PRK00476 161 LEIETPIL--TkstPEGArdylV--P-------------SRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 327 iDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS------- 395
Cdd:PRK00476 223 -DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTyaeamrr 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 396 -------------------------------MVEELEKVLGVKLPETSlfeTEETRKILDD---------------ICV- 428
Cdd:PRK00476 283 ygsdkpdlrfglelvdvtdlfkdsgfkvfagAANDGGRVKAIRVPGGA---AQLSRKQIDEltefakiygakglayIKVn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 429 --------------------ARAVECPP----------PRTTARLLDKL---VGEFLEVT---CISPTFICDHpqimsPL 472
Cdd:PRK00476 360 edglkgpiakflseeelaalLERTGAKDgdliffgadkAKVVNDALGALrlkLGKELGLIdedKFAFLWVVDF-----PM 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 473 AKW----------H----RCKEGLTERFELFVMKKEICNAY------TEL-------NDPVRQRQLF------EEQAKAK 519
Cdd:PRK00476 435 FEYdeeegrwvaaHhpftMPKDEDLDELETTDPGKARAYAYdlvlngYELgggsiriHRPEIQEKVFeilgisEEEAEEK 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2172664195 520 AAGddeamFIDenfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PRK00476 515 FGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
125-571 |
4.90e-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: 118.56 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyKSEEEFVHINNKLRRGDIIGVEG----------NPgKTKK 193
Cdd:COG0173 18 EVTLSGWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDP---DDSAEAFEKAEKLRSEYVIAVTGkvrarpegtvNP-KLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 194 GELSIVPREMTLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIET 268
Cdd:COG0173 92 GEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 269 PMMNI-IPGGA----VakPFityhneldmnlymRI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN- 332
Cdd:COG0173 167 PILTKsTPEGArdylV--PS-------------RVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 333 -PEFTT--CEfyMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS-------------- 395
Cdd:COG0173 230 qPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMTyaeamerygsdkpd 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 396 ------------------------MVEELEKVLGVKLPETSLFeteeTRKILDD---------------ICV-ARAVECP 435
Cdd:COG0173 291 lrfglelvdvtdifkdsgfkvfagAAENGGRVKAINVPGGASL----SRKQIDEltefakqygakglayIKVnEDGLKSP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 436 -----PPRTTARLLDKL---VGEFLevtcispTFICDHPQIMSPLAKWHRCK----EGLTER-------------FEL-- 488
Cdd:COG0173 367 iakflSEEELAAILERLgakPGDLI-------FFVADKPKVVNKALGALRLKlgkeLGLIDEdefaflwvvdfplFEYde 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 489 -----------FVMKKE-------------ICNAY------TEL-------NDPVRQRQLF------EEQAKAKAAGdde 525
Cdd:COG0173 440 eegrwvamhhpFTMPKDedldlletdpgkvRAKAYdlvlngYELgggsiriHDPELQEKVFellgisEEEAEEKFGF--- 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2172664195 526 amFIDenfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 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 |
2.86e-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: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 244 FIIRSKIITYIRSFLDELGFLEIETPMMN-IIPGGA----VakPFITYHNE---LDMnlymriAPELYHKMLVVGGIDRV 315
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGArdflV--PSRLHPGKfyaLPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 316 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRIS 395
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 396 MVEELEKvLGVKL------PetsLFE-TEETRKIlddicvaravecppprttarlldklvgEFLEvtcisptficdHPQI 468
Cdd:cd00777 136 YAEAMER-YGFKFlwivdfP---LFEwDEEEGRL---------------------------VSAH-----------HPFT 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 469 MsPLAKWHRCKEGLTER-----FELFVMKKEICNAYTELNDPVRQRQLFE------EQAKAKAAGddeamfidenFCTAL 537
Cdd:cd00777 174 A-PKEEDLDLLEKDPEDaraqaYDLVLNGVELGGGSIRIHDPDIQEKVFEilglseEEAEEKFGF----------LLEAF 242
|
330 340 350
....*....|....*....|....*....|....
gi 2172664195 538 EYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:cd00777 243 KYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
224-571 |
1.83e-26 |
|
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: 110.35 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 224 ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMM--NIIPGGAVAKPfITYHNEldmNLYMRIAPE 301
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFK-VSYFGK---PAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 302 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKMLSGMVRSITGSYK-----ITYH 374
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 375 PDGPEGqayeidFTPPFRRISMVEelekvlGVKLpetsLFETEETRKILDDICVARAVEcppprttaRLLDKLVGEflev 454
Cdd:cd00776 159 NRELLK------PLEPFPRITYDE------AIEL----LREKGVEEEVKWGEDLSTEHE--------RLLGEIVKG---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 455 tciSPTFICDHPQIMSPL-AKWHRCKEGLTERFELFVMKK-EICNAYTELNDPvrqrQLFEEQAKAKaaGDDEAMFidEN 532
Cdd:cd00776 211 ---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF--EW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 2172664195 533 FCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
128-402 |
7.34e-25 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 109.11 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 128 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNYKseeEFVHINNKLRRGDIIGVEG----------NPgKTKKGELS 197
Cdd:PLN02903 77 LCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDEFP---EAHRTANRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 198 IVPREMTLLSPCLHMLPHLHFGLKD------KETRYRQRYLDLILNDFVRQkFIIRSKIITYIRSFL-DELGFLEIETPM 270
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLeDVHGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 271 MN---------------IIPGGAVAKPfityhneldmnlymrIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEF 335
Cdd:PLN02903 231 LSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172664195 336 TTCEFYMAYADYHDLMEITEKMLSGMVRSITGsykityhpdgpegqayeIDFTPPFRRISMVEELEK 402
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLTYAEAMSK 345
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
125-208 |
2.18e-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: 79.92 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyksEEEFVHINNKLRRGDIIGVEGNPGKT-----KKGELSIV 199
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEE---LGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQ 76
|
....*....
gi 2172664195 200 PREMTLLSP 208
Cdd:cd04100 77 AEELEVLSK 85
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
27-571 |
1.09e-17 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 86.30 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 27 KAEKKLAEKEAKQKELSEKQLNQTTAAAATnhtadngvGAEEETLDPNqyYKIRSQAVQQLKVSGedpyphKFHVDISlt 106
Cdd:PLN02850 12 KISKKAAKKAAAKAEKLRREATAKAAAASL--------EDEDDPLASN--YGDVPLEELQSKVTG------REWTDVS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 107 qfiqeyshlQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEG 186
Cdd:PLN02850 74 ---------DLGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSRESVVDVEG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 187 ---NPGKTKKG---ELSIVPREMTLLSPCLHMLPhlhFGLKD----------------------KETRYRQRYLDLIL-- 236
Cdd:PLN02850 144 vvsVPKKPVKGttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDLRTpa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 237 NDFVrqkFIIRSKIITYIRSFLDELGFLEIETPmmNIIPG-----GAVAKpfityhneLDmnlYMRI------APELYHK 305
Cdd:PLN02850 221 NQAI---FRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGaseggSAVFR--------LD---YKGQpaclaqSPQLHKQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 306 MLVVGGIDRVYEIGRQFRNEGiDLTHNP--EFTTCEFYMAYAD-YHDLMEITEKMLSGMVRSITGSYKI------TYHPD 376
Cdd:PLN02850 285 MAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKKeleairEQYPF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 377 GPegqayeIDFTPPFRRISMVE--ELEKVLGVKLPETSLFETEETRKiLDDICVARAvecpppRTTARLLDKL---VGEF 451
Cdd:PLN02850 364 EP------LKYLPKTLRLTFAEgiQMLKEAGVEVDPLGDLNTESERK-LGQLVKEKY------GTDFYILHRYplaVRPF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 452 LEVTCIsptficDHPQimsplakwhrckegLTERFELFVMKKEICNAYTELNDPvrqrQLFEEQAKAKAAG-DDEAMFID 530
Cdd:PLN02850 431 YTMPCP------DDPK--------------YSNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEECGIDvKTISTYID 486
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2172664195 531 enfctALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PLN02850 487 -----SFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
246-359 |
1.66e-17 |
|
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: 81.40 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 246 IRSKIITYIRSFLDELGFLEIETPMMNIIPG----GAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGI----DRVYE 317
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2172664195 318 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKMLS 359
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
119-571 |
2.71e-17 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 85.04 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 119 DHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyKSEEEFVHINNKLRRGDIIGVEGNPGK-------T 191
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEG-DVPKEMIDFIGQIPTESIVDVEATVCKveqpitsT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 192 KKGELSIVPREMTLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFL 258
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 259 DELGFLEIETPMMNIIPGGAVAKPF-ITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL-THNPEFT 336
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFkLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 337 TCEFYMAYAD-YHDLMEITEKMLSGMVRSITGsykityHPDGPEGQAYEIDFTPPFRRISmvEELEKVLGVKLPETSLFE 415
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLAT------HTKELKAVCQQYPFEPLVWKLT--PERMKELGVGVISEGVEP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 416 T------------------------------EETRKILDDICVaravecppprTTARLLDKLVGEFLEVTcispTFICDH 465
Cdd:PTZ00401 377 TdkyqarvhnmdsrmlrinymhciellntvlEEKMAPTDDINT----------TNEKLLGKLVKERYGTD----FFISDR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 466 -PQIMSPLAKWhRCK--EGLTERFELFVMKKEICNAYTELNDPvrqrQLFeeQAKAKAAGDDEAMFIDenFCTALEYGLP 542
Cdd:PTZ00401 443 fPSSARPFYTM-ECKddERFTNSYDMFIRGEEISSGAQRIHDP----DLL--LARAKMLNVDLTPIKE--YVDSFRLGAW 513
|
490 500
....*....|....*....|....*....
gi 2172664195 543 PTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PTZ00401 514 PHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
114-361 |
6.94e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 84.27 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 114 HLQPGDHLTDITLkvAGRIHAKRASGGkLIFYDLRGEGVKLQVM-----ANSRNYK-----SEEEFVHINNKLRRgDIIG 183
Cdd:PRK12820 11 HLSLDDTGREVCL--AGWVDAFRDHGE-LLFIHLRDRNGFIQAVfspeaAPADVYElaaslRAEFCVALQGEVQK-RLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 184 VEgNPgKTKKGELSIVPREMTLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNDFVRQKFIIR 247
Cdd:PRK12820 87 TE-NP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 248 SKIITYIRSFLDELGFLEIETPMMNI-IPGGAvaKPFITYHNELDMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNE 325
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDE 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 2172664195 326 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGM 361
Cdd:PRK12820 238 DLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARM 273
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
127-206 |
2.18e-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: 71.11 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 127 KVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSrnykseEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLL 206
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFK------EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
246-571 |
3.26e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.20 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 246 IRSKIITYIRSFLDELGFLEIETPMMN-----IIPGGA---VAKPFITYHNEldmnlYMRIAPEL-YHKMLVVGGIDRVY 316
Cdd:PRK06462 32 VQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSdlpVKQISIDFYGV-----EYYLADSMiLHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 317 EIGRQFRNEGID---LTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYK---ITYHPDGPEgqayeidFTPP 390
Cdd:PRK06462 107 YLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEdelEFFGRDLPH-------LKRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 391 FRRISMvEELEKVLGVKLPETSLFEteetrKILDDicvaravecppprttarlldklvGE-FLEVTCISPTFICDHPQIM 469
Cdd:PRK06462 180 FKRITH-KEAVEILNEEGCRGIDLE-----ELGSE-----------------------GEkSLSEHFEEPFWIIDIPKGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 470 SPL-AKWHRCKEGLTERFELFVMKK--EICNAyTElndpvRQRQLFEEQAKAKAAGDDEAMFidENFCTALEYGLPPTAG 546
Cdd:PRK06462 231 REFyDREDPERPGVLRNYDLLLPEGygEAVSG-GE-----REYEYEEIVERIREHGVDPEKY--KWYLEMAKEGPLPSAG 302
|
330 340
....*....|....*....|....*
gi 2172664195 547 WGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PRK06462 303 FGIGVERLTRYICGLRHIREVQPFP 327
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
125-234 |
9.51e-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: 51.37 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 125 TLKVAGRIHAKRASGGkLIFYDLR-GEGVkLQVMANSRNYKSEEEFvhinNKLRRGDIIGVEG----------NPgKTKK 193
Cdd:cd04317 16 EVTLCGWVQRRRDHGG-LIFIDLRdRYGI-VQVVFDPEEAPEFELA----EKLRNESVIQVTGkvrarpegtvNP-KLPT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2172664195 194 GELSIVPREMTLLSPClhmlPHLHFGLKDK-----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 2172664195 125 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFVHINNKLRRGDIIGVEGNPGKTKK--GELSIVPRE 202
Cdd:cd04316 14 EVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPKK--KVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEE 90
|
....*
gi 2172664195 203 MTLLS 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 |
2.74e-04 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 40.24 E-value: 2.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172664195 130 GRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKK 193
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEE 69
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
539-571 |
1.28e-03 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 41.63 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|...
gi 2172664195 539 YGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFP 571
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
254-340 |
3.97e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 39.82 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664195 254 IRSFLDELGFLEIETPMMniIPGGAVAKPFITYHNEL-------DMNLYMR--IAPELYHKMLVVGGI--D--RVYEIGR 320
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYNYLRKLDRIlpDpiKIFEIGP 290
|
90 100
....*....|....*....|
gi 2172664195 321 QFRNEGIDLTHNPEFTTCEF 340
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNF 310
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
313-375 |
8.83e-03 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 37.91 E-value: 8.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172664195 313 DRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYAD--YHDLMEITEKMLSGMVRSITG-SYKITYHP 375
Cdd:cd00496 81 IRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGltFADLKGTLEEFAKELFGPITKvRFRPSYFP 146
|
|
| |
