|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-588 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1092.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 1 MMRTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDErDEALFKIASSLRAEACVQIQGEVIARD 80
Cdd:PRK00476 2 MMRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDP-DAEAFEVAESLRSEYVIQVTGTVRARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 81 ESQINKDMATGEIEVLVKNVLVYNNADVLPL--DFNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGF 158
Cdd:PRK00476 81 EGTVNPNLPTGEIEVLASELEVLNKSKTLPFpiDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 159 LDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETS 238
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 239 FLTAEEVRAIMEEMIHGLWLDRLNVDLGK-FPMMTWHEAMNRFGSDKPDLRNPLELVDVADILKDVEFKVFHEPANSpDG 317
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLGVDLPTpFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAAND-GG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 318 RVTVLRVPNG-TTLTRKQIDEYTQFVGIYGAKGLAWAKINDvnaglEGVQSPVAKFLNEEVIKALIARTNAQTGDILFFG 396
Cdd:PRK00476 320 RVKAIRVPGGaAQLSRKQIDELTEFAKIYGAKGLAYIKVNE-----DGLKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 397 ADKWQVVTDSMGALRLKVGRDLNLTDLSAWKPLWVIDFPMFERDEE-GNLSAMHHPFTSPK-GLTPEELAINPVNAVANA 474
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEYDEEeGRWVAAHHPFTMPKdEDLDELETTDPGKARAYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 475 YDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIA 554
Cdd:PRK00476 475 YDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
570 580 590
....*....|....*....|....*....|....
gi 491988310 555 FPKTTAAACLMTEAPSYANPQALEELAIQVTKSE 588
Cdd:PRK00476 555 FPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
1-586 |
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: 1087.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 1 MMRTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFD-ERDEALFKIASSLRAEACVQIQGEVIAR 79
Cdd:COG0173 1 MYRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDpDDSAEAFEKAEKLRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 80 DESQINKDMATGEIEVLVKNVLVYNNADVLP--LDFNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHG 157
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPfqIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 158 FLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVET 237
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 238 SFLTAEEVRAIMEEMIHGLWLDRLNVDL-GKFPMMTWHEAMNRFGSDKPDLRNPLELVDVADILKDVEFKVFHEPANsPD 316
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGVELpTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAE-NG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 317 GRVTVLRVPNGTTLTRKQIDEYTQFVGIYGAKGLAWAKINDvnaglEGVQSPVAKFLNEEVIKALIARTNAQTGDILFFG 396
Cdd:COG0173 320 GRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNE-----DGLKSPIAKFLSEEELAAILERLGAKPGDLIFFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 397 ADKWQVVTDSMGALRLKVGRDLNLTDLSAWKPLWVIDFPMFERDEE-GNLSAMHHPFTSPKGLTPEELAINPVNAVANAY 475
Cdd:COG0173 395 ADKPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEYDEEeGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 476 DMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAF 555
Cdd:COG0173 475 DLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
570 580 590
....*....|....*....|....*....|.
gi 491988310 556 PKTTAAACLMTEAPSYANPQALEELAIQVTK 586
Cdd:COG0173 555 PKTQSAQDLMTGAPSEVDEKQLKELHIRLRP 585
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
2-583 |
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: 932.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 2 MRTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEALfKIASSLRAEACVQIQGEVIARDE 81
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPDADAL-KLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 82 SQINKDMATGEIEVLVKNVLVYNNADVLPLDFNQNNTEEQ-RLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLD 160
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAEEEvRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 161 IETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFL 240
Cdd:TIGR00459 160 IETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSFM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 241 TAEEVRAIMEEMIHGLWLDRLNVDLGK-FPMMTWHEAMNRFGSDKPDLRNPLELVDVADILKDVEFKVFHEPANSpDGRV 319
Cdd:TIGR00459 240 TQEDVMELIEKLVSHVFLEVKGIDLKKpFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLIND-GGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 320 TVLRVPNG-TTLTRKQIDEYTQFVGIYGAKGLAWAKINDvnaglEGVQSPVAKFLNEEVIKALIARTNAQTGDILFFGAD 398
Cdd:TIGR00459 319 KAIRVPGGwAELSRKSIKELRKFAKEYGAKGLAYLKVNE-----DGINSPIKKFLDEKKGKILLERTDAQNGDILLFGAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 399 KWQVVTDSMGALRLKVGRDLNLTDLSAWKPLWVIDFPMFERDEEGNLSAMHHPFTSPKGLTPEELAINPVNAVANAYDMV 478
Cdd:TIGR00459 394 SKKIVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKDKEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 479 INGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKT 558
Cdd:TIGR00459 474 LNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKT 553
|
570 580
....*....|....*....|....*
gi 491988310 559 TAAACLMTEAPSYANPQALEELAIQ 583
Cdd:TIGR00459 554 TAAACLMTEAPSFIDEKQLEELSIK 578
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
3-588 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 636.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 3 RTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEA-LFKIASSLRAEACVQIQGEVIARDE 81
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFPeAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 82 SQINKDMATGEIEVLVKNVLVYNNAD------VLPLDFNQNN-TEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFM- 153
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVVTkslpflVTTADEQKDSiKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 154 DEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQI 233
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 234 DVETSFLTAEEVRAIMEEMIHGLWLDRLNVDLGK-FPMMTWHEAMNRFGSDKPDLRNPLELVDVADILKDVEFKVFHEPA 312
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNpFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 313 NSpDGRVTVLRVPNG----TTLTRKQIDEYTQFVGiYGAKGLAWAKINDvNAGLEGVQSPVAKfLNEEVIKALIARTNAQ 388
Cdd:PLN02903 379 ES-GGVVKAICVPDGkkisNNTALKKGDIYNEAIK-SGAKGLAFLKVLD-DGELEGIKALVES-LSPEQAEQLLAACGAG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 389 TGDILFFGADKWQVVTDSMGALRLKVGRDLNLTDLSAWKPLWVIDFPMFE-RDEEGNLSAMHHPFTSPKGLTPEELainp 467
Cdd:PLN02903 455 PGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEwNEDEQRLEALHHPFTAPNPEDMGDL---- 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 468 VNAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTE 547
Cdd:PLN02903 531 SSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAK 610
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 491988310 548 NIRDVIAFPKTTAAACLMTEAPSYANPQALEELAIQVTKSE 588
Cdd:PLN02903 611 SIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTAPP 651
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
6-582 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 529.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 6 YCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFF--DERDEALFKIASSLRAEACVQIQGEVIARDESQ 83
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFspEAAPADVYELAASLRAEFCVALQGEVQKRLEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 84 INKDMATGEIEVLVKNVLVYNNADVLPLDFNQNN-------------TEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVR 150
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFAISDKAmtagagsagadavNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 151 RFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEF 230
Cdd:PRK12820 168 DFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPEF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 231 TQIDVETSFLTAEEVRAIMEEM------IHGLWLDRlnvdlgKFPMMTWHEAMNRFGSDKPDLRNPLELVDVADILKDVE 304
Cdd:PRK12820 248 TQLDIEASFIDEEFIFELIEELtarmfaIGGIALPR------PFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 305 FKVFHEPANSpDGRVTVLRVPNGTTLTRKQI--DEYT-QFVGIYGAKGLAWAKindVNAGleGVQSPVAKFLNEEVIKAL 381
Cdd:PRK12820 322 YGIFKQILQR-GGRIKGINIKGQSEKLSKNVlqNEYAkEIAPSFGAKGMTWMR---AEAG--GLDSNIVQFFSADEKEAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 382 IARTNAQTGDILFFGAD-KWQVVTDSMGALRLKVGRDLNLTDLSAWKPLWVIDFPMFERDEEGNLSAMHHPFTSPKGLTP 460
Cdd:PRK12820 396 KRRFHAEDGDVIIMIADaSCAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGVTSSHHPFTAPDREDF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 461 EELAINPVNAV-ANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRL 539
Cdd:PRK12820 476 DPGDIEELLDLrSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRV 555
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 491988310 540 TMLITGTENIRDVIAFPKTTAAACLMTEAPSYANPQALEELAI 582
Cdd:PRK12820 556 VSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
139-559 |
2.53e-156 |
|
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: 448.95 E-value: 2.53e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 139 LKTRAKITSFVRRFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFR 218
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 219 DEDLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLWLDRLNVDL-GKFPMMTWHEAMNRFGsdkpdlrnplelvdva 297
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELtTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 298 dilkdvefkvfhepanspdgrvtvlrvpngttltrkqideytqfvgiygakglawakindvnaglegvqspvakflneev 377
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 378 ikaliartnaqtgdilffgadkwqvvtdsmgalrlkvgrdlnltdlsaWKPLWVIDFPMFERDEE-GNLSAMHHPFTSPK 456
Cdd:cd00777 145 ------------------------------------------------FKFLWIVDFPLFEWDEEeGRLVSAHHPFTAPK 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 457 GLTPEELAINPVNAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGL 536
Cdd:cd00777 177 EEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|...
gi 491988310 537 DRLTMLITGTENIRDVIAFPKTT 559
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQ 279
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
119-559 |
3.83e-137 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 401.56 E-value: 3.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 119 EEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPMLTK-ATPEGARDYLVPSRVHkGKFYALPQSPQL 197
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKsATPEGARDFLVPSRAL-GKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 198 FKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLW----------LDRLNVDLGK 267
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFkevegiakelEGGTLLDLKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 268 -FPMMTWHEAMNR----------FGSDKPDLRNPLELVdvadilkdvefkvfhepanspdgrvtvlrvpngttltrkqid 336
Cdd:pfam00152 161 pFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 337 eytqfvgiygakglawakindvnaglegvqspvakflneevikaliartnaqtgdilffgadkwqvvtdsmgalrlkvgr 416
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 417 dlnlTDLSAWKPLWVIDFPmferdeegnlsAMHHPFTSPKgltPEELainpvNAVANAYDMVINGYEVGGGSVRIFDPKM 496
Cdd:pfam00152 199 ----IDKNKFNPLWVTDFP-----------AEHHPFTMPK---DEDD-----PALAEAFDLVLNGVEIGGGSIRIHDPEL 255
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491988310 497 QQTVFNILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTT 559
Cdd:pfam00152 256 QEERFEEQGLDPEEAEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPKTR 318
|
|
| Asp_Lys_Asn_RS_core |
cd00669 |
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ... |
139-560 |
1.88e-95 |
|
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: 292.84 E-value: 1.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 139 LKTRAKITSFVRRFMDEHGFLDIETPMLTKATP-EGARDYLVPSRvHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCF 217
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 218 RDEDLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLWLDRLNV-----------DLGKFPMMTWHEAMNRFGsdkpd 286
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfeledFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 287 lrnplelvdvadilkdvefkvfhepanspdgrvtvlrvpngttltrkqideytqfvgiygakglawakindvnaglegvq 366
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 367 spvakflneevikaliartnaqtgdilffgadkwqvvtdsmgalrlkvgrdlnltdlsawKPLWVIDFPMFerdeegnls 446
Cdd:cd00669 155 ------------------------------------------------------------QPLFLTDYPAE--------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 447 aMHHPFTSPKGLTPEelainpvnaVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEKFGFLLDALKFGT 526
Cdd:cd00669 166 -MHSPLASPHDVNPE---------IADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGL 235
|
410 420 430
....*....|....*....|....*....|....
gi 491988310 527 PPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTA 560
Cdd:cd00669 236 PPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-556 |
1.10e-67 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 226.22 E-value: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 1 MMRTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFD-ERDEALFKIASSLRAEACVQIQGEVIAr 79
Cdd:PRK05159 1 MMKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKkKVDEELFETIKKLKRESVVSVTGTVKA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 80 desqinKDMATGEIEVLVKNVLVYNNADV-LPLDFNQNNTEE--QRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEH 156
Cdd:PRK05159 80 ------NPKAPGGVEVIPEEIEVLNKAEEpLPLDISGKVLAEldTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 157 GFLDIETPMLTKATPEG-----ARDYLvpsrvhkGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEF 230
Cdd:PRK05159 154 GFTEIFTPKIVASGTEGgaelfPIDYF-------EKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 231 TQIDVETSFLTAEE-VRAIMEEMIHGL----------WLDRLNVDL----GKFPMMTWHEAMnrfgsdkpdlrnplelvd 295
Cdd:PRK05159 227 TSIDVEMGFIDDHEdVMDLLENLLRYMyedvaencekELELLGIELpvpeTPIPRITYDEAI------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 296 vaDILKDVEFKvfhepanspdgrvtvlrVPNGTTLTRkqideytqfvgiygakglawakindvnaglEGvqspvakflnE 375
Cdd:PRK05159 289 --EILKSKGNE-----------------ISWGDDLDT------------------------------EG----------E 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 376 EVIKALIARTnaqTGDILFFgadkwqvvtdsmgalrlkvgrdlnltdlsawkplwVIDFPMFERdeegnlsamhhPF-TS 454
Cdd:PRK05159 310 RLLGEYVKEE---YGSDFYF-----------------------------------ITDYPSEKR-----------PFyTM 340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 455 PKGLTPEelainpvnaVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEqeqqEKFGFLLDALKFGTPPHAGLAF 534
Cdd:PRK05159 341 PDEDDPE---------ISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNP----ESFEFYLEAFKYGMPPHGGFGL 407
|
570 580
....*....|....*....|..
gi 491988310 535 GLDRLTMLITGTENIRDVIAFP 556
Cdd:PRK05159 408 GLERLTMKLLGLENIREAVLFP 429
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
3-135 |
2.36e-65 |
|
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: 209.68 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 3 RTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEALFKIASSLRAEACVQIQGEVIARDES 82
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491988310 83 QINKDMATGEIEVLVKNVLVYNNADVLPLDFN--QNNTEEQRLKYRYLDLRRPEM 135
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFEIDddVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
3-558 |
6.92e-65 |
|
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: 218.38 E-value: 6.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 3 RTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEALFKIASSLRAEACVQIQGEVIardES 82
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAKKLTTESSVEVTGTVV---ES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 83 QInkdmATGEIEVLVKNVLVYNNAD-VLPLDfNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLDI 161
Cdd:COG0017 78 PR----APQGVELQAEEIEVLGEADePYPLQ-PKRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 162 ETPMLTKATPEGAR-----DYLvpsrvhkGKFYALPQSPQLFKQLLMMSgFDRYYQIVKCFRDEDLRADRQ-PEFTQIDV 235
Cdd:COG0017 153 HTPIITASATEGGGelfpvDYF-------GKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHlAEFWMIEP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 236 ETSFLTAEEVRAIMEEMIHGLW---LDRLnvdlgkfpmmtwHEAMNRFGSDKPDLRNPLELvdvadilkdvEFKvfhepa 312
Cdd:COG0017 225 EMAFADLEDVMDLAEEMLKYIIkyvLENC------------PEELEFLGRDVERLEKVPES----------PFP------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 313 nspdgRVTvlrvpngttltrkqideYTQFVGIYGAKGLawakinDVNAGlEGVQSPVAKFLNEEVIKaliartnaqtgdi 392
Cdd:COG0017 277 -----RIT-----------------YTEAIEILKKSGE------KVEWG-DDLGTEHERYLGEEFFK------------- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 393 lffgadkwqvvtdsmgalrlkvgrdlnltdlsawKPLWVIDFP-------MFERDEEGNLSAmhhpftspkgltpeelai 465
Cdd:COG0017 315 ----------------------------------KPVFVTDYPkeikafyMKPNPDDPKTVA------------------ 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 466 npvnavanAYDMVINGY-EVGGGSVRIFDPKMQQTVFNILGINEqeqqEKFGFLLDALKFGTPPHAGLAFGLDRLTMLIT 544
Cdd:COG0017 343 --------AFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDP----EDYEWYLDLRRYGSVPHAGFGLGLERLVMWLT 410
|
570
....*....|....
gi 491988310 545 GTENIRDVIAFPKT 558
Cdd:COG0017 411 GLENIREVIPFPRD 424
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
118-559 |
1.71e-35 |
|
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: 135.77 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 118 TEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPMLTKATPEGardylvPSRVHKGKFYA----LPQ 193
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 194 SPQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETSFLTA-EEVRAIMEEMIHGLwLDRLnvdlgkfpmm 271
Cdd:cd00776 77 SPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKYI-FKRV---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 272 twheamnrfgsdkpdLRNPLELVDVADILKDVEFKVfhepaNSPDGRVTvlrvpngttltrkqideYTQFVGIYGAKGla 351
Cdd:cd00776 145 ---------------LERCAKELELVNQLNRELLKP-----LEPFPRIT-----------------YDEAIELLREKG-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 352 waKINDVNAGlEGVQSPVAKFLNEEVIKaliartnaqtgdilffgadkwqvvtdsmgalrlkvgrdlnltdlsawKPLWV 431
Cdd:cd00776 186 --VEEEVKWG-EDLSTEHERLLGEIVKG-----------------------------------------------DPVFV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 432 IDFPMFERdeegnlsamhhPF-TSPKGLTPEelainpvnaVANAYDMVINGY-EVGGGSVRIFDPKMQQTVFNILGINEq 509
Cdd:cd00776 216 TDYPKEIK-----------PFyMKPDDDNPE---------TVESFDLLMPGVgEIVGGSQRIHDYDELEERIKEHGLDP- 274
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 491988310 510 eqqEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTT 559
Cdd:cd00776 275 ---ESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRDP 321
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
308-407 |
3.36e-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: 119.29 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 308 FHEPANsPDGRVTVLRVPNGTTLTRKQIDEYTQFVGIYGAKGLAWAKINDvnaglEGVQSPVAKFLNEEVIKALIARTNA 387
Cdd:pfam02938 1 FSEALK-SGGSVKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEG-----GGHTGPIAKFLTEEEVEKLLEAVGA 74
|
90 100
....*....|....*....|
gi 491988310 388 QTGDILFFGADKWQVVTDSM 407
Cdd:pfam02938 75 EDGDALLFVADKKKTVNKAL 94
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
16-556 |
1.46e-31 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 128.95 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 16 GQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFD-----ERDEALFKIASSLRAEACVQIQGEViardesqinKDMAT 90
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADkkrldLDEEEFEKLHSLVDRGDIVGVTGTP---------GKTKK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 91 GEIEVLVKNVLVYNNAdVLPLDFNQNNTEEQRLKYR--YLDL-RRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPML- 166
Cdd:PLN02502 179 GELSIFPTSFEVLTKC-LLMLPDKYHGLTDQETRYRqrYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLn 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 167 TKATPEGARdylvPSRVHKG----KFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTA 242
Cdd:PLN02502 258 MIAGGAAAR----PFVTHHNdlnmDLY-LRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADY 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 243 EEVRAIMEEMIHGLWLdRLNvdlGKFPMMtwheamnrFGSDKPDLRNPLELVDVADILKDVEFKVFHEPANSPdgrvtvl 322
Cdd:PLN02502 333 NDMMELTEEMVSGMVK-ELT---GSYKIK--------YHGIEIDFTPPFRRISMISLVEEATGIDFPADLKSD------- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 323 rvpngtTLTRKQIDEYTQFVgiygakglawakindvnaglEGVQSP--VAKFLNeEVIKALIARTNAQtgdilffgadkw 400
Cdd:PLN02502 394 ------EANAYLIAACEKFD--------------------VKCPPPqtTGRLLN-ELFEEFLEETLVQ------------ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 401 qvvtdsmgalrlkvgrdlnltdlsawkPLWVIDFPmferdEEgnLSAMHHPFTSPKGLTPEelainpvnavanaYDMVIN 480
Cdd:PLN02502 435 ---------------------------PTFVLDHP-----VE--MSPLAKPHRSKPGLTER-------------FELFIN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 481 GYEVGGGSVRIFDPKMQQTVFnilgiNEQEQQEKFGF----LLD-----ALKFGTPPHAGLAFGLDRLTMLITGTENIRD 551
Cdd:PLN02502 468 GRELANAFSELTDPVDQRERF-----EEQVKQHNAGDdeamALDedfctALEYGLPPTGGWGLGIDRLVMLLTDSASIRD 542
|
....*
gi 491988310 552 VIAFP 556
Cdd:PLN02502 543 VIAFP 547
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
1-558 |
3.91e-31 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 126.38 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 1 MMRTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGV--VQVFFDErDEALFKIASSLRAEACVQIQGEVIA 78
Cdd:PRK03932 1 MMRVSIKDILKGKYVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFkqLQVVKDN-GEEYFEEIKKLTTGSSVIVTGTVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 79 RDESQinkdmatGEIEVLVKNVLVY-NNADVLPLDfNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHG 157
Cdd:PRK03932 80 SPRAG-------QGYELQATKIEVIgEDPEDYPIQ-KKRHSIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 158 FLDIETPMLTKATPEGA----------RDYlvpsrvhKGKFYA----LPQSPQLFKQLLMMsGFDRYYQIVKCFRDEDLR 223
Cdd:PRK03932 152 FVWVDTPIITASDCEGAgelfrvttldLDF-------SKDFFGkeayLTVSGQLYAEAYAM-ALGKVYTFGPTFRAENSN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 224 ADRQ-PEFTQIDVETSFLTAEEVRAIMEEMIHGLW---LDRLNVDLgkfpmmtwhEAMNRFgSDKPDLrnplelvdvaDI 299
Cdd:PRK03932 224 TRRHlAEFWMIEPEMAFADLEDNMDLAEEMLKYVVkyvLENCPDDL---------EFLNRR-VDKGDI----------ER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 300 LKDVefkvfhepANSPDGRVTvlrvpngttltrkqideYTQFVGIYGAKGLAWAkiNDVNAGLEgVQSPVAKFLNEEVIK 379
Cdd:PRK03932 284 LENF--------IESPFPRIT-----------------YTEAIEILQKSGKKFE--FPVEWGDD-LGSEHERYLAEEHFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 380 aliartnaqtgdilffgadkwqvvtdsmgalrlkvgrdlnltdlsawKPLWVIDFPMferdeegNLSA--MHhpftspkg 457
Cdd:PRK03932 336 -----------------------------------------------KPVFVTNYPK-------DIKAfyMR-------- 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 458 ltpeelaINPVNAVANAYDMVINGY-EVGGGSVRIFDP-----KMQQtvfniLGINEqeqqEKFGFLLDALKFGTPPHAG 531
Cdd:PRK03932 354 -------LNPDGKTVAAMDLLAPGIgEIIGGSQREERLdvleaRIKE-----LGLNK----EDYWWYLDLRRYGSVPHSG 417
|
570 580
....*....|....*....|....*..
gi 491988310 532 LAFGLDRLTMLITGTENIRDVIAFPKT 558
Cdd:PRK03932 418 FGLGFERLVAYITGLDNIRDVIPFPRT 444
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
3-556 |
4.65e-29 |
|
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: 120.91 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 3 RTNYCGELNRSH--------VGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDeRDE------ALFK------Ias 62
Cdd:COG1190 35 RTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLR-RDElgeeayELFKlldlgdI-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 63 slraeacVQIQGEVIArdeSQinkdmaTGEIEVLVKNVLVYNNAdVLPL--DFNQNNTEEQRLKYRYLDL-RRPEMAEKL 139
Cdd:COG1190 112 -------VGVEGTVFR---TK------TGELSVKVEELTLLSKS-LRPLpeKFHGLTDPETRYRQRYVDLiVNPEVRETF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 140 KTRAKITSFVRRFMDEHGFLDIETPMLTkATPEGA-------------RD-YLvpsRVhkgkfyalpqSPQLF-KQLLMm 204
Cdd:COG1190 175 RKRSKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaarpfithhnaldMDlYL---RI----------APELYlKRLIV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 205 SGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLWLDRLN----------VDLGK-FPMMTW 273
Cdd:COG1190 240 GGFERVFEIGRNFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAVLGttkvtyqgqeIDLSPpWRRITM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 274 HEAMNRF-GSDKPDLRNPLELVDVADilkdvefkvfhepanspdgrvtvlrvpngttltrkqideytqfvgiygAKGLAW 352
Cdd:COG1190 320 VEAIKEAtGIDVTPLTDDEELRALAK------------------------------------------------ELGIEV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 353 AKindvnaglegvQSPVAKFLNEevikaliartnaqtgdilFFGAdkwqvvtdsmgalrlKVGRDLnltdlsaWKPLWVI 432
Cdd:COG1190 352 DP-----------GWGRGKLIDE------------------LFEE---------------LVEPKL-------IQPTFVT 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 433 DFPmferdeegnlsamhhPFTSPkgltpeeLA-INPVN-AVANAYDMVINGYEVGGGsvriF----DPKMQQTVFNilgi 506
Cdd:COG1190 381 DYP---------------VEVSP-------LAkRHRDDpGLTERFELFIAGREIANA----FselnDPIDQRERFE---- 430
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 507 nEQEQQEKFG----------FLlDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFP 556
Cdd:COG1190 431 -EQLELKAAGddeampmdedFL-RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
19-556 |
3.61e-27 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 116.29 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIR----DREGVVQVFFDERDEALFKIASSLRAeacvqiqGEVIARDesQINKDMATGEIE 94
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRsngnELQVVGQVGEHFTREDLKKLKVSLRV-------GDIIGAD--GVPCRMQRGELS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 95 VLVKNVLV---YNNAD--VLP--LDFNQNNTEEQRLKYRYLDL-RRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPML 166
Cdd:PTZ00385 181 VAASRMLIlspYVCTDqvVCPnlRGFTVLQDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 167 -TKATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEV 245
Cdd:PTZ00385 261 hTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 246 RAIMEEMIHGLWLdRLNvdlGKFPMMTWHEamNRFGSDKP-DLRNPLELVDVADILKD---VEFKvfhePANSpdgrvtv 321
Cdd:PTZ00385 340 MPMTEDIFRQLAM-RVN---GTTVVQIYPE--NAHGNPVTvDLGKPFRRVSVYDEIQRmsgVEFP----PPNE------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 322 LRVPngttltrkqideytqfvgiygaKGLAWAKINDVNaglEGVQSPVakflneevikaliARTNAQTGDILFfgadkwq 401
Cdd:PTZ00385 403 LNTP----------------------KGIAYMSVVMLR---YNIPLPP-------------VRTAAKMFEKLI------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 402 vvtdsmgalrlkvgrDLNLTDlSAWKPLWVIDFPMFerdeegnLSAMHHPFTSPKGLtpeelainpvnavANAYDMVING 481
Cdd:PTZ00385 438 ---------------DFFITD-RVVEPTFVMDHPLF-------MSPLAKEQVSRPGL-------------AERFELFVNG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 482 YEVGGGSVRIFDP-----KMQQTVFNILGINEQEQ--QEKFgflLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIA 554
Cdd:PTZ00385 482 IEYCNAYSELNDPheqyhRFQQQLVDRQGGDEEAMplDETF---LKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGII 558
|
..
gi 491988310 555 FP 556
Cdd:PTZ00385 559 FP 560
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
19-104 |
4.45e-27 |
|
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: 104.57 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEA-LFKIASSLRAEACVQIQGEVIARDEsqinKDMATGEIEVLV 97
Cdd:cd04100 2 VTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGeFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQA 77
|
....*..
gi 491988310 98 KNVLVYN 104
Cdd:cd04100 78 EELEVLS 84
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
16-556 |
3.01e-26 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 112.49 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 16 GQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFD-----ERDEALFK------IasslraeacVQIQGEVIARDesqi 84
Cdd:PRK00484 54 EIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSkddvgEEALEAFKkldlgdI---------IGVEGTLFKTK---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 85 nkdmaTGEIEVLVKNVLVYNNAdVLPL--------DfnqnntEEQRLKYRYLDL-RRPEMAEKLKTRAKITSFVRRFMDE 155
Cdd:PRK00484 121 -----TGELSVKATELTLLTKS-LRPLpdkfhgltD------VETRYRQRYVDLiVNPESRETFRKRSKIISAIRRFLDN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 156 HGFLDIETPMLtKATPEG--AR---------D---YLvpsRVhkgkfyalpqSPQLF-KQLLmMSGFDRYYQIVKCFRDE 220
Cdd:PRK00484 189 RGFLEVETPML-QPIAGGaaARpfithhnalDidlYL---RI----------APELYlKRLI-VGGFERVYEIGRNFRNE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 221 DLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLWLDRLN----------VDLGK-FPMMTWHEAMNRFGSDKPDLRN 289
Cdd:PRK00484 254 GIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAVLGttkvtyqgteIDFGPpFKRLTMVDAIKEYTGVDFDDMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 290 PLELVDVADilkdvefkvfhepanspdgrvtvlrvpngttltrkqideytqfvgiygAKGLAWAKindvnaglegvQSPV 369
Cdd:PRK00484 334 DEEARALAK------------------------------------------------ELGIEVEK-----------SWGL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 370 AKFLNEevikaliartnaqtgdilFFGAdkwqvvtdsmgalrlKVGRDLnltdlsaWKPLWVIDFPmferdEEgnlsamh 449
Cdd:PRK00484 355 GKLINE------------------LFEE---------------FVEPKL-------IQPTFITDYP-----VE------- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 450 hpfTSPkgltpeeLA----INPvnAVANAYDMVINGYEVGGGsvriF----DPKMQQTVFnilginEQEQQEK------- 514
Cdd:PRK00484 383 ---ISP-------LAkrhrEDP--GLTERFELFIGGREIANA----FselnDPIDQRERF------EAQVEAKeagddea 440
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 491988310 515 ------FgflLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFP 556
Cdd:PRK00484 441 mfmdedF---LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
133-556 |
5.36e-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: 108.83 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 133 PEMAEKLKTRAKITSFVRRFMDEHGFLDIETPMLtKATPEG--ARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRY 210
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 211 YQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRAIMEEMIHGLwLDRLNvdlGKFPmmtwheamNRFGSDKPDLRNP 290
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGL-VKKIN---GKTK--------IEYGGKELDFTPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 291 LELVDVADILKDVefkvfhepanspdgrvtvlrvpngttlTRKQIDEYTQFvgiygaKGLAWAKINDVNAGLEGV-QSPV 369
Cdd:cd00775 148 FKRVTMVDALKEK---------------------------TGIDFPELDLE------QPEELAKLLAKLIKEKIEkPRTL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 370 AKFLNEevikaliartnaqtgdilFFGadkwQVVTDSMgalrlkvgrdlnltdlsaWKPLWVIDFPMferdEEGNLSAMH 449
Cdd:cd00775 195 GKLLDK------------------LFE----EFVEPTL------------------IQPTFIIDHPV----EISPLAKRH 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 450 HpftSPKGLTPEelainpvnavanaYDMVINGYEVGGGSVRIFDPKMQ------QTVFNILGINE-QEQQEKFgflLDAL 522
Cdd:cd00775 231 R---SNPGLTER-------------FELFICGKEIANAYTELNDPFDQrerfeeQAKQKEAGDDEaMMMDEDF---VTAL 291
|
410 420 430
....*....|....*....|....*....|....
gi 491988310 523 KFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFP 556
Cdd:cd00775 292 EYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
8-557 |
5.71e-26 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 111.72 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 8 GELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQ-VFFDERDE---ALFKIASSLRAEACVQIQGEVIARDESQ 83
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcVVFVSEVTvskGMVKYAKQLSRESVVDVEGVVSVPKKPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 84 inkDMATGEIEVLVKNVLVYNNAD-VLPL----------DFNQN-NTEEQ--------RLKYRYLDLRRPEMAEKLKTRA 143
Cdd:PLN02850 153 ---KGTTQQVEIQVRKIYCVSKALaTLPFnvedaarsesEIEKAlQTGEQlvrvgqdtRLNNRVLDLRTPANQAIFRIQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 144 KITSFVRRFMDEHGFLDIETPMLTKATPEGAR-----DYlvpsrvhKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFR 218
Cdd:PLN02850 230 QVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDY-------KGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 219 DEDLRADRQ-PEFTQIDVEtsfltaeevraiMEemIHGLWLDRLNVDLGKFPMMtwheamnrFgsDKPDLRNPLELvdvA 297
Cdd:PLN02850 303 AEDSFTHRHlCEFTGLDLE------------ME--IKEHYSEVLDVVDELFVAI--------F--DGLNERCKKEL---E 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 298 DILKDVEFkvfhEPanspdgrVTVLRvpngTTLTrkqideytqfvgiygakgLAWAkindvnaglEGVQspvakFLNEEv 377
Cdd:PLN02850 356 AIREQYPF----EP-------LKYLP----KTLR------------------LTFA---------EGIQ-----MLKEA- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 378 ikaliartnaqtGDIlffgadkwqvvTDSMGALRLKVGRDLNLTDLSAWKplwvIDFPMFERDEegnlSAMHHPFTSPkg 457
Cdd:PLN02850 388 ------------GVE-----------VDPLGDLNTESERKLGQLVKEKYG----TDFYILHRYP----LAVRPFYTMP-- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 458 lTPEelaiNPvnAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEkfgfLLDALKFGTPPHAGLAFGLD 537
Cdd:PLN02850 435 -CPD----DP--KYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST----YIDSFRYGAPPHGGFGVGLE 503
|
570 580
....*....|....*....|
gi 491988310 538 RLTMLITGTENIRDVIAFPK 557
Cdd:PLN02850 504 RVVMLFCGLNNIRKTSLFPR 523
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
141-257 |
7.44e-25 |
|
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: 102.58 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 141 TRAKITSFVRRFMDEHGFLDIETPMLTKATPEGARD----YLVPSRVHKGKFYALPQSPQLFKQLLMMS----GFDRYYQ 212
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491988310 213 IVKCFRDEDLRAD--RQPEFTQIDVETSFLTAEEvRAIMEEMIHGLW 257
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEE-ASEFEELIELTE 126
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
15-557 |
2.77e-24 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 107.00 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 15 VGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFF---DERDEALFKIASSLRAEACVQIQGEVIARDESQINKDMAtg 91
Cdd:PTZ00401 77 VDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAaveGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHS-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 92 EIEVLVKNVLVYNNA-DVLPL---DFNQNNTEE-------QRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLD 160
Cdd:PTZ00401 155 DIELKVKKIHTVTESlRTLPFtleDASRKESDEgakvnfdTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 161 IETPMLTKATPEGARDylVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETS- 238
Cdd:PTZ00401 235 IHSPKIINAPSEGGAN--VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRi 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 239 -------FLTAEEVRAIMEEMIHGLWLDRLNVdLGKFPM--MTWH---EAMNRFGsdkpdlrnplelvdVADILKDVE-F 305
Cdd:PTZ00401 313 nehyyevLDLAESLFNYIFERLATHTKELKAV-CQQYPFepLVWKltpERMKELG--------------VGVISEGVEpT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 306 KVFHEPANSPDGRVTVLRVPNGTTLTRKQIDEytqfvgiygakglAWAKINDVNAglegvqspvakfLNEEVIKALIart 385
Cdd:PTZ00401 378 DKYQARVHNMDSRMLRINYMHCIELLNTVLEE-------------KMAPTDDINT------------TNEKLLGKLV--- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 386 naqtgdilffgadkwqvvtdsmgalRLKVGRDLNLTDL--SAWKPLWVIDFPMFERdeegnlsamhhpFTspkgltpeel 463
Cdd:PTZ00401 430 -------------------------KERYGTDFFISDRfpSSARPFYTMECKDDER------------FT---------- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 464 ainpvnavaNAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQEQQEkfgfLLDALKFGTPPHAGLAFGLDRLTMLI 543
Cdd:PTZ00401 463 ---------NSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLY 529
|
570
....*....|....
gi 491988310 544 TGTENIRDVIAFPK 557
Cdd:PTZ00401 530 LGLSNVRLASLFPR 543
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
91-561 |
2.43e-20 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 94.69 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 91 GEIEVLVKNVLVYNNA-DVLPLDFNQNNTEeQRLKYRYLDLRRPEMAEK-LKTRAKITSFVRRFMDEHGFLDIETPMLT- 167
Cdd:PTZ00417 204 GELSIFPKETIILSPClHMLPMKYGLKDTE-IRYRQRYLDLMINESTRStFITRTKIINYLRNFLNDRGFIEVETPTMNl 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 168 KATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFltaeevrA 247
Cdd:PTZ00417 283 VAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAY-------A 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 248 IMEEMIHglWLDRLNVDLGKFPMMTWHEAMNRFGSDKP----DLRNPLELVDVADILKDVEFKVFHEPANSPDgrvTVLR 323
Cdd:PTZ00417 355 DFYDLIK--WSEDFFSQLVMHLFGTYKILYNKDGPEKDpieiDFTPPYPKVSIVEELEKLTNTKLEQPFDSPE---TINK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 324 VPNgttltrkQIDEYTqfvgiygakglawakindvnagLEGVQSPVAKFLNEEVIKALIARTNAQtgdilffgadkwqvv 403
Cdd:PTZ00417 430 MIN-------LIKENK----------------------IEMPNPPTAAKLLDQLASHFIENKYPN--------------- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 404 tdsmgalrlkvgrdlnltdlsawKPLWVIDFPMFerdeegnLSAMHHPFTSPKGLTpEELainpvnavanayDMVINGYE 483
Cdd:PTZ00417 466 -----------------------KPFFIIEHPQI-------MSPLAKYHRSKPGLT-ERL------------EMFICGKE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 484 VGGGSVRIFDPKMQQTVFNiLGINEQEQQEKFGFLLDA-----LKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKT 558
Cdd:PTZ00417 503 VLNAYTELNDPFKQKECFS-AQQKDREKGDAEAFQFDAafctsLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFPTM 581
|
...
gi 491988310 559 TAA 561
Cdd:PTZ00417 582 RPA 584
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
16-112 |
1.15e-19 |
|
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: 84.29 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 16 GQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFF--DERDEALFKIASSLRAEACVQIQGEVIARDEsqinkdmATGEI 93
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTApkKKVDKELFKTVRKLSRESVISVTGTVKAEPK-------APNGV 84
|
90 100
....*....|....*....|
gi 491988310 94 EVLVKNVLVYNNAD-VLPLD 112
Cdd:cd04316 85 EIIPEEIEVLSEAKtPLPLD 104
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
3-556 |
8.77e-19 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 90.79 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 3 RTNYCGELNRSHVGQNVTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFD-----ERDEALFKIASSLRAEacVQIQGEVI 77
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDasrleQGSLADFRAAVDLGDL--VEVTGTMG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 78 ARDesqinkdmaTGEIEVLVKNVLVynNADVL-PL-DFNQNNTE-EQRLKYRYLDLR-RPEMAEKLKTRAKITSFVRRFM 153
Cdd:PRK02983 716 TSR---------NGTLSLLVTSWRL--AGKCLrPLpDKWKGLTDpEARVRQRYLDLAvNPEARDLLRARSAVVRAVRETL 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 154 DEHGFLDIETPMLTK----ATpegARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPE 229
Cdd:PRK02983 785 VARGFLEVETPILQQvhggAN---ARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 230 FTQIDVETSFLTAEEVRAIMEEMIHglwldrlnvdlgkfpmmtwHEAMNRFGSD---KPDLRNPLELVDVADilkdvEFK 306
Cdd:PRK02983 861 FTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHGAPvvmRPDGDGVLEPVDISG-----PWP 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 307 VfhepanspdgrVTVlrvpngttltrkqideytqfvgiYGAkglawakindvnaglegvqspVAKFLNEEVIkaliARTN 386
Cdd:PRK02983 917 V-----------VTV-----------------------HDA---------------------VSEALGEEID----PDTP 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 387 AQTgdiLFFGADKWQVVTD---SMGALRLKVGRDL--NLTDLsawkPLWVIDFPmferdeegnLSamhhpfTSPkgLTPE 461
Cdd:PRK02983 938 LAE---LRKLCDAAGIPYRtdwDAGAVVLELYEHLveDRTTF----PTFYTDFP---------TS------VSP--LTRP 993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 462 ELAInPvnAVANAYDMVINGYEVGGGSVRIFDPKMQ------QTVFNILGINE-QEQQEKFgflLDALKFGTPPHAGLAF 534
Cdd:PRK02983 994 HRSD-P--GLAERWDLVAWGVELGTAYSELTDPVEQrrrlteQSLLAAGGDPEaMELDEDF---LQALEYAMPPTGGLGM 1067
|
570 580
....*....|....*....|..
gi 491988310 535 GLDRLTMLITGTeNIRDVIAFP 556
Cdd:PRK02983 1068 GVDRLVMLLTGR-SIRETLPFP 1088
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
120-557 |
7.16e-18 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 85.07 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 120 EQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPMLTKATPEGARD-----YLVPSRVHKGKFYALPQS 194
Cdd:PRK06462 11 EEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 195 PQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQP---EFTQIDVETSFLTAEEVRAIMEEMIHGLwLDRLnvdlgkfpmM 271
Cdd:PRK06462 91 MILHKQ-LALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYL-VKEL---------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 272 TWHEA-MNRFGSDKPDLRNPLELVDVADILKDVEfkvfhepanspdgrvtvlrvpngtTLTRKQIDEYTqfvgiYGAKGl 350
Cdd:PRK06462 160 EEHEDeLEFFGRDLPHLKRPFKRITHKEAVEILN------------------------EEGCRGIDLEE-----LGSEG- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 351 awakindvnaglEGVQSPVAKflneevikaliartnaqtgdilffgadkwqvvtdsmgalrlkvgrdlnltdlsawKPLW 430
Cdd:PRK06462 210 ------------EKSLSEHFE-------------------------------------------------------EPFW 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 431 VIDFPMFER---DEEgnlsamhhpftspkglTPEElainpvNAVANAYDMVI-NGY-EVGGGSVRIFDPKmqQTVFNILg 505
Cdd:PRK06462 223 IIDIPKGSRefyDRE----------------DPER------PGVLRNYDLLLpEGYgEAVSGGEREYEYE--EIVERIR- 277
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 491988310 506 iNEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPK 557
Cdd:PRK06462 278 -EHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
90-556 |
2.96e-16 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 81.65 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 90 TGEIEVLVKNVLVYNNA-DVLPLDFNQNNTEEQRLKYRYLDL-RRPEMAEKLKTRAKITSFVRRFMDEHGFLDIETPMLt 167
Cdd:PRK12445 133 TGELSIHCTELRLLTKAlRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 168 KATPEGA--RDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEV 245
Cdd:PRK12445 212 QVIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 246 RAIMEEMIHGLwldrLNVDLGKFPMMtwheamnrFGSDKPDLRNPLELVDVADILKDvefkvfHEPanspdgrvtvlrvp 325
Cdd:PRK12445 291 IELTESLFRTL----AQEVLGTTKVT--------YGEHVFDFGKPFEKLTMREAIKK------YRP-------------- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 326 ngttltrkqideytqfvgiygakglawakindvnaglegvQSPVAKFLNEEVIKALIARTNAQtgdilffgadkwqvVTD 405
Cdd:PRK12445 339 ----------------------------------------ETDMADLDNFDAAKALAESIGIT--------------VEK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 406 SMGALRLKVGRDLNLTDLSAWKPLWVIDFPmferdeegnlsAMHHPFTSPKGLTPEelainpvnaVANAYDMVINGYEVG 485
Cdd:PRK12445 365 SWGLGRIVTEIFDEVAEAHLIQPTFITEYP-----------AEVSPLARRNDVNPE---------ITDRFEFFIGGREIG 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491988310 486 GGSVRIFDPKMQQTVFNIlGINEQEQQEKFGFLLD-----ALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFP 556
Cdd:PRK12445 425 NGFSELNDAEDQAERFQE-QVNAKAAGDDEAMFYDedyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
19-102 |
1.51e-13 |
|
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: 65.72 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRV-RNLGRFIFMQIRDREGVVQVFFDerDEALFKIASSLRAEACVQIQGEVIARDEsqinkdmatGEIEVLV 97
Cdd:pfam01336 1 VTVAGRVTSIrRSGGKLLFLTLRDGTGSIQVVVF--KEEAEKLAKKLKEGDVVRVTGKVKKRKG---------GELELVV 69
|
....*
gi 491988310 98 KNVLV 102
Cdd:pfam01336 70 EEIEL 74
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
19-128 |
4.82e-11 |
|
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: 59.85 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIRDREGVVQ-VFFDERDEALFKIASSLRAEACVQIQGEVIARDEsqinkdmATGEIEVLV 97
Cdd:cd04319 2 VTLAGWVYRKREVGKKAFIVLRDSTGIVQaVFSKDLNEEAYREAKKVGIESSVIVEGAVKADPR-------APGGAEVHG 74
|
90 100 110
....*....|....*....|....*....|.
gi 491988310 98 KNVLVYNNADVLPLdfNQNNTEEQRLKYRYL 128
Cdd:cd04319 75 EKLEIIQNVEFFPI--TEDASDEFLLDVRHL 103
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
19-83 |
4.85e-11 |
|
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: 59.17 E-value: 4.85e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERDEALFKIASSLRAEACVQIQGEVIARDESQ 83
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKEDPRAK 66
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
512-562 |
2.98e-09 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 59.60 E-value: 2.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491988310 512 QEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAA 562
Cdd:PLN02603 513 KESYWWYLDLRRYGSVPHAGFGLGFERLVQFATGIDNIRDAIPFPRVPGSA 563
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
452-557 |
3.41e-09 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 59.65 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 452 FTSPKGLTPEELAINPVNAVANAYDMVINGY-EVGGGSVR-----IFDPKMQQTVFNIlgineqeqqEKFGFLLDALKFG 525
Cdd:PTZ00425 477 YNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIgEVIGGSQRednleRLDKMIKEKKLNM---------ESYWWYRQLRKFG 547
|
90 100 110
....*....|....*....|....*....|..
gi 491988310 526 TPPHAGLAFGLDRLTMLITGTENIRDVIAFPK 557
Cdd:PTZ00425 548 SHPHAGFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
452-562 |
9.41e-08 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 54.88 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 452 FTSPKGLTPEELAINPVNAVANAYDMVI-NGYEVGGGSvrifdpkMQQTVFNILG--INEQE-QQEKFGFLLDALKFGTP 527
Cdd:PLN02532 524 YNYPKELKPFYVRLNDDGKTVAAFDLVVpKVGTVITGS-------QNEERMDILNarIEELGlPREQYEWYLDLRRHGTV 596
|
90 100 110
....*....|....*....|....*....|....*
gi 491988310 528 PHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAA 562
Cdd:PLN02532 597 KHSGFSLGFELMVLFATGLPDVRDAIPFPRSWGKA 631
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
135-552 |
1.82e-07 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 53.01 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 135 MAEKLKTRAKITSFVRRFMDEHGFLDIETPMLTKATPEGAR------DYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFD 208
Cdd:PRK09350 1 SIPNLLKRAKIIAEIRRFFADRGVLEVETPILSQATVTDIHlvpfetRFVGPGASQGKTLW-LMTSPEYHMKRLLAAGSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 209 RYYQIVKCFRDEDLRADRQPEFTqidvetsfltaeevraimeemihglwldrlnvdlgkfpMMTWHeamnRFGSDKPDLR 288
Cdd:PRK09350 80 PIFQICKSFRNEEAGRYHNPEFT--------------------------------------MLEWY----RPHYDMYRLM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 289 NplelvDVADILKDVefkvfhepanspdgrvtvLRVPNGTTLTRKQIdeYTQFVGIYG-AKGLAWAKINDVNAGLEGVQS 367
Cdd:PRK09350 118 N-----EVDDLLQQV------------------LDCEPAESLSYQQA--FLRYLGIDPlSADKTQLREVAAKLGLSNIAD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 368 PvakflnEEVIKALIARtnaqtgdiLFfgadkwqvvtdSMGALRlKVGRDlnltdlsawKPLWVIDFPmferdeeGNLSA 447
Cdd:PRK09350 173 E------EEDRDTLLQL--------LF-----------TFGVEP-NIGKE---------KPTFVYHFP-------ASQAA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 448 mhhpftspkgltpeeLA-INPV-NAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFnilgINEQEQQEKFGF-------- 517
Cdd:PRK09350 211 ---------------LAkISTEdHRVAERFEVYFKGIELANGFHELTDAREQRQRF----EQDNRKRAARGLpqqpiden 271
|
410 420 430
....*....|....*....|....*....|....*
gi 491988310 518 LLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDV 552
Cdd:PRK09350 272 LIAALEAGLPDCSGVALGVDRLIMLALGAESISEV 306
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
152-554 |
2.37e-07 |
|
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: 52.55 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 152 FMDEHGFLDIETPMLTKAT-PEGARDYL----VPSRVHKGKFYaLPQSPQLF-KQLLMmSGFDRYYQIVKCFRDEDLRAD 225
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFatefVGPDGQGRPLY-LQTSPEYAmKRLLA-AGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 226 RQPEFTQID---VETSFltaeevRAIMEEMihglwlDRLNVDLGKFP-----MMTWHEAMNRFGSdkpdlrnplelvdvA 297
Cdd:TIGR00462 79 HNPEFTMLEwyrPGFDY------HDLMDEV------EALLQELLGDPfapaeRLSYQEAFLRYAG--------------I 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 298 DILkdvefkvfhepanspdgrvtvlrvpngtTLTRKQIDEYTQFVGIYGAKGLAWAKINDvnaglegvqspvaKFLNEEV 377
Cdd:TIGR00462 133 DPL----------------------------TASLAELQAAAAAHGIRASEEDDRDDLLD-------------LLFSEKV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 378 IKALiartnaqtgdilffgadkwqvvtdsmgalrlkvGRDlnltdlsawKPLWVIDFPmferdeeGNLSAmhhpftspkg 457
Cdd:TIGR00462 172 EPHL---------------------------------GFG---------RPTFLYDYP-------ASQAA---------- 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 458 ltpeeLA-INPVNA-VANAYDMVINGYEVGGGSVRIFDPKMQQTVFnilginEQEQQEKFG----------FLLDALKFG 525
Cdd:TIGR00462 193 -----LArISPDDPrVAERFELYIKGLELANGFHELTDAAEQRRRF------EADNALRKAlglprypldeRFLAALEAG 261
|
410 420
....*....|....*....|....*....
gi 491988310 526 TPPHAGLAFGLDRLTMLITGTENIRDVIA 554
Cdd:TIGR00462 262 LPECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
19-130 |
1.14e-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: 47.47 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIRDREGVVQVFFDERD---EALFKIASSLRAEACVQIQGEVIArdeSQinkdmaTGEIEV 95
Cdd:cd04322 2 VSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDlgeEEFEDFKKLLDLGDIIGVTGTPFK---TK------TGELSI 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 491988310 96 LVKNVLVYNNA-DVLPLDFNQNNTEEQRLKYRYLDL 130
Cdd:cd04322 73 FVKEFTLLSKSlRPLPEKFHGLTDVETRYRQRYLDL 108
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
452-564 |
1.15e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 51.53 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 452 FTSPKGLTPEELAINPVNAVANAYDMVINGY-EVGGGSVRIFDPKMQQTVFNILGIneqeQQEKFGFLLDALKFGTPPHA 530
Cdd:PLN02221 463 YNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYLDLRRYGTVKHC 538
|
90 100 110
....*....|....*....|....*....|....
gi 491988310 531 GLAFGLDRLTMLITGTENIRDVIAFPKTTAAACL 564
Cdd:PLN02221 539 GFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
16-174 |
9.99e-06 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 16 GQNVTLSGWVHRVRNLGR--FIFMQIRDRE--GVVQVFFDErdeALFKIASSLRAEACVQIQGEVIARDESQINKDmatg 91
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGKgtFAFLEVNDGScpANLQVMVDS---SLYDLSTLVATGTCVTVDGVLKVPPEGKGTKQ---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 92 EIEVLVKNVLvynnaDVLPLDFNQNNTEEQRLKYRYLdlrRPEMaeKLKTRAKITSFVRR-----------FMDEHGFLD 160
Cdd:PLN02221 123 KIELSVEKVI-----DVGTVDPTKYPLPKTKLTLEFL---RDVL--HLRSRTNSISAVARirnalafathsFFQEHSFLY 192
|
170
....*....|....
gi 491988310 161 IETPMLTKATPEGA 174
Cdd:PLN02221 193 IHTPIITTSDCEGA 206
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-104 |
5.85e-05 |
|
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: 41.92 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 18 NVTLSGWVHRVRNL-GRFIFMQIRDREG-VVQV--FFDERDEALFKiasSLRAEACVQIQGEVIARDESQINKdmaTGEI 93
Cdd:cd04321 1 KVTLNGWIDRKPRIvKKLSFADLRDPNGdIIQLvsTAKKDAFSLLK---SITAESPVQVRGKLQLKEAKSSEK---NDEW 74
|
90
....*....|.
gi 491988310 94 EVLVKNVLVYN 104
Cdd:cd04321 75 ELVVDDIQTLN 85
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
19-103 |
1.47e-04 |
|
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: 40.63 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491988310 19 VTLSGWVHRVRNLGRFIFMQIRDreGV----VQVFFDErDEALFKIASSLRAEACVQIQGEVIardESQINKdmatGEIE 94
Cdd:cd04318 2 VTVNGWVRSVRDSKKISFIELND--GSclknLQVVVDK-ELTNFKEILKLSTGSSIRVEGVLV---KSPGAK----QPFE 71
|
....*....
gi 491988310 95 VLVKNVLVY 103
Cdd:cd04318 72 LQAEKIEVL 80
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-76 |
3.73e-03 |
|
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.
Pssm-ID: 239815 [Multi-domain] Cd Length: 102 Bit Score: 37.16 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491988310 18 NVTLSGWVHRVRNLG-RFIFMQIRDR----EGVVQVFFDERDEALFKIASSLRAEACVQIQGEV 76
Cdd:cd04320 1 EVLIRARVHTSRAQGaKLAFLVLRQQgytiQGVLAASAEGVSKQMVKWAGSLSKESIVDVEGTV 64
|
|
| |
