|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
1-421 |
0e+00 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 759.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 1 MANSRNY-KSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLI 79
Cdd:PLN02502 141 YADKKRLdLDEEEFEKLHSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVLTKCLLMLPDKYHGLTDQETRYRQRYLDLI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 80 LNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRV 159
Cdd:PLN02502 221 ANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLNMIAGGAAARPFVTHHNDLNMDLYLRIATELHLKRLVVGGFERV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 160 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHpdgpegqAYDVDFTPPFRRIN 239
Cdd:PLN02502 301 YEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTGSYKIKYH-------GIEIDFTPPFRRIS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 240 MVEELEKALGMKLPEtnLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKW 319
Cdd:PLN02502 374 MISLVEEATGIDFPA--DLKSDEANAYLIAACEKFDVKCPPPQTTGRLLNELFEEFLEETLVQPTFVLDHPVEMSPLAKP 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 320 HRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVA 399
Cdd:PLN02502 452 HRSKPGLTERFELFINGRELANAFSELTDPVDQRERFEEQVKQHNAGDDEAMALDEDFCTALEYGLPPTGGWGLGIDRLV 531
|
410 420
....*....|....*....|..
gi 1802983340 400 MFLTDSNNIKEVLLFPAMKPED 421
Cdd:PLN02502 532 MLLTDSASIRDVIAFPAMKPQD 553
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
4-422 |
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: 633.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 4 SRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDF 83
Cdd:COG1190 91 RRDELGEEAYELFK-LLDLGDIVGVEGTVFRTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYRQRYVDLIVNPE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 84 VRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIG 163
Cdd:COG1190 170 VRETFRKRSKIIRAIRRFLDERGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVFEIG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 164 RQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEE 243
Cdd:COG1190 250 RNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGTTKVTY-------QGQEIDLSPPWRRITMVEA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 244 LEKALGmkLPETNLFETEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSK 323
Cdd:COG1190 323 IKEATG--IDVTPLTDDEELRALAK----ELGIEVDPGWGRGKLIDELFEELVEPKLIQPTFVTDYPVEVSPLAKRHRDD 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 324 EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLT 403
Cdd:COG1190 397 PGLTERFELFIAGREIANAFSELNDPIDQRERFEEQLELKAAGDDEAMPMDEDFLRALEYGMPPTGGLGIGIDRLVMLLT 476
|
410
....*....|....*....
gi 1802983340 404 DSNNIKEVLLFPAMKPEDK 422
Cdd:COG1190 477 DSPSIRDVILFPLMRPEKK 495
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
4-421 |
0e+00 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 631.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 4 SRNYKSEEEFIHINnKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDF 83
Cdd:PRK00484 89 SKDDVGEEALEAFK-KLDLGDIIGVEGTLFKTKTGELSVKATELTLLTKSLRPLPDKFHGLTDVETRYRQRYVDLIVNPE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 84 VRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIG 163
Cdd:PRK00484 168 SRETFRKRSKIISAIRRFLDNRGFLEVETPMLQPIAGGAAARPFITHHNALDIDLYLRIAPELYLKRLIVGGFERVYEIG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 164 RQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEE 243
Cdd:PRK00484 248 RNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGTTKVTY-------QGTEIDFGPPFKRLTMVDA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 244 LEKALGMKLPETNlfeTEETRKILDdicvAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSK 323
Cdd:PRK00484 321 IKEYTGVDFDDMT---DEEARALAK----ELGIEVEKSWGLGKLINELFEEFVEPKLIQPTFITDYPVEISPLAKRHRED 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 324 EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLT 403
Cdd:PRK00484 394 PGLTERFELFIGGREIANAFSELNDPIDQRERFEAQVEAKEAGDDEAMFMDEDFLRALEYGMPPTGGLGIGIDRLVMLLT 473
|
410
....*....|....*...
gi 1802983340 404 DSNNIKEVLLFPAMKPED 421
Cdd:PRK00484 474 DSPSIRDVILFPLMRPEK 491
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
81-419 |
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: 616.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 81 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVY 160
Cdd:cd00775 1 NEEVRQTFIVRSKIISYIRKFLDDRGFLEVETPMLQPIAGGAAARPFITHHNALDMDLYLRIAPELYLKRLIVGGFERVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 161 EIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINM 240
Cdd:cd00775 81 EIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGKTKIEY-------GGKELDFTPPFKRVTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 241 VEELEKALGMKLPETNLFETEETRKILDDICvakAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWH 320
Cdd:cd00775 154 VDALKEKTGIDFPELDLEQPEELAKLLAKLI---KEKIEKPRTLGKLLDKLFEEFVEPTLIQPTFIIDHPVEISPLAKRH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 321 RSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAM 400
Cdd:cd00775 231 RSNPGLTERFELFICGKEIANAYTELNDPFDQRERFEEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGLGIGIDRLVM 310
|
330
....*....|....*....
gi 1802983340 401 FLTDSNNIKEVLLFPAMKP 419
Cdd:cd00775 311 LLTDSNSIRDVILFPAMRP 329
|
|
| lysS_bact |
TIGR00499 |
lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; This model represents the ... |
11-419 |
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: 561.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 11 EEFIHINNK-LRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFI 89
Cdd:TIGR00499 94 EDFYEFDEYlLDLGDIIGVTGYPFKTKTGELSVKVTELQILTKCLQPLPDKWHGLTDQETRYRQRYLDLIVNPDVRQTFL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 90 IRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNE 169
Cdd:TIGR00499 174 KRSKIIKAIRRFLDDRGFIEVETPMLQSIPGGANAKPFITHHNALDMDLYLRIAPELYLKRLIVGGLEKVYEIGRVFRNE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 170 GIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEELEKALG 249
Cdd:TIGR00499 254 GVDTTHNPEFTMIEFYQAYADYEDLMDLTENLFKFLAKELLGTFIINY-------NDLEIDLKPPWKRITMVDALEMVTG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 250 MKLpetNLFETEETRKILDDICVAKAVECPPprTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTER 329
Cdd:TIGR00499 327 IDF---DILKDDETAKALAKEHGIEVAEDSL--TLGHILNKFFEQFLEHTLIQPTFITHYPAEISPLAKRDPSNPEFTER 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 330 FELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIK 409
Cdd:TIGR00499 402 FELFIAGKEIANAYSELNDPLDQRERFEQQLAEKEAGDDEAQLVDEDFVEALEYGMPPTGGLGIGIDRLVMLLTDAPSIR 481
|
410
....*....|
gi 1802983340 410 EVLLFPAMKP 419
Cdd:TIGR00499 482 DVLLFPQLRP 491
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
9-419 |
0e+00 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 546.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 9 SEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPhLHFGLKDKETRYRQRYLDLILNDFVRQKF 88
Cdd:PTZ00417 175 TKSNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETIILSPCLHMLP-MKYGLKDTEIRYRQRYLDLMINESTRSTF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 89 IIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRN 168
Cdd:PTZ00417 254 ITRTKIINYLRNFLNDRGFIEVETPTMNLVAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 169 EGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKAL 248
Cdd:PTZ00417 334 EGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFGTYKILYNKDGPEKDPIEIDFTPPYPKVSIVEELEKLT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 249 GMKLPETnlFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCIN-PTFICDHPQIMSPLAKWHRSKEGLT 327
Cdd:PTZ00417 414 NTKLEQP--FDSPETINKMINLIKENKIEMPNPPTAAKLLDQLASHFIENKYPNkPFFIIEHPQIMSPLAKYHRSKPGLT 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 328 ERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNN 407
Cdd:PTZ00417 492 ERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDAEAFQFDAAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNC 571
|
410
....*....|..
gi 1802983340 408 IKEVLLFPAMKP 419
Cdd:PTZ00417 572 IKDVILFPTMRP 583
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
22-421 |
8.82e-135 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 414.36 E-value: 8.82e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 22 RGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSF 101
Cdd:PRK02983 704 LGDLVEVTGTMGTSRNGTLSLLVTSWRLAGKCLRPLPDKWKGLTDPEARVRQRYLDLAVNPEARDLLRARSAVVRAVRET 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 102 LDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTT 181
Cdd:PRK02983 784 LVARGFLEVETPILQQVHGGANARPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEFTL 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 182 CEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpDGPEGQAYDVDFTPPFRRINMVEELEKALGMKL-PETNLfet 260
Cdd:PRK02983 864 LEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVMR--PDGDGVLEPVDISGPWPVVTVHDAVSEALGEEIdPDTPL--- 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 261 EETRKilddICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEIC 340
Cdd:PRK02983 939 AELRK----LCDAAGIPYRTDWDAGAVVLELYEHLVEDRTTFPTFYTDFPTSVSPLTRPHRSDPGLAERWDLVAWGVELG 1014
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 341 NAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTdSNNIKEVLLFPAMKPE 420
Cdd:PRK02983 1015 TAYSELTDPVEQRRRLTEQSLLAAGGDPEAMELDEDFLQALEYAMPPTGGLGMGVDRLVMLLT-GRSIRETLPFPLVKPR 1093
|
.
gi 1802983340 421 D 421
Cdd:PRK02983 1094 Q 1094
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
20-425 |
1.86e-133 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 399.02 E-value: 1.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 20 LRRGDIIGVQGNPGKTKKGELSIIPYEITLLSP--CLHML--PHLH-FG-LKDKETRYRQRYLDLILNDFVRQKFIIRSK 93
Cdd:PTZ00385 159 LRVGDIIGADGVPCRMQRGELSVAASRMLILSPyvCTDQVvcPNLRgFTvLQDNDVKYRYRFTDMMTNPCVIETIKKRHV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 94 IITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 173
Cdd:PTZ00385 239 MLQALRDYFNERNFVEVETPVLHTVASGANAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 174 THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLP 253
Cdd:PTZ00385 319 SHNPEFTSCEFYAAYHTYEDLMPMTEDIFRQLAMRVNGTTVVQIYPENAHGNPVTVDLGKPFRRVSVYDEIQRMSGVEFP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 254 ETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELF 333
Cdd:PTZ00385 399 PPNELNTPKGIAYMSVVMLRYNIPLPPVRTAAKMFEKLIDFFITDRVVEPTFVMDHPLFMSPLAKEQVSRPGLAERFELF 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 334 VMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLL 413
Cdd:PTZ00385 479 VNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLDETFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGII 558
|
410
....*....|..
gi 1802983340 414 FPAMKPEDKKEN 425
Cdd:PTZ00385 559 FPLLRQDIRSHD 570
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
23-420 |
1.65e-132 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 391.35 E-value: 1.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 23 GDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFL 102
Cdd:PRK12445 119 GDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFM 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 103 DELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTC 182
Cdd:PRK12445 199 VARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMM 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 183 EFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEELEKalgmKLPETNLFEtee 262
Cdd:PRK12445 279 ELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTY-------GEHVFDFGKPFEKLTMREAIKK----YRPETDMAD--- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 263 trkiLDDICVAKA------VECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMK 336
Cdd:PRK12445 345 ----LDNFDAAKAlaesigITVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 337 KEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPA 416
Cdd:PRK12445 421 REIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFPA 500
|
....
gi 1802983340 417 MKPE 420
Cdd:PRK12445 501 MRPQ 504
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
66-418 |
3.65e-123 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 360.34 E-value: 3.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 66 DKETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPE 145
Cdd:pfam00152 1 DEETRLKYRYLDL-RRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 146 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPdgpegq 225
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIAKELEGG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 226 aYDVDFTPPFRRINMVEELEKALGMKLPETnlfeteetrkiLDDIcvakavecppPRTTARLLDKLVgefLEVTCINPTF 305
Cdd:pfam00152 154 -TLLDLKKPFPRITYAEAIEKLNGKDVEEL-----------GYGS----------DKPDLRFLLELV---IDKNKFNPLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 306 ICDHPQIMSPLAKWHRSK-EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKaagdDEAMFIDENFCTALEYG 384
Cdd:pfam00152 209 VTDFPAEHHPFTMPKDEDdPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDP----EEAEEKFGFYLDALKYG 284
|
330 340 350
....*....|....*....|....*....|....
gi 1802983340 385 LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMK 418
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 ... |
88-419 |
2.56e-93 |
|
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238358 [Multi-domain] Cd Length: 269 Bit Score: 282.44 E-value: 2.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 88 FIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFR 167
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 168 NEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYhpdgpegQAYDVDFTPPFRRINMVEELEKA 247
Cdd:cd00669 81 NEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVTAVTY-------GFELEDFGLPFPRLTYREALERY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 248 LgmklpetnlfeteetrkilddicvakavecppprttarlldklvgeflevtciNPTFICDHP-QIMSPLAKWHRSKEGL 326
Cdd:cd00669 154 G-----------------------------------------------------QPLFLTDYPaEMHSPLASPHDVNPEI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 327 TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGddeaMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSN 406
Cdd:cd00669 181 ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAG----MEYFEFYLKALEYGLPPHGGLGIGIDRLIMLMTNSP 256
|
330
....*....|...
gi 1802983340 407 NIKEVLLFPAMKP 419
Cdd:cd00669 257 TIREVIAFPKMRR 269
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
101-412 |
1.15e-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: 188.91 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 101 FLDELGFLEIETPMMniIPGG-------AVAKPFITYHNElDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL 173
Cdd:TIGR00462 1 FFAERGVLEVETPLL--SPAPvtdphldAFATEFVGPDGQ-GRPLYLQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 174 THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhitgsykvtyhpdgpegqaydvDFTPPFRRINMVEELEKALGMKLP 253
Cdd:TIGR00462 78 RHNPEFTMLEWYRPGFDYHDLMDEVEALLQELLG----------------------DPFAPAERLSYQEAFLRYAGIDPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 254 ETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKEGLTERFE 331
Cdd:TIGR00462 136 TASLAE-------LQAAAAAHGIRASEEDDRDDLLDLLFSEKVEPHlgFGRPTFLYDYPASQAALARISPDDPRVAERFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 332 LFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEV 411
Cdd:TIGR00462 209 LYIKGLELANGFHELTDAAEQRRRFEADNALRKALGLPRYPLDERFLAALEAGLPECSGVALGVDRLLMLALGADSIDDV 288
|
.
gi 1802983340 412 L 412
Cdd:TIGR00462 289 L 289
|
|
| EpmA |
COG2269 |
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal ... |
91-412 |
3.13e-54 |
|
Elongation factor P--beta-lysine ligase (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441870 [Multi-domain] Cd Length: 309 Bit Score: 183.00 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 91 RSKIITYIRSFLDELGFLEIETPMMNIIPGGAVA-KPFITY---HNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQF 166
Cdd:COG2269 9 RARLLAAIRAFFAERGVLEVETPALSVAPGTDPHlDSFATEfigPDGGGRPLYLHTSPEFAMKRLLAAGSGPIYQIAKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 167 RNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSgmvkhitgsykvtyhpdgpegQAYDVDFTPPFRRINMVEELEK 246
Cdd:COG2269 89 RNGERGRRHNPEFTMLEWYRPGFDYEALMDEVEALLQ---------------------LVLGAAGFAPAERLSYQEAFLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 247 ALGMKLPETNLFEteetrkiLDDICVAKAVECPPPRTTARLLDKLVGEFLEVT--CINPTFICDHPQIMSPLAKWHRSKE 324
Cdd:COG2269 148 YLGIDPLTADLDE-------LAAAAAAAGLRVADDDDRDDLLDLLLSERVEPQlgRDRPTFLYDYPASQAALARISPDDP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 325 GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTD 404
Cdd:COG2269 221 RVAERFELYACGVELANGFHELTDAAEQRRRFEADNAERERLGLPPYPIDERFLAALAAGLPDCSGVALGFDRLLMLALG 300
|
....*...
gi 1802983340 405 SNNIKEVL 412
Cdd:COG2269 301 AERIDDVL 308
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
91-411 |
8.08e-42 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 150.08 E-value: 8.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 91 RSKIITYIRSFLDELGFLEIETPMM--------NIIPggaVAKPFITYHNELDMNLYMRIAPElYH-KMLVVGGIDRVYE 161
Cdd:PRK09350 8 RAKIIAEIRRFFADRGVLEVETPILsqatvtdiHLVP---FETRFVGPGASQGKTLWLMTSPE-YHmKRLLAAGSGPIFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 162 IGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHpdgpegQAY----DVDFTPPfrr 237
Cdd:PRK09350 84 ICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLD-CEPAESLSYQ------QAFlrylGIDPLSA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 238 inMVEELeKALGMKLPETNLFETEETRKILDDICVAKAVEcppprttarllDKLVGEflevtciNPTFICDHPQIMSPLA 317
Cdd:PRK09350 154 --DKTQL-REVAAKLGLSNIADEEEDRDTLLQLLFTFGVE-----------PNIGKE-------KPTFVYHFPASQAALA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 318 KWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDR 397
Cdd:PRK09350 213 KISTEDHRVAERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQPIDENLIAALEAGLPDCSGVALGVDR 292
|
330
....*....|....
gi 1802983340 398 VAMFLTDSNNIKEV 411
Cdd:PRK09350 293 LIMLALGAESISEV 306
|
|
| aspS_nondisc |
TIGR00458 |
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ... |
8-415 |
5.09e-37 |
|
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: 140.34 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 8 KSEEEFIHINNKLRRGDIIGVQGNPGKTKK--GELSIIPYEITLLSPCLHMLPHLhfgLKDK-----ETRYRQRYLDLiL 80
Cdd:TIGR00458 50 KVSKNLFKWAKKLNLESVVAVRGIVKIKEKapGGFEIIPTKIEVINEAKEPLPLD---PTEKvpaelDTRLDYRFLDL-R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 81 NDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIP--GGAVAKPfITYhneLDMNLYMRIAPELYHKMLVVGGIDR 158
Cdd:TIGR00458 126 RPTVQAIFRIRSGVLESVREFLAEEGFIEVHTPKLVASAteGGTELFP-ITY---FEREAFLGQSPQLYKQQLMAAGFER 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 159 VYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKMVsgmVKHITGSYKVTYHPDGPEGQAYDVDFTPpFRR 237
Cdd:TIGR00458 202 VYEIGPIFRAEEHNTHrHLNEATSIDIEMAFEDHHDVMDILEELV---VRVFEDVPERCAHQLETLEFKLEKPEGK-FVR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 238 INMVEELEkalgmklpetnlfeteetrkilddICVAKAVECPPPRTTARLLDKLVGEFLEvtciNPTFICDHPQ------ 311
Cdd:TIGR00458 278 LTYDEAIE------------------------MANAKGVEIGWGEDLSTEAEKALGEEMD----GLYFITDWPTeirpfy 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 312 IMSPLAKWHRSKEglterFELFVMKKEICNAYTELNDpmrqRQLFEEQAKAKAAGDDEAmfidENFCTALEYGLPPTAGW 391
Cdd:TIGR00458 330 TMPDEDNPEISKS-----FDLMYRDLEISSGAQRIHL----HDLLVERIKAKGLNPEGF----KDYLEAFSYGMPPHAGW 396
|
410 420
....*....|....*....|....
gi 1802983340 392 GMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:TIGR00458 397 GLGAERFVMFLLGLKNIREAVLFP 420
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
1-78 |
1.56e-36 |
|
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: 129.52 E-value: 1.56e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802983340 1 MANSRNYkSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDL 78
Cdd:cd04322 32 YVNKDDL-GEEEFEDFKKLLDLGDIIGVTGTPFKTKTGELSIFVKEFTLLSKSLRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
19-415 |
8.49e-35 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 134.16 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 19 KLRRGDIIGVQG----NPgKTKKGeLSIIPYEITLLSPCLHMLPhlhFGLKDK-----ETRYRQRYLDLiLNDFVRQKFI 89
Cdd:PRK05159 64 KLKRESVVSVTGtvkaNP-KAPGG-VEVIPEEIEVLNKAEEPLP---LDISGKvlaelDTRLDNRFLDL-RRPRVRAIFK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 90 IRSKIITYIRSFLDELGFLEIETPmmNIIP----GGAVAKPfITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQ 165
Cdd:PRK05159 138 IRSEVLRAFREFLYENGFTEIFTP--KIVAsgteGGAELFP-IDYFEK---EAYLAQSPQLYKQMMVGAGFERVFEIGPV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 166 FRNEGIDLT-HNPEFTTCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSYKvtyhpdgPEGQAYDVDF---TPPFRRINM 240
Cdd:PRK05159 212 FRAEEHNTSrHLNEYTSIDVEMGFIDdHEDVMDLLENLLRYMYEDVAENCE-------KELELLGIELpvpETPIPRITY 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 241 VEELE--KALGMKLPETNLFETEETRKILDDIcvakavecppprttarlLDKLVGEFLevtcinptFICDHPQIMSPL-A 317
Cdd:PRK05159 285 DEAIEilKSKGNEISWGDDLDTEGERLLGEYV-----------------KEEYGSDFY--------FITDYPSEKRPFyT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 318 KWHRSKEGLTERFELfvMKK--EICNAYTELNDpmrqRQLFEEQAKAKaaGDDEAMFidENFCTALEYGLPPTAGWGMGI 395
Cdd:PRK05159 340 MPDEDDPEISKSFDL--LFRglEITSGGQRIHR----YDMLVESIKEK--GLNPESF--EFYLEAFKYGMPPHGGFGLGL 409
|
410 420
....*....|....*....|
gi 1802983340 396 DRVAMFLTDSNNIKEVLLFP 415
Cdd:PRK05159 410 ERLTMKLLGLENIREAVLFP 429
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
88-415 |
3.52e-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: 109.59 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 88 FIIRSKIITYIRSFLDELGFLEIETPMMN-IIPGGA----VakPFITYHNE---LDMnlymriAPELYHKMLVVGGIDRV 159
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTkSTPEGArdflV--PSRLHPGKfyaLPQ------SPQLFKQLLMVSGFDRY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 160 YEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegqaydVDFTPPFRRIN 239
Cdd:cd00777 73 FQIARCFRDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLG-----------------VELTTPFPRMT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 240 MVEELEKaLGMKL------PetnLFE-TEETRKIlddicvaKAVECP---PPRTTARLLDKlvgeflevtciNPTFIcdh 309
Cdd:cd00777 136 YAEAMER-YGFKFlwivdfP---LFEwDEEEGRL-------VSAHHPftaPKEEDLDLLEK-----------DPEDA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 310 pqimsplakwhrskegLTERFELFVMKKEICNAYTELNDPMRQRQLFE------EQAKAKAAGddeamfidenFCTALEY 383
Cdd:cd00777 191 ----------------RAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEilglseEEAEEKFGF----------LLEAFKY 244
|
330 340 350
....*....|....*....|....*....|..
gi 1802983340 384 GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:cd00777 245 GAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
68-415 |
8.11e-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: 109.58 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 68 ETRYRQRYLDLiLNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMM--NIIPGGAVAKPfITYHNEldmNLYMRIAPE 145
Cdd:cd00776 5 ETLLDNRHLDL-RTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKItsTDTEGGAELFK-VSYFGK---PAYLAQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 146 LYHKMLVvGGIDRVYEIGRQFRNEGIDLT-HNPEFTTCEFYMAYA-DYHDLMEITEKMVSGMVKHITGSYK-----VTYH 218
Cdd:cd00776 80 LYKEMLI-AALERVYEIGPVFRAEKSNTRrHLSEFWMLEAEMAFIeDYNEVMDLIEELIKYIFKRVLERCAkelelVNQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 219 PDGPEGqaydvdFTPPFRRInmveELEKALGMklpetnLFETEETRKILDDICVAKAVEcppprttaRLLDKLVGEflev 298
Cdd:cd00776 159 NRELLK------PLEPFPRI----TYDEAIEL------LREKGVEEEVKWGEDLSTEHE--------RLLGEIVKG---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 299 tciNPTFICDHPQIMSPL-AKWHRSKEGLTERFELFVMKK-EICNAYTELNDPmrqrQLFEEQAKAKaaGDDEAMFidEN 376
Cdd:cd00776 211 ---DPVFVTDYPKEIKPFyMKPDDDNPETVESFDLLMPGVgEIVGGSQRIHDY----DELEERIKEH--GLDPESF--EW 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 1802983340 377 FCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:cd00776 280 YLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP 318
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
18-415 |
6.22e-26 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 110.54 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 18 NKLRRGDIIGVQG----------NPgKTKKGELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLND 82
Cdd:PRK00476 62 ESLRSEYVIQVTGtvrarpegtvNP-NLPTGEIEVLASELEVLNKS-KTLP---FPIDDEedvseELRLKYRYLDL-RRP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 83 FVRQKFIIRSKIITYIRSFLDELGFLEIETPMMniI---PGGA----VakPfityhneldmnlyMRI----------APE 145
Cdd:PRK00476 136 EMQKNLKLRSKVTSAIRNFLDDNGFLEIETPIL--TkstPEGArdylV--P-------------SRVhpgkfyalpqSPQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 146 LYHKMLVVGGIDRVYEIGRQFRNEgiDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdg 221
Cdd:PRK00476 199 LFKQLLMVAGFDRYYQIARCFRDE--DLRADrqPEFTQidIE--MSFVTQEDVMALMEGLIRHVFKEVLG---------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 222 pegqaydVDFTPPFRRINMVEELEK--------ALGMKLPE-TNLFETEE--------------------------TRKI 266
Cdd:PRK00476 265 -------VDLPTPFPRMTYAEAMRRygsdkpdlRFGLELVDvTDLFKDSGfkvfagaandggrvkairvpggaaqlSRKQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 267 LDD---------------ICV---------------------AKAVECPP----------PRTTARLLDKL---VGEFLE 297
Cdd:PRK00476 338 IDEltefakiygakglayIKVnedglkgpiakflseeelaalLERTGAKDgdliffgadkAKVVNDALGALrlkLGKELG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 298 VT---CINPTFICD-----------------HPQIMsPlakwhrsKEGLTERFELFVMKKEICNAY------TEL----- 346
Cdd:PRK00476 418 LIdedKFAFLWVVDfpmfeydeeegrwvaahHPFTM-P-------KDEDLDELETTDPGKARAYAYdlvlngYELgggsi 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802983340 347 --NDPMRQRQLF------EEQAKAKAAGddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PRK00476 490 riHRPEIQEKVFeilgisEEEAEEKFGF-----LLD-----ALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFP 556
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
18-415 |
9.02e-25 |
|
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: 107.01 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 18 NKLRRGDIIGVQG----------NPgKTKKGELSIIPYEITLLSPClHMLPhlhFGLKDK-----ETRYRQRYLDLiLND 82
Cdd:COG0173 63 EKLRSEYVIAVTGkvrarpegtvNP-KLPTGEIEVLASELEILNKA-KTPP---FQIDDDtdvseELRLKYRYLDL-RRP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 83 FVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNI-IPGGA----VakPFityhneldmnlymRI----------APELY 147
Cdd:COG0173 137 EMQKNLILRHKVTKAIRNYLDENGFLEIETPILTKsTPEGArdylV--PS-------------RVhpgkfyalpqSPQLF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 148 HKMLVVGGIDRVYEIGRQFRNEgiDLTHN--PEFTT--CEfyMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpe 223
Cdd:COG0173 202 KQLLMVSGFDRYFQIARCFRDE--DLRADrqPEFTQldIE--MSFVDQEDVFELMEGLIRHLFKEVLG------------ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 224 gqaydVDFTPPFRRINMVEELEK--------ALGMKLPE-TNLFETEE-------------------------TRKILDD 269
Cdd:COG0173 266 -----VELPTPFPRMTYAEAMERygsdkpdlRFGLELVDvTDIFKDSGfkvfagaaenggrvkainvpggaslSRKQIDE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 270 IC------------------------VAKAVecpPPRTTARLLDKL---VGEFLevtcinpTFICDHPQIMSP------- 315
Cdd:COG0173 341 LTefakqygakglayikvnedglkspIAKFL---SEEELAAILERLgakPGDLI-------FFVADKPKVVNKalgalrl 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 316 -LAKwhrsKEGLTER-------------FEL-------------FVMKKE-------------ICNAY------TEL--- 346
Cdd:COG0173 411 kLGK----ELGLIDEdefaflwvvdfplFEYdeeegrwvamhhpFTMPKDedldlletdpgkvRAKAYdlvlngYELggg 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802983340 347 ----NDPMRQRQLF------EEQAKAKAAGddeamFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:COG0173 487 siriHDPELQEKVFellgisEEEAEEKFGF-----LLE-----AFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFP 555
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
19-415 |
1.65e-24 |
|
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: 104.75 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 19 KLRRGDIIGVQG----NPGKtkKGELSIIPYEITLLSPCLHMLPhlhFGLKDK--ETRYRQRYLDLILNDFvRQKFIIRS 92
Cdd:COG0017 61 KLTTESSVEVTGtvveSPRA--PQGVELQAEEIEVLGEADEPYP---LQPKRHslEFLLDNRHLRLRTNRF-GAIFRIRS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 93 KIITYIRSFLDELGFLEIETPmmnIIPGGAV---AKPF-ITYHNEldmNLYMRIAPELYHKMLVvGGIDRVYEIGRQFRN 168
Cdd:COG0017 135 ELARAIREFFQERGFVEVHTP---IITASATeggGELFpVDYFGK---EAYLTQSGQLYKEALA-MALEKVYTFGPTFRA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 169 EGIDLT-HNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHItgsykVTYHPDgpEGQAYDVDFT-------PPFRRINM 240
Cdd:COG0017 208 EKSNTRrHLAEFWMIEPEMAFADLEDVMDLAEEMLKYIIKYV-----LENCPE--ELEFLGRDVErlekvpeSPFPRITY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 241 ---VEELEKAlGMKLPETNLFETEETRKIlddicvakavecppprtTARLLDKLVgeflevtcinptFICDHPQIMSPla 317
Cdd:COG0017 281 teaIEILKKS-GEKVEWGDDLGTEHERYL-----------------GEEFFKKPV------------FVTDYPKEIKA-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 318 kwhrskeglterfelFVMK-----KEICNA-------YTELndpmrQRqlfEEQ-----AKAKAAGDDEAMF---IDenf 377
Cdd:COG0017 329 ---------------FYMKpnpddPKTVAAfdllapgIGEIig-gsQR---EHRydvlvERIKEKGLDPEDYewyLD--- 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 1802983340 378 ctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:COG0017 387 --LRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFP 422
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
18-246 |
1.59e-22 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 100.25 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 18 NKLRRGDIIGVQG----------NPgKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKD------KETRYRQRYLDLILN 81
Cdd:PLN02903 119 NRLRNEYVVAVEGtvrsrpqespNK-KMKTGSVEVVAESVDILNVVTKSLPFLVTTADEqkdsikEEVRLRYRVLDLRRP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 82 DFVRQkFIIRSKIITYIRSFL-DELGFLEIETPMMN---------------IIPGGAVAKPfityhneldmnlymrIAPE 145
Cdd:PLN02903 198 QMNAN-LRLRHRVVKLIRRYLeDVHGFVEIETPILSrstpegardylvpsrVQPGTFYALP---------------QSPQ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 146 LYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGsykvtyhpdgpegq 225
Cdd:PLN02903 262 LFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRQVFKEIKG-------------- 327
|
250 260
....*....|....*....|.
gi 1802983340 226 aydVDFTPPFRRINMVEELEK 246
Cdd:PLN02903 328 ---VQLPNPFPRLTYAEAMSK 345
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
90-203 |
9.43e-18 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 81.40 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 90 IRSKIITYIRSFLDELGFLEIETPMMNIIPG----GAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGI----DRVYE 161
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLlekaGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1802983340 162 IGRQFRNEGI--DLTHNPEFTTCEFYMAYAD------YHDLMEITEKMVS 203
Cdd:cd00768 81 IGPAFRNEGGrrGLRRVREFTQLEGEVFGEDgeeaseFEELIELTEELLR 130
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
31-415 |
6.43e-17 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 83.11 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 31 NPgKTKKGELSIIPYEITLLSPCLhMLPhlhFGLKDK----------------ETRYRQRYLDlILNDFVRQKFIIRSKI 94
Cdd:PRK12820 89 NP-HIETGDIEVFVRELSILAASE-ALP---FAISDKamtagagsagadavneDLRLQYRYLD-IRRPAMQDHLAKRHRI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 95 ITYIRSFLDELGFLEIETPMMNI-IPGGAvaKPFITYHNELDMNLY-MRIAPELYHKMLVVGGIDRVYEIGRQFRNEGID 172
Cdd:PRK12820 163 IKCARDFLDSRGFLEIETPILTKsTPEGA--RDYLVPSRIHPKEFYaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 173 LTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKhITGSYKVTYHPDGPEGQAYD---------------VDFTPPFRR 237
Cdd:PRK12820 241 PNRQPEFTQLDIEASFIDEEFIFELIEELTARMFA-IGGIALPRPFPRMPYAEAMDttgsdrpdlrfdlkfADATDIFEN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 238 ------------------INMVEELEK-------------------ALGM--------KLpETNL---FETEETRKIL-- 267
Cdd:PRK12820 320 trygifkqilqrggrikgINIKGQSEKlsknvlqneyakeiapsfgAKGMtwmraeagGL-DSNIvqfFSADEKEALKrr 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 268 ------DDICVAKAVECPPPRTTARLLDKLVGEFLEVT---CINPTFICDHPQIMS-----------PLAKWHRSK---- 323
Cdd:PRK12820 399 fhaedgDVIIMIADASCAIVLSALGQLRLHLADRLGLIpegVFHPLWITDFPLFEAtddggvtsshhPFTAPDREDfdpg 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 324 --EGL----TERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFidenFCTALEYGLPPTAGWGMGIDR 397
Cdd:PRK12820 479 diEELldlrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGF----FLRAFDFAAPPHGGIALGLDR 554
|
490
....*....|....*...
gi 1802983340 398 VAMFLTDSNNIKEVLLFP 415
Cdd:PRK12820 555 VVSMILQTPSIREVIAFP 572
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
23-415 |
2.93e-15 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 77.73 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 23 GDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPhlhFGLKDK-------------ETRYRQRYLDLiLNDFVRQKFI 89
Cdd:PTZ00401 139 ATVCKVEQPITSTSHSDIELKVKKIHTVTESLRTLP---FTLEDAsrkesdegakvnfDTRLNSRWMDL-RTPASGAIFR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 90 IRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPF-ITYHNEldmNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRN 168
Cdd:PTZ00401 215 LQSRVCQYFRQFLIDSDFCEIHSPKIINAPSEGGANVFkLEYFNR---FAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 169 EGIDL-THNPEFTTCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSykvtyhpdgpEGQAYDVDFTPPFRRI--NMVEEL 244
Cdd:PTZ00401 292 ENSNThRHLTEFVGLDVEMRINEhYYEVLDLAESLFNYIFERLATH----------TKELKAVCQQYPFEPLvwKLTPER 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 245 EKALGMKLPETNLFETEETR-------------------KILDDICVAKAVECPPPRTT-ARLLDKLVGEFLEVTcinpT 304
Cdd:PTZ00401 362 MKELGVGVISEGVEPTDKYQarvhnmdsrmlrinymhciELLNTVLEEKMAPTDDINTTnEKLLGKLVKERYGTD----F 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 305 FICDH-PQIMSPLAKWH-RSKEGLTERFELFVMKKEICNAYTELNDPmrqrQLFeeQAKAKAAGDDEAMFIDenFCTALE 382
Cdd:PTZ00401 438 FISDRfPSSARPFYTMEcKDDERFTNSYDMFIRGEEISSGAQRIHDP----DLL--LARAKMLNVDLTPIKE--YVDSFR 509
|
410 420 430
....*....|....*....|....*....|...
gi 1802983340 383 YGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PTZ00401 510 LGAWPHGGFGVGLERVVMLYLGLSNVRLASLFP 542
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
24-415 |
3.23e-15 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 77.44 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 24 DIIGVQGNPGKTKKG---ELSIIPYEITLLSPCLHMLPhlhFGLKD----------------------KETRYRQRYLDL 78
Cdd:PLN02850 140 DVEGVVSVPKKPVKGttqQVEIQVRKIYCVSKALATLP---FNVEDaarseseiekalqtgeqlvrvgQDTRLNNRVLDL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 79 IL--NDFVrqkFIIRSKIITYIRSFLDELGFLEIETPmmNIIPG-----GAVAKpfityhneLDmnlYMRI------APE 145
Cdd:PLN02850 217 RTpaNQAI---FRIQSQVCNLFREFLLSKGFVEIHTP--KLIAGaseggSAVFR--------LD---YKGQpaclaqSPQ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 146 LYHKMLVVGGIDRVYEIGRQFRNEGiDLTHNP--EFTTCEFYMAYAD-YHDLMEITEKMVSGMVKHITGSYK------VT 216
Cdd:PLN02850 281 LHKQMAICGDFRRVFEIGPVFRAED-SFTHRHlcEFTGLDLEMEIKEhYSEVLDVVDELFVAIFDGLNERCKkeleaiRE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 217 YHPDGPegqaydVDFTPPFRRINMVE--ELEKALGMKLPETNLFETEETRKiLDDICVAKAvecpppRTTARLLDKL--- 291
Cdd:PLN02850 360 QYPFEP------LKYLPKTLRLTFAEgiQMLKEAGVEVDPLGDLNTESERK-LGQLVKEKY------GTDFYILHRYpla 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 292 VGEFLEVTCI-NPTFicdhpqimsplakwhrskeglTERFELFVMKKEICNAYTELNDPmrqrQLFEEQAKAKAAG-DDE 369
Cdd:PLN02850 427 VRPFYTMPCPdDPKY---------------------SNSFDVFIRGEEIISGAQRVHDP----ELLEKRAEECGIDvKTI 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1802983340 370 AMFIDenfctALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PLN02850 482 STYID-----SFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP 522
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
90-415 |
1.84e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.20 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 90 IRSKIITYIRSFLDELGFLEIETPMMN-----IIPGGA---VAKPFITYHNEldmnlYMRIAPEL-YHKMLVVGGIDRVY 160
Cdd:PRK06462 32 VQSSILRYTREFLDGRGFVEVLPPIISpstdpLMGLGSdlpVKQISIDFYGV-----EYYLADSMiLHKQLALRMLGKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 161 EIGRQFRNEGID---LTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHItgsykVTYHPDGPEGQAYDV-DFTPPFR 236
Cdd:PRK06462 107 YLSPNFRLEPVDkdtGRHLYEFTQLDIEIEGADLDEVMDLIEDLIKYLVKEL-----LEEHEDELEFFGRDLpHLKRPFK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 237 RINMvEELEKALGMKLPETNLFEteetrKILDDicvakavecppprttarlldklvGE-FLEVTCINPTFICDHPQIMSP 315
Cdd:PRK06462 182 RITH-KEAVEILNEEGCRGIDLE-----ELGSE-----------------------GEkSLSEHFEEPFWIIDIPKGSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 316 LakWHRSKEG-----------LTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAK-----AKAagddeamfidenfct 379
Cdd:PRK06462 233 F--YDREDPErpgvlrnydllLPEGYGEAVSGGEREYEYEEIVERIREHGVDPEKYKwylemAKE--------------- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 1802983340 380 aleyGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PRK06462 296 ----GPLPSAGFGIGVERLTRYICGLRHIREVQPFP 327
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
6-52 |
3.00e-05 |
|
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: 42.17 E-value: 3.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1802983340 6 NYKSEEEFIHINNKLRRGDIIGVQGNPGKT-----KKGELSIIPYEITLLSP 52
Cdd:cd04100 34 NKEELGEFFEEAEKLRTESVVGVTGTVVKRpegnlATGEIELQAEELEVLSK 85
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
10-50 |
1.04e-04 |
|
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: 40.30 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1802983340 10 EEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLL 50
Cdd:pfam01336 35 KEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
383-415 |
1.29e-03 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 40.86 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|...
gi 1802983340 383 YGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PRK03932 410 YGSVPHSGFGLGFERLVAYITGLDNIRDVIPFP 442
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
98-184 |
1.77e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 40.59 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802983340 98 IRSFLDELGFLEIETPMMniIPGGAVAKPFITYHNEL-------DMNLYMR--IAPELYHKMLVVGGI--D--RVYEIGR 164
Cdd:PRK09537 213 ITKFFVDRGFLEIKSPIL--IPAEYIERMGIDNDTELskqifrvDKNFCLRpmLAPGLYNYLRKLDRIlpDpiKIFEIGP 290
|
90 100
....*....|....*....|
gi 1802983340 165 QFRNEGIDLTHNPEFTTCEF 184
Cdd:PRK09537 291 CYRKESDGKEHLEEFTMVNF 310
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
382-415 |
4.60e-03 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 39.24 E-value: 4.60e-03
10 20 30
....*....|....*....|....*....|....
gi 1802983340 382 EYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFP 415
Cdd:PTZ00425 545 KFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFP 578
|
|
| |
