|
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: 1130.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 1 MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR-ADALKLASELRNEFCIQVTGTVRARD 79
Cdd:COG0173 2 YRTHYCGELRESDVGQEVTLSGWVHRRRDHGGLIFIDLRDRYGITQVVFDPDDsAEAFEKAEKLRSEYVIAVTGKVRARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 80 EKNINRDMATGEIEVLASSLTIINRADVLPL---DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHG 156
Cdd:COG0173 82 EGTVNPKLPTGEIEVLASELEILNKAKTPPFqidDDTDVS-EELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 157 FLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVET 236
Cdd:COG0173 161 FLEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDIEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 237 SFMTAPQVREVMEALVRHLWLEVKGVDL-GDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANdPK 315
Cdd:COG0173 241 SFVDQEDVFELMEGLIRHLFKEVLGVELpTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDSGFKVFAGAAE-NG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 316 GRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNErakglEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFG 395
Cdd:COG0173 320 GRVKAINVPGGASLSRKQIDELTEFAKQYGAKGLAYIKVNE-----DGLKSPIAKFLSEEELAAILERLGAKPGDLIFFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 396 ADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAY 474
Cdd:COG0173 395 ADKPKVVNKALGALRLKLGKELGLIDEDEFAFLWVVDFPLFEyDEEEGRWVAMHHPFTMPKDEDLDLLETDPGKVRAKAY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 475 DMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAF 554
Cdd:COG0173 475 DLVLNGYELGGGSIRIHDPELQEKVFELLGISEEEAEEKFGFLLEAFKYGAPPHGGIAFGLDRLVMLLAGEDSIRDVIAF 554
|
570 580 590
....*....|....*....|....*....|....
gi 16129819 555 PKTTAAACLMTEAPSFANPTALAELSIQVVKKAE 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: 1125.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 1 MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDrADALKLASELRNEFCIQVTGTVRARDE 80
Cdd:PRK00476 3 MRTHYCGELRESHVGQTVTLCGWVHRRRDHGGLIFIDLRDREGIVQVVFDPD-AEAFEVAESLRSEYVIQVTGTVRARPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 81 KNINRDMATGEIEVLASSLTIINRADVLPL---DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGF 157
Cdd:PRK00476 82 GTVNPNLPTGEIEVLASELEVLNKSKTLPFpidDEEDVS-EELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 158 LDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETS 237
Cdd:PRK00476 161 LEIETPILTKSTPEGARDYLVPSRVHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 238 FMTAPQVREVMEALVRHLWLEVKGVDLGD-FPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDpKG 316
Cdd:PRK00476 241 FVTQEDVMALMEGLIRHVFKEVLGVDLPTpFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGFKVFAGAAND-GG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 317 RVAALRVPGGAS-LTRKQIDEYGNFVKIYGAKGLAYIKVNErakglEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFG 395
Cdd:PRK00476 320 RVKAIRVPGGAAqLSRKQIDELTEFAKIYGAKGLAYIKVNE-----DGLKGPIAKFLSEEELAALLERTGAKDGDLIFFG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 396 ADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTSPKDMTAAEL-KAAPENAVANA 473
Cdd:PRK00476 395 ADKAKVVNDALGALRLKLGKELGLIDEDKFAFLWVVDFPMFEyDEEEGRWVAAHHPFTMPKDEDLDELeTTDPGKARAYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 474 YDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:PRK00476 475 YDLVLNGYELGGGSIRIHRPEIQEKVFEILGISEEEAEEKFGFLLDALKYGAPPHGGIAFGLDRLVMLLAGADSIRDVIA 554
|
570 580 590
....*....|....*....|....*....|....
gi 16129819 554 FPKTTAAACLMTEAPSFANPTALAELSIQVVKKA 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: 1013.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 1 MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDrADALKLASELRNEFCIQVTGTVRARDE 80
Cdd:TIGR00459 1 MRTHYCGQLRTEHLGQTVTLAGWVNRRRDLGGLIFIDLRDRSGIVQVVCDPD-ADALKLAKGLRNEDVVQVKGKVSARPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 81 KNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEA-RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:TIGR00459 80 GNINRNLDTGEIEILAESITLLNKSKTPPLIIEKTDAEEEvRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFLDQQGFLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 160 IETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFM 239
Cdd:TIGR00459 160 IETPMLTKSTPEGARDYLVPSRVHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDMEMSFM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 240 TAPQVREVMEALVRHLWLEVKGVDLG-DFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDpKGRV 318
Cdd:TIGR00459 240 TQEDVMELIEKLVSHVFLEVKGIDLKkPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLFKDSEFKVFSNLIND-GGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 319 AALRVPGG-ASLTRKQIDEYGNFVKIYGAKGLAYIKVNERakgleGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGAD 397
Cdd:TIGR00459 319 KAIRVPGGwAELSRKSIKELRKFAKEYGAKGLAYLKVNED-----GINSPIKKFLDEKKGKILLERTDAQNGDILLFGAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 398 NKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMV 477
Cdd:TIGR00459 394 SKKIVLDALGALRLKLGKDLGLVDPDLFSFLWVVDFPMFEKDKEGRLCAAHHPFTMPKDEDLENLEAAPEEALAEAYDLV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 478 INGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKT 557
Cdd:TIGR00459 474 LNGVELGGGSIRIHDPEVQKKVFEILGIDPEEAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGTDNIRDVIAFPKT 553
|
570 580 590
....*....|....*....|....*....|
gi 16129819 558 TAAACLMTEAPSFANPTALAELSIQ-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: 692.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 2 RTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA-DALKLASELRNEFCIQVTGTVRARDE 80
Cdd:PLN02903 59 RSHLCGALSVNDVGSRVTLCGWVDLHRDMGGLTFLDVRDHTGIVQVVTLPDEFpEAHRTANRLRNEYVVAVEGTVRSRPQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 81 KNINRDMATGEIEVLASSLTIINR-ADVLPL------DSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFM- 152
Cdd:PLN02903 139 ESPNKKMKTGSVEVVAESVDILNVvTKSLPFlvttadEQKDSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRRYLe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 153 DDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQI 232
Cdd:PLN02903 219 DVHGFVEIETPILSRSTPEGARDYLVPSRVQPGTFYALPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQPEFTQL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 233 DVETSFMTAPQVREVMEALVRHLWLEVKGVDLGD-FPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPA 311
Cdd:PLN02903 299 DMELAFTPLEDMLKLNEDLIRQVFKEIKGVQLPNpFPRLTYAEAMSKYGSDKPDLRYGLELVDVSDVFAESSFKVFAGAL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 312 NDpKGRVAALRVPGGASLT----RKQIDEYGNFVKiYGAKGLAYIKVNERAKgLEGINSPVAKfLNAEIIEDILDRTAAQ 387
Cdd:PLN02903 379 ES-GGVVKAICVPDGKKISnntaLKKGDIYNEAIK-SGAKGLAFLKVLDDGE-LEGIKALVES-LSPEQAEQLLAACGAG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 388 DGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFE-DDGEGGLTAMHHPFTSPKDMTAAELKaap 466
Cdd:PLN02903 455 PGDLILFAAGPTSSVNKTLDRLRQFIAKTLDLIDPSRHSILWVTDFPMFEwNEDEQRLEALHHPFTAPNPEDMGDLS--- 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 467 eNAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTD 546
Cdd:PLN02903 532 -SARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAK 610
|
570 580 590
....*....|....*....|....*....|....*....
gi 16129819 547 NIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVK 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: 550.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 5 YCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA--DALKLASELRNEFCIQVTGTVRARDEKN 82
Cdd:PRK12820 8 FCGHLSLDDTGREVCLAGWVDAFRDHGELLFIHLRDRNGFIQAVFSPEAApaDVYELAASLRAEFCVALQGEVQKRLEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 83 INRDMATGEIEVLASSLTIINRADVLPL--------------DSNHVNtEEARLKYRYLDLRRPEMAQRLKTRAKITSLV 148
Cdd:PRK12820 88 ENPHIETGDIEVFVRELSILAASEALPFaisdkamtagagsaGADAVN-EDLRLQYRYLDIRRPAMQDHLAKRHRIIKCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 149 RRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPE 228
Cdd:PRK12820 167 RDFLDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQPE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 229 FTQIDVETSFMTAPQVREVMEALVRHLWlEVKGVDLG-DFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVF 307
Cdd:PRK12820 247 FTQLDIEASFIDEEFIFELIEELTARMF-AIGGIALPrPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFENTRYGIF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 308 AGPANDpKGRVAALRVPGGASLTRKQI--DEYGN-FVKIYGAKGLAYIKVNErakglEGINSPVAKFLNAEIIEDILDRT 384
Cdd:PRK12820 326 KQILQR-GGRIKGINIKGQSEKLSKNVlqNEYAKeIAPSFGAKGMTWMRAEA-----GGLDSNIVQFFSADEKEALKRRF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 385 AAQDGDMIFFGAD-NKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSP--KDMTAAE 461
Cdd:PRK12820 400 HAEDGDVIIMIADaSCAIVLSALGQLRLHLADRLGLIPEGVFHPLWITDFPLFEATDDGGVTSSHHPFTAPdrEDFDPGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 462 LKAApENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTML 541
Cdd:PRK12820 480 IEEL-LDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEEDIEDKFGFFLRAFDFAAPPHGGIALGLDRVVSM 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 16129819 542 LTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSI 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 |
1.14e-162 |
|
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: 465.13 E-value: 1.14e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 138 LKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFR 217
Cdd:cd00777 1 LRLRSRVIKAIRNFLDEQGFVEIETPILTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 218 DEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDL-GDFPVMTFAEAERRYGsdkpdlrnpmeltdva 296
Cdd:cd00777 81 DEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVELtTPFPRMTYAEAMERYG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 297 dllksvefavfagpandpkgrvaalrvpggasltrkqideygnfvkiygakglayikvnerakgleginspvakflnaei 376
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 377 iedildrtaaqdgdmiffgadnkkivadamgalrlkvgkdlgltdeskWAPLWVIDFPMFE-DDGEGGLTAMHHPFTSPK 455
Cdd:cd00777 145 ------------------------------------------------FKFLWIVDFPLFEwDEEEGRLVSAHHPFTAPK 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 456 DMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGL 535
Cdd:cd00777 177 EEDLDLLEKDPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEEEAEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|...
gi 16129819 536 DRLTMLLTGTDNIRDVIAFPKTT 558
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQ 279
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
118-558 |
2.48e-140 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 409.65 E-value: 2.48e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 118 EEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTK-ATPEGARDYLVPSRVHkGKFYALPQSPQL 196
Cdd:pfam00152 2 EETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKsATPEGARDFLVPSRAL-GKFYALPQSPQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 197 FKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGV----------DL-G 265
Cdd:pfam00152 81 YKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEVEGIakeleggtllDLkK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 266 DFPVMTFAEAERR----------YGSDKPDLRNPMELTdvadllksvefavfagpandpkgrvaalrvpggasltrkqid 335
Cdd:pfam00152 161 PFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLELV------------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 336 eygnfvkiygakglayikvnerakgleginspvakflnaeiiedildrtaaqdgdmiffgadnkkivadamgalrlkvgk 415
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 416 dlglTDESKWAPLWVIDFPmfeddgeggltAMHHPFTSPKDMTaaelkaapENAVANAYDMVINGYEVGGGSVRIHNGDM 495
Cdd:pfam00152 199 ----IDKNKFNPLWVTDFP-----------AEHHPFTMPKDED--------DPALAEAFDLVLNGVEIGGGSIRIHDPEL 255
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129819 496 QQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTT 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 |
5.00e-113 |
|
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: 337.91 E-value: 5.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 138 LKTRAKITSLVRRFMDDHGFLDIETPMLTKATP-EGARDYLVPSRvHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCF 216
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGgAGARPFLVKYN-ALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 217 RDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGV-----------DLGDFPVMTFAEAERRYGsdkpd 285
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLAREVLGVtavtygfeledFGLPFPRLTYREALERYG----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 286 lrnpmeltdvadllksvefavfagpandpkgrvaalrvpggasltrkqideygnfvkiygakglayikvnerakglegin 365
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 366 spvakflnaeiiedildrtaaqdgdmiffgadnkkivadamgalrlkvgkdlgltdeskwAPLWVIDFPMFeddgegglt 445
Cdd:cd00669 155 ------------------------------------------------------------QPLFLTDYPAE--------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 446 aMHHPFTSPKDMTaaelkaapeNAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGT 525
Cdd:cd00669 166 -MHSPLASPHDVN---------PEIADAFDLFINGVEVGNGSSRLHDPDIQAEVFQEQGINKEAGMEYFEFYLKALEYGL 235
|
410 420 430
....*....|....*....|....*....|....
gi 16129819 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 |
2.35e-77 |
|
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.
Pssm-ID: 239812 [Multi-domain] Cd Length: 135 Bit Score: 240.89 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 2 RTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEK 81
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHGGLIFIDLRDRYGIVQVVFDPEEAPEFELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129819 82 NINRDMATGEIEVLASSLTIINRADVLPL---DSNHVNtEEARLKYRYLDLRRPEM 134
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTLPFeidDDVNVS-EELRLKYRYLDLRRPKM 135
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
1-555 |
2.55e-72 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 238.55 E-value: 2.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 1 MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR-ADALKLASELRNEFCIQVTGTVRArD 79
Cdd:PRK05159 2 MKRHLTSELTPELDGEEVTLAGWVHEIRDLGGIAFLILRDRSGIIQVVVKKKVdEELFETIKKLKRESVVSVTGTVKA-N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 80 EKninrdmATGEIEVLASSLTIINRADV-LPLD-SNHVNTE-EARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHG 156
Cdd:PRK05159 81 PK------APGGVEVIPEEIEVLNKAEEpLPLDiSGKVLAElDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYENG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 157 FLDIETPMLTKATPEG-----ARDYLvpsrvhkGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFT 230
Cdd:PRK05159 155 FTEIFTPKIVASGTEGgaelfPIDYF-------EKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 231 QIDVETSFMTapQVREVM---EALVRHL----------WLEVKGVDL----GDFPVMTFAEAERRYGSDkpdlrnPMELT 293
Cdd:PRK05159 228 SIDVEMGFID--DHEDVMdllENLLRYMyedvaencekELELLGIELpvpeTPIPRITYDEAIEILKSK------GNEIS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 294 DVADLlksvefavfagpanDPKGrvaalrvpggasltrkqideygnfvkiygakglayikvnERAkgleginspvakfLN 373
Cdd:PRK05159 300 WGDDL--------------DTEG---------------------------------------ERL-------------LG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 374 AEIIEDildrtaaQDGDMIFfgadnkkivadamgalrlkvgkdlgltdeskwaplwVIDFPMfeddgeggltaMHHPF-T 452
Cdd:PRK05159 314 EYVKEE-------YGSDFYF------------------------------------ITDYPS-----------EKRPFyT 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 453 SPKDmtaaelkAAPEnaVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEeeqrEKFGFLLDALKYGTPPHAGLA 532
Cdd:PRK05159 340 MPDE-------DDPE--ISKSFDLLFRGLEITSGGQRIHRYDMLVESIKEKGLNP----ESFEFYLEAFKYGMPPHGGFG 406
|
570 580
....*....|....*....|...
gi 16129819 533 FGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK05159 407 LGLERLTMKLLGLENIREAVLFP 429
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-557 |
4.21e-70 |
|
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: 232.25 E-value: 4.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 2 RTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRArDEK 81
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGGISFLILRDGSGFIQVVVKKDKLENFEEAKKLTTESSVEVTGTVVE-SPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 82 ninrdmATGEIEVLASSLTIINRAD-VLPLD-SNHvnTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:COG0017 80 ------APQGVELQAEEIEVLGEADePYPLQpKRH--SLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQERGFVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 160 IETPMLTKATPEGAR-----DYLvpsrvhkGKFYALPQSPQLFKQLLMMSgFDRYYQIVKCFRDEDLRADRQ-PEFTQID 233
Cdd:COG0017 152 VHTPIITASATEGGGelfpvDYF-------GKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNTRRHlAEFWMIE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 234 VETSFMTAPQVREVMEALVRHL----------WLEVKGVDL--------GDFPVMTFAEAerrygsdkpdlrnpmeltdv 295
Cdd:COG0017 224 PEMAFADLEDVMDLAEEMLKYIikyvlencpeELEFLGRDVerlekvpeSPFPRITYTEA-------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 296 adllksvefavfagpandpkgrvaalrvpggasltrkqideygnfVKIYGAKGlayikvnerakgleginspvakflnaE 375
Cdd:COG0017 284 ---------------------------------------------IEILKKSG--------------------------E 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 376 IIEDILDrtaaqdgdmifFGADNKKIVADamgalrlKVGKDlgltdeskwaPLWVIDFPM----F-----EDDGEgglta 446
Cdd:COG0017 293 KVEWGDD-----------LGTEHERYLGE-------EFFKK----------PVFVTDYPKeikaFymkpnPDDPK----- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 447 mhhpftspkdmtaaelkaapenaVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGINEEEqrekFGFLLDALKYGT 525
Cdd:COG0017 340 -----------------------TVAAFDLLAPGIgEIIGGSQREHRYDVLVERIKEKGLDPED----YEWYLDLRRYGS 392
|
570 580 590
....*....|....*....|....*....|..
gi 16129819 526 PPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKT 557
Cdd:COG0017 393 VPHAGFGLGLERLVMWLTGLENIREVIPFPRD 424
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
2-555 |
1.45e-40 |
|
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: 154.04 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 2 RTEYCGQLRLSH--------VGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRadalkLASELRNEFC----- 68
Cdd:COG1190 35 RTHTAAEIREKYdeleaeeeTGDEVSVAGRIMAKRDMGKASFADLQDGSGRIQLYLRRDE-----LGEEAYELFKlldlg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 69 --IQVTGTV-RARdekninrdmaTGEIEVLASSLTIINRAdVLPL-DSNHVNTE-EARLKYRYLDL-RRPEMAQRLKTRA 142
Cdd:COG1190 110 diVGVEGTVfRTK----------TGELSVKVEELTLLSKS-LRPLpEKFHGLTDpETRYRQRYVDLiVNPEVRETFRKRS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 143 KITSLVRRFMDDHGFLDIETPMLTkATPEGA-------------RD-YLvpsRVhkgkfyalpqSPQLF-KQLLMmSGFD 207
Cdd:COG1190 179 KIIRAIRRFLDERGFLEVETPMLQ-PIAGGAaarpfithhnaldMDlYL---RI----------APELYlKRLIV-GGFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 208 RYYQIVKCFRDEDLRADRQPEFTQI-------DVETsfmtapqVREVMEALVRHLWLEVKG----------VDL-GDFPV 269
Cdd:COG1190 244 RVFEIGRNFRNEGIDTTHNPEFTMLelyqayaDYND-------MMDLTEELIREAAEAVLGttkvtyqgqeIDLsPPWRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 270 MTFAEAERRYGSdkpdlRNPMELTDVADLlksvefavfagpandpkgrvaalrvpggasltRKQIDEYGnfvkiygakgl 349
Cdd:COG1190 317 ITMVEAIKEATG-----IDVTPLTDDEEL--------------------------------RALAKELG----------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 350 ayIKVNERA-KGleginspvakflnaEIIEDILDRtaaqdgdmiffgadnkkivadamgalrlKVGKDLgltdeskWAPL 428
Cdd:COG1190 349 --IEVDPGWgRG--------------KLIDELFEE----------------------------LVEPKL-------IQPT 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 429 WVIDFPmfeddgeggltamhhPFTSPkdmtaaeL-KAAPEN-AVANAYDMVINGYEVGggsvrihNGdmqqtvFgilgiN 506
Cdd:COG1190 378 FVTDYP---------------VEVSP-------LaKRHRDDpGLTERFELFIAGREIA-------NA------F-----S 417
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129819 507 E----EEQREKF---------G----------FLlDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:COG1190 418 ElndpIDQRERFeeqlelkaaGddeampmdedFL-RALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
117-558 |
8.12e-38 |
|
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.
Pssm-ID: 238399 [Multi-domain] Cd Length: 322 Bit Score: 142.32 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 117 TEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGardylvPSRVHKGKFYA----LPQ 192
Cdd:cd00776 3 NLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEG------GAELFKVSYFGkpayLAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 193 SPQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETSFMTA-PQVREVMEALVRHLW---LEVKGVDLgdf 267
Cdd:cd00776 77 SPQLYKE-MLIAALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFIEDyNEVMDLIEELIKYIFkrvLERCAKEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 268 pvmtfaEAERRYGSDKPDLRNP---MELTDVADLLKSvefavfAGPANDPKgrvaalrvpggasltrkqideYGnfvkiy 344
Cdd:cd00776 153 ------ELVNQLNRELLKPLEPfprITYDEAIELLRE------KGVEEEVK---------------------WG------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 345 gakglayikvnerakglEGINSPVAKFLNAEIiedildrtaaqDGDMIFfgadnkkivadamgalrlkvgkdlgLTDesk 424
Cdd:cd00776 194 -----------------EDLSTEHERLLGEIV-----------KGDPVF-------------------------VTD--- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 425 WaPLWVIDFPMFEDDGEGGLTamhhpftspkdmtaaelkaapenavaNAYDMVINGY-EVGGGSVRIHNGDMQQTVFGIL 503
Cdd:cd00776 218 Y-PKEIKPFYMKPDDDNPETV--------------------------ESFDLLMPGVgEIVGGSQRIHDYDELEERIKEH 270
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129819 504 GINeeeqREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTT 558
Cdd:cd00776 271 GLD----PESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFPRDP 321
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
15-555 |
7.54e-35 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 138.58 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 15 GQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFC-----IQVTGTVRaRDEKninrdmat 89
Cdd:PLN02502 108 DVSVSVAGRIMAKRAFGKLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKLHSLVdrgdiVGVTGTPG-KTKK-------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 90 GEIEVLASSLTIINRAdVLPLDSNHVNTE--EARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPML- 165
Cdd:PLN02502 179 GELSIFPTSFEVLTKC-LLMLPDKYHGLTdqETRYRQRYLDLiANPEVRDIFRTRAKIISYIRRFLDDRGFLEVETPMLn 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 166 TKATPEGARdylvPSRVHKG----KFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTA 241
Cdd:PLN02502 258 MIAGGAAAR----PFVTHHNdlnmDLY-LRIATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADY 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 242 PQVREVMEALVRHLWLEVKgvdlGDFPVMtfaeaerrYGSDKPDLRNPMELTDVADLLKsvefavfagpandpkgRVAAL 321
Cdd:PLN02502 333 NDMMELTEEMVSGMVKELT----GSYKIK--------YHGIEIDFTPPFRRISMISLVE----------------EATGI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 322 RVPGGASltrkqideygnfvkiyGAKGLAYIKVNErAKGLEGINSP--VAKFLNaEIIEDILDRTAAQdgdmiffgadnk 399
Cdd:PLN02502 385 DFPADLK----------------SDEANAYLIAAC-EKFDVKCPPPqtTGRLLN-ELFEEFLEETLVQ------------ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 400 kivadamgalrlkvgkdlgltdeskwaPLWVIDFPMfeddgEGGLTAMHHpfTSPKDMTAA-ELKAApENAVANAY---- 474
Cdd:PLN02502 435 ---------------------------PTFVLDHPV-----EMSPLAKPH--RSKPGLTERfELFIN-GRELANAFselt 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 475 DMVINgYEVGGGSVRIHNGDMQQTVFgilgINEEeqrekfgfLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAF 554
Cdd:PLN02502 480 DPVDQ-RERFEEQVKQHNAGDDEAMA----LDED--------FCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAF 546
|
.
gi 16129819 555 P 555
Cdd:PLN02502 547 P 547
|
|
| GAD |
pfam02938 |
GAD domain; This domain is found in some members of the GatB and aspartyl tRNA synthetases. |
307-406 |
1.31e-34 |
|
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: 125.84 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 307 FAGPANdPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNErakglEGINSPVAKFLNAEIIEDILDRTAA 386
Cdd:pfam02938 1 FSEALK-SGGSVKALRVPGAAGLSRKEIDELERFAKEYGAKGLAWIKVEG-----GGHTGPIAKFLTEEEVEKLLEAVGA 74
|
90 100
....*....|....*....|
gi 16129819 387 QDGDMIFFGADNKKIVADAM 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 |
5.68e-34 |
|
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: 123.83 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADAL-KLASELRNEFCIQVTGTVRARDEKNinrdMATGEIEVL 95
Cdd:cd04100 1 EVTLAGWVHSRRDHGGLIFIDLRDGSGIVQVVVNKEELGEFfEEAEKLRTESVVGVTGTVVKRPEGN----LATGEIELQ 76
|
....*....
gi 16129819 96 ASSLTIINR 104
Cdd:cd04100 77 AEELEVLSK 85
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
11-555 |
2.66e-32 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 130.21 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 11 LSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDradalKLASELRNEF-------CIQVTGTVRARDekni 83
Cdd:PRK00484 50 LEELEIEVSVAGRVMLKRVMGKASFATLQDGSGRIQLYVSKD-----DVGEEALEAFkkldlgdIIGVEGTLFKTK---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 84 nrdmaTGEIEVLASSLTIINRAdVLPL-DSNH-VNTEEARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDI 160
Cdd:PRK00484 121 -----TGELSVKATELTLLTKS-LRPLpDKFHgLTDVETRYRQRYVDLiVNPESRETFRKRSKIISAIRRFLDNRGFLEV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 161 ETPMLtKATPEG--AR---------D---YLvpsRVhkgkfyalpqSPQLF-KQLLmMSGFDRYYQIVKCFRDEDLRADR 225
Cdd:PRK00484 195 ETPML-QPIAGGaaARpfithhnalDidlYL---RI----------APELYlKRLI-VGGFERVYEIGRNFRNEGIDTRH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 226 QPEFTQI-------DVETSfMtapqvrEVMEALVRHLWLEVKG----------VDLG-DFPVMTFAEAERRYGSDKPDLR 287
Cdd:PRK00484 260 NPEFTMLefyqayaDYNDM-M------DLTEELIRHLAQAVLGttkvtyqgteIDFGpPFKRLTMVDAIKEYTGVDFDDM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 288 NPMELTDVADLLKsvefavfagpandpkgrvaalrvpggasltrkqideygnfvkiygakglayIKVNERAKgleginsp 367
Cdd:PRK00484 333 TDEEARALAKELG---------------------------------------------------IEVEKSWG-------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 368 VAKFLNAeiiedildrtaaqdgdmiFFGAdnkkivadamgalrlKVGKDLgltdeskWAPLWVIDFPmFEddgeggltam 447
Cdd:PRK00484 354 LGKLINE------------------LFEE---------------FVEPKL-------IQPTFITDYP-VE---------- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 448 hhpfTSPkdmtaaeL-KAAPEN-AVANAYDMVINGYEVGggsvrihNGdmqqtvFgilgiNE----EEQREKF------- 514
Cdd:PRK00484 383 ----ISP-------LaKRHREDpGLTERFELFIGGREIA-------NA------F-----SElndpIDQRERFeaqveak 433
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 16129819 515 --G----------FlLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK00484 434 eaGddeamfmdedF-LRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
13-557 |
2.03e-29 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 121.37 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 13 HVGQQVTLCGWVNRRRDLGSLIFIDMRDREGI--VQVFFDPDrADALKLASELRNEFCIQVTGTVRArDEKninrdmATG 90
Cdd:PRK03932 14 YVGQEVTVRGWVRTKRDSGKIAFLQLRDGSCFkqLQVVKDNG-EEYFEEIKKLTTGSSVIVTGTVVE-SPR------AGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 91 EIEVLASSLTII-NRADVLPLDS-NHvnTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKA 168
Cdd:PRK03932 86 GYELQATKIEVIgEDPEDYPIQKkRH--SIEFLREIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNENGFVWVDTPIITAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 169 TPEGA----------RDYlvpsrvhKGKFYA----LPQSPQLFKQLLMMsGFDRYYQIVKCFRDEDLRADRQ-PEFTQID 233
Cdd:PRK03932 164 DCEGAgelfrvttldLDF-------SKDFFGkeayLTVSGQLYAEAYAM-ALGKVYTFGPTFRAENSNTRRHlAEFWMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 234 VETSFMTAPQVREVMEALVRHLwleVKGV------DLGDFpvmtfaeaERRYgsDKPDLrnpmeltdvaDLLKSVefavf 307
Cdd:PRK03932 236 PEMAFADLEDNMDLAEEMLKYV---VKYVlencpdDLEFL--------NRRV--DKGDI----------ERLENF----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 308 agpANDPKGRVaalrvpggasltrkqidEYGNFVKIYGAKGlayikvnerakgleginspvAKFLNAeiiedildrtaaq 387
Cdd:PRK03932 288 ---IESPFPRI-----------------TYTEAIEILQKSG--------------------KKFEFP------------- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 388 dgdmIFFGAdnkkivadamgalrlkvgkDLGlTDESKW-------APLWVIDFpmfeddgeggltamhhpftsPKDMTAA 460
Cdd:PRK03932 315 ----VEWGD-------------------DLG-SEHERYlaeehfkKPVFVTNY--------------------PKDIKAF 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 461 ELKAAPENAVANAYDMVINGY-EVGGGSVRIHNGD-----MQQtvfgiLGINEEEqrekFGFLLDALKYGTPPHAGLAFG 534
Cdd:PRK03932 351 YMRLNPDGKTVAAMDLLAPGIgEIIGGSQREERLDvlearIKE-----LGLNKED----YWWYLDLRRYGSVPHSGFGLG 421
|
570 580
....*....|....*....|...
gi 16129819 535 LDRLTMLLTGTDNIRDVIAFPKT 557
Cdd:PRK03932 422 FERLVAYITGLDNIRDVIPFPRT 444
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
7-556 |
5.67e-27 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 114.80 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 7 GQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQ--VFFDPDRADA--LKLASELRNEFCIQVTGTVrARDEKN 82
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGKGKSAFLVLRQSGFTVQcvVFVSEVTVSKgmVKYAKQLSRESVVDVEGVV-SVPKKP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 83 InrDMATGEIEVLASSLTIINRAD-VLPL--------DSN------------HVNtEEARLKYRYLDLRRPEMAQRLKTR 141
Cdd:PLN02850 152 V--KGTTQQVEIQVRKIYCVSKALaTLPFnvedaarsESEiekalqtgeqlvRVG-QDTRLNNRVLDLRTPANQAIFRIQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 142 AKITSLVRRFMDDHGFLDIETPMLTKATPEGAR-----DYlvpsrvhKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCF 216
Cdd:PLN02850 229 SQVCNLFREFLLSKGFVEIHTPKLIAGASEGGSavfrlDY-------KGQPACLAQSPQLHKQMAICGDFRRVFEIGPVF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 217 RDEDLRADRQ-PEFTQIDVEtsfMtapqvrEVMEalvrHlwlevkgvdlgdfpvmtfaeaerrYgsdkpdlrnpMELTDV 295
Cdd:PLN02850 302 RAEDSFTHRHlCEFTGLDLE---M------EIKE----H------------------------Y----------SEVLDV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 296 ADLLksvefavfagpandpkgrvaalrvpggasltrkqideygnFVKIYGakglayiKVNER-AKGLEGINS-----PVa 369
Cdd:PLN02850 335 VDEL----------------------------------------FVAIFD-------GLNERcKKELEAIREqypfePL- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 370 KFLN-------AEIIEdILDrtaaQDGDMIffgadnkkivaDAMGALRLKVGKDLGLTDESKWAplwvIDFPMfeddgeg 442
Cdd:PLN02850 367 KYLPktlrltfAEGIQ-MLK----EAGVEV-----------DPLGDLNTESERKLGQLVKEKYG----TDFYI------- 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 443 gltaMH------HPF-TSPkdmtaaelkaAPEN-AVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREkf 514
Cdd:PLN02850 420 ----LHryplavRPFyTMP----------CPDDpKYSNSFDVFIRGEEIISGAQRVHDPELLEKRAEECGIDVKTIST-- 483
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 16129819 515 gfLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PLN02850 484 --YIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPR 523
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
140-258 |
6.55e-27 |
|
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: 108.36 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 140 TRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARD----YLVPSRVHKGKFYALPQSPQLFKQLLMMS----GFDRYYQ 211
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGhepkDLLPVGAENEEDLYLRPTLEPGLVRLFVShirkLPLRLAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16129819 212 IVKCFRDEDLRAD--RQPEFTQIDVETSFMTAP------QVREVMEALVRHLWLE 258
Cdd:cd00768 81 IGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEeasefeELIELTEELLRALGIK 135
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
18-555 |
1.03e-25 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 112.05 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 18 VTLCGWVNRRRDLGSLIFIDMR----DREGIVQVFFDPDRADALKLASELRnefciqvTGTVRARDekNINRDMATGEIE 93
Cdd:PTZ00385 110 VRVAGRVTSVRDIGKIIFVTIRsngnELQVVGQVGEHFTREDLKKLKVSLR-------VGDIIGAD--GVPCRMQRGELS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 94 VLASSLTIIN----RADVLPLDSN---HVNTEEARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPML 165
Cdd:PTZ00385 181 VAASRMLILSpyvcTDQVVCPNLRgftVLQDNDVKYRYRFTDMmTNPCVIETIKKRHVMLQALRDYFNERNFVEVETPVL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 166 -TKATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQV 244
Cdd:PTZ00385 261 hTVASGANAKSFVTHHNANAMDLF-LRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSCEFYAAYHTYEDL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 245 REVMEALVRHLWLEVKGVdlgdfpVMTFAEAERRYGSDKP-DLRNPMELTDVADLLKS---VEFAvfagPANDpkgrvaa 320
Cdd:PTZ00385 340 MPMTEDIFRQLAMRVNGT------TVVQIYPENAHGNPVTvDLGKPFRRVSVYDEIQRmsgVEFP----PPNE------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 321 LRVPggasltrkqideygnfvkiygaKGLAYIKVnerAKGLEGINSPVAKfLNAEIIEDILDrtaaqdgdmiFFGADnkK 400
Cdd:PTZ00385 403 LNTP----------------------KGIAYMSV---VMLRYNIPLPPVR-TAAKMFEKLID----------FFITD--R 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 401 IVadamgalrlkvgkdlgltdeskwAPLWVIDFPMfeddgeggltamhhpFTSPkdmTAAELKAAPenAVANAYDMVING 480
Cdd:PTZ00385 445 VV-----------------------EPTFVMDHPL---------------FMSP---LAKEQVSRP--GLAERFELFVNG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 481 YEVGGGSVRIHNGD-----MQQTVFGILGINEEEQ--REKFgflLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:PTZ00385 482 IEYCNAYSELNDPHeqyhrFQQQLVDRQGGDEEAMplDETF---LKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGII 558
|
..
gi 16129819 554 FP 555
Cdd:PTZ00385 559 FP 560
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
2-555 |
3.63e-25 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 110.82 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 2 RTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLAsELRNEF----CIQVTGTV-R 76
Cdd:PRK02983 638 PTHTVAEALDAPTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLEQGSLA-DFRAAVdlgdLVEVTGTMgT 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 77 ARdekninrdmaTGEIEVLASSLTIINRaDVLPLDSNHV--NTEEARLKYRYLDLR-RPEMAQRLKTRAKITSLVRRFMD 153
Cdd:PRK02983 717 SR----------NGTLSLLVTSWRLAGK-CLRPLPDKWKglTDPEARVRQRYLDLAvNPEARDLLRARSAVVRAVRETLV 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 154 DHGFLDIETPMLTK----ATpegARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEF 229
Cdd:PRK02983 786 ARGFLEVETPILQQvhggAN---ARPFVTHINAYDMDLY-LRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNPEF 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 230 TqidvetsfmtapqvreVMEALVRHlwlevkgvdlGDFPVMtfaeaerrygsdkpdlrnpMELTDvaDLLKSVEFAVFag 309
Cdd:PRK02983 862 T----------------LLEAYQAH----------ADYDTM-------------------RDLTR--ELIQNAAQAAH-- 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 310 pandpkGRVAALRVPGGASLTRKQIDEYGNFVKIYGAkglayikVNErAKGLE-GINSPVAKflnaeiiediLDRTAAQD 388
Cdd:PRK02983 893 ------GAPVVMRPDGDGVLEPVDISGPWPVVTVHDA-------VSE-ALGEEiDPDTPLAE----------LRKLCDAA 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 389 GdmIFFGADnkkivADAmGALRLKVGKdlGLTDESKWAPLWVIDFPMfeddgEGGLTAMHHPfTSPKdmtaaelkaapen 468
Cdd:PRK02983 949 G--IPYRTD-----WDA-GAVVLELYE--HLVEDRTTFPTFYTDFPT-----SVSPLTRPHR-SDPG------------- 999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 469 aVANAYDMVINGYEVGGG-----------------SVRIHNGD---MqqtvfgilgineeEQREKFgflLDALKYGTPPH 528
Cdd:PRK02983 1000 -LAERWDLVAWGVELGTAyseltdpveqrrrlteqSLLAAGGDpeaM-------------ELDEDF---LQALEYAMPPT 1062
|
570 580
....*....|....*....|....*..
gi 16129819 529 AGLAFGLDRLTMLLTGTdNIRDVIAFP 555
Cdd:PRK02983 1063 GGLGMGVDRLVMLLTGR-SIRETLPFP 1088
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
132-555 |
5.06e-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: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 132 PEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLtKATPEG--ARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRY 209
Cdd:cd00775 2 EEVRQTFIVRSKIISYIRKFLDDRGFLEVETPML-QPIAGGaaARPFITHHNALDMDLY-LRIAPELYLKRLIVGGFERV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 210 YQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGvdlgdfpvmtfaEAERRYGSDKPDLRNP 289
Cdd:cd00775 80 YEIGRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGLVKKING------------KTKIEYGGKELDFTPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 290 MELTDVADLLKsvefavfagpandpkgrvaalrvpggasltrkqidEYGNfVKIYGAKGLAYIKVnERAKGLEGINSPVA 369
Cdd:cd00775 148 FKRVTMVDALK-----------------------------------EKTG-IDFPELDLEQPEEL-AKLLAKLIKEKIEK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 370 KFLNAEIIEDILDRtaaqdgdmiffgadnkkivadamgalrlKVGKDLgltdeskWAPLWVIDFPmfeddgeggltAMHH 449
Cdd:cd00775 191 PRTLGKLLDKLFEE----------------------------FVEPTL-------IQPTFIIDHP-----------VEIS 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 450 PFTspkdmtaaelKAAPENA-VANAYDMVINGYEVGGGSVRIHNGDMQQTVFgilginEEEQREK-------------Fg 515
Cdd:cd00775 225 PLA----------KRHRSNPgLTERFELFICGKEIANAYTELNDPFDQRERF------EEQAKQKeagddeammmdedF- 287
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16129819 516 flLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:cd00775 288 --VTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
11-555 |
6.32e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 99.37 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 11 LSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDradalKLASELRNE-FCIQVTGTVRARDEKNINRDmaT 89
Cdd:PRK12445 61 LESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARD-----SLPEGVYNDqFKKWDLGDIIGARGTLFKTQ--T 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 90 GEIEVLASSLTIINRA-DVLPLDSNHVNTEEARLKYRYLDL-RRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLtK 167
Cdd:PRK12445 134 GELSIHCTELRLLTKAlRPLPDKFHGLQDQEVRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMM-Q 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 168 ATPEGA--RDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVR 245
Cdd:PRK12445 213 VIPGGAsaRPFITHHNALDLDMY-LRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 246 EVMEALVRHLWLEVKGvdlgdfpvmtfaEAERRYGSDKPDLRNPMELTDVADLLKSvefavfagpaNDPKGRVAALrvpg 325
Cdd:PRK12445 292 ELTESLFRTLAQEVLG------------TTKVTYGEHVFDFGKPFEKLTMREAIKK----------YRPETDMADL---- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 326 gasltrkqideyGNFvkiYGAKGLAyikvnerakglEGINSPVAKFLN-AEIIEDILDRTAaqDGDMIffgadnkkivad 404
Cdd:PRK12445 346 ------------DNF---DAAKALA-----------ESIGITVEKSWGlGRIVTEIFDEVA--EAHLI------------ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 405 amgalrlkvgkdlgltdeskwAPLWVIDFPmfeddgeggltAMHHPFTSPKDMTaaelkaaPEnaVANAYDMVINGYEVG 484
Cdd:PRK12445 386 ---------------------QPTFITEYP-----------AEVSPLARRNDVN-------PE--ITDRFEFFIGGREIG 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129819 485 GGSVRIHNGDMQQTVFGIlGINEEEQREKFGFLLD-----ALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFP 555
Cdd:PRK12445 425 NGFSELNDAEDQAERFQE-QVNAKAAGDDEAMFYDedyvtALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
15-111 |
2.72e-21 |
|
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: 88.91 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 15 GQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFF--DPDRADALKLASELRNEFCIQVTGTVRArDEKninrdmATGEI 92
Cdd:cd04316 12 GEEVTVAGWVHEIRDLGGIKFVILRDREGIVQVTApkKKVDKELFKTVRKLSRESVISVTGTVKA-EPK------APNGV 84
|
90 100
....*....|....*....|
gi 16129819 93 EVLASSLTIINRAD-VLPLD 111
Cdd:cd04316 85 EIIPEEIEVLSEAKtPLPLD 104
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
14-556 |
1.57e-19 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 92.36 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 14 VGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDR---ADALKLASELRNEFCIQVTGTVrARDEKNINrDMATG 90
Cdd:PTZ00401 77 VDKTVLIRARVSTTRKKGKMAFMVLRDGSDSVQAMAAVEGdvpKEMIDFIGQIPTESIVDVEATV-CKVEQPIT-STSHS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 91 EIEVLASSLTIINRA-DVLPL---DSNHVNTEEA-------RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLD 159
Cdd:PTZ00401 155 DIELKVKKIHTVTESlRTLPFtleDASRKESDEGakvnfdtRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFCE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 160 IETPMLTKATPEGARDylVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQ-PEFTQIDVETSF 238
Cdd:PTZ00401 235 IHSPKIINAPSEGGAN--VFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 239 MTA-PQVREVMEALVRHLWLEVKGVDlgdfpvmtfAEAE---RRYGSDkpdlrnPMELTDVADLLKsvEFAVfagpandp 314
Cdd:PTZ00401 313 NEHyYEVLDLAESLFNYIFERLATHT---------KELKavcQQYPFE------PLVWKLTPERMK--ELGV-------- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 315 kgrvaalrvpGGASLTRKQIDEYGNFVKIYGAKGLAyikvnerakglegINSPVAkflnAEIIEDILDRTAAQDGDMiff 394
Cdd:PTZ00401 368 ----------GVISEGVEPTDKYQARVHNMDSRMLR-------------INYMHC----IELLNTVLEEKMAPTDDI--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 395 GADNKKIvadaMGAL-RLKVGKDLGLTDE--SKWAPLWVIDFPmfeDDGEggltamhhpFTspkdmtaaelkaapenava 471
Cdd:PTZ00401 418 NTTNEKL----LGKLvKERYGTDFFISDRfpSSARPFYTMECK---DDER---------FT------------------- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 472 NAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREkfgfLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDV 551
Cdd:PTZ00401 463 NSYDMFIRGEEISSGAQRIHDPDLLLARAKMLNVDLTPIKE----YVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLA 538
|
....*
gi 16129819 552 IAFPK 556
Cdd:PTZ00401 539 SLFPR 543
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
90-560 |
1.65e-17 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 85.83 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 90 GEIEVLASSLTIINRA-DVLPLDSNHVNTEeARLKYRYLDLRRPEMAQR-LKTRAKITSLVRRFMDDHGFLDIETPMLT- 166
Cdd:PTZ00417 204 GELSIFPKETIILSPClHMLPMKYGLKDTE-IRYRQRYLDLMINESTRStFITRTKIINYLRNFLNDRGFIEVETPTMNl 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 167 KATPEGARDYLVPSRVHKGKFYaLPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQV-- 244
Cdd:PTZ00417 283 VAGGANARPFITHHNDLDLDLY-LRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADFYDLik 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 245 --REVMEALVRHLWlevkgvdlGDFPVMtfaeaerrYGSDKPDlRNPMEL--------TDVADLLKSVEFAVFAGPANDP 314
Cdd:PTZ00417 362 wsEDFFSQLVMHLF--------GTYKIL--------YNKDGPE-KDPIEIdftppypkVSIVEELEKLTNTKLEQPFDSP 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 315 kgrvaalrvpggasltrKQIDEYGNFVKiygakglayikvnerAKGLEGINSPVAKFLnaeiiediLDRTAAQdgdmiFF 394
Cdd:PTZ00417 425 -----------------ETINKMINLIK---------------ENKIEMPNPPTAAKL--------LDQLASH-----FI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 395 gadnkkivadamgalrlkvgkdlgltdESKW--APLWVIDFPMfeddgeggltamhhpFTSPkdmTAAELKAAPenAVAN 472
Cdd:PTZ00417 460 ---------------------------ENKYpnKPFFIIEHPQ---------------IMSP---LAKYHRSKP--GLTE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 473 AYDMVINGYEVGGGSVRIHNGDMQQTVFGIlginEEEQREKF---GFLLDA-----LKYGTPPHAGLAFGLDRLTMLLTG 544
Cdd:PTZ00417 493 RLEMFICGKEVLNAYTELNDPFKQKECFSA----QQKDREKGdaeAFQFDAafctsLEYGLPPTGGLGLGIDRITMFLTN 568
|
490
....*....|....*.
gi 16129819 545 TDNIRDVIAFPKTTAA 560
Cdd:PTZ00417 569 KNCIKDVILFPTMRPA 584
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
18-102 |
2.41e-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: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 18 VTLCGWV-NRRRDLGSLIFIDMRDREGIVQVFFDPDraDALKLASELRNEFCIQVTGTVRARDEkninrdmatGEIEVLA 96
Cdd:pfam01336 1 VTVAGRVtSIRRSGGKLLFLTLRDGTGSIQVVVFKE--EAEKLAKKLKEGDVVRVTGKVKKRKG---------GELELVV 69
|
....*.
gi 16129819 97 SSLTII 102
Cdd:pfam01336 70 EEIELL 75
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
119-556 |
1.38e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 71.97 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 119 EARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARD-----YLVPSRVHKGKFYALPQS 193
Cdd:PRK06462 11 EEFLRMSWKHISSEKYRKVLKVQSSILRYTREFLDGRGFVEVLPPIISPSTDPLMGLgsdlpVKQISIDFYGVEYYLADS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 194 PQLFKQlLMMSGFDRYYQIVKCFRDEDLRADRQP---EFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFpvm 270
Cdd:PRK06462 91 MILHKQ-LALRMLGKIFYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYLVKELLEEHEDEL--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 271 tfaeaeRRYGSDKPDLRNPMELTDVADLLKSVEfavfagpandpkgrvaalrvpggaSLTRKQIDEygnfvkiygakgla 350
Cdd:PRK06462 167 ------EFFGRDLPHLKRPFKRITHKEAVEILN------------------------EEGCRGIDL-------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 351 yikvnerakglEGINSPVAKFLNAEIIEdildrtaaqdgdmiffgadnkkivadamgalrlkvgkdlgltdeskwaPLWV 430
Cdd:PRK06462 203 -----------EELGSEGEKSLSEHFEE------------------------------------------------PFWI 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 431 IDFPM-------FEDDGEGGltamhhpftspkdmtaaelkaapenaVANAYDMVI-NGY-EVGGGSVRIHngDMQQTVFG 501
Cdd:PRK06462 224 IDIPKgsrefydREDPERPG--------------------------VLRNYDLLLpEGYgEAVSGGEREY--EYEEIVER 275
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129819 502 IL--GINEeeqrEKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PRK06462 276 IRehGVDP----EKYKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPR 328
|
|
| PhAsnRS_like_N |
cd04319 |
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ... |
17-127 |
4.40e-13 |
|
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: 65.62 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRA-DALKLASELRNEFCIQVTGTVRArDEKninrdmATGEIEVL 95
Cdd:cd04319 1 KVTLAGWVYRKREVGKKAFIVLRDSTGIVQAVFSKDLNeEAYREAKKVGIESSVIVEGAVKA-DPR------APGGAEVH 73
|
90 100 110
....*....|....*....|....*....|..
gi 16129819 96 ASSLTIINRADVLPLDSNhvNTEEARLKYRYL 127
Cdd:cd04319 74 GEKLEIIQNVEFFPITED--ASDEFLLDVRHL 103
|
|
| PLN02603 |
PLN02603 |
asparaginyl-tRNA synthetase |
454-561 |
2.21e-12 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 178213 [Multi-domain] Cd Length: 565 Bit Score: 69.62 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 454 PKDMTAAELKAAPENAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGINeeeqREKFGFLLDALKYGTPPHAGLA 532
Cdd:PLN02603 459 PKEIKAFYMRENDDGKTVAAMDMLVPRVgELIGGSQREERLEYLEARLDELKLN----KESYWWYLDLRRYGSVPHAGFG 534
|
90 100
....*....|....*....|....*....
gi 16129819 533 FGLDRLTMLLTGTDNIRDVIAFPKTTAAA 561
Cdd:PLN02603 535 LGFERLVQFATGIDNIRDAIPFPRVPGSA 563
|
|
| PTZ00425 |
PTZ00425 |
asparagine-tRNA ligase; Provisional |
451-556 |
4.72e-11 |
|
asparagine-tRNA ligase; Provisional
Pssm-ID: 240414 [Multi-domain] Cd Length: 586 Bit Score: 65.43 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 451 FTSPKDMTAAELKAAPENAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFgilgINEEEQREKFGFLLDALKYGTPPHA 529
Cdd:PTZ00425 477 YNYPKDLKAFYMKLNEDQKTVAAMDVLVPKIgEVIGGSQREDNLERLDKMI----KEKKLNMESYWWYRQLRKFGSHPHA 552
|
90 100
....*....|....*....|....*..
gi 16129819 530 GLAFGLDRLTMLLTGTDNIRDVIAFPK 556
Cdd:PTZ00425 553 GFGLGFERLIMLVTGVDNIKDTIPFPR 579
|
|
| LysRS_N |
cd04322 |
LysRS_N: N-terminal, anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These ... |
17-129 |
1.72e-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: 52.48 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 17 QVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLAsELRNEF----CIQVTGTV-RARdekninrdmaTGE 91
Cdd:cd04322 1 EVSVAGRIMSKRGSGKLSFADLQDESGKIQVYVNKDDLGEEEFE-DFKKLLdlgdIIGVTGTPfKTK----------TGE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 16129819 92 IEVLASSLTIINRAdVLPLDSNH--VNTEEARLKYRYLDL 129
Cdd:cd04322 70 LSIFVKEFTLLSKS-LRPLPEKFhgLTDVETRYRQRYLDL 108
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
15-563 |
1.82e-08 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 57.31 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 15 GQQVTLCGWVNRRRDLG--SLIFIDMRDRE--GIVQVFFDPDRADALKLASelrNEFCIQVTGTVRARDEKNINRDmatg 90
Cdd:PLN02221 50 GQKVRIGGWVKTGREQGkgTFAFLEVNDGScpANLQVMVDSSLYDLSTLVA---TGTCVTVDGVLKVPPEGKGTKQ---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 91 EIEvlassLTIINRADVLPLDSNHVNTEEARLKYRYLdlrRPEMaqRLKTRAKITSLVRR-----------FMDDHGFLD 159
Cdd:PLN02221 123 KIE-----LSVEKVIDVGTVDPTKYPLPKTKLTLEFL---RDVL--HLRSRTNSISAVARirnalafathsFFQEHSFLY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 160 IETPMLTKATPEGArdylvpsrvhkgkfyalpqsPQLFKQLLMMSGFDRYyqivkcfrDEDLRADRQPefTQIDVETSFM 239
Cdd:PLN02221 193 IHTPIITTSDCEGA--------------------GEMFQVTTLINYTERL--------EQDLIDNPPP--TEADVEAARL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 240 TAPQVREVM------EALVRHLWLEVKGVDLGDfpvMTFAEAERRyGSDKPDLRNPMELTDVAdllksvefavfagpaND 313
Cdd:PLN02221 243 IVKERGEVVaqlkaaKASKEEITAAVAELKIAK---ESLAHIEER-SKLKPGLPKKDGKIDYS---------------KD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 314 PKGRVAALRVPGgasltRKQIDEYG-------NFVKIYGAKG----------------LAYIKVNERAKGLEGINSPVAK 370
Cdd:PLN02221 304 FFGRQAFLTVSG-----QLQVETYAcalssvyTFGPTFRAENshtsrhlaefwmvepeIAFADLEDDMNCAEAYVKYMCK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 371 FL------NAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAplwvIDFPmfeDDGEGGL 444
Cdd:PLN02221 379 WLldkcfdDMELMAKNFDSGCIDRLRMVASTPFGRITYTEAIELLEEAVAKGKEFDNNVEWG----IDLA---SEHERYL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 445 TAM--HHP---FTSPKDMTAAELKAAPENAVANAYDMVINGY-EVGGGSVRIHNGDMQQTVFGILGIneeeQREKFGFLL 518
Cdd:PLN02221 452 TEVlfQKPlivYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVgELIGGSQREERYDVIKQRIEEMGL----PIEPYEWYL 527
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 16129819 519 DALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACL 563
Cdd:PLN02221 528 DLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGKADL 572
|
|
| AsnRS_cyto_like_N |
cd04323 |
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ... |
18-77 |
1.84e-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: 1.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 18 VTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRA 77
Cdd:cd04323 2 VKVFGWVHRLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAKSLTQESSVEVTGEVKE 61
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
151-553 |
3.77e-08 |
|
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: 55.25 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 151 FMDDHGFLDIETPMLTKAT-PEGARDYL----VPSRVHKGKFYaLPQSPQLF-KQLLMmSGFDRYYQIVKCFRDEDLRAD 224
Cdd:TIGR00462 1 FFAERGVLEVETPLLSPAPvTDPHLDAFatefVGPDGQGRPLY-LQTSPEYAmKRLLA-AGSGPIFQICKVFRNGERGRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 225 RQPEFTQIDVETSFMTAPQVREVMEALVRHLwlevkgvdlgdfpvmtfaeaerrygsdKPDLRNPMELTDVADLlksveF 304
Cdd:TIGR00462 79 HNPEFTMLEWYRPGFDYHDLMDEVEALLQEL---------------------------LGDPFAPAERLSYQEA-----F 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 305 AVFAGPanDPkgrvaalrvpggASLTRKQIDEYGNFVKIYGAKGLAYikvnerakgleginspvakflnaeiiEDILDRt 384
Cdd:TIGR00462 127 LRYAGI--DP------------LTASLAELQAAAAAHGIRASEEDDR--------------------------DDLLDL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 385 aaqdgdmiffgadnkkivadamgALRLKVGKDLGltdesKWAPLWVIDFpmfeddgeggltamhhpftsPKDMTA-AELK 463
Cdd:TIGR00462 166 -----------------------LFSEKVEPHLG-----FGRPTFLYDY--------------------PASQAAlARIS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 464 AAPENaVANAYDMVINGYEVGggsvrihNGdmqqtvFGILgINEEEQREKF------------------GFLLDALKYGT 525
Cdd:TIGR00462 198 PDDPR-VAERFELYIKGLELA-------NG------FHEL-TDAAEQRRRFeadnalrkalglprypldERFLAALEAGL 262
|
410 420
....*....|....*....|....*...
gi 16129819 526 PPHAGLAFGLDRLTMLLTGTDNIRDVIA 553
Cdd:TIGR00462 263 PECSGVALGVDRLLMLALGADSIDDVLA 290
|
|
| PLN02532 |
PLN02532 |
asparagine-tRNA synthetase |
451-561 |
8.98e-08 |
|
asparagine-tRNA synthetase
Pssm-ID: 215291 [Multi-domain] Cd Length: 633 Bit Score: 55.26 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 451 FTSPKDMTAAELKAAPENAVANAYDMVI-NGYEVGGGSVRIHNGDMQQTVFGILGIneeeQREKFGFLLDALKYGTPPHA 529
Cdd:PLN02532 524 YNYPKELKPFYVRLNDDGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIEELGL----PREQYEWYLDLRRHGTVKHS 599
|
90 100 110
....*....|....*....|....*....|..
gi 16129819 530 GLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAA 561
Cdd:PLN02532 600 GFSLGFELMVLFATGLPDVRDAIPFPRSWGKA 631
|
|
| ScAspRS_mt_like_N |
cd04321 |
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
18-103 |
1.60e-07 |
|
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: 49.24 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 18 VTLCGWVNRRRDL-GSLIFIDMRDREG-IVQVfFDPDRADALKLASELRNEFCIQVTGTVRARDEKNinrDMATGEIEVL 95
Cdd:cd04321 2 VTLNGWIDRKPRIvKKLSFADLRDPNGdIIQL-VSTAKKDAFSLLKSITAESPVQVRGKLQLKEAKS---SEKNDEWELV 77
|
....*...
gi 16129819 96 ASSLTIIN 103
Cdd:cd04321 78 VDDIQTLN 85
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
467-551 |
1.67e-07 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 53.39 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 467 ENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFgilgINEEEQREKFGF--------LLDALKYGTPPHAGLAFGLDRL 538
Cdd:PRK09350 218 DHRVAERFEVYFKGIELANGFHELTDAREQRQRF----EQDNRKRAARGLpqqpidenLIAALEAGLPDCSGVALGVDRL 293
|
90
....*....|...
gi 16129819 539 TMLLTGTDNIRDV 551
Cdd:PRK09350 294 IMLALGAESISEV 306
|
|
| EcAsnRS_like_N |
cd04318 |
EcAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
17-102 |
3.04e-05 |
|
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: 42.55 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129819 17 QVTLCGWVNRRRDLGSLIFIDMRDreGI----VQVFFDPDRADAlKLASELRNEFCIQVTGTVRARDEKNinrdmatGEI 92
Cdd:cd04318 1 EVTVNGWVRSVRDSKKISFIELND--GSclknLQVVVDKELTNF-KEILKLSTGSSIRVEGVLVKSPGAK-------QPF 70
|
90
....*....|
gi 16129819 93 EVLASSLTII 102
Cdd:cd04318 71 ELQAEKIEVL 80
|
|
| PRK04036 |
PRK04036 |
DNA-directed DNA polymerase II small subunit; |
10-75 |
2.37e-03 |
|
DNA-directed DNA polymerase II small subunit;
Pssm-ID: 235208 [Multi-domain] Cd Length: 504 Bit Score: 40.70 E-value: 2.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129819 10 RLSHVGQQVTLCGWVNRRRDLGS-LIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTV 75
Cdd:PRK04036 148 KLKRGGEEVSIIGMVSDIRSTKNgHKIVELEDTTGTFPVLIMKDREDLAELADELLLDEVIGVEGTL 214
|
|
| |
