|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
3-1064 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 1518.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 3 GRKGTAKVDFLKEIEKEAQQKWEAEKVFEVSASRlekqKQSSKG-KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRL 81
Cdd:PLN02959 5 GGKSTARRDRLLEIEVAVQKWWEEEKVFEAEAGD----EPPKPGeKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 82 KGKSCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPEEEEEEEE-----SSAKPGDIVVRDKAKGKKSKAAAKAGSS 156
Cdd:PLN02959 81 RGANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEDEDEAAavaaaKAEAEAAAAPPDKFKGKKSKAVAKSGTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 157 KYQWDIMKSLGLSDDDIVKFSEAEHWLDYFPPLAVQDLKTIGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFG 236
Cdd:PLN02959 161 KYQWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTDVNPYYDAFVRWQFRKLKKKGKIVKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 237 KRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLVKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYI 316
Cdd:PLN02959 241 KRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPPFPGKLKALEGKKVFLAAATLRPETMYGQTNCWVLPDGKYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 317 GFETANGDIFICTQRAARNMSYQGFTKHNGVVPVVKELMGEEILGASLSAPLTCYKVVYVLPMLTIKEDKGTGVVTSVPS 396
Cdd:PLN02959 321 AYEINDTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSVPS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 397 DSPDDLAALRDLKKKQALRTKFGIRDDMVLPFEPVPVLEIPGIGNLPAVTVCDELKIQSQNDREKLAEAKEKLYLRGFYD 476
Cdd:PLN02959 401 DSPDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGFTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 477 GVMLVDGFKGQKIQHVKKTIQKNMIDAGDALIYMEPEKQVMSRSADECVVALCDQWYLDYGDENWKKQTFQCLKNMETFC 556
Cdd:PLN02959 481 GTMLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNLYS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 557 EESRKNFEASLDWLQEHACSRTYGLGTRLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGDLNGQAESPlgIRPQQMTKDV 636
Cdd:PLN02959 561 DETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGKDKSS--IKPEQMTDEV 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 637 WDYVfFKDAPFPKT-QIPKEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNHVAMWPEqsDKWPVSVRANGHLLLN 715
Cdd:PLN02959 639 WDFV-FCGGPLPKSsDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAE--EHWPRGFRCNGHLMLN 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 716 SEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMLASCSSLRSGPADSFN 795
Cdd:PLN02959 716 SEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLTKEIAWMEEVLAAESSLRTGPPSTYA 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 796 DRVFASEMNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYR-ELATEGMHRELVFRFIEVQTILLTPFCPHLCEHIW- 873
Cdd:PLN02959 796 DRVFENEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRlSCGSGGMNRDLVWRFMDVQTRLITPICPHYAEHVWr 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 874 TLLGKPDSIMHASWPVAGPVDESLIRSSQYLMEVAHDLRLRLKNYMMPAKGKKTDKQPAQRPSHCT---IYVAKNYPVWQ 950
Cdd:PLN02959 876 EILKKEGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKGGAPVTLPEKKLaglIYVAEKYDGWK 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 951 HITLTTLRSHFEANNGKL-PDNKVIA----SELGSLPELKKYMKKVMPFVAMIKENMEKKGPRVLDLELEFDEQAVLMEN 1025
Cdd:PLN02959 956 EECLRILQSKFDSQSRTFaPDAEILEalkeSSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQALDLKLPFDEIEVLQEN 1035
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 120537241 1026 IVYLTNSLELEHIEVKFASEAEDKVREEC----------CPGKPLNVFR 1064
Cdd:PLN02959 1036 LELIKRQLGLEEVEILSASDPDAVAKAGAhasllkqnppSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
14-1059 |
0e+00 |
|
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both archaeal and cytosolic eukaryotic leucyl-tRNA synthetases; the eubacterial and mitochondrial forms differ so substantially that some other tRNA ligases score higher by this model than does any eubacterial LeuS. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273056 [Multi-domain] Cd Length: 938 Bit Score: 869.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 14 KEIEKEAQQKWEAEKVFEVSASrlekqkqsSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLH 93
Cdd:TIGR00395 1 IAIEKKWQKRWEEAHIFEADPD--------DREKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 94 CTGMPIKACADKLKREIELYGcppdfpeeeeeeeessakpgdivvrdkakgkkskaaakagsskyqWDIMKSLGLSDDDI 173
Cdd:TIGR00395 73 VTGTPILGLAELIKRRDELTI---------------------------------------------KNYTEVHAIPREEL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 174 VKFSEAEHWLDYFPPLAVQDLKTIGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDH 253
Cdd:TIGR00395 108 LKFTDPEYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDH 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 254 DRQTGEGVGPQEYTLVKLKVLEpypsklsglkgKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETaNGDIFICTQRAA 333
Cdd:TIGR00395 186 DLLSGEGVTIVEYILIKFELED-----------GAFYFVAATLRPETVYGVTNCWVNPTITYVIAEV-GGEKWITSKEAF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 334 RNMSYQGFTkhngvVPVVKELMGEEILGASLSAPLTcYKVVYVLPMLTIKEDKGTGVVTSVPSDSPDDLAALRDLKKKQA 413
Cdd:TIGR00395 254 ENLSYQKLK-----YKPIEEVPGKQFIGKKVHNPVV-GPEVPILPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDPE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 414 LrtkFGIRDdMVLPFEPVPVLEIPGIGNLPAVTVCDELKIQSQNDREKLAEAKEKLYLRGFYDGVML--VDGFKGQKIQH 491
Cdd:TIGR00395 328 Y---LGIKP-VVIDIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIynIPPYKGMKVSE 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 492 VKKTIQKNMIDAGDALIYMEP-EKQVMSRSADECVVALC-DQWYLDYGDENWKKQTFQCLKNMETFCEESRKNFEASLDW 569
Cdd:TIGR00395 404 AKEKVKADLIDAGLADVMYEFsESPVICRCGTDCIVKVVeDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDW 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 570 LQEHACSRTYGLGTRLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGDlngqaesplgIRPQQMTKDVWDYVFFKDAPFPK 649
Cdd:TIGR00395 484 LKDWACCRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDY----------YGNEQMTDEFFDYIFLGKGDVKN 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 650 TQIPKEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNHVAMWPEqsDKWPVSVRANGHLLLNSEKMSKSTGNFLTL 729
Cdd:TIGR00395 554 TNIPLPAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPE--KFWPRGIVVNGYVMLEGKKMSKSKGNVLTL 631
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 730 SQAVDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEmLASCSSLRSGPADSFNDRVFASEMNAGIIK 809
Cdd:TIGR00395 632 EQAVEKFGADVARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEE-ITKESNLETGEETSFIDRWLESRMNAAIKE 710
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 810 TDQNYEKMMFKEALKTGFFEFQAAKDKYRElATEGMHRELVFRFIEVQTILLTPFCPHLCEHIWTLLGKPDSIMHASWPV 889
Cdd:TIGR00395 711 TYEAMENFQTRKAVKYALFDLQADVDWYRR-RGGVNHKDVLARYLETWIKLLAPFAPHFAEEMWEEVGNEGFVSLAKFPE 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 890 AG--PVDESLIRSSQYLMEVAHDLRlrlknymmpakgkKTDKQPAQRPSHCTIYVAknyPVWQHITLTTLRSHFEANNGK 967
Cdd:TIGR00395 790 ASepAVDKEVEAAEEYLRNLVRDIQ-------------EIAKIDASKPKRVYLYTS---EDWKSQCLKIVAELFGEDTGE 853
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 968 lpDNKVIASElgslPELKKYMKKVMPFVAMIKENMEKKGprvldlELEFDEQAVLMENIVYLTNSLELEHI-EVKFASEA 1046
Cdd:TIGR00395 854 --DMKKVMEE----PEERKRGKEVISLVKQIIKDEKKED------ELQISEIEVLKAAARFIKKEVGALVIiEFSADSFP 921
|
1050
....*....|...
gi 120537241 1047 EDKVReECCPGKP 1059
Cdd:TIGR00395 922 ENKKR-NAVPGKP 933
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
61-1059 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 746.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 61 LHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIKACADKLKReielygcppdfpeeeeeeeessakpgdivvRD 140
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR------------------------------GD 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 141 KAkgkkskaaakagsskyQWDIMKSL-GLSDDDIVKFSEAEHWLDYFPPLAVQDLKTIGLKVDWRRSFITTDvnPYYDSF 219
Cdd:PRK12300 51 PE----------------TIELYKSLyGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--PEYSKF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 220 VRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLVKLKvlepypsklsglKGKNIFLVAATLRPE 299
Cdd:PRK12300 113 IEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFE------------ESEDLILPAATLRPE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 300 TMFGQTNCWVRPDMKYIGFETaNGDIFICTQRAARNMSYQGFTkhngvVPVVKELMGEEILGASLSAPLTCyKVVYVLPM 379
Cdd:PRK12300 181 TIFGVTNLWVNPDATYVKAEV-DGEKWIVSKEAAEKLSFQDRD-----VEIIEEIKGSELIGKKVKNPVTG-KEVPILPA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 380 LTIKEDKGTGVVTSVPSDSPDDLAALRDLKKKQALrtkfgirddmVLPFEPVPVLEIPGIGNLPAVTVCDELKIQSQNDR 459
Cdd:PRK12300 254 DFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNKEL----------LDVIEPIPLIEVEGYGEFPAKEVVEKLGIKSQEDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 460 eKLAEAKEKLYLRGFYDGVMLVD--GFKGQKIQHVKKTIQKNMIDAGDALIYME-PEKQVMSRSADECVVA-LCDQWYLD 535
Cdd:PRK12300 324 -ELEEATKEVYRAEFHKGVLKENtgEYAGKPVREAREKITKDLIEKGIADIMYEfSNRPVYCRCGTECVVKvVKDQWFID 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 536 YGDENWKKQTFQCLKNMETFCEESRKNFEASLDWLQEHACSRTYGLGTRLPWDEQWLIESLSDSTIYMAFYTVAHLLQGG 615
Cdd:PRK12300 403 YSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAHKIREY 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 616 dlngqaesplGIRPQQMTKDVWDYVF----FKDAPFPKTQIPKEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNH 691
Cdd:PRK12300 483 ----------GIKPEQLTPEFFDYVFlgkgDPEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFIFNH 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 692 VAMWPEqsDKWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYT 771
Cdd:PRK12300 553 VAIFPE--EKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQLER 630
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 772 WVEWVKEMLascsSLRSGPADSFNDRVFASEMNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELaTEGMHRELVF 851
Cdd:PRK12300 631 FYELAKELI----EIGGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRR-VGEANNKVLR 705
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 852 RFIEVQTILLTPFCPHLCEHIWTLLGKPDSIMHASWPVAGP--VDESLIRSSQYLMEVAHDLRlRLKNYmmpAKGKktdk 929
Cdd:PRK12300 706 EVLEIWIRLLAPFTPHLAEELWHKLGGEGFVSLEKWPEPDEskIDEEAELAEEYVKRLIEDIR-EILKV---AKIK---- 777
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 930 qpaqrPSHCTIYVAknyPVWQHITLTTLRshfeanngKLPDNKVIASELGSLPELKKYMKKVMPFVAMIKENMEKKGPRV 1009
Cdd:PRK12300 778 -----PKKVYIYVA---PDWKYEVLEIAA--------ENGDVKEAIKELMKDEELRKHGKEVAKLAQKIVKEVLKLDKEV 841
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 120537241 1010 LDLELE-FDEQAVLMENIVYLTNSLELEhIEVKFASEAE-DKVREECCPGKP 1059
Cdd:PRK12300 842 RKLILKnIDEEEVLEEAKDFLEKELGVE-VEIYGADDPGkKKKKKKALPLKP 892
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
527-759 |
1.87e-72 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 244.08 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 527 ALCDQWYLDYGDENWKKQTFQCLKNMETFCEESRKNFEASLDwlqehaCSRTYGLGTRLPWdeQWLIESLSDSTIYMAFY 606
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 607 TVAHLLQGGDlngqaesplgirpqqmtkdvwdyvffkdapfpktqipKEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSY 686
Cdd:cd00812 199 TDAHNLEQPY-------------------------------------EGDLEFDREEFEYWYPVDIYIGGKEHAPNHLLY 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120537241 687 YIYNHVAMWPEQ--SDKWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDtvEDANFVE 759
Cdd:cd00812 242 SRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFDW 314
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
757-876 |
2.17e-50 |
|
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153413 [Multi-domain] Cd Length: 117 Bit Score: 173.55 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 757 FVEAMADAGILRLYTWVEWVKEMLASCSSLrsgPADSFNDRVFASEMNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDK 836
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 120537241 837 YRELATEGMHRELVFRFIEVQTILLTPFCPHLCEHIWTLL 876
Cdd:cd07959 78 YRERGGAGMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
47-231 |
1.14e-28 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 117.73 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 47 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIKACADKLKReielygcppdfpeeeeee 126
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 127 eessakpgdivvrdkakgkkskaaakagsskyqwdimkslglsdddivkfsEAEHWLDYFPPLAVQDLKTIGLKVDWRRS 206
Cdd:cd00812 63 ---------------------------------------------------DPEDWTEYNIKKMKEQLKRMGFSYDWRRE 91
|
170 180
....*....|....*....|....*
gi 120537241 207 FITTDvnPYYDSFVRWQFLTLRERN 231
Cdd:cd00812 92 FTTCD--PEYYKFTQWLFLKLYEKG 114
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
14-927 |
1.35e-25 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 114.39 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 14 KEIEKEAQQKWEAEKVFEVSASrlekqkqSSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLH 93
Cdd:TIGR00422 8 HEVEKKWYKKWEKSGFFKPDGN-------SNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 94 CTGMPIKACADK-LKREIELYGcppDFPeeeeeeeessakpgdivvRDkakgkkskaaakagsskyqwdimkslglsddd 172
Cdd:TIGR00422 81 HAGIATQVKVEKkLGAEGKTKH---DLG------------------RE-------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 173 ivKFSE-AEHWLDYFPPLAVQDLKTIGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCM 251
Cdd:TIGR00422 108 --EFREkIWEWKEESGGTIKNQIKRLGASLDWSRERFTMD--EGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAIS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 252 DHDrqtgegvgpQEYTLVKLKvLEPYPSKLSGlkGKNIFLVAATLRPETMFGQTNCWVRP-DMKYigfetangdifictq 330
Cdd:TIGR00422 184 DIE---------VEYKEVKGK-LYYIRYPLAN--GSKDYLVVATTRPETMFGDTAVAVHPeDERY--------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 331 raarnmsyqgftkhngvvpvvKELMGEEILgaslsAPLTCYKVvyvlPMLT---IKEDKGTGVVTSVPSDSPDDLAalrd 407
Cdd:TIGR00422 237 ---------------------KHLIGKKVI-----LPLTGRKI----PIIAdeyVDMEFGTGAVKVTPAHDFNDYE---- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 408 LKKKQALRTKFGIRDDMVLPFEpvpVLEIPGIGNLPAvtvcdelkiqsqndREKLAEAKEKLylrGFYDGVMLVDgfkgQ 487
Cdd:TIGR00422 283 WGKRHNLEFINILDEDGLLNEN---AGKYQGLTRFEA--------------RKKIVEDLKEE---GLLVKIEPHT----H 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 488 KIQHVKKTiqKNMIDagdalIYMEPEKQVMSRSADECVVALCDQWYLDYGDENWKKQTFQCLKNMEtfceesrknfeasl 567
Cdd:TIGR00422 339 NVGTCWRS--GTVVE-----PLLSKQWFVKVEKLADKALEAAEEGEIKFVPKRMEKRYLNWLRNIK-------------- 397
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 568 DWlqehaC-SRTYGLGTRLPwdeqwlieslsdstiymAFYTVahllQGGDLNGQAESPLGIRPQQMT--------KDVWD 638
Cdd:TIGR00422 398 DW-----CiSRQLIWGHRIP-----------------VWYCK----ECGEVYVAKEEPLPDDKTNTGpsveleqdTDVLD 451
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 639 yVFFKDA--PFPKTQIPKEKLDqlkqeFEFWYPVDLRASGKDLIPNHLSYYIYNHVAmwpeQSDKWPVS-------VR-A 708
Cdd:TIGR00422 452 -TWFSSSlwPFSTLGWPDETKD-----LKKFYPTDLLVTGYDIIFFWVARMIFRSLA----LTGQVPFKevyihglVRdE 521
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 709 NGHlllnseKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANFVEAMADAG---ILRLYTWVEWVKeMLASCSS 785
Cdd:TIGR00422 522 QGR------KMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESArnfLNKLWNASRFVL-MNLSDDL 594
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 786 LRSGPADSFN--DRVFASEMNAGIIKTDQNYEKMMFKEALKtGFFEFQAAK--DKYRELA-------TEGMHRELVFR-- 852
Cdd:TIGR00422 595 ELSGGEEKLSlaDRWILSKLNRTIKEVRKALDKYRFAEAAK-ALYEFIWNDfcDWYIELVkyrlyngNEAEKKAARDTly 673
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120537241 853 -FIEVQTILLTPFCPHLCEHIW-TLLGKPDSIMHASWPVAGP--VDESLIRSSQYLMEVAHDLRLRLKNYMMPAKGKKT 927
Cdd:TIGR00422 674 yVLDKALRLLHPFMPFITEEIWqHFKEGADSIMLQSYPVVDAefVDEEAEKAFELLKEIIVSIRNLKAESNIPPNAPLK 752
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
501-746 |
1.56e-22 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 99.80 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 501 IDAGDALIYMEPE-KQVMSRS-----------ADECVVALCDQWYLDYGDenWKKQTFQCLKNMETFCEESRKNFEASLD 568
Cdd:cd00668 99 YDWSDEYITTEPEySKAVELIfsrlyekgliyRGTHPVRITEQWFFDMPK--FKEKLLKALRRGKIVPEHVKNRMEAWLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 569 WLQEHACSRTYGLGTRLPwdeQWLIESLSDSTIYMAFYTvahllqggdlngqaesplgirpqqmtkdvwdyvffkDAPFp 648
Cdd:cd00668 177 SLLDWAISRQRYWGTPLP---EDVFDVWFDSGIGPLGSL------------------------------------GYPE- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 649 ktqipkekldqLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNHVAMWPEqsdKWPVSVRANGHLLLN-SEKMSKSTGNFL 727
Cdd:cd00668 217 -----------EKEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGE---IPPKNLLVHGFVLDEgGQKMSKSKGNVI 282
|
250
....*....|....*....
gi 120537241 728 TLSQAVDKFSADGMRLALA 746
Cdd:cd00668 283 DPSDVVEKYGADALRYYLT 301
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
21-757 |
6.93e-22 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 101.72 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 21 QQKWEAEKVFEVSasrLEKQKQssKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIk 100
Cdd:pfam00133 3 YEFWDEQGYFKPE---LEKRKG--KPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 101 acadklkreielygcppdfpeeeeeeeessakpgdivvrdkakgkkskaaakagsskyQWDIMKSLGLSDDDIV-KFSEA 179
Cdd:pfam00133 77 ----------------------------------------------------------EQVVEKKLGIKEKKTRhKYGRE 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 180 EH------WLDYFPPLAVQDLKTIGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDH 253
Cdd:pfam00133 99 EFrekcreWKMEYADEIRKQFRRLGRSIDWDREYFTMD--PELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 254 DRQTGEGVGPQEYTLVKLKVlepypsklsglkGKNIFLVAATLRPETMFGQTNCWVRPDMKYIgfetANGDIFICTQRAA 333
Cdd:pfam00133 177 EVEYKDVKGPSIHVAFPLAD------------DEGASLVIWTTTPWTLPGNTAVAVNPEFDYV----ITGEGYILAEALL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 334 RNMSYQGFTKhngvvPVVKELMGEEILGASLSAPLTCYKVvyvlPMLT---IKEDKGTGVVTSVPSDSPDDLAAlrdlkk 410
Cdd:pfam00133 241 KSLYKKGTDK-----KILEDFRGKELEGKEAIHPFVNREI----PIITddyVDMEFGTGAVHIAPAHGENDYEV------ 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 411 kqalrtkfGIRDdmvlpfepvpvleipgigNLPAVTVCDElkiqsqndreklaeakeklylrgfyDGVMLVDG--FKGQK 488
Cdd:pfam00133 306 --------GQRH------------------NLEVINPVDD-------------------------DGTFTEEApdFQGVY 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 489 IQHVKKTIQKNMIDAGdalIYMEPEKQVMS-----RSADECVVALCDQWYLDYgdENWKKQTFQCLKNMETFCEESRKNF 563
Cdd:pfam00133 335 RFDARKKIVELLTEKG---LLLKIEPFTHSypfcwRSGTPIIPRATPQWFVRM--DELADQALEAVEKVQFVPKSGEKRY 409
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 564 EASLDWLQEHACSRTYGLGTRLPWdeqWLIESLSDstIYMA---FYTVAHLLQGG----DLNGQAESPLGIRPQQMTK-- 634
Cdd:pfam00133 410 FNWLANIQDWCISRQRWWGHPIPA---WVSKDTEE--VVCRgelFELVAGRFEEEgsikWLHREAKDKLGYGKGTLEQde 484
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 635 DVWDyVFFKDAPFPKTQIpkEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNHVAMWPEQSDKwpvSVRANGhLLL 714
Cdd:pfam00133 485 DVLD-TWFSSGSWPFSTL--GWPFVNTEEFKKFFPADMLLEGSDQTRGWFYRMIMLSTALTGSVPFK---NVLVHG-LVR 557
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 120537241 715 NSE--KMSKSTGNFLTLSQAVDKFSADGMRLALADAgDTVEDANF 757
Cdd:pfam00133 558 DEQgrKMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
796-912 |
1.62e-16 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 77.44 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 796 DRVFASEMNAGIIKTDQNYEKMMFKEALKTGFFEFQ---------AAKDKYRELATEGMHRELVFRFIEVQTILLTPFCP 866
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWndlsdwyleLIKDRLYGEEPDSRAQTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 120537241 867 HLCEHIWtllgKPDSIMHASWPV-AGPVDESLIRSSQYLMEVAHDLR 912
Cdd:pfam08264 81 FITEELW----QKESIHLAPWPEdAELEEAELEEAFELRQEIVQAIR 123
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
676-890 |
5.60e-15 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 79.39 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 676 GKDlIpnhlsyyIYNHVAMWP---EQSD-KWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDT 751
Cdd:COG0143 289 GKD-I-------IRFHAIIWPamlMAAGlPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPF 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 752 VEDANF-VEAMAD------AGIL-----RlytwvewVKEMLAS--CSSLRSGPADSFNDRVFASEMNAGIIKTDQNYEKM 817
Cdd:COG0143 361 GQDGDFsWEDFVArvnsdlANDLgnlasR-------TLSMIHKyfDGKVPEPGELTEADEELLAEAEAALEEVAEAMEAF 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 818 MFKEALKT---------GFFEFQA----AKDKYRELATEGMHREL-VFRFIevqTILLTPFCPHLCEHIWTLLGKPDSIM 883
Cdd:COG0143 434 EFRKALEEimalaraanKYIDETApwklAKDEDPERLATVLYTLLeALRIL---AILLKPFLPETAEKILEQLGLEGDEL 510
|
250
....*....|
gi 120537241 884 ---HASWPVA 890
Cdd:COG0143 511 tweDAGWPLP 520
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
706-898 |
1.85e-12 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 72.01 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 706 VRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLAL------------ADAGdtVEDAN-FVEamadagilRLYTW 772
Cdd:COG0495 577 VGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEmfagpperdlewSDSG--VEGAYrFLN--------RVWRL 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 773 VEWVKEMLASCSSLRSGPadsfnDRVFASEMNAGIIKTDQNYEKMMFKEA------LKTGFFEFQAAKDKYRELATEGMh 846
Cdd:COG0495 647 VVDEAEALKLDVADLSEA-----DKELRRALHKTIKKVTEDIERLRFNTAiaalmeLVNALYKAKDSGEADRAVLREAL- 720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 120537241 847 relvfrfiEVQTILLTPFCPHLCEHIWTLLGKPDSIMHASWPVagpVDESLI 898
Cdd:COG0495 721 --------ETLVLLLAPFAPHIAEELWERLGHEGSVADAPWPE---ADEAAL 761
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
47-244 |
6.16e-12 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 68.21 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 47 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIKACADKLKreielygcppdfpeeeeee 126
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 127 eesSAKPGDIVvrdkakgkkskaaakagsskyqwdimkslglsdddIVKFSEA-EHWLDYFPPLAVQDLKTIGLKVDWRR 205
Cdd:cd00668 62 ---GRKKKTIW-----------------------------------IEEFREDpKEFVEEMSGEHKEDFRRLGISYDWSD 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 120537241 206 SFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSP 244
Cdd:cd00668 104 EYITTE--PEYSKAVELIFSRLYEKGLIYRGTHPVRITE 140
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
13-99 |
2.02e-11 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 68.30 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 13 LKEIEKEAQQKWEAEKVFevsasrleKQKQSSKGKYFV--TfPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPF 90
Cdd:PRK13208 12 PEELEEKWQKIWEEEGTY--------KFDPDERKPVYSidT-PPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQ 82
|
....*....
gi 120537241 91 GLHCTGMPI 99
Cdd:PRK13208 83 GWDDNGLPT 91
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
718-907 |
1.96e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 65.23 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 718 KMSKSTGNFLTLSQAVDKFSADGMRLaladagdtvedanFVEAMadaGILR-LYTW----VEWVKEMLASCSSLRSG--- 789
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRL-------------YEMFM---GPLRdSKTWstsgVEGVHRFLGRTWRLVVGapl 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 790 PADSFNDRVFASE----------MNAGIIKTDQNYEKMMFKEALkTGFFEFQAAKDKYRELATEgmhrelvfrFIEVQTI 859
Cdd:PLN02563 787 PDGSFRDGTVVTDeepsleqlrlLHKCIAKVTEEIESTRFNTAI-SAMMEFTNAAYKWDKVPRE---------AIEPFVL 856
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 120537241 860 LLTPFCPHLCEHIWTLLGKPDSIMHASWPVAgpvDESLIRSSQYLMEV 907
Cdd:PLN02563 857 LLSPYAPHLAEELWFRLGHSNSLAYEPWPEA---NPSYLVDDTVVLPV 901
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
718-926 |
3.82e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 64.36 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 718 KMSKSTGNF---LTLsqaVDKFSADGMRLALAdagdtvedanfveAMADAGI-LRL-YTWVE---------W-----VKE 778
Cdd:PRK05729 520 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIRFdEERVEgyrnfanklWnasrfVLM 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 779 MLASCSSLRSGPADSFN--DRVFASEMNAGIIKTDQNYEKMMFKEALKT--GFF--EF-----QAAKDKYRELATEGMHR 847
Cdd:PRK05729 584 NLEGADVGELPDPEELSlaDRWILSRLNRTVAEVTEALDKYRFDEAARAlyEFIwnEFcdwylELAKPVLQEAAKRATRA 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 848 ELVFRFIEVQtILLTPFCPHLCEHIWTLL---GKPDSIMHASWPVAGPV-DESLIRSSQYLMEVAHDLRlRLKNYMMPAK 923
Cdd:PRK05729 664 TLAYVLEQIL-RLLHPFMPFITEELWQKLaplGIEESIMLAPWPEADEAiDEAAEAEFEWLKELITAIR-NIRAEMNIPP 741
|
...
gi 120537241 924 GKK 926
Cdd:PRK05729 742 SKK 744
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
676-880 |
4.13e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 60.94 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 676 GKDLIpnhlsyyiYNHVAMWP---EQSD-KWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALA-DAGD 750
Cdd:PRK00133 291 GKDII--------YFHTLFWPamlEGAGyRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAaKLPE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 751 TVEDANFveamadagilrlyTWVEWVK----EM------LAScsslRS----------GPADSFNDRVFASEMNAGIIKT 810
Cdd:PRK00133 363 TIDDLDF-------------NWEDFQQrvnsELvgkvvnFAS----RTagfinkrfdgKLPDALADPELLEEFEAAAEKI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 811 DQNYEKMMFKEALKT---------GFFEFQA----AKDKYRELATEgMHREL-VFRFIevqTILLTPFCPHLCEHIWTLL 876
Cdd:PRK00133 426 AEAYEAREFRKALREimaladfanKYVDDNEpwklAKQDGERLQAV-CSVGLnLFRAL---AIYLKPVLPELAERAEAFL 501
|
....
gi 120537241 877 GKPD 880
Cdd:PRK00133 502 NLEE 505
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
718-912 |
7.77e-09 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 60.06 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 718 KMSKSTGNF---LTLsqaVDKFSADGMRLALAdagdtvedanfveAMADAGI-LRLYT-WVE---------W-----VKE 778
Cdd:COG0525 522 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIKFDEeRVEgyrnfanklWnasrfVLM 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 779 MLASCSSLRSGPADSFN--DRVFASEMNAGIIKTDQNYEKMMFKEALKT--GFF--EFQaakDKYRELA-------TEGM 845
Cdd:COG0525 586 NLEGFDPGLDPDPEELSlaDRWILSRLNKTIAEVTEALEKYRFDEAAQAlyDFVwnEFC---DWYLELAkprlyggDEAA 662
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120537241 846 HRE----LVfRFIEVQTILLTPFCPHLCEHIWTLLGKP---DSIMHASWPVAGP--VDESLIRSSQYLMEVAHDLR 912
Cdd:COG0525 663 KREtratLV-YVLEQILRLLHPFMPFITEEIWQKLPPRkegESIMLAPWPEADEelIDEEAEAEFEWLKEVISAIR 737
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
639-757 |
1.05e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 58.84 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 639 YVFFkDAPFPKTQIPKEkLDQLKQEFEFWYPVDLRAS-----GKDLIpnhlsyyiYNHVAMWP----EQSDKWPVSVRAN 709
Cdd:pfam09334 246 YVWL-DAPIGYISATKE-LSGNEEKWKEWWPNDPDTElvhfiGKDII--------YFHTIFWPamllGAGYRLPTTVFAH 315
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 120537241 710 GHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANF 757
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDF 363
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
709-745 |
2.21e-08 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 58.19 E-value: 2.21e-08
10 20 30
....*....|....*....|....*....|....*..
gi 120537241 709 NGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLAL 745
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
709-745 |
3.77e-08 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 55.28 E-value: 3.77e-08
10 20 30
....*....|....*....|....*....|....*..
gi 120537241 709 NGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLAL 745
Cdd:cd00672 165 TGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
695-896 |
5.91e-08 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 57.31 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 695 WPEQSDK----WPVSVRANGHLLL--------------------------------NSEKMSKSTGNFLTLSQAVDKFSA 738
Cdd:PRK14900 479 WPEQTDTlrtfYPTSVMETGHDIIffwvarmmmmglhfmgevpfrtvylhpmvrdeKGQKMSKTKGNVIDPLVITEQYGA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 739 DGMRLALAD----------AGDTVEDAN-FVEAMADAGILRLYTWVEWVKEMLASCSSLRSgPADsfndRVFASEMNAGI 807
Cdd:PRK14900 559 DALRFTLAAltaqgrdiklAKERIEGYRaFANKLWNASRFALMNLSGYQERGEDPARLART-PAD----RWILARLQRAV 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 808 IKTDQNYEKMMFKEALKTGF-FEFQAAKDKYRELATEGMH----------RELVFRFIEVQTILLTPFCPHLCEHIWTLL 876
Cdd:PRK14900 634 NETVEALEAFRFNDAANAVYaFVWHELCDWYIELAKEALAsedpearrsvQAVLVHCLQTSYRLLHPFMPFITEELWHVL 713
|
250 260
....*....|....*....|....*..
gi 120537241 877 -------GKPDSIMHASWPVAGPVDES 896
Cdd:PRK14900 714 raqvgasAWADSVLAAEYPRKGEADEA 740
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
666-882 |
7.79e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 56.43 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 666 FWyPVDLRASGKDLIPNHLSYyiynhvamWPEQ--SDKWPV--SVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGM 741
Cdd:PRK11893 252 YW-PADVHLIGKDILRFHAVY--------WPAFlmAAGLPLpkRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 742 RLALA-------DaGDTVED----------ANFVEAMADAGILRLYTWVEW-VKEMLASCSSlrsgpadsfnDRVFASEM 803
Cdd:PRK11893 323 RYFLLreipfgqD-GDFSREafinrinadlANDLGNLAQRTLSMIAKNFDGkVPEPGALTEA----------DEALLEAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 804 NAGIIKTDQNYEKMMFKEALK---------TGFFEFQA----AKDKYRELATEGMHRELVFRFIevqTILLTPFCPHLCE 870
Cdd:PRK11893 392 AALLERVRAAMDNLAFDKALEailalvraaNKYIDEQApwslAKTDPERLATVLYTLLEVLRGI---AVLLQPVMPELAA 468
|
250
....*....|..
gi 120537241 871 HIWTLLGKPDSI 882
Cdd:PRK11893 469 KILDQLGVEEDE 480
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
639-757 |
6.26e-07 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 52.92 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 639 YVFFkDAPFPKTQIPKEkLDQLKQEFEFWYPVDLRAS---GKDLIPNHlsyyiynhVAMWP---EQSDKWPVS-VRANGH 711
Cdd:cd00814 204 YVWF-DALIGYISATGY-YNEEWGNSWWWKDGWPELVhfiGKDIIRFH--------AIYWPamlLGAGLPLPTrIVAHGY 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 120537241 712 LLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANF 757
Cdd:cd00814 274 LTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
15-230 |
2.15e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 52.13 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 15 EIEKEAQQKWEAEKVFevsasRLEKQKQSSKGKYFV--TFPYPYMNGrLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGL 92
Cdd:PLN02563 84 EIEPKWQRYWEENRTF-----RTPDDVDTSKPKFYVldMFPYPSGAG-LHVGHPEGYTATDILARYKRMQGYNVLHPMGW 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 93 HCTGMPIKACAdklkreIElygcppdfpeeeeeeeeSSAKPGDIVVRdkakgkkskaaakagsskyqwdimkslglsddD 172
Cdd:PLN02563 158 DAFGLPAEQYA------IE-----------------TGTHPKITTLK--------------------------------N 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 120537241 173 IVKFSeaehwldyfpplavQDLKTIGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRER 230
Cdd:PLN02563 183 IARFR--------------SQLKSLGFSYDWDREISTTE--PEYYKWTQWIFLQLLKR 224
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
668-748 |
4.23e-06 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 50.06 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 668 YPVDLRASGKDLI-PNHlsyyiYNHVAMWPEQSDKWPVSV-RANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLAL 745
Cdd:pfam01406 206 DQIDIHGGGIDLAfPHH-----ENEIAQSEAAFDKQLANYwLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFL 280
|
...
gi 120537241 746 ADA 748
Cdd:pfam01406 281 LSV 283
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
46-98 |
8.84e-06 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 49.55 E-value: 8.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 120537241 46 GKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMP 98
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA 53
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
668-743 |
1.26e-05 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 49.64 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 668 YPVDLRASGKDLI-PNHlsyyiYNHVAmwpeQS------DKWpvsvrAN-----GHLLLNSEKMSKSTGNFLTLSQAVDK 735
Cdd:PTZ00399 267 DPIDIHSGGIDLKfPHH-----DNELA----QSeayfdkHQW-----VNyflhsGHLHIKGLKMSKSLKNFITIRQALSK 332
|
....*...
gi 120537241 736 FSADGMRL 743
Cdd:PTZ00399 333 YTARQIRL 340
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
13-99 |
1.50e-05 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 49.31 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 13 LKEIEKEAQQKWEAEKVFEvsasrleKQKQSSKGK-YFVtF---PyPYMNGRLHLGHTfsLSKC--EFAVGYQRLKGKSC 86
Cdd:COG0060 18 LPKREPEILKFWEENDIYE-------KSREARAGRpKFV-LhdgP-PYANGDIHIGHA--LNKIlkDIIVRYKTMRGFDV 86
|
90
....*....|...
gi 120537241 87 LFPFGLHCTGMPI 99
Cdd:COG0060 87 PYVPGWDCHGLPI 99
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
516-757 |
3.26e-05 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 47.63 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 516 VMSRSADECVVALCDQWYLDYGDEnwKKQTFQCLKN--METFCEESRKNFEASLDWLQEHACSRTYGLGTRLPwdeQWLI 593
Cdd:cd00817 155 VCSRSGDVIEPLLKPQWFVKVKDL--AKKALEAVKEgdIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIP---AWYC 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 594 ESLSDstIYMAFYTVAHLLQGGDLNGQAESPLGIRPQqmtKDVWDyVFFKDA--PFPKTQIPKEKLDqlkqeFEFWYPVD 671
Cdd:cd00817 230 KDGGH--WVVAREEDEAIDKAAPEACVPCGGEELKQD---EDVLD-TWFSSSlwPFSTLGWPEETKD-----LKKFYPTS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 672 LRASGKDLIPNHLSYYIYNHVAMwpeqSDKWPVS-------VR-ANGhlllnsEKMSKSTGNFLTLSQAVDKFSADGMRL 743
Cdd:cd00817 299 LLVTGHDIIFFWVARMIMRGLKL----TGKLPFKevylhglVRdEDG------RKMSKSLGNVIDPLDVIDGYGADALRF 368
|
250
....*....|....
gi 120537241 744 ALADAGDTVEDANF 757
Cdd:cd00817 369 TLASAATQGRDINL 382
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
17-99 |
5.42e-05 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 47.46 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 17 EKEAQQKWEAEKVFEVSASRlekqkqsSKGKYFVTF--PyPYMNGRLHLGHtfSLSKC--EFAVGYQRLKGKSCLFPFGL 92
Cdd:PLN02843 9 EPEIQKLWEENQVYKRVSDR-------NNGESFTLHdgP-PYANGDLHIGH--ALNKIlkDFINRYQLLQGKKVHYVPGW 78
|
....*..
gi 120537241 93 HCTGMPI 99
Cdd:PLN02843 79 DCHGLPI 85
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
47-88 |
2.85e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.87 E-value: 2.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 120537241 47 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLF 88
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFF 43
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
48-107 |
3.71e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 44.20 E-value: 3.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 48 YFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIKACADKLK 107
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEG 60
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
668-745 |
5.73e-04 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 44.15 E-value: 5.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 120537241 668 YPVDLRASGKDLIPNHLSYYIYNHVAMWPEQSDKWPVSvraNGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLAL 745
Cdd:PLN02946 276 HSFDIHGGGMDLVFPHHENEIAQSCAACCDSNISYWIH---NGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL 350
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
14-88 |
7.63e-04 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 43.84 E-value: 7.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120537241 14 KEIEKEAQQKWEAEKVFEVSasrlEKQKQSSKGKYFV-TFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLF 88
Cdd:PTZ00419 31 KEVESGWYEWWEKSGFFKPA----EDAKSLNSGKKFViVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLW 102
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
670-806 |
3.18e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 41.45 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 670 VDLRASGKDLIPNHLSyyiyNHVAmwpeQSD-----KWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDK-FSADGMRL 743
Cdd:PRK14536 234 CDIHIGGVDHIRVHHT----NEIA----QCEaatgkPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRF 305
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120537241 744 ALADAGDTVEDANFVEAM--ADAGILRLYTWV-EWVKEMLASCSSLRSGPADSFNDRVFASEMNAG 806
Cdd:PRK14536 306 FLLGGHYRSQLAFSWEALktAKAARRSLVRRVaRVVDAARATTGSVRGTLAECAAERVAESRASES 371
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
656-754 |
3.62e-03 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 41.62 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120537241 656 KLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYiynhVAMWPEQSDKWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDK 735
Cdd:PLN02224 308 KQQNLETAVSFGWPASLHLIGKDILRFHAVYW----PAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQK 383
|
90 100
....*....|....*....|....*
gi 120537241 736 FSADGMR------LALADAGDTVED 754
Cdd:PLN02224 384 FGPDAVRyfflreVEFGNDGDYSED 408
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
837-876 |
4.32e-03 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes bacterial and eukaryotic mitochondrial members, as well as LeuRS from the archaeal Halobacteria. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153412 [Multi-domain] Cd Length: 117 Bit Score: 38.35 E-value: 4.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 120537241 837 YRELATEGMHRELVFRFIEVQTILLTPFCPHLCEHIWTLL 876
Cdd:cd07958 78 YKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
55-114 |
7.85e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 39.91 E-value: 7.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 120537241 55 PYMNGRLHLGHTfsLSKC--EFAVGYQRLKGKSCLFPFGLHCTGMPI-----KACADKLKREIELYG 114
Cdd:cd00818 10 PYANGLPHYGHA--LNKIlkDIINRYKTMQGYYVPRRPGWDCHGLPIelkveKELGISGKKDIEKMG 74
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
858-907 |
8.62e-03 |
|
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 38.69 E-value: 8.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 120537241 858 TILLTPFCPHLCEHIWT-----LLGKPDSImH-ASWPVA--GPVDESLIRSSQYLMEV 907
Cdd:cd07961 122 SRLMAPFTPFITEEIYQnlrreLGDAPESV-HlLDWPEVdeSLIDEELEEAMELVREI 178
|
|
|