|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
48-605 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 893.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 48 RSELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNhttdnGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKF 127
Cdd:PLN02502 10 KNALKKRLKAKQAEEEKAAKEEAKAAAAAAAAKGRSRK-----SAAADDETMDPTQYRANRLKKVEALRAKGVEPYPYKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 128 HVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNY-KSEEEFIHINNKLRR 206
Cdd:PLN02502 85 DVTHTAPELQEKYGSLENGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLdLDEEEFEKLHSLVDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 207 GDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFL 286
Cdd:PLN02502 164 GDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLIANPEVRDIFRTRAKIISYIRRFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 287 DELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTC 366
Cdd:PLN02502 244 DDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTC 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 367 EFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHpdgpegqAYDVDFTPPFRRINMVEELEKALGMKLPEtnLFETEE 446
Cdd:PLN02502 324 EFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRISMISLVEEATGIDFPA--DLKSDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 447 TRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNA 526
Cdd:PLN02502 395 ANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKPHRSKPGLTERFELFINGRELANA 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194272210 527 YTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPED 605
Cdd:PLN02502 475 FSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
96-606 |
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: 704.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 96 EESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDhLTDITLKVAGRIHAKRaSGGKLIFYDL 175
Cdd:COG1190 2 SEEEDLNEQIRVRREKLEELREAGIDPYPNKFPRTHTAAEIREKYDELEAEE-ETGDEVSVAGRIMAKR-DMGKASFADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 176 RGEGVKLQVMAnSRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRY 255
Cdd:COG1190 80 QDGSGRIQLYL-RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 256 RQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKML 335
Cdd:COG1190 158 RQRYVDLIVNPEVRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 336 VVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDF 415
Cdd:COG1190 238 IVGGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 416 TPPFRRINMVEELEKALGmkLPETNLFETEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQ 495
Cdd:COG1190 311 SPPWRRITMVEAIKEATG--IDVTPLTDDEELRALAK----ELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 496 IMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGW 575
Cdd:COG1190 385 EVSPLAKRHRDDPGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGL 464
|
490 500 510
....*....|....*....|....*....|.
gi 194272210 576 GMGIDRVAMFLTDSNNIKEVLLFPAMKPEDK 606
Cdd:COG1190 465 GIGIDRLVMLLTDSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
100-605 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 696.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 100 DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGD-HLTDITLKVAGRIHAKRaSGGKLIFYDLRGE 178
Cdd:PRK00484 2 ELNEQIAVRREKLAELREQGIDPYPNKFERTHTAAELRAKYDDKEKEElEELEIEVSVAGRVMLKR-VMGKASFATLQDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 179 GVKLQVMAnSRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQR 258
Cdd:PRK00484 81 SGRIQLYV-SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 259 YLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVG 338
Cdd:PRK00484 159 YVDLIVNPESRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 339 GIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPP 418
Cdd:PRK00484 239 GFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 419 FRRINMVEELEKALGMKLPETNlfeTEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMS 498
Cdd:PRK00484 312 FKRLTMVDAIKEYTGVDFDDMT---DEEARALAK----ELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEIS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 499 PLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMG 578
Cdd:PRK00484 385 PLAKRHREDPGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIG 464
|
490 500
....*....|....*....|....*..
gi 194272210 579 IDRVAMFLTDSNNIKEVLLFPAMKPED 605
Cdd:PRK00484 465 IDRLVMLLTDSPSIRDVILFPLMRPEK 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
39-603 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 646.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 39 HKDKSFSDQRSELKRRLKAEKKVAEKEAKQKELSEkqlsqataaatnhttdngvgpEEESVDPNQYYKIRSQAIHQLKVN 118
Cdd:PTZ00417 41 HCKQCFVTMSEKKEHVMEGEKKVRSVQASKDKKKE---------------------EEAEVDPRLYYENRSKFIQEQKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 119 GEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMAN-SRNYKSEEEF 197
Cdd:PTZ00417 100 GINPYPHKFERTITVPEFVEKYQDLASGEHLEDTILNVTGRIMRVSASGQKLRFFDLVGDGAKIQVLANfAFHDHTKSNF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 198 IHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPhLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSK 277
Cdd:PTZ00417 180 AECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-MKYGLKDTEIRYRQRYLDLMINESTRSTFITRTK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 278 IITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 357
Cdd:PTZ00417 259 IINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 358 THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLP 437
Cdd:PTZ00417 339 THNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEIDFTPPYPKVSIVEELEKLTNTKLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 438 ETnlFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCIN-PTFICDHPQIMSPLAKWHRSKEGLTERFEL 516
Cdd:PTZ00417 419 QP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLTERLEM 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 517 FVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVL 596
Cdd:PTZ00417 497 FICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVI 576
|
....*..
gi 194272210 597 LFPAMKP 603
Cdd:PTZ00417 577 LFPTMRP 583
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
100-603 |
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: 639.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 100 DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH-LTDITLKVAGRIHAKRaSGGKLIFYDLRGE 178
Cdd:TIGR00499 1 ELNDQAQQRLEKLNRLRQTGNNPYLHKFERTHSAQEFQEKYADLSNEELkEKELKVSIAGRIKAIR-SMGKATFITLQDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 179 GVKLQVMANSRNYKseEEFIHINNK-LRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQ 257
Cdd:TIGR00499 80 SGQIQLYVNKNKLP--EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 258 RYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVV 337
Cdd:TIGR00499 158 RYLDLIVNPDVRQTFLKRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 338 GGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTP 417
Cdd:TIGR00499 238 GGLEKVYEIGRVFRNEGVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 418 PFRRINMVEELEKALGMKLpetNLFETEETRKILDDICVAKAVECPPprTTARLLDKLVGEFLEVTCINPTFICDHPQIM 497
Cdd:TIGR00499 311 PWKRITMVDALEMVTGIDF---DILKDDETAKALAKEHGIEVAEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 498 SPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGM 577
Cdd:TIGR00499 386 SPLAKRDPSNPEFTERFELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGI 465
|
490 500
....*....|....*....|....*.
gi 194272210 578 GIDRVAMFLTDSNNIKEVLLFPAMKP 603
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 ... |
265-603 |
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: 626.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 265 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVY 344
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 345 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINM 424
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 425 VEELEKALGMKLPETNLFETEETRKILDDICvakAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWH 504
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 505 RSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAM 584
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 194272210 585 FLTDSNNIKEVLLFPAMKP 603
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
132-609 |
2.75e-145 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 436.00 E-value: 2.75e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 132 SLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRaSGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIG 211
Cdd:PTZ00385 88 PISEVRERYGYLASGDRAAQATVRVAGRVTSVR-DIGKIIFVTIRSNGNELQVVGQVGEHFTREDLKKLKVSLRVGDIIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 212 VQGNPGKTKKGELSIIPYEITLLSP--CLHML--PHLH-FG-LKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSF 285
Cdd:PTZ00385 167 ADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHVMLQALRDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 286 LDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTT 365
Cdd:PTZ00385 247 FNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 366 CEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETE 445
Cdd:PTZ00385 327 CEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFPPPNELNTP 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 446 ETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICN 525
Cdd:PTZ00385 407 KGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELFVNGIEYCN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 526 AYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPED 605
Cdd:PTZ00385 487 AYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFPLLRQDI 566
|
....
gi 194272210 606 KKEN 609
Cdd:PTZ00385 567 RSHD 570
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
115-605 |
1.92e-141 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 438.63 E-value: 1.92e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 115 LKVNGEDPYPhkfhVDISLTDFIQkyshlQPGDHLTDITLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANsrnyKSE 194
Cdd:PRK02983 624 LRAAGVDPYP----VGVPPTHTVA-----EALDAPTGEEVSVSGRVLRIRDYGG-VLFADLRDWSGELQVLLD----ASR 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 195 EEFIHINNKLR---RGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQK 271
Cdd:PRK02983 690 LEQGSLADFRAavdLGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 272 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 351
Cdd:PRK02983 770 LRARSAVVRAVRETLVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFR 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 352 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpDGPEGQAYDVDFTPPFRRINMVEELEKA 431
Cdd:PRK02983 850 NEGVDATHNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEA 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 432 LGMKL-PETNLfetEETRKilddICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGL 510
Cdd:PRK02983 928 LGEEIdPDTPL---AELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGL 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 511 TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTdSN 590
Cdd:PRK02983 1001 AERWDLVAWGVELGTAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GR 1079
|
490
....*....|....*
gi 194272210 591 NIKEVLLFPAMKPED 605
Cdd:PRK02983 1080 SIRETLPFPLVKPRQ 1094
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
96-604 |
8.04e-135 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 404.06 E-value: 8.04e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 96 EESVDPNQYYKIRSQAIHQLKVNGEdPYPHKFHVDISlTDFIQKYSHLQPGDHLT--DITLKVAGRIHAKRASGgKLIFY 173
Cdd:PRK12445 10 NEAIDFNDELRNRREKLAALRQQGV-AFPNDFRRDHT-SDQLHEEFDAKDNQELEslNIEVSVAGRMMTRRIMG-KASFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 174 DLRGEGVKLQVMAnSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKET 253
Cdd:PRK12445 87 TLQDVGGRIQLYV-ARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 254 RYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHK 333
Cdd:PRK12445 166 RYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 334 MLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDV 413
Cdd:PRK12445 246 RLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-------GEHVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 414 DFTPPFRRINMVEELEKalgmKLPETNLFEteetrkiLDDICVAKA------VECPPPRTTARLLDKLVGEFLEVTCINP 487
Cdd:PRK12445 319 DFGKPFEKLTMREAIKK----YRPETDMAD-------LDNFDAAKAlaesigITVEKSWGLGRIVTEIFDEVAEAHLIQP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 488 TFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEY 567
Cdd:PRK12445 388 TFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEY 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 194272210 568 GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPE 604
Cdd:PRK12445 468 GLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
250-602 |
2.44e-122 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 364.96 E-value: 2.44e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 250 DKETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPE 329
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 330 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPdgpegq 409
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 410 aYDVDFTPPFRRINMVEELEKALGMKLPETnlfeteetrkiLDDIcvakavecppPRTTARLLDKLVgefLEVTCINPTF 489
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVEEL-----------GYGS----------DKPDLRFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 490 ICDHPQIMSPLAKWHRSK-EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKaagdDEAMFIDENFCTALEYG 568
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 194272210 569 LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMK 602
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 ... |
272-603 |
1.11e-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: 286.68 E-value: 1.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 272 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 351
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 352 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEELEKA 431
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 432 LgmklpetnlfeteetrkilddicvakavecppprttarlldklvgeflevtciNPTFICDHP-QIMSPLAKWHRSKEGL 510
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 511 TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGddeaMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSN 590
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 194272210 591 NIKEVLLFPAMKP 603
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
285-596 |
2.48e-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: 189.68 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 285 FLDELGFLEIETPMMniIPGG-------AVAKPFITYHNElDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 357
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 358 THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhitgsykvtyhpdgpegqaydvDFTPPFRRINMVEELEKALGMKLP 437
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 438 ETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKEGLTERFE 515
Cdd:TIGR00462 136 TASLAE-------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 516 LFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEV 595
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 194272210 596 L 596
Cdd:TIGR00462 289 L 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
275-596 |
1.32e-52 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 183.00 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 275 RSKIITYIRSFLDELGFLEIETPMMNIIPGGAVA-KPFITY---HNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 350
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 351 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSgmvkhitgsykvtyhpdgpegQAYDVDFTPPFRRINMVEELEK 430
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 431 ALGMKLPETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKE 508
Cdd:COG2269 148 YLGIDPLTADLDE-------LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQlgRDRPTFLYDYPASQAALARISPDDP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 509 GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD 588
Cdd:COG2269 221 RVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALG 300
|
....*...
gi 194272210 589 SNNIKEVL 596
Cdd:COG2269 301 AERIDDVL 308
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
153-262 |
1.90e-52 |
|
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: 175.36 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYkSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEIT 232
Cdd:cd04322 1 EVSVAGRIMSKRGSG-KLSFADLQDESGKIQVYVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFT 78
|
90 100 110
....*....|....*....|....*....|
gi 194272210 233 LLSPCLHMLPHLHFGLKDKETRYRQRYLDL 262
Cdd:cd04322 79 LLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
275-595 |
5.88e-41 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 150.85 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 275 RSKIITYIRSFLDELGFLEIETPMM--------NIIPggaVAKPFITYHNELDMNLYMRIAPElYH-KMLVVGGIDRVYE 345
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 346 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHpdgpegQAY----DVDFTPPfrr 421
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-CEPAESLSYQ------QAFlrylGIDPLSA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 422 inMVEELeKALGMKLPETNLFETEETRKILDDICVAKAVEcppprttarllDKLVGEflevtciNPTFICDHPQIMSPLA 501
Cdd:PRK09350 154 --DKTQL-REVAAKLGLSNIADEEEDRDTLLQLLFTFGVE-----------PNIGKE-------KPTFVYHFPASQAALA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 502 KWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDR 581
Cdd:PRK09350 213 KISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDR 292
|
330
....*....|....
gi 194272210 582 VAMFLTDSNNIKEV 595
Cdd:PRK09350 293 LIMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
156-599 |
1.87e-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: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 156 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFIHINNKLRRGDIIGVQGNPGKTKK--GELSIIPYEITL 233
Cdd:TIGR00458 17 FMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAK--KVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 234 LSPCLHMLPHLhfgLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIP--GGA 306
Cdd:TIGR00458 94 INEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-RRPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 307 VAKPfITYhneLDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKM 385
Cdd:TIGR00458 170 ELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 386 VsgmvkhitgsykVTYHPDGPEgqaydvdftppfRRINMVEELEKALgmKLPETNL--FETEETRKILDdicvAKAVECP 463
Cdd:TIGR00458 246 V------------VRVFEDVPE------------RCAHQLETLEFKL--EKPEGKFvrLTYDEAIEMAN----AKGVEIG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 464 PPRTTARLLDKLVGEFLEvtciNPTFICDHPQ------IMSPLAKWHRSKEglterFELFVMKKEICNAYTELNDpmrqR 537
Cdd:TIGR00458 296 WGEDLSTEAEKALGEEMD----GLYFITDWPTeirpfyTMPDEDNPEISKS-----FDLMYRDLEISSGAQRIHL----H 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194272210 538 QLFEEQAKAKAAGDDEAmfidENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:TIGR00458 363 DLLVERIKAKGLNPEGF----KDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFP 420
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
153-599 |
5.92e-38 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 146.10 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMAnsRNYKSEEEFIHINnKLRRGDIIGVQG----NPgKTKKGeLSIIP 228
Cdd:PRK05159 18 EVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVV--KKKVDEELFETIK-KLKRESVVSVTGtvkaNP-KAPGG-VEVIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 229 YEITLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPmmNIIP 303
Cdd:PRK05159 92 EEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFKIRSEVLRAFREFLYENGFTEIFTP--KIVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 304 ----GGAVAKPfITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYAD-YHD 377
Cdd:PRK05159 166 sgteGGAELFP-IDYFEK---EAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSrHLNEYTSIDVEMGFIDdHED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 378 LMEITEKMVSGMVKHITGSYKvtyhpdgPEGQAYDVDF---TPPFRRINMVEELE--KALGMKLPETNLFETEETRKILD 452
Cdd:PRK05159 242 VMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITYDEAIEilKSKGNEISWGDDLDTEGERLLGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 453 DIcvakavecppprttarlLDKLVGEFLevtcinptFICDHPQIMSPL-AKWHRSKEGLTERFELfvMKK--EICNAYTE 529
Cdd:PRK05159 315 YV-----------------KEEYGSDFY--------FITDYPSEKRPFyTMPDEDDPEISKSFDL--LFRglEITSGGQR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 530 LNDpmrqRQLFEEQAKAKaaGDDEAMFidENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:PRK05159 368 IHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
153-599 |
1.87e-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: 121.31 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGgKLIFYDLR-GEGVkLQVMANSRNYKSEEEFihinNKLRRGDIIGVQG----NPGKtkKGELSII 227
Cdd:COG0017 16 EVTVAGWVRTKRDSG-GISFLILRdGSGF-IQVVVKKDKLENFEEA----KKLTTESSVEVTGtvveSPRA--PQGVELQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 228 PYEITLLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLILNDFvRQKFIIRSKIITYIRSFLDELGFLEIETPmmnIIPGG 305
Cdd:COG0017 88 AEEIEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRSELARAIREFFQERGFVEVHTP---IITAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 306 AV---AKPF-ITYHNEldmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLME 380
Cdd:COG0017 161 ATeggGELFpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRrHLAEFWMIEPEMAFADLEDVMD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 381 ITEKMVSGMVKHItgsykVTYHPDgpEGQAYDVDFT-------PPFRRINM---VEELEKAlGMKLPETNLFETEETRKI 450
Cdd:COG0017 237 LAEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITYteaIEILKKS-GEKVEWGDDLGTEHERYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 451 lddicvakavecppprtTARLLDKLVgeflevtcinptFICDHPQIMSPlakwhrskeglterfelFVMK-----KEICN 525
Cdd:COG0017 309 -----------------GEEFFKKPV------------FVTDYPKEIKA-----------------FYMKpnpddPKTVA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 526 A-------YTELndpmrQRqlfEEQ-----AKAKAAGDDEAMF---IDenfctALEYGLPPTAGWGMGIDRVAMFLTDSN 590
Cdd:COG0017 343 AfdllapgIGEIig-gsQR---EHRydvlvERIKEKGLDPEDYewyLD-----LRRYGSVPHAGFGLGLERLVMWLTGLE 413
|
....*....
gi 194272210 591 NIKEVLLFP 599
Cdd:COG0017 414 NIREVIPFP 422
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
153-599 |
2.94e-29 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 122.48 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyksEEEFIHINNKLRRGDIIGVQG----------NPgKTKK 221
Cdd:PRK00476 19 TVTLCGWVHRRRDHGG-LIFIDLRDrEGI-VQVVFDP-----DAEAFEVAESLRSEYVIQVTGtvrarpegtvNP-NLPT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 222 GELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLilndfvR-----QKFIIRSKIITYIRSFLDELGF 291
Cdd:PRK00476 91 GEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL------RrpemqKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 292 LEIETPMMniI---PGGA----VakPfityhneldmnlyMRI----------APELYHKMLVVGGIDRVYEIGRQFRNEg 354
Cdd:PRK00476 161 LEIETPIL--TkstPEGArdylV--P-------------SRVhpgkfyalpqSPQLFKQLLMVAGFDRYYQIARCFRDE- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 355 iDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK 430
Cdd:PRK00476 223 -DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG-----------------VDLPTPFPRMTYAEAMRR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 431 --------ALGMKLPE-TNLFETEE--------------------------TRKILDD---------------ICV---- 456
Cdd:PRK00476 283 ygsdkpdlRFGLELVDvTDLFKDSGfkvfagaandggrvkairvpggaaqlSRKQIDEltefakiygakglayIKVnedg 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 457 -----------------AKAVECPP----------PRTTARLLDKL---VGEFLEVT---CINPTFICD----------- 492
Cdd:PRK00476 363 lkgpiakflseeelaalLERTGAKDgdliffgadkAKVVNDALGALrlkLGKELGLIdedKFAFLWVVDfpmfeydeeeg 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 493 ------HPQIMsPlakwhrsKEGLTERFELFVMKKEICNAY------TEL-------NDPMRQRQLF------EEQAKAK 547
Cdd:PRK00476 443 rwvaahHPFTM-P-------KDEDLDELETTDPGKARAYAYdlvlngYELgggsiriHRPEIQEKVFeilgisEEEAEEK 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 194272210 548 AAGddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:PRK00476 515 FGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
153-599 |
3.24e-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: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGGkLIFYDLRG-EGVkLQVMANSrnyKSEEEFIHINNKLRRGDIIGVQG----------NPgKTKK 221
Cdd:COG0173 18 EVTLSGWVHRRRDHGG-LIFIDLRDrYGI-TQVVFDP---DDSAEAFEKAEKLRSEYVIAVTGkvrarpegtvNP-KLPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 222 GELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIET 296
Cdd:COG0173 92 GEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRPEMQKNLILRHKVTKAIRNYLDENGFLEIET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 297 PMMNI-IPGGA----VakPFityhneldmnlymRI----------APELYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN- 360
Cdd:COG0173 167 PILTKsTPEGArdylV--PS-------------RVhpgkfyalpqSPQLFKQLLMVSGFDRYFQIARCFRDE--DLRADr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 361 -PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK------- 430
Cdd:COG0173 230 qPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG-----------------VELPTPFPRMTYAEAMERygsdkpd 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 431 -ALGMKLPE-TNLFETEE-------------------------TRKILDDIC------------------------VAKA 459
Cdd:COG0173 291 lRFGLELVDvTDIFKDSGfkvfagaaenggrvkainvpggaslSRKQIDELTefakqygakglayikvnedglkspIAKF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 460 VecpPPRTTARLLDKL---VGEFLevtcinpTFICDHPQIMSP--------LAKwhrsKEGLTER-------------FE 515
Cdd:COG0173 371 L---SEEELAAILERLgakPGDLI-------FFVADKPKVVNKalgalrlkLGK----ELGLIDEdefaflwvvdfplFE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 516 L-------------FVMKKE-------------ICNAY------TEL-------NDPMRQRQLF------EEQAKAKAAG 550
Cdd:COG0173 437 YdeeegrwvamhhpFTMPKDedldlletdpgkvRAKAYdlvlngYELgggsiriHDPELQEKVFellgisEEEAEEKFGF 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 194272210 551 ddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:COG0173 517 -----LLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
272-599 |
3.68e-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: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 272 FIIRSKIITYIRSFLDELGFLEIETPMMN-IIPGGA----VakPFITYHNE---LDMnlymriAPELYHKMLVVGGIDRV 343
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGArdflV--PSRLHPGKfyaLPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 344 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRIN 423
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 424 MVEELEKaLGMKL------PetnLFE-TEETRKIlddicvaKAVECP---PPRTTARLLDKlvgeflevtciNPTFIcdh 493
Cdd:cd00777 136 YAEAMER-YGFKFlwivdfP---LFEwDEEEGRL-------VSAHHPftaPKEEDLDLLEK-----------DPEDA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 494 pqimsplakwhrskegLTERFELFVMKKEICNAYTELNDPMRQRQLFE------EQAKAKAAGddeamfidenFCTALEY 567
Cdd:cd00777 191 ----------------RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEilglseEEAEEKFGF----------LLEAFKY 244
|
330 340 350
....*....|....*....|....*....|..
gi 194272210 568 GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:cd00777 245 GAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
252-599 |
8.26e-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: 111.50 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 252 ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMM--NIIPGGAVAKPfITYHNEldmNLYMRIAPE 329
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFK-VSYFGK---PAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 330 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKMVSGMVKHITGSYK-----VTYH 402
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 403 PDGPEGqaydvdFTPPFRRInmveELEKALGMklpetnLFETEETRKILDDICVAKAVEcppprttaRLLDKLVGEflev 482
Cdd:cd00776 159 NRELLK------PLEPFPRI----TYDEAIEL------LREKGVEEEVKWGEDLSTEHE--------RLLGEIVKG---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 483 tciNPTFICDHPQIMSPL-AKWHRSKEGLTERFELFVMKK-EICNAYTELNDPmrqrQLFEEQAKAKaaGDDEAMFidEN 560
Cdd:cd00776 211 ---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF--EW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 194272210 561 FCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
156-430 |
1.91e-24 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 108.34 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 156 VAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNYKSEEEFIhinNKLRRGDIIGVQG----------NPgKTKKGELS 225
Cdd:PLN02903 77 LCGWVDLHRDMGG-LTFLDVRDHTGIVQVVTLPDEFPEAHRTA---NRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 226 IIPYEITLLSPCLHMLPHLHFGLKD------KETRYRQRYLDLILNDFVRQkFIIRSKIITYIRSFL-DELGFLEIETPM 298
Cdd:PLN02903 152 VVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLRRPQMNAN-LRLRHRVVKLIRRYLeDVHGFVEIETPI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 299 MN---------------IIPGGAVAKPfityhneldmnlymrIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEF 363
Cdd:PLN02903 231 LSrstpegardylvpsrVQPGTFYALP---------------QSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEF 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194272210 364 TTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRINMVEELEK 430
Cdd:PLN02903 296 TQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-----------------VQLPNPFPRLTYAEAMSK 345
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
56-599 |
8.58e-19 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 90.15 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 56 KAEKKVAEKEAKQKELSEKQLSQATAAATNhttdngvgPEEESVDPNQYYKIRSQAIhQLKVNGedpyphKFHVDISltd 135
Cdd:PLN02850 12 KISKKAAKKAAAKAEKLRREATAKAAAASL--------EDEDDPLASNYGDVPLEEL-QSKVTG------REWTDVS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 136 fiqkyshlQPGDHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRG---DIIGV 212
Cdd:PLN02850 74 --------DLGEELAGSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFVSEVTVSKGMVKYAKQLSREsvvDVEGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 213 QGNPGKTKKG---ELSIIPYEITLLSPCLHMLPhlhFGLKD----------------------KETRYRQRYLDLIL--N 265
Cdd:PLN02850 145 VSVPKKPVKGttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDLRTpaN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 266 DFVrqkFIIRSKIITYIRSFLDELGFLEIETPmmNIIPG-----GAVAKpfityhneLDmnlYMRI------APELYHKM 334
Cdd:PLN02850 222 QAI---FRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGaseggSAVFR--------LD---YKGQpaclaqSPQLHKQM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 335 LVVGGIDRVYEIGRQFRNEGiDLTHNP--EFTTCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSYK------VTYHPDG 405
Cdd:PLN02850 286 AICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKkeleaiREQYPFE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 406 PegqaydVDFTPPFRRINMVE--ELEKALGMKLPETNLFETEETRKiLDDICVAKAvecpppRTTARLLDKL---VGEFL 480
Cdd:PLN02850 365 P------LKYLPKTLRLTFAEgiQMLKEAGVEVDPLGDLNTESERK-LGQLVKEKY------GTDFYILHRYplaVRPFY 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 481 EVTCI-NPTFicdhpqimsplakwhrskeglTERFELFVMKKEICNAYTELNDPmrqrQLFEEQAKAKAAG-DDEAMFID 558
Cdd:PLN02850 432 TMPCPdDPKY---------------------SNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEECGIDvKTISTYID 486
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 194272210 559 enfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:PLN02850 487 -----SFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
147-599 |
7.64e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 86.97 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 147 DHLTDITLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNyKSEEEFIHINNKLRRGDIIGVQGNPGK-------T 219
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAVEG-DVPKEMIDFIGQIPTESIVDVEATVCKveqpitsT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 220 KKGELSIIPYEITLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFL 286
Cdd:PTZ00401 152 SHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 287 DELGFLEIETPMMNIIPGGAVAKPF-ITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL-THNPEFT 364
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGANVFkLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNThRHLTEFV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 365 TCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSykvtyhpdgpEGQAYDVDFTPPFRRI--NMVEELEKALGMKLPETNL 441
Cdd:PTZ00401 305 GLDVEMRINEhYYEVLDLAESLFNYIFERLATH----------TKELKAVCQQYPFEPLvwKLTPERMKELGVGVISEGV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 442 FETEETR-------------------KILDDICVAKAVECPPPRTT-ARLLDKLVGEFLEVTcinpTFICDH-PQIMSPL 500
Cdd:PTZ00401 375 EPTDKYQarvhnmdsrmlrinymhciELLNTVLEEKMAPTDDINTTnEKLLGKLVKERYGTD----FFISDRfPSSARPF 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 501 AKWH-RSKEGLTERFELFVMKKEICNAYTELNDPmrqrQLFeeQAKAKAAGDDEAMFIDenFCTALEYGLPPTAGWGMGI 579
Cdd:PTZ00401 451 YTMEcKDDERFTNSYDMFIRGEEISSGAQRIHDP----DLL--LARAKMLNVDLTPIKE--YVDSFRLGAWPHGGFGVGL 522
|
490 500
....*....|....*....|
gi 194272210 580 DRVAMFLTDSNNIKEVLLFP 599
Cdd:PTZ00401 523 ERVVMLYLGLSNVRLASLFP 542
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
142-599 |
8.97e-18 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 87.35 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 142 HLQPGDHLTDITLkvAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRNykSEEEFIHINNKLRRGDIIGVQG------- 214
Cdd:PRK12820 11 HLSLDDTGREVCL--AGWVDAFRDHGE-LLFIHLRDRNGFIQAVFSPEA--APADVYELAASLRAEFCVALQGevqkrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 215 ---NPgKTKKGELSIIPYEITLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNDFVRQKFIIR 275
Cdd:PRK12820 86 eteNP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 276 SKIITYIRSFLDELGFLEIETPMMNI-IPGGAvaKPFITYHNELDMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNE 353
Cdd:PRK12820 160 HRIIKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 354 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHPDGPEGQAYD---------------VDFTPP 418
Cdd:PRK12820 238 DLRPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFA-IGGIALPRPFPRMPYAEAMDttgsdrpdlrfdlkfADATDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 419 FRR------------------INMVEELEK-------------------ALGM--------KLpETNL---FETEETRKI 450
Cdd:PRK12820 317 FENtrygifkqilqrggrikgINIKGQSEKlsknvlqneyakeiapsfgAKGMtwmraeagGL-DSNIvqfFSADEKEAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 451 L--------DDICVAKAVECPPPRTTARLLDKLVGEFLEVT---CINPTFICDHPQIMS-----------PLAKWHRSK- 507
Cdd:PRK12820 396 KrrfhaedgDVIIMIADASCAIVLSALGQLRLHLADRLGLIpegVFHPLWITDFPLFEAtddggvtsshhPFTAPDREDf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 508 -----EGL----TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFidenFCTALEYGLPPTAGWGMG 578
Cdd:PRK12820 476 dpgdiEELldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGF----FLRAFDFAAPPHGGIALG 551
|
570 580
....*....|....*....|.
gi 194272210 579 IDRVAMFLTDSNNIKEVLLFP 599
Cdd:PRK12820 552 LDRVVSMILQTPSIREVIAFP 572
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
153-236 |
1.20e-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: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGgKLIFYDLRGEGVKLQVMANSRNYKSEEEFIhinNKLRRGDIIGVQGNPGKT-----KKGELSII 227
Cdd:cd04100 1 EVTLAGWVHSRRDHG-GLIFIDLRDGSGIVQVVVNKEELGEFFEEA---EKLRTESVVGVTGTVVKRpegnlATGEIELQ 76
|
....*....
gi 194272210 228 PYEITLLSP 236
Cdd:cd04100 77 AEELEVLSK 85
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
274-387 |
1.69e-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: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 274 IRSKIITYIRSFLDELGFLEIETPMMNIIPG----GAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGI----DRVYE 345
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 194272210 346 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKMVS 387
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
155-234 |
6.18e-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: 69.96 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 155 KVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSrnykseEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLL 234
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLTLRDGTGSIQVVVFK------EEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
274-599 |
2.16e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.59 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 274 IRSKIITYIRSFLDELGFLEIETPMMN-----IIPGGA---VAKPFITYHNEldmnlYMRIAPEL-YHKMLVVGGIDRVY 344
Cdd:PRK06462 32 VQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSdlpVKQISIDFYGV-----EYYLADSMiLHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 345 EIGRQFRNEG---IDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHItgsykVTYHPDGPEGQAYDV-DFTPPFR 420
Cdd:PRK06462 107 YLSPNFRLEPvdkDTGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKEL-----LEEHEDELEFFGRDLpHLKRPFK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 421 RINMvEELEKALGMKLPETNLFEteetrKILDDicvakavecppprttarlldklvGE-FLEVTCINPTFICDHPQIMSP 499
Cdd:PRK06462 182 RITH-KEAVEILNEEGCRGIDLE-----ELGSE-----------------------GEkSLSEHFEEPFWIIDIPKGSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 500 LakWHRSKEG-----------LTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAK-----AKAagddeamfidenfct 563
Cdd:PRK06462 233 F--YDREDPErpgvlrnydllLPEGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKwylemAKE--------------- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 194272210 564 aleyGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:PRK06462 296 ----GPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
153-262 |
2.13e-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: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGGkLIFYDLR-GEGVkLQVMANSRNYKSEEEFihinNKLRRGDIIGVQG----------NPgKTKK 221
Cdd:cd04317 16 EVTLCGWVQRRRDHGG-LIFIDLRdRYGI-VQVVFDPEEAPEFELA----EKLRNESVIQVTGkvrarpegtvNP-KLPT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 194272210 222 GELSIIPYEITLLSPClhmlPHLHFGLKDK-----ETRYRQRYLDL 262
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 ... |
153-235 |
4.49e-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: 43.07 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 153 TLKVAGRIHAKRASGGkLIFYDLRGEGVKLQVMANSRnyKSEEEFIHINNKLRRGDIIGVQGNPGKTKK--GELSIIPYE 230
Cdd:cd04316 14 EVTVAGWVHEIRDLGG-IKFVILRDREGIVQVTAPKK--KVDKELFKTVRKLSRESVISVTGTVKAEPKapNGVEIIPEE 90
|
....*
gi 194272210 231 ITLLS 235
Cdd:cd04316 91 IEVLS 95
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
158-221 |
1.22e-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: 38.70 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194272210 158 GRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKK 221
Cdd:cd04320 6 ARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEE 69
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
567-599 |
1.86e-03 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 41.25 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|...
gi 194272210 567 YGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 599
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
282-368 |
3.08e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 40.21 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272210 282 IRSFLDELGFLEIETPMMniIPGGAVAKPFITYHNEL-------DMNLYMR--IAPELYHKMLVVGGI--D--RVYEIGR 348
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYNYLRKLDRIlpDpiKIFEIGP 290
|
90 100
....*....|....*....|
gi 194272210 349 QFRNEGIDLTHNPEFTTCEF 368
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNF 310
|
|
| |
