|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
4-592 |
0e+00 |
|
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: 1192.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAREE 83
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDSAEAFEKAEKLRSEYVIAVTGKVRARPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 84 ATVNPNLKTGRIEIQAESVEVLSAAKTPPFAISDQAaEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGF 163
Cdd:COG0173 83 GTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDT-DVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 164 LDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 243
Cdd:COG0173 162 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 244 FMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFKVFASAVTSGGA 323
Cdd:COG0173 242 FVDQEDVFELMEGLIRHLFKEVLGVELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAENGGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 324 VKAINVKGAAaNYSRKDIDALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDAADGDLLLFVADKLEV 403
Cdd:COG0173 322 VKAINVPGGA-SLSRKQIDELTEFAKQYGAKGLAYIKVNEDGLKSPIAKFLSEEELAAILERLGAKPGDLIFFVADKPKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 404 ANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEYDAEEGRYYAAHHPFTMPVREDLKLIETNPQDMKAQAYDLVLNG 483
Cdd:COG0173 401 VNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAYDLVLNG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 484 YELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKTASA 563
Cdd:COG0173 481 YELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAFPKTQSA 560
|
570 580
....*....|....*....|....*....
gi 1140945906 564 SCLMTEAPSEVDNAQLDELHLEIKHKIRQ 592
Cdd:COG0173 561 QDLMTGAPSEVDEKQLKELHIRLRPPEKK 589
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-589 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1167.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 1 MFGRTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDvsKAALETAESIRSEYVLDITGKVVA 80
Cdd:PRK00476 1 HMMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD--AEAFEVAESLRSEYVIQVTGTVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 81 REEATVNPNLKTGRIEIQAESVEVLSAAKTPPFAISDQAaEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDD 160
Cdd:PRK00476 79 RPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEE-DVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 161 NGFLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDI 240
Cdd:PRK00476 158 NGFLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 241 EMSFMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFKVFASAVTS 320
Cdd:PRK00476 238 EMSFVTQEDVMALMEGLIRHVFKEVLGVDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAAND 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 321 GGAVKAINVKGAAANYSRKDIDALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDAADGDLLLFVADK 400
Cdd:PRK00476 318 GGRVKAIRVPGGAAQLSRKQIDELTEFAKIYGAKGLAYIKVNEDGLKGPIAKFLSEEELAALLERTGAKDGDLIFFGADK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 401 LEVANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEYDAEEGRYYAAHHPFTMPVREDLKLIET-NPQDMKAQAYDL 479
Cdd:PRK00476 398 AKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLDELETtDPGKARAYAYDL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 480 VLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPK 559
Cdd:PRK00476 478 VLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIAFPK 557
|
570 580 590
....*....|....*....|....*....|
gi 1140945906 560 TASASCLMTEAPSEVDNAQLDELHLEIKHK 589
Cdd:PRK00476 558 TQSAQDLLTGAPSPVDEKQLRELGIRLRKK 587
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
3-591 |
0e+00 |
|
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). 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_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 211576 [Multi-domain] Cd Length: 583 Bit Score: 944.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 3 GRTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDvsKAALETAESIRSEYVLDITGKVVARE 82
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD--ADALKLAKGLRNEDVVQVKGKVSARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 83 EATVNPNLKTGRIEIQAESVEVLSAAKTPPFAISDQAAEvsEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNG 162
Cdd:TIGR00459 79 EGNINRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAE--EEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 163 FLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEM 242
Cdd:TIGR00459 157 FLEIETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 243 SFMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFKVFASAVTSGG 322
Cdd:TIGR00459 237 SFMTQEDVMELIEKLVSHVFLEVKGIDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLINDGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 323 AVKAINVKGAAANYSRKDIDALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDAADGDLLLFVADKLE 402
Cdd:TIGR00459 317 RVKAIRVPGGWAELSRKSIKELRKFAKEYGAKGLAYLKVNEDGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAGSKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 403 VANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEYDaEEGRYYAAHHPFTMPVREDLKLIETNPQDMKAQAYDLVLN 482
Cdd:TIGR00459 397 IVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKD-KEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLVLN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 483 GYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKTAS 562
Cdd:TIGR00459 476 GVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKTTA 555
|
570 580
....*....|....*....|....*....
gi 1140945906 563 ASCLMTEAPSEVDNAQLDELHleIKHKIR 591
Cdd:TIGR00459 556 AACLMTEAPSFIDEKQLEELS--IKYVVK 582
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
4-587 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 754.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAREE 83
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 84 ATVNPNLKTGRIEIQAESVEVLSAAKTP-PFAIS---DQAAEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFL- 158
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVVTKSlPFLVTtadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 159 DDNGFLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQI 238
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 239 DIEMSFMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFKVFASAV 318
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNPFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 319 TSGGAVKAINVKGAAANYS---RKDIDALGEfAANYGAKGLAWLKTEADG-LKGPIA--KFFAGEKQEALVQALDAADGD 392
Cdd:PLN02903 379 ESGGVVKAICVPDGKKISNntaLKKGDIYNE-AIKSGAKGLAFLKVLDDGeLEGIKAlvESLSPEQAEQLLAACGAGPGD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 393 LLLFVADKLEVANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEYDAEEGRYYAAHHPFTMPVREDLKLIETnpqdM 472
Cdd:PLN02903 458 LILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEWNEDEQRLEALHHPFTAPNPEDMGDLSS----A 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 473 KAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLR 552
Cdd:PLN02903 534 RALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIR 613
|
570 580 590
....*....|....*....|....*....|....*
gi 1140945906 553 DTIAFPKTASASCLMTEAPSEVDNAQLDELHLEIK 587
Cdd:PLN02903 614 DVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIAST 648
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
2-584 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 637.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 2 FGRTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAAL-ETAESIRSEYVLDITGKVVA 80
Cdd:PRK12820 3 ENDRSFCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAAPADVyELAASLRAEFCVALQGEVQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 81 REEATVNPNLKTGRIEIQAESVEVLSAAKTPPFAISDQAA----------EVSEDIRLKHRYLDLRRPEMFNSLKMRHNV 150
Cdd:PRK12820 83 RLEETENPHIETGDIEVFVRELSILAASEALPFAISDKAMtagagsagadAVNEDLRLQYRYLDIRRPAMQDHLAKRHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 151 TKAVRRFLDDNGFLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRAD 230
Cdd:PRK12820 163 IKCARDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 231 RQPEFTQIDIEMSFMSQEDIMKLSEEMMAHvMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSD 310
Cdd:PRK12820 243 RQPEFTQLDIEASFIDEEFIFELIEELTAR-MFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 311 FKVFASAVTSGGAVKAINVKGAAANYSRKDI--DALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDA 388
Cdd:PRK12820 322 YGIFKQILQRGGRIKGINIKGQSEKLSKNVLqnEYAKEIAPSFGAKGMTWMRAEAGGLDSNIVQFFSADEKEALKRRFHA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 389 ADGDLLLFVAD-KLEVANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEyDAEEGRYYAAHHPFTMPVREDLKLIET 467
Cdd:PRK12820 402 EDGDVIIMIADaSCAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFE-ATDDGGVTSSHHPFTAPDREDFDPGDI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 468 NP-QDMKAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLS 546
Cdd:PRK12820 481 EElLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSMIL 560
|
570 580 590
....*....|....*....|....*....|....*...
gi 1140945906 547 GRTNLRDTIAFPKTASASCLMTEAPSEVDNAQLDELHL 584
Cdd:PRK12820 561 QTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
144-562 |
2.98e-177 |
|
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: 502.11 E-value: 2.98e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 144 LKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFR 223
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 224 DEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGsdkpdtrfgmlltdvs 303
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELTTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 304 eavkdsdfkvfasavtsggavkainvkgaaanysrkdidalgefaanygakglawlkteadglkgpiakffagekqealv 383
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 384 qaldaadgdlllfvadklevandalgalrlklgkelnlideslFNFLWVVDWPLLEYDAEEGRYYAAHHPFTMPVREDLK 463
Cdd:cd00777 145 -------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEEDLD 181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 464 LIETNPQDMKAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVM 543
Cdd:cd00777 182 LLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGLDRLVM 261
|
410
....*....|....*....
gi 1140945906 544 LLSGRTNLRDTIAFPKTAS 562
Cdd:cd00777 262 LLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
123-560 |
5.41e-148 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 429.29 E-value: 5.41e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 123 SEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLTKS-TPEGARDYLVPSRVHeGEFYALPQSPQ 201
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSaTPEGARDFLVPSRAL-GKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 202 IFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGI----------EIS 271
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtllDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 272 LPLPRMSYEDAMNR----------YGSDKPDTRFGMLLTdvseavkdsdfkvfasavtsggavkainvkgaaanysrkdi 341
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV----------------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 342 dalgefaanygakglawlkteadglkgpiakffagekqealvqaldaadgdlllfvadklevandalgalrlklgkelnl 421
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 422 IDESLFNFLWVVDWPlleydaeegryyAAHHPFTMPVREDLKlietnpqdMKAQAYDLVLNGYELGGGSIRIFEKDVQEK 501
Cdd:pfam00152 199 IDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP--------ALAEAFDLVLNGVEIGGGSIRIHDPELQEE 258
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1140945906 502 MFGLLGFSEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:pfam00152 259 RFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKT 317
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
4-558 |
1.38e-88 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 280.92 E-value: 1.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAree 83
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVDEELFETIKKLKRESVVSVTGTVKA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 84 atvNPNLKTGrIEIQAESVEVLSAAKTP-PFAISDqaaEVSEDI--RLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDD 160
Cdd:PRK05159 80 ---NPKAPGG-VEVIPEEIEVLNKAEEPlPLDISG---KVLAELdtRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 161 NGFLDIETPVLTKSTPEGARDyLVPSRVHEGEFYaLPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQID 239
Cdd:PRK05159 153 NGFTEIFTPKIVASGTEGGAE-LFPIDYFEKEAY-LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSID 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 240 IEMSFM-SQEDIMKLSEEMMAHVMR----------ETHGIEISLP---LPRMSYEDAMNrygsdkpdtrfgmLLTDVSEA 305
Cdd:PRK05159 231 VEMGFIdDHEDVMDLLENLLRYMYEdvaencekelELLGIELPVPetpIPRITYDEAIE-------------ILKSKGNE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 306 VKDSDfkvfasavtsggavkainvkgaaanysrkDIDAlgefaanygakglawlkteadglkgpiakffAGEKqealvqa 385
Cdd:PRK05159 298 ISWGD-----------------------------DLDT-------------------------------EGER------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 386 ldaadgdlllfvadklevandalgalrlKLGKELNLIDESLFNFlwVVDWPlleydaeegryyAAHHPF-TMPVREDLKL 464
Cdd:PRK05159 311 ----------------------------LLGEYVKEEYGSDFYF--ITDYP------------SEKRPFyTMPDEDDPEI 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 465 IEtnpqdmkaqAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSeeeaKEQFGFLLEAFEYGAPPHGGIALGLDRLVML 544
Cdd:PRK05159 349 SK---------SFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLN----PESFEFYLEAFKYGMPPHGGFGLGLERLTMK 415
|
570
....*....|....
gi 1140945906 545 LSGRTNLRDTIAFP 558
Cdd:PRK05159 416 LLGLENIREAVLFP 429
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
144-560 |
4.49e-87 |
|
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: 271.27 E-value: 4.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 144 LKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTP-EGARDYLVPSRvHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCF 222
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 223 RDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRE----------THGIEISLPLPRMSYEDAMNRYGsdkpd 292
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREvlgvtavtygFELEDFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 293 trfgmlltdvseavkdsdfkvfasavtsggavkainvkgaaanysrkdidalgefaanygakglawlkteadglkgpiak 372
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 373 ffagekqealvqaldaadgdlllfvadklevandalgalrlklgkelnlideslfNFLWVVDWPLLeydaeegryyaAHH 452
Cdd:cd00669 155 -------------------------------------------------------QPLFLTDYPAE-----------MHS 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 453 PFTMPVREDLKLietnpqdmkAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFEYGAPPHG 532
Cdd:cd00669 169 PLASPHDVNPEI---------ADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGLPPHG 239
|
410 420
....*....|....*....|....*...
gi 1140945906 533 GIALGLDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:cd00669 240 GLGIGIDRLIMLMTNSPTIREVIAFPKM 267
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-560 |
7.28e-77 |
|
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: 250.35 E-value: 7.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDvSKAALETAESIRSEYVLDITGKVVAREE 83
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKD-KLENFEEAKKLTTESSVEVTGTVVESPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 84 AtvnpnlKTGrIEIQAESVEVLSAAKTP-PFAISdqaaEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNG 162
Cdd:COG0017 80 A------PQG-VELQAEEIEVLGEADEPyPLQPK----RHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 163 FLDIETPVLTKSTPEGAR-----DYlvpsrvHEGEFYaLPQSPQIFKQlLMVSGFDRYYQIARCFRDEDLRADRQ-PEFT 236
Cdd:COG0017 149 FVEVHTPIITASATEGGGelfpvDY------FGKEAY-LTQSGQLYKE-ALAMALEKVYTFGPTFRAEKSNTRRHlAEFW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 237 QIDIEMSFMSQEDIMKLSEEMMAHVMR----------ETHGIEISL-------PLPRMSYEDAMNRYGSDKPDTRFGMll 299
Cdd:COG0017 221 MIEPEMAFADLEDVMDLAEEMLKYIIKyvlencpeelEFLGRDVERlekvpesPFPRITYTEAIEILKKSGEKVEWGD-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 300 tdvseavkdsDFkvfasavtsggavkainvkgaaanysrkdidalgefaanyGAKGLAWLkTEadglkgpiaKFFAGekq 379
Cdd:COG0017 299 ----------DL----------------------------------------GTEHERYL-GE---------EFFKK--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 380 ealvqaldaadgdlllfvadklevandalgalrlklgkelnlideslfnFLWVVDWPlleydaEEGRyyaahhPF-TMPV 458
Cdd:COG0017 316 -------------------------------------------------PVFVTDYP------KEIK------AFyMKPN 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 459 REDLKLIEtnpqdmkaqAYDLVLNGY-ELGGGSIRIFEKDVQEKMFGLLGFSEEEakeqFGFLLEAFEYGAPPHGGIALG 537
Cdd:COG0017 335 PDDPKTVA---------AFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPED----YEWYLDLRRYGSVPHAGFGLG 401
|
570 580
....*....|....*....|...
gi 1140945906 538 LDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:COG0017 402 LERLVMWLTGLENIREVIPFPRD 424
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
4-140 |
8.51e-77 |
|
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: 239.73 E-value: 8.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDvSKAALETAESIRSEYVLDITGKVVAREE 83
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPE-EAPEFELAEKLRNESVIQVTGKVRARPE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1140945906 84 ATVNPNLKTGRIEIQAESVEVLSAAKTPPFAISDQaAEVSEDIRLKHRYLDLRRPEM 140
Cdd:cd04317 80 GTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDD-VNVSEELRLKYRYLDLRRPKM 135
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
2-558 |
1.76e-39 |
|
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: 150.96 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 2 FGRTYYCGEITEK--------AIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPD-VSKAALETAESirseyvL 72
Cdd:COG1190 33 FPRTHTAAEIREKydeleaeeETGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDeLGEEAYELFKL------L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 73 DI------TGKVVAreeaTvnpnlKTGRIEIQAESVEVLSAAKTPP----FAISDQaaevseDIRLKHRYLDL-RRPEMF 141
Cdd:COG1190 107 DLgdivgvEGTVFR----T-----KTGELSVKVEELTLLSKSLRPLpekfHGLTDP------ETRYRQRYVDLiVNPEVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 142 NSLKMRHNVTKAVRRFLDDNGFLDIETPVLTkSTPEGA--RdylvPSRVH----EGEFYaLPQSPQIF-KQLLmVSGFDR 214
Cdd:COG1190 172 ETFRKRSKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaaR----PFITHhnalDMDLY-LRIAPELYlKRLI-VGGFER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 215 YYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHG----------IEISLPLPRMSYEDAMN 284
Cdd:COG1190 245 VFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGttkvtyqgqeIDLSPPWRRITMVEAIK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 285 RYGSDKPDTrfgmlLTDVSEAVKdsdfkvfasavtsggAVKAINVkgaaanysrkdidalgEFAANYGAKGLawlktead 364
Cdd:COG1190 325 EATGIDVTP-----LTDDEELRA---------------LAKELGI----------------EVDPGWGRGKL-------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 365 glkgpIAKFFagekqEALVQaldaadgdlllfvadklevandalgalrlklgkelnlidESLFNFLWVVDWPlleydaee 444
Cdd:COG1190 361 -----IDELF-----EELVE---------------------------------------PKLIQPTFVTDYP-------- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 445 gryyAAHHPFTMPVREDLKLIEtnpqdmkaqAYDLVLNGYELGGG----------SIRiFEKDVQEKMFGllgfsEEEAK 514
Cdd:COG1190 384 ----VEVSPLAKRHRDDPGLTE---------RFELFIAGREIANAfselndpidqRER-FEEQLELKAAG-----DDEAM 444
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1140945906 515 ---EQFgflLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFP 558
Cdd:COG1190 445 pmdEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
121-560 |
3.77e-38 |
|
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: 143.48 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 121 EVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGardylvPSRVHEGEFYA----L 196
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 197 PQSPQIFKQlLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQIDIEMSFM-SQEDIMKLSEEMMAHV---MRETHGIEIS 271
Cdd:cd00776 75 AQSPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIeDYNEVMDLIEELIKYIfkrVLERCAKELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 272 L-------------PLPRMSYEDAmnrygsdkpdtrfgmlltdvseavkdsdfkvfasavtsggavkainVKGAAANYSR 338
Cdd:cd00776 154 LvnqlnrellkplePFPRITYDEA----------------------------------------------IELLREKGVE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 339 KDIDALGEFAAnygakglawlkteadglkgpiakffAGEKqealvqaldaadgdlllfvadklevandalgalrlKLGKE 418
Cdd:cd00776 188 EEVKWGEDLST-------------------------EHER-----------------------------------LLGEI 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 419 lnlIDESLFnflWVVDWPLleydaeEGRyyaahhPFTMPVREDlklietNPQdmKAQAYDLVLNGY-ELGGGSIRIFEKD 497
Cdd:cd00776 208 ---VKGDPV---FVTDYPK------EIK------PFYMKPDDD------NPE--TVESFDLLMPGVgEIVGGSQRIHDYD 261
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140945906 498 VQEKMFGLLGFSEEEakeqFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:cd00776 262 ELEERIKEHGLDPES----FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRD 320
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
9-559 |
2.72e-37 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 145.23 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 9 GEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVF---NPDVSKAALETAESIRSEYVLDITGKVVAREEAT 85
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQCVVfvsEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 86 VNpnlKTGRIEIQAESVEVLSAAKTP-PFAISD----------------QAAEVSEDIRLKHRYLDLRRPEMFNSLKMRH 148
Cdd:PLN02850 153 KG---TTQQVEIQVRKIYCVSKALATlPFNVEDaarseseiekalqtgeQLVRVGQDTRLNNRVLDLRTPANQAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 149 NVTKAVRRFLDDNGFLDIETPVLTKSTPEGAR-----DYLvpsrvheGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFR 223
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDYK-------GQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 224 DEDLRADRQ-PEFTQIDIEMSFMSQED-IMKLSEEMMAHVMrethgieislplprmsyedamnrygsDKPDTRFGMLLtd 301
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLEMEIKEHYSeVLDVVDELFVAIF--------------------------DGLNERCKKEL-- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 302 vsEAVKdsdfkvfasavtsggavkainvkgaaANYSRKDIDALGEFAANYGAKGLAWLKTeadglkgpiakffAGEKQEA 381
Cdd:PLN02850 355 --EAIR--------------------------EQYPFEPLKYLPKTLRLTFAEGIQMLKE-------------AGVEVDP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 382 LvqaldaadGDLllfvadklevandaLGALRLKLGKelnLIDESLFNFLWVVDwplleydaeegRYYAAHHPF-TMPVRE 460
Cdd:PLN02850 394 L--------GDL--------------NTESERKLGQ---LVKEKYGTDFYILH-----------RYPLAVRPFyTMPCPD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 461 DLKLieTNpqdmkaqAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEqfgfLLEAFEYGAPPHGGIALGLDR 540
Cdd:PLN02850 438 DPKY--SN-------SFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST----YIDSFRYGAPPHGGFGVGLER 504
|
570
....*....|....*....
gi 1140945906 541 LVMLLSGRTNLRDTIAFPK 559
Cdd:PLN02850 505 VVMLFCGLNNIRKTSLFPR 523
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
11-560 |
1.91e-36 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 141.40 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 11 ITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAREEAtvnpnl 90
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFKQLQVVKDNGEEYFEEIKKLTTGSSVIVTGTVVESPRA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 91 kTGRIEIQAESVEVLSAAkTPPFAIsdQAAEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPV 170
Cdd:PRK03932 84 -GQGYELQATKIEVIGED-PEDYPI--QKKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 171 LTKSTPEGArdylvpsrvheGEFYALPQSPQIFKQL-------LMVSG----------FDRYYQIARCFRDEDLRADRQ- 232
Cdd:PRK03932 160 ITASDCEGA-----------GELFRVTTLDLDFSKDffgkeayLTVSGqlyaeayamaLGKVYTFGPTFRAENSNTRRHl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 233 PEFTQIDIEMSFMSQEDIMKLSEEMMAHVMREThgieislpLPRMSYE-DAMNRygsdkpdtRFGMLLTDVSEAVKDSDF 311
Cdd:PRK03932 229 AEFWMIEPEMAFADLEDNMDLAEEMLKYVVKYV--------LENCPDDlEFLNR--------RVDKGDIERLENFIESPF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 312 KVfasavtsggavkainvkgaaanysrkdIDalgefaanYgakglawlkTEAdglkgpiakffagekqealvqaldaadg 391
Cdd:PRK03932 293 PR---------------------------IT--------Y---------TEA---------------------------- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 392 dlllfvadklevandalgalrlklgkeLNLIDESLFNFLWVVDWPLleyD--AEEGRYYAAHHpFTMPVredlklIETN- 468
Cdd:PRK03932 301 ---------------------------IEILQKSGKKFEFPVEWGD---DlgSEHERYLAEEH-FKKPV------FVTNy 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 469 PQDMKA------------QAYDLVLNGY-ELGGGSIRIFEKDVQEKMFGLLGFSEEEakeqFGFLLEAFEYGAPPHGGIA 535
Cdd:PRK03932 344 PKDIKAfymrlnpdgktvAAMDLLAPGIgEIIGGSQREERLDVLEARIKELGLNKED----YWWYLDLRRYGSVPHSGFG 419
|
570 580
....*....|....*....|....*
gi 1140945906 536 LGLDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:PRK03932 420 LGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
20-106 |
4.79e-36 |
|
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: 129.61 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAREEatvnPNLKTGRIEIQA 99
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQA 77
|
....*..
gi 1140945906 100 ESVEVLS 106
Cdd:cd04100 78 EELEVLS 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
2-558 |
7.54e-34 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 134.83 E-value: 7.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 2 FGRTYYCGEITEK----------AIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPD-VSKAALETAESirsey 70
Cdd:PRK00484 29 FERTHTAAELRAKyddkekeeleELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKDdVGEEALEAFKK----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 71 vLDI------TGKVVAreeaTvnpnlKTGRIEIQAESVEVLSAAKTPP----FAISDQaaevseDIRLKHRYLDL-RRPE 139
Cdd:PRK00484 104 -LDLgdiigvEGTLFK----T-----KTGELSVKATELTLLTKSLRPLpdkfHGLTDV------ETRYRQRYVDLiVNPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 140 MFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLtKSTPEG--ARdylvPSRVH----EGEFYaLPQSPQIF-KQLLmVSGF 212
Cdd:PRK00484 168 SRETFRKRSKIISAIRRFLDNRGFLEVETPML-QPIAGGaaAR----PFITHhnalDIDLY-LRIAPELYlKRLI-VGGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 213 DRYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHG----------IEISLPLPRMSYEDA 282
Cdd:PRK00484 241 ERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGttkvtyqgteIDFGPPFKRLTMVDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 283 mnrygsdkpdtrfgmlltdVSEAvkdsdfkvfasavtsggavkainvkgAAANYSRKDIDALGEFAANYGakglawLKTE 362
Cdd:PRK00484 321 -------------------IKEY--------------------------TGVDFDDMTDEEARALAKELG------IEVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 363 ADGLKGP-IAKFFagekqEALVqaldaadgdlllfvadklevandalgalrlklgkELNLIDESlFnflwVVDWPlleyd 441
Cdd:PRK00484 350 KSWGLGKlINELF-----EEFV----------------------------------EPKLIQPT-F----ITDYP----- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 442 aeegryyAAHHPFTMPVREDLKLIEtnpqdmkaqAYDLVLNGYELGGG----------SIRiFEKDVQEKMFGllgfsEE 511
Cdd:PRK00484 381 -------VEISPLAKRHREDPGLTE---------RFELFIGGREIANAfselndpidqRER-FEAQVEAKEAG-----DD 438
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1140945906 512 EA---KEQFgflLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFP 558
Cdd:PRK00484 439 EAmfmDEDF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
314-408 |
1.84e-32 |
|
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases.
Pssm-ID: 397199 [Multi-domain] Cd Length: 94 Bit Score: 120.06 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 314 FASAVTSGGAVKAINVKGAAaNYSRKDIDALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDAADGDL 393
Cdd:pfam02938 1 FSEALKSGGSVKALRVPGAA-GLSRKEIDELERFAKEYGAKGLAWIKVEGGGHTGPIAKFLTEEEVEKLLEAVGAEDGDA 79
|
90
....*....|....*
gi 1140945906 394 LLFVADKLEVANDAL 408
Cdd:pfam02938 80 LLFVADKKKTVNKAL 94
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
2-558 |
2.18e-30 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 125.49 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 2 FGRTYYCGEITEK---------AIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFnpDVSKAALETAESIRSEYVL 72
Cdd:PLN02502 84 FDVTHTAPELQEKygslengeeLEDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYA--DKKRLDLDEEEFEKLHSLV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 73 DItGKVVAreeATVNP-NLKTGRIEIQAESVEVLSAAKTP----PFAISDQaaevseDIRLKHRYLDL-RRPEMFNSLKM 146
Cdd:PLN02502 162 DR-GDIVG---VTGTPgKTKKGELSIFPTSFEVLTKCLLMlpdkYHGLTDQ------ETRYRQRYLDLiANPEVRDIFRT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 147 RHNVTKAVRRFLDDNGFLDIETPVLtKSTPEGA--RdylvPSRVHEGE----FYaLPQSPQIFKQLLMVSGFDRYYQIAR 220
Cdd:PLN02502 232 RAKIISYIRRFLDDRGFLEVETPML-NMIAGGAaaR----PFVTHHNDlnmdLY-LRIATELHLKRLVVGGFERVYEIGR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 221 CFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGieiSLPLPRMSYEDAMNRygsdkPDTRFGMLlt 300
Cdd:PLN02502 306 QFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSGMVKELTG---SYKIKYHGIEIDFTP-----PFRRISMI-- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 301 dvsEAVKdsdfkvfasavtsggavkainvkgaaanysrkdidalgefaanygakglawlktEADGLKGPiakffAGEKQE 380
Cdd:PLN02502 376 ---SLVE------------------------------------------------------EATGIDFP-----ADLKSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 381 ALVQALDAADgdlllfVADKLEVAN-DALGALRLKLGKElnLIDESLFNFLWVVDWPlleydaEEGRYYAAHHpftmpvR 459
Cdd:PLN02502 394 EANAYLIAAC------EKFDVKCPPpQTTGRLLNELFEE--FLEETLVQPTFVLDHP------VEMSPLAKPH------R 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 460 EDLKLIETnpqdmkaqaYDLVLNGYELGGGSIRIFEKDVQEKMFgllgfsEEEAK-------------EQFgflLEAFEY 526
Cdd:PLN02502 454 SKPGLTER---------FELFINGRELANAFSELTDPVDQRERF------EEQVKqhnagddeamaldEDF---CTALEY 515
|
570 580 590
....*....|....*....|....*....|..
gi 1140945906 527 GAPPHGGIALGLDRLVMLLSGRTNLRDTIAFP 558
Cdd:PLN02502 516 GLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
13-559 |
2.84e-30 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 125.11 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 13 EKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQ--VVFNPDVSKAALETAESIRSEYVLDITGKVVAREEATVNPN- 89
Cdd:PTZ00401 74 PELVDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQamAAVEGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSh 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 90 ----LKTGRIEIQAESVEVLsaaktpPFAI-------SDQAAEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFL 158
Cdd:PTZ00401 154 sdieLKVKKIHTVTESLRTL------PFTLedasrkeSDEGAKVNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 159 DDNGFLDIETPVLTKSTPEGARDylVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQ-PEFTQ 237
Cdd:PTZ00401 228 IDSDFCEIHSPKIINAPSEGGAN--VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 238 IDIEMSFMSQ-EDIMKLSEEMMAHVMRE--THGIEISLPLPRMSYEDAMNRYgsdKPDTRFGMLLTDVSEAVKDSDfkvf 314
Cdd:PTZ00401 306 LDVEMRINEHyYEVLDLAESLFNYIFERlaTHTKELKAVCQQYPFEPLVWKL---TPERMKELGVGVISEGVEPTD---- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 315 asavTSGGAVKAINVKGAAANYsrkdidalgefaanygAKGLAWLKTEADGLKGPiakffagekqealvqaldaadgdll 394
Cdd:PTZ00401 379 ----KYQARVHNMDSRMLRINY----------------MHCIELLNTVLEEKMAP------------------------- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 395 lfvADKLEVANDALgalrlkLGKelnLIDESLFNFLWVVDwplleydaeegRYYAAHHPF-TMPVREDLKLieTNpqdmk 473
Cdd:PTZ00401 414 ---TDDINTTNEKL------LGK---LVKERYGTDFFISD-----------RFPSSARPFyTMECKDDERF--TN----- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 474 aqAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEqfgfLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRD 553
Cdd:PTZ00401 464 --SYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRL 537
|
....*.
gi 1140945906 554 TIAFPK 559
Cdd:PTZ00401 538 ASLFPR 543
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
4-558 |
1.88e-26 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 115.06 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 4 RTYYCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVfnpdVSKAALETAESIRSEYVLDI------TGK 77
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVL----LDASRLEQGSLADFRAAVDLgdlvevTGT 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 78 VVAReeatvnpnlKTGRIEIQAESVEVLSAAKTPP----FAISDQAAevsediRLKHRYLDLR-RPEMFNSLKMRHNVTK 152
Cdd:PRK02983 714 MGTS---------RNGTLSLLVTSWRLAGKCLRPLpdkwKGLTDPEA------RVRQRYLDLAvNPEARDLLRARSAVVR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 153 AVRRFLDDNGFLDIETPVLtkSTPEG---ARDYLVPSRVHEGEFYaLPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRA 229
Cdd:PRK02983 779 AVRETLVARGFLEVETPIL--QQVHGganARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDA 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 230 DRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGIEISLplprmsyedamnrygsdKPDTRFGMLLTDVSEavkds 309
Cdd:PRK02983 856 THNPEFTLLEAYQAHADYDTMRDLTRELIQNAAQAAHGAPVVM-----------------RPDGDGVLEPVDISG----- 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 310 DFKVfasaVTSGGAVkainvkgaaanySRkdidALGEfaanygakglawlktEADglkgpiakffagekqealvqaldaA 389
Cdd:PRK02983 914 PWPV----VTVHDAV------------SE----ALGE---------------EID------------------------P 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 390 DGDL--LLFVADKLEVANDA---LGALRLKLGKEL--NLIDESLFnflwVVDWPlleydaeegryyAAHHPFTMPVREDL 462
Cdd:PRK02983 935 DTPLaeLRKLCDAAGIPYRTdwdAGAVVLELYEHLveDRTTFPTF----YTDFP------------TSVSPLTRPHRSDP 998
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 463 KLietnpqdmkAQAYDLVLNGYELGGG-----------------SIRIFEKDVqEKMfgllgfseeEAKEQFgflLEAFE 525
Cdd:PRK02983 999 GL---------AERWDLVAWGVELGTAyseltdpveqrrrlteqSLLAAGGDP-EAM---------ELDEDF---LQALE 1056
|
570 580 590
....*....|....*....|....*....|...
gi 1140945906 526 YGAPPHGGIALGLDRLVMLLSGRtNLRDTIAFP 558
Cdd:PRK02983 1057 YAMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
138-558 |
2.43e-26 |
|
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: 109.98 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 138 PEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLtKSTPEGA--RDYLVPSRVHEGEFYaLPQSPQIFKQLLMVSGFDRY 215
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGAaaRPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 216 YQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHG--------IEISL--PLPRMSYEDAMNr 285
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKINGktkieyggKELDFtpPFKRVTMVDALK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 286 ygsdkpdtrfgmlltdvseavkdsdfkvfasavtsggavKAINVkgaaanysrkDIDALGEFAANYGAKGLAWLKteadg 365
Cdd:cd00775 159 ---------------------------------------EKTGI----------DFPELDLEQPEELAKLLAKLI----- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 366 lkgpiakffagekqealvqaldaadgdlllfvaDKLEVANDALGALRLKLGKElnLIDESLFNFLWVVDWPlleydaeeg 445
Cdd:cd00775 185 ---------------------------------KEKIEKPRTLGKLLDKLFEE--FVEPTLIQPTFIIDHP--------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 446 ryyAAHHPFTMPVREDLKLIETnpqdmkaqaYDLVLNGYELGGGSIRI---------FEKDVQEKMFGllgfsEEEAK-- 514
Cdd:cd00775 221 ---VEISPLAKRHRSNPGLTER---------FELFICGKEIANAYTELndpfdqrerFEEQAKQKEAG-----DDEAMmm 283
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1140945906 515 -EQFgflLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFP 558
Cdd:cd00775 284 dEDF---VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
7-112 |
2.36e-25 |
|
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: 100.47 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 7 YCGEITEKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPD-VSKAALETAESIRSEYVLDITGKVVAREEAt 85
Cdd:cd04316 2 YSAEITPELDGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTAPKKkVDKELFKTVRKLSRESVISVTGTVKAEPKA- 80
|
90 100
....*....|....*....|....*..
gi 1140945906 86 vnpnlKTGrIEIQAESVEVLSAAKTPP 112
Cdd:cd04316 81 -----PNG-VEIIPEEIEVLSEAKTPL 101
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
13-558 |
3.30e-24 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 107.43 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 13 EKAIGESVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVfnpdVSKAALETAESIRSEYVLDITGKVVAREeaTVNPNLKT 92
Cdd:PTZ00385 103 DRAAQATVRVAGRVTSVRDIGKIIFVTIRSNGNELQVV----GQVGEHFTREDLKKLKVSLRVGDIIGAD--GVPCRMQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 93 GRIEIQAESVEVLSaaktpPFAISDQ---------AAEVSEDIRLKHRYLDL-RRPEMFNSLKMRHNVTKAVRRFLDDNG 162
Cdd:PTZ00385 177 GELSVAASRMLILS-----PYVCTDQvvcpnlrgfTVLQDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERN 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 163 FLDIETPVL-TKSTPEGARDYLVPSRVHEGEFYaLPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIE 241
Cdd:PTZ00385 252 FVEVETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFY 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 242 MSFMSQEDIMKLSEEMMAHVMRETHG---IEIslplprmsyedamnrygsdKPDTRFGMLLTdvseavkdsdfkvfasaV 318
Cdd:PTZ00385 331 AAYHTYEDLMPMTEDIFRQLAMRVNGttvVQI-------------------YPENAHGNPVT-----------------V 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 319 TSGGAVKAINVKGAAANYSRKDIDALGEFAAnygAKGLAWLktEADGLKGPI--------AKFFagekqEALVQaldaad 390
Cdd:PTZ00385 375 DLGKPFRRVSVYDEIQRMSGVEFPPPNELNT---PKGIAYM--SVVMLRYNIplppvrtaAKMF-----EKLID------ 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 391 gdllLFVADKlevandalgalrlklgkelnlIDESLFnflwVVDWPLleydaeegryyaahhpFTMPVREdlkliETNPQ 470
Cdd:PTZ00385 439 ----FFITDR---------------------VVEPTF----VMDHPL----------------FMSPLAK-----EQVSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 471 DMKAQAYDLVLNGYELGGGSIRI---------FEKDVQEKMFGllgfsEEEAKEQFGFLLEAFEYGAPPHGGIALGLDRL 541
Cdd:PTZ00385 469 PGLAERFELFVNGIEYCNAYSELndpheqyhrFQQQLVDRQGG-----DEEAMPLDETFLKSLQVGLPPTAGWGMGIDRA 543
|
570
....*....|....*..
gi 1140945906 542 VMLLSGRTNLRDTIAFP 558
Cdd:PTZ00385 544 LMLLTNSSNIRDGIIFP 560
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
147-258 |
1.23e-19 |
|
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: 87.56 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 147 RHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGARD----YLVPSRVHEGEFYALPQSPQIFKQLLMVS----GFDRYYQI 218
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAEI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1140945906 219 ARCFRDEDLRAD--RQPEFTQIDIEMsFMSQEDIMKLSEEMM 258
Cdd:cd00768 82 GPAFRNEGGRRGlrRVREFTQLEGEV-FGEDGEEASEFEELI 122
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
20-105 |
3.98e-18 |
|
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: 78.82 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWV-QKRRDLGGLIFIDLRDRTGIVQVVFNPdvsKAALETAESIRSEYVLDITGKVVAReeatvnpnlKTGRIEIQ 98
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFK---EEAEKLAKKLKEGDVVRVTGKVKKR---------KGGELELV 68
|
....*..
gi 1140945906 99 AESVEVL 105
Cdd:pfam01336 69 VEEIELL 75
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
20-558 |
8.07e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 86.65 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDvskaalETAESIRSEYV--LDITGKVVAREEATvnpNLKTGRIEI 97
Cdd:PRK12445 68 VSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARD------SLPEGVYNDQFkkWDLGDIIGARGTLF---KTQTGELSI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 98 QAESVEVLSAAKTPpfaISDQAAEVS-EDIRLKHRYLDL-RRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLtKST 175
Cdd:PRK12445 139 HCTELRLLTKALRP---LPDKFHGLQdQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM-QVI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 176 PEGA--RDYLVPSRVHEGEFYaLPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKL 253
Cdd:PRK12445 215 PGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 254 SEEMMAHVMRETHGIEislplpRMSYEDAMNRYGsdKPDTRFGMlltdvSEAVKDsdfkvfasavtsggavkainvkgaa 333
Cdd:PRK12445 294 TESLFRTLAQEVLGTT------KVTYGEHVFDFG--KPFEKLTM-----REAIKK------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 334 aNYSRKDIDALGEFAAnygAKGLAwlktEADGLKgpiakffaGEKQEALvqaldaadGDLLLFVADklEVAndalgalrl 413
Cdd:PRK12445 336 -YRPETDMADLDNFDA---AKALA----ESIGIT--------VEKSWGL--------GRIVTEIFD--EVA--------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 414 klgkELNLIDESLfnflwvvdwpLLEYDAEEGryyaahhpfTMPVREDLklietNPQdmKAQAYDLVLNGYELGGGSIRI 493
Cdd:PRK12445 381 ----EAHLIQPTF----------ITEYPAEVS---------PLARRNDV-----NPE--ITDRFEFFIGGREIGNGFSEL 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1140945906 494 FEKDVQEKMFGLLGFSEEEAKEQFGFLLE----AFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFP 558
Cdd:PRK12445 431 NDAEDQAERFQEQVNAKAAGDDEAMFYDEdyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
135-312 |
6.05e-17 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 82.37 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 135 LRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGARD-----YLVPSRVHEGEFYALPQSPQIFKQLlMV 209
Cdd:PRK06462 21 ISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADSMILHKQL-AL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 210 SGFDRYYQIARCFRDEDLRADRQP---EFTQIDIEMSFMSQEDIMKLSEEMMAHVMRE---THGIEI----------SLP 273
Cdd:PRK06462 100 RMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKElleEHEDELeffgrdlphlKRP 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1140945906 274 LPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFK 312
Cdd:PRK06462 180 FKRITHKEAVEILNEEGCRGIDLEELGSEGEKSLSEHFE 218
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
20-133 |
6.67e-15 |
|
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal 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.
Pssm-ID: 239814 [Multi-domain] Cd Length: 103 Bit Score: 70.63 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAALETAESIRSEYVLDITGKVVAREEAtvnpnlkTGRIEIQA 99
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNEEAYREAKKVGIESSVIVEGAVKADPRA-------PGGAEVHG 74
|
90 100 110
....*....|....*....|....*....|....
gi 1140945906 100 ESVEVLSAAKtpPFAISDQAaevSEDIRLKHRYL 133
Cdd:cd04319 75 EKLEIIQNVE--FFPITEDA---SDEFLLDVRHL 103
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
125-564 |
3.18e-14 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 75.43 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 125 DIRLKHRYLDLRRPEMFNS-LKMRHNVTKAVRRFLDDNGFLDIETPVLT-KSTPEGARDYLVPSRVHEGEFYaLPQSPQI 202
Cdd:PTZ00417 233 EIRYRQRYLDLMINESTRStFITRTKIINYLRNFLNDRGFIEVETPTMNlVAGGANARPFITHHNDLDLDLY-LRIATEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 203 FKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGieislplprmSYEDA 282
Cdd:PTZ00417 312 PLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIKWSEDFFSQLVMHLFG----------TYKIL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 283 MNRYGSDKPDTRFgmlltdvseavkdsDFkvfasavtsggavkainvkgaAANYSRKDIDALGEFAANygakglawlkte 362
Cdd:PTZ00417 382 YNKDGPEKDPIEI--------------DF---------------------TPPYPKVSIVEELEKLTN------------ 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 363 aDGLKGPiakFFAGEKQEALVQaldaadgdllLFVADKLEVANDALGAlrlklgkelNLIDESLFNFlwvvdwplLEYDA 442
Cdd:PTZ00417 415 -TKLEQP---FDSPETINKMIN----------LIKENKIEMPNPPTAA---------KLLDQLASHF--------IENKY 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 443 EEGRYYAAHHPFTM-PVRedlKLIETNPQdmKAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAK-EQFGF- 519
Cdd:PTZ00417 464 PNKPFFIIEHPQIMsPLA---KYHRSKPG--LTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKDREKGDaEAFQFd 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1140945906 520 --LLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKTASAS 564
Cdd:PTZ00417 539 aaFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTMRPAN 585
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
19-106 |
1.92e-13 |
|
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. 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 synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and 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: 239818 [Multi-domain] Cd Length: 84 Bit Score: 65.72 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 19 SVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKAAlETAESIRSEYVLDITGKVVAREEATVNPnlktGRIEIQ 98
Cdd:cd04323 1 RVKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEF-YDAKSLTQESSVEVTGEVKEDPRAKQAP----GGYELQ 75
|
....*...
gi 1140945906 99 AESVEVLS 106
Cdd:cd04323 76 VDYLEIIG 83
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
16-564 |
1.28e-11 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 67.31 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 16 IGESVVLKGWVQKRRDLGGLIFIDLRDRTGI--VQVVFNPDVskaalETAESIRSEYVLdiTGKVVAREEATVNPNLKTG 93
Cdd:PLN02603 106 VGKTLNVMGWVRTLRAQSSVTFIEVNDGSCLsnMQCVMTPDA-----EGYDQVESGLIT--TGASVLVQGTVVSSQGGKQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 94 RIEIQAESVEVLSAAKtPPFAIsdQAAEVS-EDIRLKHRyldLR-RPEMFNSL-KMRHNVTKAVRRFLDDNGFLDIETPV 170
Cdd:PLN02603 179 KVELKVSKIVVVGKSD-PSYPI--QKKRVSrEFLRTKAH---LRpRTNTFGAVaRVRNALAYATHKFFQENGFVWVSSPI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 171 LTKSTPEGARDY-----LVPSRVHEG-------------------EFYALPQSPQIFKQL---LMVSGFDRYYQIARCFR 223
Cdd:PLN02603 253 ITASDCEGAGEQfcvttLIPNSAENGgslvddipktkdglidwsqDFFGKPAFLTVSGQLngeTYATALSDVYTFGPTFR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 224 DEDLRADRQ-PEFTQIDIEMSFMSQEDIMKLSEEMMAHVMREthgieislplprmsyedamnrygsdkpdtrfgmLLTDV 302
Cdd:PLN02603 333 AENSNTSRHlAEFWMIEPELAFADLNDDMACATAYLQYVVKY---------------------------------ILENC 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 303 SEavkDSDFkvFASAVTSGgavkainvkgaaanysrkDIDALGEFAanygakglawlkteadglkgpiakffagEKQeaL 382
Cdd:PLN02603 380 KE---DMEF--FNTWIEKG------------------IIDRLSDVV----------------------------EKN--F 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 383 VQaldaadgdllLFVADKLEvandalgaLRLKLGKElnlideslfnFLWVVDWPlLEYDAEEGRYYAAHHPFTMPVredl 462
Cdd:PLN02603 407 VQ----------LSYTDAIE--------LLLKAKKK----------FEFPVKWG-LDLQSEHERYITEEAFGGRPV---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 463 kLIETNPQDMKA------------QAYD-LVLNGYELGGGSIRIFEKDVQEKMFGLLGFSeeeaKEQFGFLLEAFEYGAP 529
Cdd:PLN02603 454 -IIRDYPKEIKAfymrenddgktvAAMDmLVPRVGELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSV 528
|
570 580 590
....*....|....*....|....*....|....*
gi 1140945906 530 PHGGIALGLDRLVMLLSGRTNLRDTIAFPKTASAS 564
Cdd:PLN02603 529 PHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSA 563
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
19-107 |
3.10e-11 |
|
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) 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 fungal 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. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239816 [Multi-domain] Cd Length: 86 Bit Score: 59.64 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 19 SVVLKGWVQKRRDLGG-LIFIDLRDRTG-IVQVVFNPdvSKAALETAESIRSEYVLDITGKVVAREEATvnpNLKTGRIE 96
Cdd:cd04321 1 KVTLNGWIDRKPRIVKkLSFADLRDPNGdIIQLVSTA--KKDAFSLLKSITAESPVQVRGKLQLKEAKS---SEKNDEWE 75
|
90
....*....|.
gi 1140945906 97 IQAESVEVLSA 107
Cdd:cd04321 76 LVVDDIQTLNA 86
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
20-117 |
1.42e-10 |
|
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: 58.34 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWVQKRRDLGG-LIFIDLRDRTGIVQVVF---NPDVSKAALETAESIRSEYVLDITGKVVAREE----ATVNpnlk 91
Cdd:cd04320 2 VLIRARVHTSRAQGAkLAFLVLRQQGYTIQGVLaasAEGVSKQMVKWAGSLSKESIVDVEGTVKKPEEpiksCTQQ---- 77
|
90 100
....*....|....*....|....*..
gi 1140945906 92 tgRIEIQAESVEVLSAAKTP-PFAISD 117
Cdd:cd04320 78 --DVELHIEKIYVVSEAAEPlPFQLED 102
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
157-556 |
3.93e-10 |
|
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: 61.03 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 157 FLDDNGFLDIETPVLTKST-PEGARDYL---VPSRVHEGEFYALPQSPQIF-KQLLmVSGFDRYYQIARCFRDEDLRADR 231
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFateFVGPDGQGRPLYLQTSPEYAmKRLL-AAGSGPIFQICKVFRNGERGRRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 232 QPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRethgiEISLPLPRMSYEDAMNRYgsdkpdTRFGMLLTDVSEavkdsdf 311
Cdd:TIGR00462 80 NPEFTMLEWYRPGFDYHDLMDEVEALLQELLG-----DPFAPAERLSYQEAFLRY------AGIDPLTASLAE------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 312 kvfasavtsggavkainvkgaaanysrkdIDALGEFAANYGAKGLAWlkteadglkgpiakffagekqEALVQaldaadg 391
Cdd:TIGR00462 142 -----------------------------LQAAAAAHGIRASEEDDR---------------------DDLLD------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 392 dlLLFVaDKLEVandalgalrlKLGKElnlideslfNFLWVVDWPlleydAEEgryyAAhhpftmpvredlkLIETNPQD 471
Cdd:TIGR00462 165 --LLFS-EKVEP----------HLGFG---------RPTFLYDYP-----ASQ----AA-------------LARISPDD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 472 MK-AQAYDLVLNGYELGGGS---------IRIFEKDVQEKmfGLLGFSEEEAKEQFgflLEAFEYGAPPHGGIALGLDRL 541
Cdd:TIGR00462 201 PRvAERFELYIKGLELANGFheltdaaeqRRRFEADNALR--KALGLPRYPLDERF---LAALEAGLPECSGVALGVDRL 275
|
410
....*....|....*
gi 1140945906 542 VMLLSGRTNLRDTIA 556
Cdd:TIGR00462 276 LMLALGADSIDDVLA 290
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
20-105 |
9.47e-09 |
|
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli asparaginyl-tRNA synthetase (AsnRS) and, in Arabidopsis thaliana and Saccharomyces cerevisiae mitochondrial (mt) AsnRS. 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. S. cerevisiae mtAsnRS can charge E.coli tRNA with asparagines. Mutations in the gene for S. cerevisiae mtAsnRS has been found to induce a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.
Pssm-ID: 239813 [Multi-domain] Cd Length: 82 Bit Score: 52.57 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 20 VVLKGWVQKRRDLGGLIFIDLRDRTGI--VQVVFNPDVSKAA----LETAESIRseyvldITGKVVAREEatvnpnlKTG 93
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELNDGSCLknLQVVVDKELTNFKeilkLSTGSSIR------VEGVLVKSPG-------AKQ 68
|
90
....*....|..
gi 1140945906 94 RIEIQAESVEVL 105
Cdd:cd04318 69 PFELQAEKIEVL 80
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
433-559 |
1.38e-07 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 54.26 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 433 VDWPLlEYDAEEGRYyAAHHPFTMPVredlkLIETNPQDMKA------------QAYD-LVLNGYELGGGSIR-----IF 494
Cdd:PTZ00425 451 VKWGM-DLQSEHERF-VAEQIFKKPV-----IVYNYPKDLKAfymklnedqktvAAMDvLVPKIGEVIGGSQRednleRL 523
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140945906 495 EKDVQEKMFGLlgfseeeakEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPK 559
Cdd:PTZ00425 524 DKMIKEKKLNM---------ESYWWYRQLRKFGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
19-135 |
1.21e-06 |
|
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: 47.09 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 19 SVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFN-PDVSKAALETAESIrseyvLDI------TGKVVareeATvnpnlK 91
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNkDDLGEEEFEDFKKL-----LDLgdiigvTGTPF----KT-----K 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1140945906 92 TGRIEIQAESVEVLSAA-KTPPfaiSDQAAEVSEDIRLKHRYLDL 135
Cdd:cd04322 67 TGELSIFVKEFTLLSKSlRPLP---EKFHGLTDVETRYRQRYLDL 108
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
17-559 |
2.43e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 50.38 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 17 GESVVLKGWVQKRRDLG--GLIFIDLRDRT--GIVQVVFNP---DVSKAaLETAESIRSEYVLDITgkvvareeatvnPN 89
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGkgTFAFLEVNDGScpANLQVMVDSslyDLSTL-VATGTCVTVDGVLKVP------------PE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 90 LKTGRIEIQAESVEVLSAAKTPPFAISDQAAEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETP 169
Cdd:PLN02221 117 GKGTKQKIELSVEKVIDVGTVDPTKYPLPKTKLTLEFLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 170 VLTKSTPEGArdylvpsrvheGEfyalpqspqIFKQLLMVSGFDRYyqiarcfrDEDLRADRQPefTQIDIEMSFM---- 245
Cdd:PLN02221 197 IITTSDCEGA-----------GE---------MFQVTTLINYTERL--------EQDLIDNPPP--TEADVEAARLivke 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 246 -------------SQEDI------MKLSEEMMAHVmRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLltdvseav 306
Cdd:PLN02221 247 rgevvaqlkaakaSKEEItaavaeLKIAKESLAHI-EERSKLKPGLPKKDGKIDYSKDFFGRQAFLTVSGQL-------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 307 kdsDFKVFASAVTS----GGAVKAINvkgaaANYSRKdidaLGEFaanygakglaWLkteadgLKGPIAkfFAGEKQ--- 379
Cdd:PLN02221 318 ---QVETYACALSSvytfGPTFRAEN-----SHTSRH----LAEF----------WM------VEPEIA--FADLEDdmn 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 380 --EALVQ-----ALDAADGDLLLFVA-------DKLE-VANDALGalRLKLGKELNLIDESLF-------NFLWVVDWpl 437
Cdd:PLN02221 368 caEAYVKymckwLLDKCFDDMELMAKnfdsgciDRLRmVASTPFG--RITYTEAIELLEEAVAkgkefdnNVEWGIDL-- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 438 leydAEEGRYYAAHHPFTMPVredlkLIETNPQDMKAqaYDLVLNGYELGGGSIRIFEKDVQEkmfgLLGFSEEEAK--- 514
Cdd:PLN02221 444 ----ASEHERYLTEVLFQKPL-----IVYNYPKGIKA--FYMRLNDDEKTVAAMDVLVPKVGE----LIGGSQREERydv 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1140945906 515 -----EQFGFLLEAFE-------YGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPK 559
Cdd:PLN02221 509 ikqriEEMGLPIEPYEwyldlrrYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPR 565
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
464-553 |
1.06e-05 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 47.62 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 464 LIETNPQDMK-AQAYDLVLNGYELGGG---------SIRIFEKDVQEKMfgLLGFSEEEAKEqfgFLLEAFEYGAPPHGG 533
Cdd:PRK09350 211 LAKISTEDHRvAERFEVYFKGIELANGfheltdareQRQRFEQDNRKRA--ARGLPQQPIDE---NLIAALEAGLPDCSG 285
|
90 100
....*....|....*....|
gi 1140945906 534 IALGLDRLVMLLSGRTNLRD 553
Cdd:PRK09350 286 VALGVDRLIMLALGAESISE 305
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
453-560 |
6.94e-05 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 45.63 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 453 PFTMPVREDLKlietnpqdmKAQAYDLVL-NGYELGGGSIRIFEKDVQEKMFGLLGFSeeeaKEQFGFLLEAFEYGAPPH 531
Cdd:PLN02532 532 PFYVRLNDDGK---------TVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGLP----REQYEWYLDLRRHGTVKH 598
|
90 100
....*....|....*....|....*....
gi 1140945906 532 GGIALGLDRLVMLLSGRTNLRDTIAFPKT 560
Cdd:PLN02532 599 SGFSLGFELMVLFATGLPDVRDAIPFPRS 627
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
144-286 |
4.37e-04 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 42.61 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 144 LKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGArdYLVPSRVH-EGEFYA------LPQSPQIFKQLLMVSGFDRYY 216
Cdd:PRK09350 5 LLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDI--HLVPFETRfVGPGASqgktlwLMTSPEYHMKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140945906 217 QIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMrethgieISLPLPRMSYEDAMNRY 286
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL-------DCEPAESLSYQQAFLRY 145
|
|
| |
