|
Name |
Accession |
Description |
Interval |
E-value |
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
1-588 |
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: 1124.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 1 MRTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR-ADALKLASELRNEFCIQVTGTVRARD 79
Cdd:COG0173 2 YRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDsAEAFEKAEKLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 80 AKNVNAEMATGEIEVLASDLTIINRSDSLPL---DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHG 156
Cdd:COG0173 82 EGTVNPKLPTGEIEVLASELEILNKAKTPPFqidDDTDVS-EELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 157 FLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVET 236
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 237 SFMTAPQVREVMEALVRNLWLEVKGVDL-GDFPIMTFAEAERRYGSDKPDLRNPMELVDVADLVKDVEFAVFSGPANdAK 315
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGVELpTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAE-NG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 316 GRVAALRVPGGAALSRKQIDDYGNFIKIYGAKGLAYIKVTErakglEGITSPVAKFLNAEIVEAILARTGAQDGDMIFFG 395
Cdd:COG0173 320 GRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNE-----DGLKSPIAKFLSEEELAAILERLGAKPGDLIFFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 396 ADNKKVVADAMGALRLKLGKDLNITDEAKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTAPKDMTAAELKAAPEDAVANAY 474
Cdd:COG0173 395 ADKPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEyDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 475 DMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAF 554
Cdd:COG0173 475 DLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
570 580 590
....*....|....*....|....*....|....
gi 489125063 555 PKTTAAACLMTEAPSFANEAALAELSIQVVKKAE 588
Cdd:COG0173 555 PKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
1-587 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 1123.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 1 MRTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDrADALKLASELRNEFCIQVTGTVRARDA 80
Cdd:PRK00476 3 MRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD-AEAFEVAESLRSEYVIQVTGTVRARPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 81 KNVNAEMATGEIEVLASDLTIINRSDSLPL---DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGF 157
Cdd:PRK00476 82 GTVNPNLPTGEIEVLASELEVLNKSKTLPFpidDEEDVS-EELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 158 LDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETS 237
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 238 FMTAPQVREVMEALVRNLWLEVKGVDLGD-FPIMTFAEAERRYGSDKPDLRNPMELVDVADLVKDVEFAVFSGPANDaKG 316
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLGVDLPTpFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAAND-GG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 317 RVAALRVPGGAA-LSRKQIDDYGNFIKIYGAKGLAYIKVTErakglEGITSPVAKFLNAEIVEAILARTGAQDGDMIFFG 395
Cdd:PRK00476 320 RVKAIRVPGGAAqLSRKQIDELTEFAKIYGAKGLAYIKVNE-----DGLKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 396 ADNKKVVADAMGALRLKLGKDLNITDEAKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTAPKDMTAAEL-KAAPEDAVANA 473
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEyDEEEGRWVAAHHPFTMPKDEDLDELeTTDPGKARAYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 474 YDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:PRK00476 475 YDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
570 580 590
....*....|....*....|....*....|....
gi 489125063 554 FPKTTAAACLMTEAPSFANEAALAELSIQVVKKA 587
Cdd:PRK00476 555 FPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
1-586 |
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: 990.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 1 MRTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDrADALKLASELRNEFCIQVTGTVRARDA 80
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD-ADALKLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 81 KNVNAEMATGEIEVLASDLTIINRSDSLPLDSNHVNTEEA-RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAEEEvRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 160 IETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFM 239
Cdd:TIGR00459 160 IETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSFM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 240 TAPQVREVMEALVRNLWLEVKGVDLG-DFPIMTFAEAERRYGSDKPDLRNPMELVDVADLVKDVEFAVFSGPANDaKGRV 318
Cdd:TIGR00459 240 TQEDVMELIEKLVSHVFLEVKGIDLKkPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLIND-GGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 319 AALRVPGGAA-LSRKQIDDYGNFIKIYGAKGLAYIKVTERakgleGITSPVAKFLNAEIVEAILARTGAQDGDMIFFGAD 397
Cdd:TIGR00459 319 KAIRVPGGWAeLSRKSIKELRKFAKEYGAKGLAYLKVNED-----GINSPIKKFLDEKKGKILLERTDAQNGDILLFGAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 398 NKKVVADAMGALRLKLGKDLNITDEAKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPKDMTAAELKAAPEDAVANAYDMV 477
Cdd:TIGR00459 394 SKKIVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKDKEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 478 INGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKT 557
Cdd:TIGR00459 474 LNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKT 553
|
570 580 590
....*....|....*....|....*....|
gi 489125063 558 TAAACLMTEAPSFANEAALAELSIQ-VVKK 586
Cdd:TIGR00459 554 TAAACLMTEAPSFIDEKQLEELSIKyVVKK 583
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
2-585 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 691.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 2 RTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA-DALKLASELRNEFCIQVTGTVRARDA 80
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFpEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 81 KNVNAEMATGEIEVLASDLTIINR-SDSLPL------DSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFM- 152
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVvTKSLPFlvttadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 153 DDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQI 232
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 233 DVETSFMTAPQVREVMEALVRNLWLEVKGVDLGD-FPIMTFAEAERRYGSDKPDLRNPMELVDVADLVKDVEFAVFSGPA 311
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNpFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 312 NDAkGRVAALRVPGGAALS----RKQIDDYGNFIKiYGAKGLAYIKVTERAKgLEGITSPVAKfLNAEIVEAILARTGAQ 387
Cdd:PLN02903 379 ESG-GVVKAICVPDGKKISnntaLKKGDIYNEAIK-SGAKGLAFLKVLDDGE-LEGIKALVES-LSPEQAEQLLAACGAG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 388 DGDMIFFGADNKKVVADAMGALRLKLGKDLNITDEAKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTAPKDMTAAELKAAP 466
Cdd:PLN02903 455 PGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEwNEDEQRLEALHHPFTAPNPEDMGDLSSAR 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 467 edavANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTD 546
Cdd:PLN02903 535 ----ALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAK 610
|
570 580 590
....*....|....*....|....*....|....*....
gi 489125063 547 NIRDVIAFPKTTAAACLMTEAPSFANEAALAELSIQVVK 585
Cdd:PLN02903 611 SIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIASTA 649
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
5-581 |
0e+00 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 549.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 5 YCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA--DALKLASELRNEFCIQVTGTVRARDAKN 82
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAApaDVYELAASLRAEFCVALQGEVQKRLEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 83 VNAEMATGEIEVLASDLTIINRSDSLPL--------------DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLV 148
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFaisdkamtagagsaGADAVN-EDLRLQYRYLDIRRPAMQDHLAKRHRIIKCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 149 RRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPE 228
Cdd:PRK12820 167 RDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 229 FTQIDVETSFMTAPQVREVMEALVRNLWlEVKGVDLG-DFPIMTFAEAERRYGSDKPDLRNPMELVDVADLVKDVEFAVF 307
Cdd:PRK12820 247 FTQLDIEASFIDEEFIFELIEELTARMF-AIGGIALPrPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 308 SGPANDAkGRVAALRVPGGAALSRKQI--DDYGNFI-KIYGAKGLAYIKVTErakglEGITSPVAKFLNAEIVEAILART 384
Cdd:PRK12820 326 KQILQRG-GRIKGINIKGQSEKLSKNVlqNEYAKEIaPSFGAKGMTWMRAEA-----GGLDSNIVQFFSADEKEALKRRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 385 GAQDGDMIFFGAD-NKKVVADAMGALRLKLGKDLNITDEAKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAP--KDMTAAE 461
Cdd:PRK12820 400 HAEDGDVIIMIADaSCAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGVTSSHHPFTAPdrEDFDPGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 462 LKAApEDAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTML 541
Cdd:PRK12820 480 IEEL-LDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSM 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 489125063 542 LTGTDNIRDVIAFPKTTAAACLMTEAPSFANEAALAELSI 581
Cdd:PRK12820 559 ILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLAELGL 598
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
138-558 |
1.51e-160 |
|
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: 459.73 E-value: 1.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 138 LKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFR 217
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 218 DEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRNLWLEVKGVDL-GDFPIMTFAEAERRYGsdkpdlrnpmelvdva 296
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELtTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 297 dlvkdvefavfsgpandakgrvaalrvpggaalsrkqiddygnfikiygakglayikvterakglegitspvakflnaei 376
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 377 veailartgaqdgdmiffgadnkkvvadamgalrlklgkdlnitdeakWAPLWVIDFPMFE-DDGEGGLTAMHHPFTAPK 455
Cdd:cd00777 145 ------------------------------------------------FKFLWIVDFPLFEwDEEEGRLVSAHHPFTAPK 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 456 DMTAAELKAAPEDAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGL 535
Cdd:cd00777 177 EEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|...
gi 489125063 536 DRLTMLLTGTDNIRDVIAFPKTT 558
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQ 279
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
118-558 |
1.69e-140 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 410.03 E-value: 1.69e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 118 EEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTK-ATPEGARDYLVPSRVHkGKFYALPQSPQL 196
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKsATPEGARDFLVPSRAL-GKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 197 FKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRNLWLEVKGV----------DL-G 265
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtllDLkK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 266 DFPIMTFAEAERR----------YGSDKPDLRNPMELVdvadlvkdvefavfsgpandakgrvaalrvpggaalsrkqid 335
Cdd:pfam00152 161 PFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 336 dygnfikiygakglayikvterakglegitspvakflnaeiveailartgaqdgdmiffgadnkkvvadamgalrlklgk 415
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 416 dlniTDEAKWAPLWVIDFPmfeddgeggltAMHHPFTAPKDMTaaelkaapEDAVANAYDMVINGYEVGGGSVRIHNGDM 495
Cdd:pfam00152 199 ----IDKNKFNPLWVTDFP-----------AEHHPFTMPKDED--------DPALAEAFDLVLNGVEIGGGSIRIHDPEL 255
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125063 496 QQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTT 558
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 ... |
138-559 |
4.53e-110 |
|
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: 330.59 E-value: 4.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 138 LKTRAKITSLVRRFMDDHGFLDIETPMLTKATP-EGARDYLVPSRvHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCF 216
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 217 RDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRNLWLEVKGV-----------DLGDFPIMTFAEAERRYGsdkpd 285
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfeledFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 286 lrnpmelvdvadlvkdvefavfsgpandakgrvaalrvpggaalsrkqiddygnfikiygakglayikvterakglegit 365
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 366 spvakflnaeiveailartgaqdgdmiffgadnkkvvadamgalrlklgkdlnitdeakwAPLWVIDFPMFeddgegglt 445
Cdd:cd00669 155 ------------------------------------------------------------QPLFLTDYPAE--------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 446 aMHHPFTAPKDMTaaelkaaPEdaVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFLLDALKYGT 525
Cdd:cd00669 166 -MHSPLASPHDVN-------PE--IADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGL 235
|
410 420 430
....*....|....*....|....*....|....
gi 489125063 526 PPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTA 559
Cdd:cd00669 236 PPHGGLGIGIDRLIMLMTNSPTIREVIAFPKMRR 269
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
2-134 |
2.58e-75 |
|
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: 235.49 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 2 RTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAK 81
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125063 82 NVNAEMATGEIEVLASDLTIINRSDSLPL---DSNHVNtEEARLKYRYLDLRRPEM 134
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFeidDDVNVS-EELRLKYRYLDLRRPKM 135
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-555 |
1.54e-71 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 236.24 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 1 MRTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR-ADALKLASELRNEFCIQVTGTVRArd 79
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVdEELFETIKKLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 80 aknvnAEMATGEIEVLASDLTIINRSDS-LPLD-SNHVNTE-EARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHG 156
Cdd:PRK05159 80 -----NPKAPGGVEVIPEEIEVLNKAEEpLPLDiSGKVLAElDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 157 FLDIETPMLTKATPEG-----ARDYLvpsrvhkGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFT 230
Cdd:PRK05159 155 FTEIFTPKIVASGTEGgaelfPIDYF-------EKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 231 QIDVETSFMTapQVREVM---EALVRNL----------WLEVKGVDL----GDFPIMTFAEAerrygsdkpdlrnpMELV 293
Cdd:PRK05159 228 SIDVEMGFID--DHEDVMdllENLLRYMyedvaencekELELLGIELpvpeTPIPRITYDEA--------------IEIL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 294 dvadlvkdvefavfsgpanDAKGRvaalRVPGGAALSRKQiddygnfikiygakglayikvtERAKGlegitspvakfln 373
Cdd:PRK05159 292 -------------------KSKGN----EISWGDDLDTEG----------------------ERLLG------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 374 aEIVEailartGAQDGDMIFfgadnkkvvadamgalrlklgkdlnitdeakwaplwVIDFPMfeddgeggltaMHHPF-T 452
Cdd:PRK05159 314 -EYVK------EEYGSDFYF------------------------------------ITDYPS-----------EKRPFyT 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 453 APKDmtaaelkAAPEdaVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEqeqrEKFGFLLDALKYGTPPHAGLA 532
Cdd:PRK05159 340 MPDE-------DDPE--ISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNP----ESFEFYLEAFKYGMPPHGGFG 406
|
570 580
....*....|....*....|...
gi 489125063 533 FGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK05159 407 LGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-557 |
6.78e-68 |
|
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: 226.47 E-value: 6.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 2 RTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRArdak 81
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAKKLTTESSVEVTGTVVE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 82 nvnAEMATGEIEVLASDLTIINRSDS-LPLD-SNHvnTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:COG0017 77 ---SPRAPQGVELQAEEIEVLGEADEpYPLQpKRH--SLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 160 IETPMLTKATPEGAR-----DYLvpsrvhkGKFYALPQSPQLFKQLLMMSgFDRYYQIVKCFRDEDLRADRQ-PEFTQID 233
Cdd:COG0017 152 VHTPIITASATEGGGelfpvDYF-------GKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHlAEFWMIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 234 VETSFMTAPQVREVMEALVRNLwlevkgvdlgdfpimtFAEAERRYGSDkpdlrnpMEL--VDVADLVKDVEfavfsgpa 311
Cdd:COG0017 224 PEMAFADLEDVMDLAEEMLKYI----------------IKYVLENCPEE-------LEFlgRDVERLEKVPE-------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 312 ndakgrvaalrvpggaalsrkqiddyGNFIKI-YgakglayikvterakglegitspvakflnAEIVEaILARTGAQdgd 390
Cdd:COG0017 273 --------------------------SPFPRItY-----------------------------TEAIE-ILKKSGEK--- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 391 mIFFGADnkkvvadaMGALRLKLgkdlnITDEAKWAPLWVIDFPMfeddgeggltamhhpftapkdmtaaELKA-----A 465
Cdd:COG0017 294 -VEWGDD--------LGTEHERY-----LGEEFFKKPVFVTDYPK-------------------------EIKAfymkpN 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 466 PED-AVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGINEqeqrEKFGFLLDALKYGTPPHAGLAFGLDRLTMLLT 543
Cdd:COG0017 335 PDDpKTVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDP----EDYEWYLDLRRYGSVPHAGFGLGLERLVMWLT 410
|
570
....*....|....
gi 489125063 544 GTDNIRDVIAFPKT 557
Cdd:COG0017 411 GLENIREVIPFPRD 424
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
2-555 |
5.65e-37 |
|
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: 144.02 E-value: 5.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 2 RTEYCGQLRLSHE--------GQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRadalkLASELRNEFC----- 68
Cdd:COG1190 35 RTHTAAEIREKYDeleaeeetGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDE-----LGEEAYELFKlldlg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 69 --IQVTGTV-RARdaknvnaemaTGEIEVLASDLTIInrSDSL-PL-DSNHVNTE-EARLKYRYLDL-RRPEMAQRLKTR 141
Cdd:COG1190 110 diVGVEGTVfRTK----------TGELSVKVEELTLL--SKSLrPLpEKFHGLTDpETRYRQRYVDLiVNPEVRETFRKR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 142 AKITSLVRRFMDDHGFLDIETPMLTkATPEGA-------------RD-YLvpsRVhkgkfyalpqSPQLF-KQLLMmSGF 206
Cdd:COG1190 178 SKIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaarpfithhnaldMDlYL---RI----------APELYlKRLIV-GGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 207 DRYYQIVKCFRDEDLRADRQPEFTQI-------DVETsfmtapqVREVMEALVRNLWLEVKG----------VDL-GDFP 268
Cdd:COG1190 243 ERVFEIGRNFRNEGIDTTHNPEFTMLelyqayaDYND-------MMDLTEELIREAAEAVLGttkvtyqgqeIDLsPPWR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 269 IMTFAEAERRYGSdkpdlrnpmelVDVADLvKDVEFAvfsgpandakgrvaalrvpggaalsRKQIDDYGnfikiygakg 348
Cdd:COG1190 316 RITMVEAIKEATG-----------IDVTPL-TDDEEL-------------------------RALAKELG---------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 349 layIKVTERA-KGlegitspvakflnaEIVEAIlartgaqdgdmifFGadnkKVVADamgalrlKLgkdlnitdeakWAP 427
Cdd:COG1190 349 ---IEVDPGWgRG--------------KLIDEL-------------FE----ELVEP-------KL-----------IQP 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 428 LWVIDFPmfeddgeggltamhhpftapkdmtaAEL----KAAPED-AVANAYDMVINGYEVGggsvrihNGdmqqtvFgi 502
Cdd:COG1190 377 TFVTDYP-------------------------VEVsplaKRHRDDpGLTERFELFIAGREIA-------NA------F-- 416
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125063 503 lgiNEQ----EQREKF---------G----------FLlDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:COG1190 417 ---SELndpiDQRERFeeqlelkaaGddeampmdedFL-RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
117-558 |
3.10e-36 |
|
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: 138.08 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 117 TEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGardylvPSRVHKGKFYA----LPQ 192
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 193 SPQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETSFMTapqvrevmealvrnlwlevkgvDLGDfpIMT 271
Cdd:cd00776 77 SPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIE----------------------DYNE--VMD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 272 FAEaerrygsdkpdlrnpmelvdvaDLVKDVefavfsgpandakgrVAALRvpggaalsrkqiDDYGNFIKIYGAKGLAY 351
Cdd:cd00776 132 LIE----------------------ELIKYI---------------FKRVL------------ERCAKELELVNQLNREL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 352 IKVTErakglegitspvaKFLNAEIVEAIlartgaqdgdmiffgadnkKVVADAMGALRLKLGKDLN------ITDEAKW 425
Cdd:cd00776 163 LKPLE-------------PFPRITYDEAI-------------------ELLREKGVEEEVKWGEDLSteherlLGEIVKG 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 426 APLWVIDFPmfeddgeggltAMHHPFTAPKDmtaaelkaAPEDAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILG 504
Cdd:cd00776 211 DPVFVTDYP-----------KEIKPFYMKPD--------DDNPETVESFDLLMPGVgEIVGGSQRIHDYDELEERIKEHG 271
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489125063 505 INeqeqREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTT 558
Cdd:cd00776 272 LD----PESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRDP 321
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
14-555 |
1.99e-35 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 140.13 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 14 EGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFC-----IQVTGTVRARDaknvnaema 88
Cdd:PLN02502 107 EDVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVdrgdiVGVTGTPGKTK--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 89 TGEIEVLASDLTIINRSdSLPLDSNHVNTE--EARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPML 165
Cdd:PLN02502 178 KGELSIFPTSFEVLTKC-LLMLPDKYHGLTdqETRYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPML 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 166 -TKATPEGARdylvPSRVHKG----KFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMT 240
Cdd:PLN02502 257 nMIAGGAAAR----PFVTHHNdlnmDLY-LRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYAD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 241 APQVREVMEALVRNLWLEVKgvdlGDFPIMtfaeaerrYGSDKPDLRNPMELVDVADLVKDvefavfsgpandakgrVAA 320
Cdd:PLN02502 332 YNDMMELTEEMVSGMVKELT----GSYKIK--------YHGIEIDFTPPFRRISMISLVEE----------------ATG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 321 LRVPGGAAlsrkqiddygnfikiyGAKGLAYIKVTErAKGLEGITSP--VAKFLNaEIVEAILARTGAQdgdmiffgadn 398
Cdd:PLN02502 384 IDFPADLK----------------SDEANAYLIAAC-EKFDVKCPPPqtTGRLLN-ELFEEFLEETLVQ----------- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 399 kkvvadamgalrlklgkdlnitdeakwaPLWVIDFPMfeddgEGGLTAMHHpfTAPKDMTAA-ELKAAPEDaVANAY--- 474
Cdd:PLN02502 435 ----------------------------PTFVLDHPV-----EMSPLAKPH--RSKPGLTERfELFINGRE-LANAFsel 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 475 -DMVINgYEVGGGSVRIHNGDMQQTVFgilgineqeQREKFgflLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:PLN02502 479 tDPVDQ-RERFEEQVKQHNAGDDEAMA---------LDEDF---CTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIA 545
|
..
gi 489125063 554 FP 555
Cdd:PLN02502 546 FP 547
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
307-406 |
1.54e-33 |
|
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: 123.14 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 307 FSGPANdAKGRVAALRVPGGAALSRKQIDDYGNFIKIYGAKGLAYIKVTErakglEGITSPVAKFLNAEIVEAILARTGA 386
Cdd:pfam02938 1 FSEALK-SGGSVKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEG-----GGHTGPIAKFLTEEEVEKLLEAVGA 74
|
90 100
....*....|....*....|
gi 489125063 387 QDGDMIFFGADNKKVVADAM 406
Cdd:pfam02938 75 EDGDALLFVADKKKTVNKAL 94
|
|
| Asp_Lys_Asn_RS_N |
cd04100 |
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ... |
17-104 |
1.89e-33 |
|
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: 122.29 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADAL-KLASELRNEFCIQVTGTVRARDAKNvnaeMATGEIEVL 95
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFfEEAEKLRTESVVGVTGTVVKRPEGN----LATGEIELQ 76
|
....*....
gi 489125063 96 ASDLTIINR 104
Cdd:cd04100 77 AEELEVLSK 85
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
11-555 |
2.15e-30 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 124.82 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 11 LSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDradalKLASELRNEF-------CIQVTGTVRARDaknv 83
Cdd:PRK00484 50 LEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKD-----DVGEEALEAFkkldlgdIIGVEGTLFKTK---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 84 naemaTGEIEVLASDLTIInrSDSL-PL-DSNH-VNTEEARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:PRK00484 121 -----TGELSVKATELTLL--TKSLrPLpDKFHgLTDVETRYRQRYVDLiVNPESRETFRKRSKIISAIRRFLDNRGFLE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 160 IETPMLtKATPEG--AR---------D---YLvpsRVhkgkfyalpqSPQLF-KQLLmMSGFDRYYQIVKCFRDEDLRAD 224
Cdd:PRK00484 194 VETPML-QPIAGGaaARpfithhnalDidlYL---RI----------APELYlKRLI-VGGFERVYEIGRNFRNEGIDTR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 225 RQPEFTQIdvetsfmtapqvrEVMEAlvrnlwlevkgvdlgdfpimtfaeaerrYGsdkpDLRNPMELVDvaDLVKDVef 304
Cdd:PRK00484 259 HNPEFTML-------------EFYQA----------------------------YA----DYNDMMDLTE--ELIRHL-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 305 avfsgpandakgrvaALRVPGGAALSR--KQIDDYGNFIKIygakglayikvterakglegitspvakflnaEIVEAILA 382
Cdd:PRK00484 290 ---------------AQAVLGTTKVTYqgTEIDFGPPFKRL-------------------------------TMVDAIKE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 383 RTGAQdgdmiffgadnkkvVADAMGALRLKLGKDLNITDEAKWAPLWVIDFpMFEDDGEGGLTA----MHHPftapkdmt 458
Cdd:PRK00484 324 YTGVD--------------FDDMTDEEARALAKELGIEVEKSWGLGKLINE-LFEEFVEPKLIQptfiTDYP-------- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 459 aAEL----KAAPED-AVANAYDMVINGYEVGggsvrihNGdmqqtvFgilgiNE----QEQREKF---------G----- 515
Cdd:PRK00484 381 -VEIsplaKRHREDpGLTERFELFIGGREIA-------NA------F-----SElndpIDQRERFeaqveakeaGddeam 441
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 489125063 516 -----FlLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK00484 442 fmdedF-LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
13-557 |
4.98e-29 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 120.21 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 13 HEGQQVTLCGWVNRRRDLGSLIFIDMRDREGI--VQVFFDPDrADALKLASELRNEFCIQVTGTVRARDAKNVNAEMATG 90
Cdd:PRK03932 14 YVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFkqLQVVKDNG-EEYFEEIKKLTTGSSVIVTGTVVESPRAGQGYELQAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 91 EIEVLASDltiinrSDSLPLDS-NHvnTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKAT 169
Cdd:PRK03932 93 KIEVIGED------PEDYPIQKkRH--SIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 170 PEGA----------RDYlvpsrvhKGKFYA----LPQSPQLFKQLLMMsGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDV 234
Cdd:PRK03932 165 CEGAgelfrvttldLDF-------SKDFFGkeayLTVSGQLYAEAYAM-ALGKVYTFGPTFRAENSNTRRHlAEFWMIEP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 235 ETSFMTAPQVREVMEALVRNLwleVKGVdlgdfpimtfaeaerrygsdkpdLRNPMElvdvadlvkDVEFavfsgpanda 314
Cdd:PRK03932 237 EMAFADLEDNMDLAEEMLKYV---VKYV-----------------------LENCPD---------DLEF---------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 315 kgrvaalrvpggaalsrkqiddYGNFIKiygaKGLayikvTERakgLEGITSPvaKFLNAEIVEAI--LARTGAQDGDMI 392
Cdd:PRK03932 272 ----------------------LNRRVD----KGD-----IER---LENFIES--PFPRITYTEAIeiLQKSGKKFEFPV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 393 FFGADnkkvvadamgalrlkLGkdlniTDEAKW-------APLWVIDFpmfeddgeggltamhhpftaPKDMTAAELKAA 465
Cdd:PRK03932 316 EWGDD---------------LG-----SEHERYlaeehfkKPVFVTNY--------------------PKDIKAFYMRLN 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 466 PEDAVANAYDMVINGY-EVGGGSVRIHNGD-----MQQtvfgiLGINEqeqrEKFGFLLDALKYGTPPHAGLAFGLDRLT 539
Cdd:PRK03932 356 PDGKTVAAMDLLAPGIgEIIGGSQREERLDvlearIKE-----LGLNK----EDYWWYLDLRRYGSVPHSGFGLGFERLV 426
|
570
....*....|....*...
gi 489125063 540 MLLTGTDNIRDVIAFPKT 557
Cdd:PRK03932 427 AYITGLDNIRDVIPFPRT 444
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
7-556 |
1.14e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 117.11 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 7 GQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQ--VFFDPDRADA--LKLASELRNEFCIQVTGTVRARDAKn 82
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKgmVKYAKQLSRESVVDVEGVVSVPKKP- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 83 vnAEMATGEIEVLASDLTIINRSDS-LPL--------DSN------------HVNtEEARLKYRYLDLRRPEMAQRLKTR 141
Cdd:PLN02850 152 --VKGTTQQVEIQVRKIYCVSKALAtLPFnvedaarsESEiekalqtgeqlvRVG-QDTRLNNRVLDLRTPANQAIFRIQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 142 AKITSLVRRFMDDHGFLDIETPMLTKATPEGAR-----DYlvpsrvhKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCF 216
Cdd:PLN02850 229 SQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDY-------KGQPACLAQSPQLHKQMAICGDFRRVFEIGPVF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 217 RDEDLRADRQ-PEFTQIDVEtsfmtapqvrevMEalVRNLWLEVkgvdlgdfpimtfaeaerrygsdkpdlrnpMELVDv 295
Cdd:PLN02850 302 RAEDSFTHRHlCEFTGLDLE------------ME--IKEHYSEV------------------------------LDVVD- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 296 aDLVKdvefAVFSGPANDAKGRVAALrvpggaalsRKQiddygnfikiYGAKGLAYIKVTERAKGLEGItspvakflnae 375
Cdd:PLN02850 337 -ELFV----AIFDGLNERCKKELEAI---------REQ----------YPFEPLKYLPKTLRLTFAEGI----------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 376 iveAILARTGAQDGDMIFFGADNKKvvadAMGALRL-KLGKDLNITDEakwAPLWVIDFpmfeddgeggltamhhpFTAP 454
Cdd:PLN02850 382 ---QMLKEAGVEVDPLGDLNTESER----KLGQLVKeKYGTDFYILHR---YPLAVRPF-----------------YTMP 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 455 kdmtaaelkaAPED-AVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINeqeqREKFGFLLDALKYGTPPHAGLAF 533
Cdd:PLN02850 435 ----------CPDDpKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGID----VKTISTYIDSFRYGAPPHGGFGV 500
|
570 580
....*....|....*....|...
gi 489125063 534 GLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PLN02850 501 GLERVVMLFCGLNNIRKTSLFPR 523
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
140-258 |
5.25e-26 |
|
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: 106.05 E-value: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 140 TRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARD----YLVPSRVHKGKFYALPQSPQLFKQLLMMS----GFDRYYQ 211
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489125063 212 IVKCFRDEDLRAD--RQPEFTQIDVETSFMTAP------QVREVMEALVRNLWLE 258
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEeasefeELIELTEELLRALGIK 135
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
2-555 |
2.93e-25 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 111.21 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 2 RTEYCGQLRLSHEGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLAsELRNEF----CIQVTGTV-R 76
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLA-DFRAAVdlgdLVEVTGTMgT 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 77 ARdaknvnaemaTGEIEVLASDLTIInrSDSL-PLDSNHV--NTEEARLKYRYLDLR-RPEMAQRLKTRAKITSLVRRFM 152
Cdd:PRK02983 717 SR----------NGTLSLLVTSWRLA--GKCLrPLPDKWKglTDPEARVRQRYLDLAvNPEARDLLRARSAVVRAVRETL 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 153 DDHGFLDIETPMLTK----ATpegARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPE 228
Cdd:PRK02983 785 VARGFLEVETPILQQvhggAN---ARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 229 FTQIdvetsfmtapqvrevmealvrnlwlevkgvdlgdfpimtfaEAERRYGsdkpDLRNPMELVDvaDLVKDVEFAVFs 308
Cdd:PRK02983 861 FTLL-----------------------------------------EAYQAHA----DYDTMRDLTR--ELIQNAAQAAH- 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 309 gpandakGRVAALRvpGGAALSRKQIDDYGNF--IKIYGAkglayikVTErAKGlEGIT--SPVAKflnaeiVEAILART 384
Cdd:PRK02983 893 -------GAPVVMR--PDGDGVLEPVDISGPWpvVTVHDA-------VSE-ALG-EEIDpdTPLAE------LRKLCDAA 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 385 GaqdgdmIFFGADnkkvvADAmGALRLKLGKDLniTDEAKWAPLWVIDFPmfeddgegglTAMhHPFTAPKdmtaaelka 464
Cdd:PRK02983 949 G------IPYRTD-----WDA-GAVVLELYEHL--VEDRTTFPTFYTDFP----------TSV-SPLTRPH--------- 994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 465 aPEDA-VANAYDMVINGYEVGGG-----------------SVRIHNGD---MqqtvfgilgineqEQREKFgflLDALKY 523
Cdd:PRK02983 995 -RSDPgLAERWDLVAWGVELGTAyseltdpveqrrrlteqSLLAAGGDpeaM-------------ELDEDF---LQALEY 1057
|
570 580 590
....*....|....*....|....*....|..
gi 489125063 524 GTPPHAGLAFGLDRLTMLLTGTdNIRDVIAFP 555
Cdd:PRK02983 1058 AMPPTGGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
18-555 |
7.17e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 109.35 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 18 VTLCGWVNRRRDLGSLIFIDMR----DREGIVQVFFDPDRADALKLASELRnefciqvTGTVRArdAKNVNAEMATGEIE 93
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRsngnELQVVGQVGEHFTREDLKKLKVSLR-------VGDIIG--ADGVPCRMQRGELS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 94 VLASDLTII------------NRSDSLPLDSNHVnteeaRLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDI 160
Cdd:PTZ00385 181 VAASRMLILspyvctdqvvcpNLRGFTVLQDNDV-----KYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 161 ETPML-TKATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFM 239
Cdd:PTZ00385 256 ETPVLhTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 240 TAPQVREVMEALVRNLWLEVKGVDLGDFpimtfaEAERRYGSDKP-DLRNPMELVDVADLVKD---VEFAvfsgPANDak 315
Cdd:PTZ00385 335 TYEDLMPMTEDIFRQLAMRVNGTTVVQI------YPENAHGNPVTvDLGKPFRRVSVYDEIQRmsgVEFP----PPNE-- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 316 grvaaLRVPggaalsrkqiddygnfikiygaKGLAYIKVTERAKGLEgiTSPVakflnaeiveailaRTGAQDGDMIFfg 395
Cdd:PTZ00385 403 -----LNTP----------------------KGIAYMSVVMLRYNIP--LPPV--------------RTAAKMFEKLI-- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 396 adnkkvvadamgalrlklgkDLNITDEAKwAPLWVIDFPMfeddgeggltamhhpFTAPkdmTAAELKAAPedAVANAYD 475
Cdd:PTZ00385 438 --------------------DFFITDRVV-EPTFVMDHPL---------------FMSP---LAKEQVSRP--GLAERFE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 476 MVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREKFGFL----LDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDV 551
Cdd:PTZ00385 477 LFVNGIEYCNAYSELNDPHEQYHRFQQQLVDRQGGDEEAMPLdetfLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDG 556
|
....
gi 489125063 552 IAFP 555
Cdd:PTZ00385 557 IIFP 560
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
132-555 |
5.72e-24 |
|
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: 103.05 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 132 PEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLtKATPEG--ARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRY 209
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 210 YQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRNLWLEVKGvdlgdfpimtfaEAERRYGSDKPDLRNP 289
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING------------KTKIEYGGKELDFTPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 290 MELVDVADLVKDVEFAVFSGPANDakgrvaalrvpggaalsrkQIDDYgnfikiygAKGLAYIKVTERAKGLegitsPVA 369
Cdd:cd00775 148 FKRVTMVDALKEKTGIDFPELDLE-------------------QPEEL--------AKLLAKLIKEKIEKPR-----TLG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 370 KFLNA---EIVEAILartgaqdgdmiffgadnkkvvadamgalrlklgkdlnitdeakWAPLWVIDFPmfeddgeggltA 446
Cdd:cd00775 196 KLLDKlfeEFVEPTL-------------------------------------------IQPTFIIDHP-----------V 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 447 MHHPFTapkdmtaaelKAAPEDA-VANAYDMVINGYEVGGGSVRIHNGDMQQTVFgilgINEQEQREKFG---FLLD--- 519
Cdd:cd00775 222 EISPLA----------KRHRSNPgLTERFELFICGKEIANAYTELNDPFDQRERF----EEQAKQKEAGDdeaMMMDedf 287
|
410 420 430
....*....|....*....|....*....|....*...
gi 489125063 520 --ALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:cd00775 288 vtALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
17-555 |
3.46e-23 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 103.22 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDradalKLASELRNE-FCIQVTGTVRArdAKNVNAEMATGEIEVL 95
Cdd:PRK12445 67 EVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARD-----SLPEGVYNDqFKKWDLGDIIG--ARGTLFKTQTGELSIH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 96 ASDLTIINRS-DSLPLDSNHVNTEEARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLtKATPEGA 173
Cdd:PRK12445 140 CTELRLLTKAlRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM-QVIPGGA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 174 --RDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEAL 251
Cdd:PRK12445 219 saRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 252 VRNLWLEVKGvdlgdfpimtfaEAERRYGSDKPDLRNPMELVDVADLVKDVEfavfsgPANDakgrvaalrvpggaalsr 331
Cdd:PRK12445 298 FRTLAQEVLG------------TTKVTYGEHVFDFGKPFEKLTMREAIKKYR------PETD------------------ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 332 kqIDDYGNFikiygakglayikvterakglegitspvakflnaeiveailartgaqdgdmiffgaDNKKVVADAMGalrl 411
Cdd:PRK12445 342 --MADLDNF--------------------------------------------------------DAAKALAESIG---- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 412 klgkdlnITDEAKWApLWVIDFPMFEDDGEGGLTAMHHPFTAPKDMTAAELKAAPEDAVANAYDMVINGYEVGGGSVRIH 491
Cdd:PRK12445 360 -------ITVEKSWG-LGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELN 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125063 492 NGDMQQTVFGIlGINEQEQREKFGFLLD-----ALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK12445 432 DAEDQAERFQE-QVNAKAAGDDEAMFYDedyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
14-111 |
1.93e-20 |
|
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: 86.60 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 14 EGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFF--DPDRADALKLASELRNEFCIQVTGTVRArdaknvnAEMATGE 91
Cdd:cd04316 11 DGEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTApkKKVDKELFKTVRKLSRESVISVTGTVKA-------EPKAPNG 83
|
90 100
....*....|....*....|.
gi 489125063 92 IEVLASDLTIINRSDS-LPLD 111
Cdd:cd04316 84 VEIIPEEIEVLSEAKTpLPLD 104
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
15-556 |
4.02e-18 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 87.74 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 15 GQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR---ADALKLASELRNEFCIQVTGTVrARDAKNVNAeMATGE 91
Cdd:PTZ00401 78 DKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGdvpKEMIDFIGQIPTESIVDVEATV-CKVEQPITS-TSHSD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 92 IEVLASDLTIINRS-DSLPL---DSNHVNTEEA-------RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDI 160
Cdd:PTZ00401 156 IELKVKKIHTVTESlRTLPFtleDASRKESDEGakvnfdtRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCEI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 161 ETPMLTKATPEGARDylVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETSFm 239
Cdd:PTZ00401 236 HSPKIINAPSEGGAN--VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRI- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 240 tapqvrevmealvrnlwlevkgvdlgdfpimtfaeAERRYgsdkpdlrnpmELVDVADLVKDVEFAVFSGPANDAKgrva 319
Cdd:PTZ00401 313 -----------------------------------NEHYY-----------EVLDLAESLFNYIFERLATHTKELK---- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 320 alrvpggaalsrkqiddygNFIKIYGAKGLAYIKVTERAKGLE-GITSPvakflNAEIVEAILARTGAQDGDMIFFGADN 398
Cdd:PTZ00401 343 -------------------AVCQQYPFEPLVWKLTPERMKELGvGVISE-----GVEPTDKYQARVHNMDSRMLRINYMH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 399 KKVVADAMGALRLKLGKDLNITDEAKWAPL----WVIDFpmFEDDgegGLTAMHHPF-TAPkdmtaaelkaAPEDA-VAN 472
Cdd:PTZ00401 399 CIELLNTVLEEKMAPTDDINTTNEKLLGKLvkerYGTDF--FISD---RFPSSARPFyTME----------CKDDErFTN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 473 AYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEQEQREkfgfLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVI 552
Cdd:PTZ00401 464 SYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLAS 539
|
....
gi 489125063 553 AFPK 556
Cdd:PTZ00401 540 LFPR 543
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
18-102 |
2.65e-17 |
|
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: 76.50 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 18 VTLCGWV-NRRRDLGSLIFIDMRDREGIVQVFFDPDraDALKLASELRNEFCIQVTGTVRARDaknvnaemaTGEIEVLA 96
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKE--EAEKLAKKLKEGDVVRVTGKVKKRK---------GGELELVV 69
|
....*.
gi 489125063 97 SDLTII 102
Cdd:pfam01336 70 EEIELL 75
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
90-560 |
1.24e-16 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 83.14 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 90 GEIEVLASDLTIINRS-DSLPLDSNHVNTEeARLKYRYLDLRRPEMAQR-LKTRAKITSLVRRFMDDHGFLDIETPMLT- 166
Cdd:PTZ00417 204 GELSIFPKETIILSPClHMLPMKYGLKDTE-IRYRQRYLDLMINESTRStFITRTKIINYLRNFLNDRGFIEVETPTMNl 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 167 KATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVRE 246
Cdd:PTZ00417 283 VAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLIK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 247 VMEALVRNLWLEVkgvdLGDFPIMtfaeaerrYGSDKPDlRNPMElVDvadlvkdvefavFSGPandakgrvaalrvpgg 326
Cdd:PTZ00417 362 WSEDFFSQLVMHL----FGTYKIL--------YNKDGPE-KDPIE-ID------------FTPP---------------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 327 aalsrkqiddygnfikiygakglaYIKVTeRAKGLEGITSPVAK--FLNAEIVEailartgaqdgDMIFFGADNKKVVAD 404
Cdd:PTZ00417 400 ------------------------YPKVS-IVEELEKLTNTKLEqpFDSPETIN-----------KMINLIKENKIEMPN 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 405 AMGALRL--KLGKDLnITDEAKWAPLWVIDFPMFEDDgegglTAMHHpftapkdmtaaelKAAPedAVANAYDMVINGYE 482
Cdd:PTZ00417 444 PPTAAKLldQLASHF-IENKYPNKPFFIIEHPQIMSP-----LAKYH-------------RSKP--GLTERLEMFICGKE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 483 VGGGSVRIHNGDMQQTVFGIlginEQEQREKF---GFLLDA-----LKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAF 554
Cdd:PTZ00417 503 VLNAYTELNDPFKQKECFSA----QQKDREKGdaeAFQFDAafctsLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILF 578
|
....*.
gi 489125063 555 PKTTAA 560
Cdd:PTZ00417 579 PTMRPA 584
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
119-556 |
1.07e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 72.36 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 119 EARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARD-----YLVPSRVHKGKFYALPQS 193
Cdd:PRK06462 11 EEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 194 PQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQP---EFTQIDVETSFMTAPQVREVMEALVRNLWLEVKGVDLGDFpim 270
Cdd:PRK06462 91 MILHKQ-LALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 271 tfaeaeRRYGSDKPDLRNPMELVDVADLVKDVEfavfsgpandakgrvaalrvpggaALSRKQIDdygnfIKIYGAKGla 350
Cdd:PRK06462 167 ------EFFGRDLPHLKRPFKRITHKEAVEILN------------------------EEGCRGID-----LEELGSEG-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 351 yikvterakglegitspvakflnaeivEAILArtgaqdgdmiffgadnkkvvadamgalrlklgkdlNITDEakwaPLWV 430
Cdd:PRK06462 210 ---------------------------EKSLS-----------------------------------EHFEE----PFWI 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 431 IDFPM-------FEDDGEGGltamhhpftapkdmtaaelkaapedaVANAYDMVI-NGY-EVGGGSVRIHngDMQQTVFG 501
Cdd:PRK06462 224 IDIPKgsrefydREDPERPG--------------------------VLRNYDLLLpEGYgEAVSGGEREY--EYEEIVER 275
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489125063 502 ILgiNEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PRK06462 276 IR--EHGVDPEKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
17-127 |
2.15e-12 |
|
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: 63.70 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA-DALKLASELRNEFCIQVTGTVRARdaknvnaEMATGEIEVL 95
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNeEAYREAKKVGIESSVIVEGAVKAD-------PRAPGGAEVH 73
|
90 100 110
....*....|....*....|....*....|..
gi 489125063 96 ASDLTIINRSDSLPLDSNhvNTEEARLKYRYL 127
Cdd:cd04319 74 GEKLEIIQNVEFFPITED--ASDEFLLDVRHL 103
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
454-561 |
2.93e-12 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 69.23 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 454 PKDMTAAELKAAPEDAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGINeqeqREKFGFLLDALKYGTPPHAGLA 532
Cdd:PLN02603 459 PKEIKAFYMRENDDGKTVAAMDMLVPRVgELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSVPHAGFG 534
|
90 100
....*....|....*....|....*....
gi 489125063 533 FGLDRLTMLLTGTDNIRDVIAFPKTTAAA 561
Cdd:PLN02603 535 LGFERLVQFATGIDNIRDAIPFPRVPGSA 563
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
451-556 |
1.20e-10 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 64.27 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 451 FTAPKDMTAAELKAAPEDAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFgilgINEQEQREKFGFLLDALKYGTPPHA 529
Cdd:PTZ00425 477 YNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIgEVIGGSQREDNLERLDKMI----KEKKLNMESYWWYRQLRKFGSHPHA 552
|
90 100
....*....|....*....|....*..
gi 489125063 530 GLAFGLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PTZ00425 553 GFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
451-563 |
1.52e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 57.31 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 451 FTAPKDMTAAELKAAPEDAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGIneqeQREKFGFLLDALKYGTPPHA 529
Cdd:PLN02221 463 YNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYLDLRRYGTVKHC 538
|
90 100 110
....*....|....*....|....*....|....
gi 489125063 530 GLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACL 563
Cdd:PLN02221 539 GFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
18-77 |
1.72e-08 |
|
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: 51.85 E-value: 1.72e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 18 VTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRA 77
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKE 61
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
17-129 |
3.05e-08 |
|
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: 51.71 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLAsELRNEF----CIQVTGTV-RARdaknvnaemaTGE 91
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFE-DFKKLLdlgdIIGVTGTPfKTK----------TGE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489125063 92 IEVLASDLTIInrSDSL-PLDSNH--VNTEEARLKYRYLDL 129
Cdd:cd04322 70 LSIFVKEFTLL--SKSLrPLPEKFhgLTDVETRYRQRYLDL 108
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-103 |
3.16e-08 |
|
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: 51.16 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 18 VTLCGWVNRRRDL-GSLIFIDMRDREG-IVQVfFDPDRADALKLASELRNEFCIQVTGTVRARDAKnvnAEMATGEIEVL 95
Cdd:cd04321 2 VTLNGWIDRKPRIvKKLSFADLRDPNGdIIQL-VSTAKKDAFSLLKSITAESPVQVRGKLQLKEAK---SSEKNDEWELV 77
|
....*...
gi 489125063 96 ASDLTIIN 103
Cdd:cd04321 78 VDDIQTLN 85
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
459-551 |
9.42e-08 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 54.16 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 459 AAELKAAPED-AVANAYDMVINGYEVGGGSVRIHNGDMQQTVFgilgINEQEQREKFGF--------LLDALKYGTPPHA 529
Cdd:PRK09350 209 AALAKISTEDhRVAERFEVYFKGIELANGFHELTDAREQRQRF----EQDNRKRAARGLpqqpidenLIAALEAGLPDCS 284
|
90 100
....*....|....*....|..
gi 489125063 530 GLAFGLDRLTMLLTGTDNIRDV 551
Cdd:PRK09350 285 GVALGVDRLIMLALGAESISEV 306
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
451-561 |
1.20e-07 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 54.49 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 451 FTAPKDMTAAELKAAPEDAVANAYDMVI-NGYEVGGGSVRIHNGDMQQTVFGILGIneqeQREKFGFLLDALKYGTPPHA 529
Cdd:PLN02532 524 YNYPKELKPFYVRLNDDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGL----PREQYEWYLDLRRHGTVKHS 599
|
90 100 110
....*....|....*....|....*....|..
gi 489125063 530 GLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAA 561
Cdd:PLN02532 600 GFSLGFELMVLFATGLPDVRDAIPFPRSWGKA 631
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
151-553 |
1.35e-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: 53.32 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 151 FMDDHGFLDIETPMLTKAT-PEGARDYL----VPSRVHKGKFYaLPQSPQLF-KQLLMmSGFDRYYQIVKCFRDEDLRAD 224
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFatefVGPDGQGRPLY-LQTSPEYAmKRLLA-AGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 225 RQPEFTQIDVETSFMTAPQVREVMEALVRnlwlEVKGVDLGDFPIMTFAEAERRYGSdkpdlrnpmelVDvadlvkdvef 304
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQ----ELLGDPFAPAERLSYQEAFLRYAG-----------ID---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 305 aVFSGPANDAKGRVAALRVPGGAALSRKQIDDygnfikiygakglayikvterakglegitspvakFLNAEIVEAilart 384
Cdd:TIGR00462 134 -PLTASLAELQAAAAAHGIRASEEDDRDDLLD----------------------------------LLFSEKVEP----- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 385 gaqdgdmiffgadnkkvvadamgalrlKLGKDlnitdeakwAPLWVIDFPmfeddgeggltamhhpftAPkdmTAAELKA 464
Cdd:TIGR00462 174 ---------------------------HLGFG---------RPTFLYDYP------------------AS---QAALARI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 465 APEDA-VANAYDMVINGYEVGggsvrihNGdmqqtvFGILgINEQEQREKF------------------GFLLDALKYGT 525
Cdd:TIGR00462 197 SPDDPrVAERFELYIKGLELA-------NG------FHEL-TDAAEQRRRFeadnalrkalglprypldERFLAALEAGL 262
|
410 420
....*....|....*....|....*...
gi 489125063 526 PPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:TIGR00462 263 PECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
17-95 |
8.03e-06 |
|
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: 44.09 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125063 17 QVTLCGWVNRRRDLGSLIFIDMRDreGI----VQVFFDPDRADAlKLASELRNEFCIQVTGTVRARDAKNVNAEMATGEI 92
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSclknLQVVVDKELTNF-KEILKLSTGSSIRVEGVLVKSPGAKQPFELQAEKI 77
|
...
gi 489125063 93 EVL 95
Cdd:cd04318 78 EVL 80
|
|
| PRK04036 |
PRK04036 |
DNA-directed DNA polymerase II small subunit; |
10-75 |
3.42e-04 |
|
DNA-directed DNA polymerase II small subunit;
Pssm-ID: 235208 [Multi-domain] Cd Length: 504 Bit Score: 43.40 E-value: 3.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125063 10 RLSHEGQQVTLCGWVNRRRDLGS-LIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTV 75
Cdd:PRK04036 148 KLKRGGEEVSIIGMVSDIRSTKNgHKIVELEDTTGTFPVLIMKDREDLAELADELLLDEVIGVEGTL 214
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