|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
1-1008 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 1462.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 1 MNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFP--DEEEEEEETSVKTE 78
Cdd:PLN02959 56 MNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPeeDEDEAAAVAAAKAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 79 DI---IIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTD 155
Cdd:PLN02959 136 AEaaaAPPDKFKGKKSKAVAKSGTQKYQWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 156 VNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFL 235
Cdd:PLN02959 216 VNPYYDAFVRWQFRKLKKKGKIVKDKRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPPFPGKLKALEGKKVFL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 236 VAATLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSY 315
Cdd:PLN02959 296 AAATLRPETMYGQTNCWVLPDGKYGAYEINDTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 316 KVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDEL 395
Cdd:PLN02959 376 EVIYALPMLTILTDKGTGVVTSVPSDSPDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 396 KIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQ 475
Cdd:PLN02959 456 KIKSQNDKEKLAEAKRLTYLKGFTDGTMLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 476 WYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHL 555
Cdd:PLN02959 536 WYLTYGEEEWKKKAEKCLSKMNLYSDETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHL 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 556 LQGGNLHGQAESPlgIRPQQMTKEVWDYVFFKeAPFPKT-QIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYN 634
Cdd:PLN02959 616 LQGGDMYGKDKSS--IKPEQMTDEVWDFVFCG-GPLPKSsDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYN 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 635 HVAMWPEqsDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLY 714
Cdd:PLN02959 693 HTAIWAE--EHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLT 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 715 TWVEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYR-ELAVEGMHREL 793
Cdd:PLN02959 771 KEIAWMEEVLAAESSLRTGPPSTYADRVFENEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRlSCGSGGMNRDL 850
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 794 VFRFIEVQTLLLAPFCPHLCEHIW-TLLGKPDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKKTD 872
Cdd:PLN02959 851 VWRFMDVQTRLITPICPHYAEHVWrEILKKEGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKG 930
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 873 KQPLQKPSHCT---IYVAKNYPPWQHTTLSVLRKHFEANNGKL-PDNKVIA----SELGSMPELKKYMKKVMPFVAMIKE 944
Cdd:PLN02959 931 GAPVTLPEKKLaglIYVAEKYDGWKEECLRILQSKFDSQSRTFaPDAEILEalkeSSVGQEANFKQVQKLCMPFVKFKKD 1010
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767937779 945 NLEKMGPRILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIR----------EDCCPGKPLNVFR 1008
Cdd:PLN02959 1011 EAIAVGPQALDLKLPFDEIEVLQENLELIKRQLGLEEVEILSASDPDAVAKagahasllkqNPPSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
1-1003 |
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: 832.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 1 MNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGcppdfpdeeeeeeetsvktedi 80
Cdd:TIGR00395 36 LNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVTGTPILGLAELIKRRDELTI---------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 81 iikdkakgkkskaaakagsskyqWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYY 160
Cdd:TIGR00395 94 -----------------------KNYTEVHAIPREELLKFTDPEYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 161 DSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEpypsklsglkgKNIFLVAATL 240
Cdd:TIGR00395 149 DRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDHDLLSGEGVTIVEYILIKFELED-----------GAFYFVAATL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 241 RPETMFGQTNCWVRPDMKYIGFEtVNGDIFICTQKAARNMSYQGFTkdngvVPVVKELMGEEILGASLSAPLTsYKVIYV 320
Cdd:TIGR00395 218 RPETVYGVTNCWVNPTITYVIAE-VGGEKWITSKEAFENLSYQKLK-----YKPIEEVPGKQFIGKKVHNPVV-GPEVPI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 321 LPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALrakYGIRDdMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQ 400
Cdd:TIGR00395 291 LPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDPEY---LGIKP-VVIDIEPVPLIHTDGYGDLPAKEIVEEKGIKSQ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 401 NDREKLAEAKEKIYLKGFYEGIML--VDGFKGQKVQDVKKTIQKKMIDAGDALIYMEP-EKQVMSRSSDECVVALC-DQW 476
Cdd:TIGR00395 367 KDKNLLEEATKILYKEEYHTGVMIynIPPYKGMKVSEAKEKVKADLIDAGLADVMYEFsESPVICRCGTDCIVKVVeDQW 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 477 YLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLL 556
Cdd:TIGR00395 447 FVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDWLKDWACCRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 557 QGGNlhgqaesplgIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHV 636
Cdd:TIGR00395 527 NKDY----------YGNEQMTDEFFDYIFLGKGDVKNTNIPLPAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHV 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 637 AMWPEqsDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTW 716
Cdd:TIGR00395 597 AIFPE--KFWPRGIVVNGYVMLEGKKMSKSKGNVLTLEQAVEKFGADVARLYIADAAETVQDADWKESEVEGTILRLERL 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 717 VEWVKEmVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRElAVEGMHRELVFR 796
Cdd:TIGR00395 675 YEFAEE-ITKESNLETGEETSFIDRWLESRMNAAIKETYEAMENFQTRKAVKYALFDLQADVDWYRR-RGGVNHKDVLAR 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 797 FIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAG--PVNEVLIHSSQYLMEVTHDLRlrlknymmpaKGKKTDKq 874
Cdd:TIGR00395 753 YLETWIKLLAPFAPHFAEEMWEEVGNEGFVSLAKFPEASepAVDKEVEAAEEYLRNLVRDIQ----------EIAKIDA- 821
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 875 plQKPSHCTIYVAknyPPWQHTTLSVLRKHFEANNGKlpDNKVIASElgsmPELKKYMKKVMPFVAMIKENLEKmgpril 954
Cdd:TIGR00395 822 --SKPKRVYLYTS---EDWKSQCLKIVAELFGEDTGE--DMKKVMEE----PEERKRGKEVISLVKQIIKDEKK------ 884
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 767937779 955 DLQLEFDEKAVLMENIVYLTNSLELEHI-EVKFASEAEDKiREDCCPGKP 1003
Cdd:TIGR00395 885 EDELQISEIEVLKAAARFIKKEVGALVIiEFSADSFPENK-KRNAVPGKP 933
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
5-1003 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 751.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 5 LHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKReielygcppdfpdeeeeeeetsvKTEDIIikd 84
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR-----------------------GDPETI--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 85 kakgkkskaaakagsskyqwGIMKSL-GLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDSF 163
Cdd:PRK12300 55 --------------------ELYKSLyGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--PEYSKF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 164 VRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKvlepypsklsglKGKNIFLVAATLRPE 243
Cdd:PRK12300 113 IEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFE------------ESEDLILPAATLRPE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 244 TMFGQTNCWVRPDMKYIGFEtVNGDIFICTQKAARNMSYQGFTkdngvVPVVKELMGEEILGASLSAPLTSYKVIyVLPM 323
Cdd:PRK12300 181 TIFGVTNLWVNPDATYVKAE-VDGEKWIVSKEAAEKLSFQDRD-----VEIIEEIKGSELIGKKVKNPVTGKEVP-ILPA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 324 LTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKygirddmvlpFEPVPVIEIPGFGNLSAVTICDELKIQSQNDR 403
Cdd:PRK12300 254 DFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNKELLDV----------IEPIPLIEVEGYGEFPAKEVVEKLGIKSQEDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 404 eKLAEAKEKIYLKGFYEGIMLVD--GFKGQKVQDVKKTIQKKMIDAGDALIYME-PEKQVMSRSSDECVVA-LCDQWYLD 479
Cdd:PRK12300 324 -ELEEATKEVYRAEFHKGVLKENtgEYAGKPVREAREKITKDLIEKGIADIMYEfSNRPVYCRCGTECVVKvVKDQWFID 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 480 YGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGG 559
Cdd:PRK12300 403 YSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAHKIREY 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 560 nlhgqaesplGIRPQQMTKEVWDYVF----FKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNH 635
Cdd:PRK12300 483 ----------GIKPEQLTPEFFDYVFlgkgDPEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFIFNH 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 636 VAMWPEqsDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLyt 715
Cdd:PRK12300 553 VAIFPE--EKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQL-- 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 716 wvEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELaVEGMHRELVF 795
Cdd:PRK12300 629 --ERFYELAKELIEIGGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRR-VGEANNKVLR 705
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 796 RFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGP--VNEVLIHSSQYLMEVTHDLRlRLKNYmmpAKGkktdk 873
Cdd:PRK12300 706 EVLEIWIRLLAPFTPHLAEELWHKLGGEGFVSLEKWPEPDEskIDEEAELAEEYVKRLIEDIR-EILKV---AKI----- 776
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 874 qplqKPSHCTIYVAknyPPWQHTTLSVLRkhfeanngKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRI 953
Cdd:PRK12300 777 ----KPKKVYIYVA---PDWKYEVLEIAA--------ENGDVKEAIKELMKDEELRKHGKEVAKLAQKIVKEVLKLDKEV 841
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 767937779 954 LDL-QLEFDEKAVLMENIVYLTNSLELEhIEVKFASEAE-DKIREDCCPGKP 1003
Cdd:PRK12300 842 RKLiLKNIDEEEVLEEAKDFLEKELGVE-VEIYGADDPGkKKKKKKALPLKP 892
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
471-703 |
9.34e-73 |
|
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: 244.46 E-value: 9.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 471 ALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGwlqehaCSRTYGLGTHLPWdeQWLIESLSDSTIYMAFY 550
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 551 TVAHLLQggnlhgqaesplgirpqqmtkevwdyvffkeapfpktQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSY 630
Cdd:cd00812 199 TDAHNLE-------------------------------------QPYEGDLEFDREEFEYWYPVDIYIGGKEHAPNHLLY 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767937779 631 YLYNHVAMWPEQ--SDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDtvEDANFVE 703
Cdd:cd00812 242 SRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFDW 314
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
701-820 |
2.38e-51 |
|
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: 176.24 E-value: 2.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 701 FVEAMADAGILRLYTWVEWVKEMVANWDSLrsgPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDK 780
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767937779 781 YRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLL 820
Cdd:cd07959 78 YRERGGAGMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
1-175 |
4.42e-22 |
|
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: 98.47 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 1 MNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKReielygcppdfpdeeeeeeetsvktedi 80
Cdd:cd00812 11 PSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGR---------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 81 iikdkakgkkskaaakagsskyqwgimkslglsdeeivkfsEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYY 160
Cdd:cd00812 63 -----------------------------------------DPEDWTEYNIKKMKEQLKRMGFSYDWRREFTTCD--PEY 99
|
170
....*....|....*
gi 767937779 161 DSFVRWQFLTLRERN 175
Cdd:cd00812 100 YKFTQWLFLKLYEKG 114
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
442-690 |
1.83e-20 |
|
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: 93.64 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 442 KKMIDAGdaLIYmepekqvmsrsSDECVVALCDQWYLDYGEenWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSR 521
Cdd:cd00668 121 SRLYEKG--LIY-----------RGTHPVRITEQWFFDMPK--FKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 522 TYGLGTHLPwdeQWLIESLSDSTIYMAFYTvahllqgGNLHGqaesplgirpqqmtkevwdyvffkeapfpktqiakekl 601
Cdd:cd00668 186 QRYWGTPLP---EDVFDVWFDSGIGPLGSL-------GYPEE-------------------------------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 602 dqlKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEqsdKWPTAVRANGHLLLN-SEKMSKSTGNFLTLTQAIDKF 680
Cdd:cd00668 218 ---KEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGE---IPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKY 291
|
250
....*....|
gi 767937779 681 SADGMRLALA 690
Cdd:cd00668 292 GADALRYYLT 301
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
3-998 |
1.18e-18 |
|
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: 92.04 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 3 GRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPikacadklkreielygcppdfpdeeeeeeeTSVKTEDIIi 82
Cdd:TIGR00422 46 GSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIA------------------------------TQVKVEKKL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 83 kdkakgkkskaaakagsskyqWGIMKSLG-LSDEEIVKfsEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYD 161
Cdd:TIGR00422 95 ---------------------GAEGKTKHdLGREEFRE--KIWEWKEESGGTIKNQIKRLGASLDWSRERFTMD--EGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 162 SFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKvlepypsklsglKGKNIFLVAATLR 241
Cdd:TIGR00422 150 KAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVEYKEVKGKLYYIRYPLA------------NGSKDYLVVATTR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 242 PETMFGQTNCWVRP-DMKYigfetvngdifictqkaarnmsyqgftkdngvvpvvKELMGEEILgaslsAPLTSYKViyv 320
Cdd:TIGR00422 218 PETMFGDTAVAVHPeDERY------------------------------------KHLIGKKVI-----LPLTGRKI--- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 321 lPMLT---IKEDKGTGVVTSVPSDSPDDIAalrdLKKKQALrakygirddmvlpfEPVPVIEIPGFGNLSAvticdeLKI 397
Cdd:TIGR00422 254 -PIIAdeyVDMEFGTGAVKVTPAHDFNDYE----WGKRHNL--------------EFINILDEDGLLNENA------GKY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 398 QSQndreKLAEAKEKIylkgfyegimlvdgfkgqkVQDVKKtiQKKmidagdaLIYMEPEKQ---VMSRSSDECVVALCD 474
Cdd:TIGR00422 309 QGL----TRFEARKKI-------------------VEDLKE--EGL-------LVKIEPHTHnvgTCWRSGTVVEPLLSK 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 475 QWYLDYgeENWKKQTSQCLKNLE-TFCEEtrrNFEATL-GWLQEHA--C-SRTYGLGTHLPwdeqwlieslsdstiymAF 549
Cdd:TIGR00422 357 QWFVKV--EKLADKALEAAEEGEiKFVPK---RMEKRYlNWLRNIKdwCiSRQLIWGHRIP-----------------VW 414
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 550 YTVahllQGGNLHGQAESPLGIRPQQMT--------KEVWDyVFFKEA--PFPKTQIAKEKLDqlkqeFEFWYPVDLRVS 619
Cdd:TIGR00422 415 YCK----ECGEVYVAKEEPLPDDKTNTGpsveleqdTDVLD-TWFSSSlwPFSTLGWPDETKD-----LKKFYPTDLLVT 484
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 620 GKDLVPNHLSYYLYNHVAMwpEQSDKWPTA-----VR-ANGHlllnseKMSKSTGNFLTLTQAIDKFSADGMRLALADAG 693
Cdd:TIGR00422 485 GYDIIFFWVARMIFRSLAL--TGQVPFKEVyihglVRdEQGR------KMSKSLGNVIDPLDVIEKYGADALRFTLASLV 556
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 694 DTVEDANFVEAMADAG---ILRLYTWVEWVKEMVANWDSLrSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEALK 768
Cdd:TIGR00422 557 TPGDDINFDWKRVESArnfLNKLWNASRFVLMNLSDDLEL-SGGEEKLSlaDRWILSKLNRTIKEVRKALDKYRFAEAAK 635
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 769 tGFFEF----------QAAK--DKYRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIW-TLLGKPDSIMNASWPVAG 835
Cdd:TIGR00422 636 -ALYEFiwndfcdwyiELVKyrLYNGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWqHFKEGADSIMLQSYPVVD 714
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 836 P--VNEVLIHSSQYLMEVTHDLRLRLKNYMMPAkgkktdKQPLQKpshCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLp 913
Cdd:TIGR00422 715 AefVDEEAEKAFELLKEIIVSIRNLKAESNIPP------NAPLKV---LLIYTEAETAERLKLNAVDIKGAINFSEVEV- 784
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 914 dnkviaseLGSMPELKKYMKKVMPFVAMI--KENLEKMGPRILDLQLEFDEKavLMENIVyLTNSLELEHIEVKFASEAE 991
Cdd:TIGR00422 785 --------VIEKPEVTEAVVELVPGFEIIipVKGLINKAKELARLQKQLDKE--KKEVIR-IEGKLENEGFVKKAPKEVI 853
|
....*..
gi 767937779 992 DKIREDC 998
Cdd:TIGR00422 854 EKEKEKL 860
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
740-856 |
3.70e-17 |
|
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: 79.37 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 740 DRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQ---------AAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCP 810
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWndlsdwyleLIKDRLYGEEPDSRAQTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767937779 811 HLCEHIWtllgKPDSIMNASWPVAGPVNEVLIHSS-QYLMEVTHDLR 856
Cdd:pfam08264 81 FITEELW----QKESIHLAPWPEDAELEEAELEEAfELRQEIVQAIR 123
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
2-701 |
1.26e-16 |
|
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: 84.77 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 2 NGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKAcadklkrEIElygcppdfpdeeeeeeetsvktedii 81
Cdd:pfam00133 35 TGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQ-------VVE-------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 82 ikdkakgkkskaaakagsskyqwgimKSLGLSDEEIV-KFSEAEH------WLDYFPPLAIQDLKRMGLKVDWRRSFITT 154
Cdd:pfam00133 82 --------------------------KKLGIKEKKTRhKYGREEFrekcreWKMEYADEIRKQFRRLGRSIDWDREYFTM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 155 DvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVlepypsklsglkGKNIF 234
Cdd:pfam00133 136 D--PELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVEYKDVKGPSIHVAFPLAD------------DEGAS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 235 LVAATLRPETMFGQTNCWVRPDMKYIgfetVNGDIFICTQKAARNMSYQGFTKDngvvpVVKELMGEEILGASLSAPLTS 314
Cdd:pfam00133 202 LVIWTTTPWTLPGNTAVAVNPEFDYV----ITGEGYILAEALLKSLYKKGTDKK-----ILEDFRGKELEGKEAIHPFVN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 315 YKViyvlPMLT---IKEDKGTGVVTSVPSDSPDDIAALRdlkkkqalraKYGIrdDMVLPFEPVPVIeipgfgnlsavti 391
Cdd:pfam00133 273 REI----PIITddyVDMEFGTGAVHIAPAHGENDYEVGQ----------RHNL--EVINPVDDDGTF------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 392 cdelkiqsqndREKLAEakekiylkgfyegimlvdgFKGQKVQDVKKTIQKKMIDAGdalIYMEPEKQVMS-----RSSD 466
Cdd:pfam00133 324 -----------TEEAPD-------------------FQGVYRFDARKKIVELLTEKG---LLLKIEPFTHSypfcwRSGT 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 467 ECVVALCDQWYLdygeeNWKKQTSQCLKNLE--TFCEETRRN-FEATLGWLQEHACSRTYGLGTHLPWdeqWLIESLSDs 543
Cdd:pfam00133 371 PIIPRATPQWFV-----RMDELADQALEAVEkvQFVPKSGEKrYFNWLANIQDWCISRQRWWGHPIPA---WVSKDTEE- 441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 544 tIYMA---FYTVAHLLQGG----NLHGQAESPLGIRPQQMTK--EVWDyVFFKEAPFPKTQIakEKLDQLKQEFEFWYPV 614
Cdd:pfam00133 442 -VVCRgelFELVAGRFEEEgsikWLHREAKDKLGYGKGTLEQdeDVLD-TWFSSGSWPFSTL--GWPFVNTEEFKKFFPA 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 615 DLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKwptAVRANGhLLLNSE--KMSKSTGNFLTLTQAIDKFSADGMRLALADA 692
Cdd:pfam00133 518 DMLLEGSDQTRGWFYRMIMLSTALTGSVPFK---NVLVHG-LVRDEQgrKMSKSLGNVIDPLDVIDKYGADALRLWLANS 593
|
....*....
gi 767937779 693 gDTVEDANF 701
Cdd:pfam00133 594 -DYGRDINL 601
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
620-834 |
1.76e-16 |
|
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: 84.01 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 620 GKDLVpnhlsyylYNHVAMWP---EQSD-KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDT 695
Cdd:COG0143 289 GKDII--------RFHAIIWPamlMAAGlPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPF 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 696 VEDANFveamadagilrlyTWVEWV----KEMVANWDSL--RS--------------GPASTFNDRVFASELNAGIIKTD 755
Cdd:COG0143 361 GQDGDF-------------SWEDFVarvnSDLANDLGNLasRTlsmihkyfdgkvpePGELTEADEELLAEAEAALEEVA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 756 QNYEKMMFKEALKT---------GFFEFQA----AKDKYRELAVEGMHREL-VFRFIevqTLLLAPFCPHLCEHIWTLLG 821
Cdd:COG0143 428 EAMEAFEFRKALEEimalaraanKYIDETApwklAKDEDPERLATVLYTLLeALRIL---AILLKPFLPETAEKILEQLG 504
|
250
....*....|....*.
gi 767937779 822 KPDSIMN---ASWPVA 834
Cdd:COG0143 505 LEGDELTwedAGWPLP 520
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
648-834 |
1.84e-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: 71.62 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 648 TAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL------------ADAGdtVEDAN-FVEamadagilRLY 714
Cdd:COG0495 575 LEVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEmfagpperdlewSDSG--VEGAYrFLN--------RVW 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 715 TwvewvkeMVANWDSLRSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEA------LKTGFFEFQAAKDKYRELAV 786
Cdd:COG0495 645 R-------LVVDEAEALKLDVADLSeaDKELRRALHKTIKKVTEDIERLRFNTAiaalmeLVNALYKAKDSGEADRAVLR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767937779 787 EGMhrelvfrfiEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVA 834
Cdd:COG0495 718 EAL---------ETLVLLLAPFAPHIAEELWERLGHEGSVADAPWPEA 756
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
608-834 |
8.06e-11 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 66.37 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 608 FEFWYPVDLRVSGKDLVPNHL------SYYLYNHVAmwpeqsdkWpTAVRANGHLL-LNSEKMSKSTGNFLTLTQAIDKF 680
Cdd:PRK13208 481 FEKVFPMDLRPQGHDIIRTWLfytilrAYLLTGKLP--------W-KNIMISGMVLdPDGKKMSKSKGNVVTPEELLEKY 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 681 SADGMRLALADA--GDtveDANFVEAMADAG-------------ILRLYTWVEWVKEMVANwdslrsgPAstfnDRVFAS 745
Cdd:PRK13208 552 GADAVRYWAASArlGS---DTPFDEKQVKIGrrlltklwnasrfVLHFSADPEPDKAEVLE-------PL----DRWILA 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 746 ELNAGIIKTDQNYEKMMFKEALKT--GFF--EFQaakDKYRELA--------VEGMHRELVF---RFIEVQTLLLAPFCP 810
Cdd:PRK13208 618 KLAKVVEKATEALENYDFAKALEEieSFFwhVFC---DDYLELVksraygedEEEEQKSARYtlyTVLDTLLRLLAPFLP 694
|
250 260
....*....|....*....|....
gi 767937779 811 HLCEHIWTLLGKpDSIMNASWPVA 834
Cdd:PRK13208 695 FITEEVWSWLYG-GSVHRASWPEP 717
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
620-824 |
1.31e-10 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 65.56 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 620 GKDLVpnhlsyylYNHVAMWP---EQSD-KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALA-DAGD 694
Cdd:PRK00133 291 GKDII--------YFHTLFWPamlEGAGyRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAaKLPE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 695 TVEDANFveamadagilrlyTWVEWVK----EMVANWDSL--RS----------GPASTFNDRVFASELNAGIIKTDQNY 758
Cdd:PRK00133 363 TIDDLDF-------------NWEDFQQrvnsELVGKVVNFasRTagfinkrfdgKLPDALADPELLEEFEAAAEKIAEAY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 759 EKMMFKEALKT---------GFFEFQA----AKDKYRELAvEGMHREL-VFRFIevqTLLLAPFCPHLCEHIWTLLGKPD 824
Cdd:PRK00133 430 EAREFRKALREimaladfanKYVDDNEpwklAKQDGERLQ-AVCSVGLnLFRAL---AIYLKPVLPELAERAEAFLNLEE 505
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
662-870 |
3.74e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 64.36 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 662 KMSKSTGNF---LTLtqaIDKFSADGMRLALAdagdtvedanfveAMADAGI-LRL-YTWVE---------W-----VKE 722
Cdd:PRK05729 520 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIRFdEERVEgyrnfanklWnasrfVLM 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 723 MVANWDSLRSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEALKT--GFF--EF-----QAAKDKYRELAVEGMHR 791
Cdd:PRK05729 584 NLEGADVGELPDPEELSlaDRWILSRLNRTVAEVTEALDKYRFDEAARAlyEFIwnEFcdwylELAKPVLQEAAKRATRA 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 792 ELVfRFIEvQTL-LLAPFCPHLCEHIWTLL---GKPDSIMNASWPVAGPV-NEVLIHSSQYLMEVTHDLRlRLKNYMMPA 866
Cdd:PRK05729 664 TLA-YVLE-QILrLLHPFMPFITEELWQKLaplGIEESIMLAPWPEADEAiDEAAEAEFEWLKELITAIR-NIRAEMNIP 740
|
....
gi 767937779 867 KGKK 870
Cdd:PRK05729 741 PSKK 744
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
581-836 |
3.89e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 64.46 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 581 WDYVFFKEAPFPKTQIAKEKLdqlkqefEFWYPVDLRVSGKDLVPNHLSY------YLYN--------------HVAM-- 638
Cdd:PLN02563 591 WYYLRFMDPKNSNALVDKEKE-------KYWMPVDLYVGGAEHAVLHLLYarfwhkVLYDigvvstkepfqclvNQGMil 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 639 -------WPEQSDKWPTAVRANGHLLLNSE-----------------------------KMSKSTGNFLTLTQAIDKFSA 682
Cdd:PLN02563 664 geveytaFKDSDGEYVSADTADRLGELQQEkipeekviksgdsfvlkddpsirliarahKMSKSRGNVVNPDDVVSEYGA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 683 DGMRLaladagdtvedanFVEAMadaGILR-LYTW----VEWVKEMVAN-WDSLRSGPAS--TFNDRVFASE-------- 746
Cdd:PLN02563 744 DSLRL-------------YEMFM---GPLRdSKTWstsgVEGVHRFLGRtWRLVVGAPLPdgSFRDGTVVTDeepsleql 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 747 --LNAGIIKTDQNYEKMMFKEALkTGFFEFQAAKDKYRELAVEgmhrelvfrFIEVQTLLLAPFCPHLCEHIWTLLGKPD 824
Cdd:PLN02563 808 rlLHKCIAKVTEEIESTRFNTAI-SAMMEFTNAAYKWDKVPRE---------AIEPFVLLLSPYAPHLAEELWFRLGHSN 877
|
330
....*....|..
gi 767937779 825 SIMNASWPVAGP 836
Cdd:PLN02563 878 SLAYEPWPEANP 889
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
662-856 |
8.29e-10 |
|
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: 63.15 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 662 KMSKSTGNF---LTLtqaIDKFSADGMRLALAdagdtvedanfveAMADAGI-LRLYT-WVE------------------ 718
Cdd:COG0525 522 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIKFDEeRVEgyrnfanklwnasrfvlm 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 719 WVKEMVANWDSLRSgpASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKT--GFF--EFQaakDKYRELA-------VE 787
Cdd:COG0525 586 NLEGFDPGLDPDPE--ELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQAlyDFVwnEFC---DWYLELAkprlyggDE 660
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767937779 788 GMHRELVFRFIEV--QTL-LLAPFCPHLCEHIWTLLGKP---DSIMNASWPVAGP--VNEVLIHSSQYLMEVTHDLR 856
Cdd:COG0525 661 AAKRETRATLVYVleQILrLLHPFMPFITEEIWQKLPPRkegESIMLAPWPEADEelIDEEAEAEFEWLKEVISAIR 737
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
583-701 |
1.44e-09 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 61.54 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 583 YVFFkEAPFPKTQIAKEkLDQLKQEFEFWYPVDLRVS-----GKDLVpnhlsyylYNHVAMWP----EQSDKWPTAVRAN 653
Cdd:pfam09334 246 YVWL-DAPIGYISATKE-LSGNEEKWKEWWPNDPDTElvhfiGKDII--------YFHTIFWPamllGAGYRLPTTVFAH 315
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767937779 654 GHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANF 701
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDF 363
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
610-826 |
2.23e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 61.44 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 610 FWyPVDLRVSGKDLVPNHLSYylynhvamWPEQ--SD--KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGM 685
Cdd:PRK11893 252 YW-PADVHLIGKDILRFHAVY--------WPAFlmAAglPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 686 RLALA-------DaGDTVED----------ANFVEAMADAgilrlytwvewVKEMVANW--DSLRSGPASTFNDRVFASE 746
Cdd:PRK11893 323 RYFLLreipfgqD-GDFSREafinrinadlANDLGNLAQR-----------TLSMIAKNfdGKVPEPGALTEADEALLEA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 747 LNAGIIKTDQNYEKMMFKEALK---------TGFFEFQA----AKDKYRELAVEGMHRELVFRFIevqTLLLAPFCPHLC 813
Cdd:PRK11893 391 AAALLERVRAAMDNLAFDKALEailalvraaNKYIDEQApwslAKTDPERLATVLYTLLEVLRGI---AVLLQPVMPELA 467
|
250
....*....|...
gi 767937779 814 EHIWTLLGKPDSI 826
Cdd:PRK11893 468 AKILDQLGVEEDE 480
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
639-839 |
6.51e-09 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 60.39 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 639 WPEQSDK----WPTAVRANGHLLL--------------------------------NSEKMSKSTGNFLTLTQAIDKFSA 682
Cdd:PRK14900 479 WPEQTDTlrtfYPTSVMETGHDIIffwvarmmmmglhfmgevpfrtvylhpmvrdeKGQKMSKTKGNVIDPLVITEQYGA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 683 DGMRLALAD----------AGDTVEDAN-FVEAMADAGILRLYTWVEWVKEMVanwDSLRSgpASTFNDRVFASELNAGI 751
Cdd:PRK14900 559 DALRFTLAAltaqgrdiklAKERIEGYRaFANKLWNASRFALMNLSGYQERGE---DPARL--ARTPADRWILARLQRAV 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 752 IKTDQNYEKMMFKEALKTGF-FEFQAAKDKYRELAVEGMH----------RELVFRFIEVQTLLLAPFCPHLCEHIWTLL 820
Cdd:PRK14900 634 NETVEALEAFRFNDAANAVYaFVWHELCDWYIELAKEALAsedpearrsvQAVLVHCLQTSYRLLHPFMPFITEELWHVL 713
|
250 260
....*....|....*....|....*.
gi 767937779 821 -------GKPDSIMNASWPVAGPVNE 839
Cdd:PRK14900 714 raqvgasAWADSVLAAEYPRKGEADE 739
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
2-188 |
8.14e-09 |
|
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: 58.58 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 2 NGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLkreielygcppdfpdeeeeeeetsvktedii 81
Cdd:cd00668 12 NGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERK------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 82 ikdkakgkkskaaakagsskyqwGIMKSlglSDEEIVKFSEA-EHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYY 160
Cdd:cd00668 61 -----------------------GGRKK---KTIWIEEFREDpKEFVEEMSGEHKEDFRRLGISYDWSDEYITTE--PEY 112
|
170 180
....*....|....*....|....*...
gi 767937779 161 DSFVRWQFLTLRERNKIKFGKRYTIYSP 188
Cdd:cd00668 113 SKAVELIFSRLYEKGLIYRGTHPVRITE 140
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
583-701 |
1.11e-08 |
|
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: 57.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 583 YVFFkEAPFPKTQIAKEKLDQLKQEFEFWY--PVDLRVSGKDLVPNHlsyylynhVAMWP---EQSDKW-PTAVRANGHL 656
Cdd:cd00814 204 YVWF-DALIGYISATGYYNEEWGNSWWWKDgwPELVHFIGKDIIRFH--------AIYWPamlLGAGLPlPTRIVAHGYL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767937779 657 LLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANF 701
Cdd:cd00814 275 TVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
653-689 |
2.01e-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: 2.01e-08
10 20 30
....*....|....*....|....*....|....*..
gi 767937779 653 NGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 689
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
653-689 |
1.81e-07 |
|
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: 52.97 E-value: 1.81e-07
10 20 30
....*....|....*....|....*....|....*..
gi 767937779 653 NGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 689
Cdd:cd00672 165 TGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
612-692 |
1.06e-05 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 48.52 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 612 YPVDLRVSGKDLV-PNHlsyylYNHVAMWPEQSDK-WPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 689
Cdd:pfam01406 206 DQIDIHGGGIDLAfPHH-----ENEIAQSEAAFDKqLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFL 280
|
...
gi 767937779 690 ADA 692
Cdd:pfam01406 281 LSV 283
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
603-701 |
1.50e-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: 48.78 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 603 QLKQEFEFWYPVDLRVSGKDLvpnhLSYYLYNHVAMWPEQSDKWP-TAVRANGhLLLNSE--KMSKSTGNFLTLTQAIDK 679
Cdd:cd00817 286 EETKDLKKFYPTSLLVTGHDI----IFFWVARMIMRGLKLTGKLPfKEVYLHG-LVRDEDgrKMSKSLGNVIDPLDVIDG 360
|
90 100
....*....|....*....|..
gi 767937779 680 FSADGMRLALADAGDTVEDANF 701
Cdd:cd00817 361 YGADALRFTLASAATQGRDINL 382
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
654-687 |
2.04e-05 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 48.87 E-value: 2.04e-05
10 20 30
....*....|....*....|....*....|....
gi 767937779 654 GHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRL 687
Cdd:PTZ00399 307 GHLHIKGLKMSKSLKNFITIRQALSKYTARQIRL 340
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
662-878 |
2.67e-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: 48.54 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 662 KMSKSTGNFLTLTQAIDKFSADGMRLALAdAGDTVEDANF----VEAMADAgILRLY-TWV---------EWVKEMVA-- 725
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVA-SSDYWGDLRFsdeiLKEVRDV-YRRLRnTYRfllanlddfDPAEDAVPye 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 726 NWDSLrsgpastfnDRVFASELNAGIIKTDQNYEKMMFKEALKT--GF-------FEFQAAKD---------KYRELAVE 787
Cdd:COG0060 681 DLPEL---------DRWILSRLNELIKEVTEAYDNYDFHRAYRAlhNFcvedlsnWYLDISKDrlyteaadsLDRRAAQT 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 788 GMHRELvfrfiEVQTLLLAPFCPHLCEHIWTLL--GKPDSIMNASWPVA--GPVNEVLIHSSQYLMEVTHDLRLRLKNym 863
Cdd:COG0060 752 TLYEVL-----ETLVRLLAPILPFTAEEIWQNLpgEAEESVHLADWPEVdeELIDEELEAKWDLVREVRSAVLKALEA-- 824
|
250
....*....|....*
gi 767937779 864 mpAKGKKTDKQPLQK 878
Cdd:COG0060 825 --ARKEKLIRQPLEA 837
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
3-191 |
5.38e-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: 46.86 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 3 GRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPikacadklkreielygcppdfpdeeeeeeeTSVKTEDIII 82
Cdd:cd00817 14 GSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA------------------------------TQVVVEKKLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 83 KDkakgkkskaaakagsskyqwGIMKSlGLSDEEIVKfsEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDS 162
Cdd:cd00817 64 IE--------------------GKTRH-DLGREEFLE--KCWEWKEESGGKIREQLKRLGASVDWSREYFTMD--PGLSR 118
|
170 180
....*....|....*....|....*....
gi 767937779 163 FVRWQFLTLRERNKIKFGKRYTIYSPKDG 191
Cdd:cd00817 119 AVQEAFVRLYEKGLIYRDNRLVNWCPKLR 147
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
3-43 |
1.24e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 46.34 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767937779 3 GRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPI 43
Cdd:PRK13208 51 GSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLPT 91
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
781-820 |
3.52e-04 |
|
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: 41.44 E-value: 3.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767937779 781 YRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLL 820
Cdd:cd07958 78 YKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
612-689 |
5.46e-04 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 44.15 E-value: 5.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767937779 612 YPVDLRVSGKDLV-PNHLSYYLYNHVAMWPEQSDKWPtavrANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 689
Cdd:PLN02946 276 HSFDIHGGGMDLVfPHHENEIAQSCAACCDSNISYWI----HNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL 350
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
662-836 |
1.37e-03 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 42.84 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 662 KMSKSTGNFLTLTQAID---------KFSADGMRLALAD---AGDTVEDANFVEAMADA-----GILR--LYTWVEWVKE 722
Cdd:PLN02843 611 KMSKSLGNVVDPRLVIEggknqkqepAYGADVLRLWVASvdyTGDVLIGPQILKQMSDIyrklrGTLRylLGNLHDWKPD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 723 MVANWDSLrsgPAStfnDRVFASELNAGIIKTDQNYEKMMFKEALKT---------GFFEFQAAKDKyreLAVEGMHRel 793
Cdd:PLN02843 691 NAVPYEDL---PSI---DKYALFQLENVVNEIEESYDNYQFFKIFQIlqrftivdlSNFYLDVAKDR---LYVGGTTS-- 759
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767937779 794 vFRFIEVQTLL----------LAPFCPHLCEHIWTLL------GKPDSIMNASWPVAGP 836
Cdd:PLN02843 760 -FTRRSCQTVLaahllsllraIAPILPHLAEDAWQNLpfqedgSAAESVFEAGWPTPNE 817
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
600-698 |
1.43e-03 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 42.78 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767937779 600 KLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYlynhVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDK 679
Cdd:PLN02224 308 KQQNLETAVSFGWPASLHLIGKDILRFHAVYW----PAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQK 383
|
90 100
....*....|....*....|....*
gi 767937779 680 FSADGMR------LALADAGDTVED 698
Cdd:PLN02224 384 FGPDAVRyfflreVEFGNDGDYSED 408
|
|
| |
