|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
5-1062 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 1517.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 5 KGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKgKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCC 84
Cdd:PLN02959 7 KSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPKPGE-KFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 85 LFPFGLHCTGMPIKACADKLKREIELYGCPPDFP--DEEEEEEETSVKTEDI---IIKDKAKGKKSKAAAKAGSSKYQWG 159
Cdd:PLN02959 86 LLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPeeDEDEAAAVAAAKAEAEaaaAPPDKFKGKKSKAVAKSGTQKYQWE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 160 IMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTI 239
Cdd:PLN02959 166 IMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTDVNPYYDAFVRWQFRKLKKKGKIVKDKRYTI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 240 YSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETV 319
Cdd:PLN02959 246 YSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPPFPGKLKALEGKKVFLAAATLRPETMYGQTNCWVLPDGKYGAYEIN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 320 NGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDD 399
Cdd:PLN02959 326 DTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSVPSDSPDD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 400 IAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLV 479
Cdd:PLN02959 406 YMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGFTDGTMLV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 480 DGFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRR 559
Cdd:PLN02959 486 GEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNLYSDETRH 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 560 NFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNLHGQAESPlgIRPQQMTKEVWDYVF 639
Cdd:PLN02959 566 GFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGKDKSS--IKPEQMTDEVWDFVF 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 640 FKeAPFPKT-QIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEqsDKWPTAVRANGHLLLNSEKMS 718
Cdd:PLN02959 644 CG-GPLPKSsDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAE--EHWPRGFRCNGHLMLNSEKMS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 719 KSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTFNDRVFA 798
Cdd:PLN02959 721 KSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLTKEIAWMEEVLAAESSLRTGPPSTYADRVFE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 799 SELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYR-ELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIW-TLLGK 876
Cdd:PLN02959 801 NEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRlSCGSGGMNRDLVWRFMDVQTRLITPICPHYAEHVWrEILKK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 877 PDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCT---IYVAKNYPPWQHTTLS 953
Cdd:PLN02959 881 EGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKGGAPVTLPEKKLaglIYVAEKYDGWKEECLR 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 954 VLRKHFEANNGKL-PDNKVIA----SELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVLMENIVYLT 1028
Cdd:PLN02959 961 ILQSKFDSQSRTFaPDAEILEalkeSSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQALDLKLPFDEIEVLQENLELIK 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 48428689 1029 NSLELEHIEVKFASEAEDKIR----------EDCCPGKPLNVFR 1062
Cdd:PLN02959 1041 RQLGLEEVEILSASDPDAVAKagahasllkqNPPSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
14-1057 |
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: 862.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 14 KKIEKEIQQKWDTERVFEVNASNLEKqtskgkYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCT 93
Cdd:TIGR00395 1 IAIEKKWQKRWEEAHIFEADPDDREK------FFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 94 GMPIKACADKLKREIELYGcppdfpdeeeeeeetsvktediiikdkakgkkskaaakagsskyqWGIMKSLGLSDEEIVK 173
Cdd:TIGR00395 75 GTPILGLAELIKRRDELTI---------------------------------------------KNYTEVHAIPREELLK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 174 FSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDR 253
Cdd:TIGR00395 110 FTDPEYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDHDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 254 QTGEGVGPQEYTLLKLKVLEpypsklsglkgKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFEtVNGDIFICTQKAARN 333
Cdd:TIGR00395 188 LSGEGVTIVEYILIKFELED-----------GAFYFVAATLRPETVYGVTNCWVNPTITYVIAE-VGGEKWITSKEAFEN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 334 MSYQGFTkdngvVPVVKELMGEEILGASLSAPLTsYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALr 413
Cdd:TIGR00395 256 LSYQKLK-----YKPIEEVPGKQFIGKKVHNPVV-GPEVPILPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDPEY- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 414 akYGIRDdMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIML--VDGFKGQKVQDVK 491
Cdd:TIGR00395 329 --LGIKP-VVIDIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIynIPPYKGMKVSEAK 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 492 KTIQKKMIDAGDALIYMEP-EKQVMSRSSDECVVALC-DQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQ 569
Cdd:TIGR00395 406 EKVKADLIDAGLADVMYEFsESPVICRCGTDCIVKVVeDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDWLK 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 570 EHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNlhgqaesplgIRPQQMTKEVWDYVFFKEAPFPKTQ 649
Cdd:TIGR00395 486 DWACCRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDY----------YGNEQMTDEFFDYIFLGKGDVKNTN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 650 IAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEqsDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQ 729
Cdd:TIGR00395 556 IPLPAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPE--KFWPRGIVVNGYVMLEGKKMSKSKGNVLTLEQ 633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 730 AIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEmVANWDSLRSGPASTFNDRVFASELNAGIIKTD 809
Cdd:TIGR00395 634 AVEKFGADVARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEE-ITKESNLETGEETSFIDRWLESRMNAAIKETY 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 810 QNYEKMMFKEALKTGFFEFQAAKDKYRElAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAG 889
Cdd:TIGR00395 713 EAMENFQTRKAVKYALFDLQADVDWYRR-RGGVNHKDVLARYLETWIKLLAPFAPHFAEEMWEEVGNEGFVSLAKFPEAS 791
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 890 --PVNEVLIHSSQYLMEVTHDLRlrlknymmpaKGKKTDKqplQKPSHCTIYVAknyPPWQHTTLSVLRKHFEANNGKlp 967
Cdd:TIGR00395 792 epAVDKEVEAAEEYLRNLVRDIQ----------EIAKIDA---SKPKRVYLYTS---EDWKSQCLKIVAELFGEDTGE-- 853
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 968 DNKVIASElgsmPELKKYMKKVMPFVAMIKENLEKmgprilDLQLEFDEKAVLMENIVYLTNSLELEHI-EVKFASEAED 1046
Cdd:TIGR00395 854 DMKKVMEE----PEERKRGKEVISLVKQIIKDEKK------EDELQISEIEVLKAAARFIKKEVGALVIiEFSADSFPEN 923
|
1050
....*....|.
gi 48428689 1047 KiREDCCPGKP 1057
Cdd:TIGR00395 924 K-KRNAVPGKP 933
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
59-1057 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 749.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 59 LHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKReielygcppdfpdeeeeeeetsvKTEDIIikd 138
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR-----------------------GDPETI--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 139 kakgkkskaaakagsskyqwGIMKSL-GLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDSF 217
Cdd:PRK12300 55 --------------------ELYKSLyGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--PEYSKF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 218 VRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKvlepypsklsglKGKNIFLVAATLRPE 297
Cdd:PRK12300 113 IEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFE------------ESEDLILPAATLRPE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 298 TMFGQTNCWVRPDMKYIGFEtVNGDIFICTQKAARNMSYQGFTkdngvVPVVKELMGEEILGASLSAPLTSYKVIyVLPM 377
Cdd:PRK12300 181 TIFGVTNLWVNPDATYVKAE-VDGEKWIVSKEAAEKLSFQDRD-----VEIIEEIKGSELIGKKVKNPVTGKEVP-ILPA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 378 LTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKygirddmvlpFEPVPVIEIPGFGNLSAVTICDELKIQSQNDR 457
Cdd:PRK12300 254 DFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNKELLDV----------IEPIPLIEVEGYGEFPAKEVVEKLGIKSQEDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 458 eKLAEAKEKIYLKGFYEGIMLVD--GFKGQKVQDVKKTIQKKMIDAGDALIYME-PEKQVMSRSSDECVVA-LCDQWYLD 533
Cdd:PRK12300 324 -ELEEATKEVYRAEFHKGVLKENtgEYAGKPVREAREKITKDLIEKGIADIMYEfSNRPVYCRCGTECVVKvVKDQWFID 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 534 YGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGG 613
Cdd:PRK12300 403 YSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAHKIREY 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 614 nlhgqaesplGIRPQQMTKEVWDYVF----FKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNH 689
Cdd:PRK12300 483 ----------GIKPEQLTPEFFDYVFlgkgDPEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFIFNH 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 690 VAMWPEqsDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLyt 769
Cdd:PRK12300 553 VAIFPE--EKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQL-- 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 770 wvEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELaVEGMHRELVF 849
Cdd:PRK12300 629 --ERFYELAKELIEIGGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRR-VGEANNKVLR 705
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 850 RFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGP--VNEVLIHSSQYLMEVTHDLRlRLKNYmmpAKGkktdk 927
Cdd:PRK12300 706 EVLEIWIRLLAPFTPHLAEELWHKLGGEGFVSLEKWPEPDEskIDEEAELAEEYVKRLIEDIR-EILKV---AKI----- 776
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 928 qplqKPSHCTIYVAknyPPWQHTTLSVLRkhfeanngKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRI 1007
Cdd:PRK12300 777 ----KPKKVYIYVA---PDWKYEVLEIAA--------ENGDVKEAIKELMKDEELRKHGKEVAKLAQKIVKEVLKLDKEV 841
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 48428689 1008 LDL-QLEFDEKAVLMENIVYLTNSLELEhIEVKFASEAE-DKIREDCCPGKP 1057
Cdd:PRK12300 842 RKLiLKNIDEEEVLEEAKDFLEKELGVE-VEIYGADDPGkKKKKKKALPLKP 892
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
525-757 |
2.01e-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: 243.69 E-value: 2.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 525 ALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGwlqehaCSRTYGLGTHLPWdeQWLIESLSDSTIYMAFY 604
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 605 TVAHLLQggnlhgqaesplgirpqqmtkevwdyvffkeapfpktQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSY 684
Cdd:cd00812 199 TDAHNLE-------------------------------------QPYEGDLEFDREEFEYWYPVDIYIGGKEHAPNHLLY 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48428689 685 YLYNHVAMWPEQ--SDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDtvEDANFVE 757
Cdd:cd00812 242 SRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFDW 314
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
755-874 |
3.60e-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: 175.47 E-value: 3.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 755 FVEAMADAGILRLYTWVEWVKEMVANWDSLrsgPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDK 834
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 48428689 835 YRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLL 874
Cdd:cd07959 78 YRERGGAGMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
45-229 |
2.34e-29 |
|
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: 119.66 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 45 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKReielygcppdfpdeeeee 124
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 125 eetsvktediiikdkakgkkskaaakagsskyqwgimkslglsdeeivkfsEAEHWLDYFPPLAIQDLKRMGLKVDWRRS 204
Cdd:cd00812 63 ---------------------------------------------------DPEDWTEYNIKKMKEQLKRMGFSYDWRRE 91
|
170 180
....*....|....*....|....*
gi 48428689 205 FITTDvnPYYDSFVRWQFLTLRERN 229
Cdd:cd00812 92 FTTCD--PEYYKFTQWLFLKLYEKG 114
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
14-1052 |
2.25e-24 |
|
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: 110.53 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 14 KKIEKEIQQKWDTERVFEVNASnlekqTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCT 93
Cdd:TIGR00422 8 HEVEKKWYKKWEKSGFFKPDGN-----SNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 94 GMPikacadklkreielygcppdfpdeeeeeeeTSVKTEDIIikdkakgkkskaaakagsskyqWGIMKSLG-LSDEEIV 172
Cdd:TIGR00422 83 GIA------------------------------TQVKVEKKL----------------------GAEGKTKHdLGREEFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 173 KfsEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHD 252
Cdd:TIGR00422 111 E--KIWEWKEESGGTIKNQIKRLGASLDWSRERFTMD--EGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 253 RQTGEGVGPQEYTLLKLKvlepypsklsglKGKNIFLVAATLRPETMFGQTNCWVRP-DMKYigfetvngdifictqkaa 331
Cdd:TIGR00422 187 VEYKEVKGKLYYIRYPLA------------NGSKDYLVVATTRPETMFGDTAVAVHPeDERY------------------ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 332 rnmsyqgftkdngvvpvvKELMGEEILgaslsAPLTSYKViyvlPMLT---IKEDKGTGVVTSVPSDSPDDIAalrdLKK 408
Cdd:TIGR00422 237 ------------------KHLIGKKVI-----LPLTGRKI----PIIAdeyVDMEFGTGAVKVTPAHDFNDYE----WGK 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 409 KQALrakygirddmvlpfEPVPVIEIPGFGNLSAvticdeLKIQSQndreKLAEAKEKIylkgfyegimlvdgfkgqkVQ 488
Cdd:TIGR00422 286 RHNL--------------EFINILDEDGLLNENA------GKYQGL----TRFEARKKI-------------------VE 322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 489 DVKKtiQKKmidagdaLIYMEPEKQ---VMSRSSDECVVALCDQWYLDYgeENWKKQTSQCLKNLE-TFCEEtrrNFEAT 564
Cdd:TIGR00422 323 DLKE--EGL-------LVKIEPHTHnvgTCWRSGTVVEPLLSKQWFVKV--EKLADKALEAAEEGEiKFVPK---RMEKR 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 565 L-GWLQEHA--C-SRTYGLGTHLPwdeqwlieslsdstiymAFYTVahllQGGNLHGQAESPLGIRPQQMT--------K 632
Cdd:TIGR00422 389 YlNWLRNIKdwCiSRQLIWGHRIP-----------------VWYCK----ECGEVYVAKEEPLPDDKTNTGpsveleqdT 447
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 633 EVWDyVFFKEA--PFPKTQIAKEKLDqlkqeFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMwpEQSDKWPTA-----VR 705
Cdd:TIGR00422 448 DVLD-TWFSSSlwPFSTLGWPDETKD-----LKKFYPTDLLVTGYDIIFFWVARMIFRSLAL--TGQVPFKEVyihglVR 519
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 706 -ANGHlllnseKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAG---ILRLYTWVEWVKEMVANW 781
Cdd:TIGR00422 520 dEQGR------KMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESArnfLNKLWNASRFVLMNLSDD 593
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 782 DSLrSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEALKtGFFEF----------QAAK--DKYRELAVEGMHREL 847
Cdd:TIGR00422 594 LEL-SGGEEKLSlaDRWILSKLNRTIKEVRKALDKYRFAEAAK-ALYEFiwndfcdwyiELVKyrLYNGNEAEKKAARDT 671
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 848 VFRFIEVQTLLLAPFCPHLCEHIW-TLLGKPDSIMNASWPVAGP--VNEVLIHSSQYLMEVTHDLRLRLKNYMMPAkgkk 924
Cdd:TIGR00422 672 LYYVLDKALRLLHPFMPFITEEIWqHFKEGADSIMLQSYPVVDAefVDEEAEKAFELLKEIIVSIRNLKAESNIPP---- 747
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 925 tdKQPLQKpshCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLpdnkviaseLGSMPELKKYMKKVMPFVAMI--KENLEK 1002
Cdd:TIGR00422 748 --NAPLKV---LLIYTEAETAERLKLNAVDIKGAINFSEVEV---------VIEKPEVTEAVVELVPGFEIIipVKGLIN 813
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 48428689 1003 MGPRILDLQLEFDEKavLMENIVyLTNSLELEHIEVKFASEAEDKIREDC 1052
Cdd:TIGR00422 814 KAKELARLQKQLDKE--KKEVIR-IEGKLENEGFVKKAPKEVIEKEKEKL 860
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
20-755 |
8.53e-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: 101.33 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 20 IQQKWDTERVFEvnaSNLEKQTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKA 99
Cdd:pfam00133 2 IYEFWDEQGYFK---PELEKRKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 100 cadklkrEIElygcppdfpdeeeeeeetsvktediiikdkakgkkskaaakagsskyqwgimKSLGLSDEEIV-KFSEAE 178
Cdd:pfam00133 79 -------VVE----------------------------------------------------KKLGIKEKKTRhKYGREE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 179 H------WLDYFPPLAIQDLKRMGLKVDWRRSFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHD 252
Cdd:pfam00133 100 FrekcreWKMEYADEIRKQFRRLGRSIDWDREYFTMD--PELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 253 RQTGEGVGPQEYTLLKLKVlepypsklsglkGKNIFLVAATLRPETMFGQTNCWVRPDMKYIgfetVNGDIFICTQKAAR 332
Cdd:pfam00133 178 VEYKDVKGPSIHVAFPLAD------------DEGASLVIWTTTPWTLPGNTAVAVNPEFDYV----ITGEGYILAEALLK 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 333 NMSYQGFTKDngvvpVVKELMGEEILGASLSAPLTSYKViyvlPMLT---IKEDKGTGVVTSVPSDSPDDIAALRdlkkk 409
Cdd:pfam00133 242 SLYKKGTDKK-----ILEDFRGKELEGKEAIHPFVNREI----PIITddyVDMEFGTGAVHIAPAHGENDYEVGQ----- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 410 qalraKYGIrdDMVLPFEPVPVIeipgfgnlsavticdelkiqsqndREKLAEakekiylkgfyegimlvdgFKGQKVQD 489
Cdd:pfam00133 308 -----RHNL--EVINPVDDDGTF------------------------TEEAPD-------------------FQGVYRFD 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 490 VKKTIQKKMIDAGdalIYMEPEKQVMS-----RSSDECVVALCDQWYLdygeeNWKKQTSQCLKNLE--TFCEETRRN-F 561
Cdd:pfam00133 338 ARKKIVELLTEKG---LLLKIEPFTHSypfcwRSGTPIIPRATPQWFV-----RMDELADQALEAVEkvQFVPKSGEKrY 409
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 562 EATLGWLQEHACSRTYGLGTHLPWdeqWLIESLSDstIYMA---FYTVAHLLQGG----NLHGQAESPLGIRPQQMTK-- 632
Cdd:pfam00133 410 FNWLANIQDWCISRQRWWGHPIPA---WVSKDTEE--VVCRgelFELVAGRFEEEgsikWLHREAKDKLGYGKGTLEQde 484
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 633 EVWDyVFFKEAPFPKTQIakEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKwptAVRANGhLLL 712
Cdd:pfam00133 485 DVLD-TWFSSGSWPFSTL--GWPFVNTEEFKKFFPADMLLEGSDQTRGWFYRMIMLSTALTGSVPFK---NVLVHG-LVR 557
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 48428689 713 NSE--KMSKSTGNFLTLTQAIDKFSADGMRLALADAgDTVEDANF 755
Cdd:pfam00133 558 DEQgrKMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
496-744 |
2.45e-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: 93.25 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 496 KKMIDAGdaLIYmepekqvmsrsSDECVVALCDQWYLDYGEenWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSR 575
Cdd:cd00668 121 SRLYEKG--LIY-----------RGTHPVRITEQWFFDMPK--FKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 576 TYGLGTHLPwdeQWLIESLSDSTIYMAFYTvahllqgGNLHGqaesplgirpqqmtkevwdyvffkeapfpktqiakekl 655
Cdd:cd00668 186 QRYWGTPLP---EDVFDVWFDSGIGPLGSL-------GYPEE-------------------------------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 656 dqlKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEqsdKWPTAVRANGHLLLN-SEKMSKSTGNFLTLTQAIDKF 734
Cdd:cd00668 218 ---KEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGE---IPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKY 291
|
250
....*....|
gi 48428689 735 SADGMRLALA 744
Cdd:cd00668 292 GADALRYYLT 301
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
794-910 |
4.81e-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: 78.98 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 794 DRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQ---------AAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCP 864
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWndlsdwyleLIKDRLYGEEPDSRAQTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 48428689 865 HLCEHIWtllgKPDSIMNASWPVAGPVNEVLIHSS-QYLMEVTHDLR 910
Cdd:pfam08264 81 FITEELW----QKESIHLAPWPEDAELEEAELEEAfELRQEIVQAIR 123
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
674-888 |
2.03e-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: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 674 GKDLVpnhlsyylYNHVAMWP---EQSD-KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDT 749
Cdd:COG0143 289 GKDII--------RFHAIIWPamlMAAGlPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPF 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 750 VEDANFveamadagilrlyTWVEWV----KEMVANWDSL--RS--------------GPASTFNDRVFASELNAGIIKTD 809
Cdd:COG0143 361 GQDGDF-------------SWEDFVarvnSDLANDLGNLasRTlsmihkyfdgkvpePGELTEADEELLAEAEAALEEVA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 810 QNYEKMMFKEALKT---------GFFEFQA----AKDKYRELAVEGMHREL-VFRFIevqTLLLAPFCPHLCEHIWTLLG 875
Cdd:COG0143 428 EAMEAFEFRKALEEimalaraanKYIDETApwklAKDEDPERLATVLYTLLeALRIL---AILLKPFLPETAEKILEQLG 504
|
250
....*....|....*.
gi 48428689 876 KPDSIMN---ASWPVA 888
Cdd:COG0143 505 LEGDELTwedAGWPLP 520
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
45-242 |
5.72e-13 |
|
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: 71.30 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 45 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLkreielygcppdfpdeeeee 124
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERK-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 125 eetsvktediiikdkakgkkskaaakagsskyqwGIMKSlglSDEEIVKFSEA-EHWLDYFPPLAIQDLKRMGLKVDWRR 203
Cdd:cd00668 61 ----------------------------------GGRKK---KTIWIEEFREDpKEFVEEMSGEHKEDFRRLGISYDWSD 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 48428689 204 SFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSP 242
Cdd:cd00668 104 EYITTE--PEYSKAVELIFSRLYEKGLIYRGTHPVRITE 140
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
702-888 |
2.21e-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: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 702 TAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL------------ADAGdtVEDAN-FVEamadagilRLY 768
Cdd:COG0495 575 LEVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEmfagpperdlewSDSG--VEGAYrFLN--------RVW 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 769 TwvewvkeMVANWDSLRSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEA------LKTGFFEFQAAKDKYRELAV 840
Cdd:COG0495 645 R-------LVVDEAEALKLDVADLSeaDKELRRALHKTIKKVTEDIERLRFNTAiaalmeLVNALYKAKDSGEADRAVLR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 48428689 841 EGMhrelvfrfiEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVA 888
Cdd:COG0495 718 EAL---------ETLVLLLAPFAPHIAEELWERLGHEGSVADAPWPEA 756
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
662-888 |
1.00e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 65.98 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 662 FEFWYPVDLRVSGKDLVPNHL------SYYLYNHVAmwpeqsdkWpTAVRANGHLL-LNSEKMSKSTGNFLTLTQAIDKF 734
Cdd:PRK13208 481 FEKVFPMDLRPQGHDIIRTWLfytilrAYLLTGKLP--------W-KNIMISGMVLdPDGKKMSKSKGNVVTPEELLEKY 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 735 SADGMRLALADA--GDtveDANFVEAMADAG-------------ILRLYTWVEWVKEMVANwdslrsgPAstfnDRVFAS 799
Cdd:PRK13208 552 GADAVRYWAASArlGS---DTPFDEKQVKIGrrlltklwnasrfVLHFSADPEPDKAEVLE-------PL----DRWILA 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 800 ELNAGIIKTDQNYEKMMFKEALKT--GFF--EFQaakDKYRELA--------VEGMHRELVF---RFIEVQTLLLAPFCP 864
Cdd:PRK13208 618 KLAKVVEKATEALENYDFAKALEEieSFFwhVFC---DDYLELVksraygedEEEEQKSARYtlyTVLDTLLRLLAPFLP 694
|
250 260
....*....|....*....|....
gi 48428689 865 HLCEHIWTLLGKpDSIMNASWPVA 888
Cdd:PRK13208 695 FITEEVWSWLYG-GSVHRASWPEP 717
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
674-878 |
1.69e-10 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 65.17 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 674 GKDLVpnhlsyylYNHVAMWP---EQSD-KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALA-DAGD 748
Cdd:PRK00133 291 GKDII--------YFHTLFWPamlEGAGyRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAaKLPE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 749 TVEDANFveamadagilrlyTWVEWVK----EMVANWDSL--RS----------GPASTFNDRVFASELNAGIIKTDQNY 812
Cdd:PRK00133 363 TIDDLDF-------------NWEDFQQrvnsELVGKVVNFasRTagfinkrfdgKLPDALADPELLEEFEAAAEKIAEAY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 813 EKMMFKEALKT---------GFFEFQA----AKDKYRELAvEGMHREL-VFRFIevqTLLLAPFCPHLCEHIWTLLGKPD 878
Cdd:PRK00133 430 EAREFRKALREimaladfanKYVDDNEpwklAKQDGERLQ-AVCSVGLnLFRAL---AIYLKPVLPELAERAEAFLNLEE 505
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
13-97 |
1.96e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 65.21 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 13 LKKIEKEIQQKWDTERVFEVNASNLEKQtskgkYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHC 92
Cdd:PRK13208 12 PEELEEKWQKIWEEEGTYKFDPDERKPV-----YSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDD 86
|
....*
gi 48428689 93 TGMPI 97
Cdd:PRK13208 87 NGLPT 91
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
635-890 |
4.14e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 64.46 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 635 WDYVFFKEAPFPKTQIAKEKLdqlkqefEFWYPVDLRVSGKDLVPNHLSY------YLYN--------------HVAM-- 692
Cdd:PLN02563 591 WYYLRFMDPKNSNALVDKEKE-------KYWMPVDLYVGGAEHAVLHLLYarfwhkVLYDigvvstkepfqclvNQGMil 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 693 -------WPEQSDKWPTAVRANGHLLLNSE-----------------------------KMSKSTGNFLTLTQAIDKFSA 736
Cdd:PLN02563 664 geveytaFKDSDGEYVSADTADRLGELQQEkipeekviksgdsfvlkddpsirliarahKMSKSRGNVVNPDDVVSEYGA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 737 DGMRLaladagdtvedanFVEAMadaGILR-LYTW----VEWVKEMVAN-WDSLRSGPAS--TFNDRVFASE-------- 800
Cdd:PLN02563 744 DSLRL-------------YEMFM---GPLRdSKTWstsgVEGVHRFLGRtWRLVVGAPLPdgSFRDGTVVTDeepsleql 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 801 --LNAGIIKTDQNYEKMMFKEALkTGFFEFQAAKDKYRELAVEgmhrelvfrFIEVQTLLLAPFCPHLCEHIWTLLGKPD 878
Cdd:PLN02563 808 rlLHKCIAKVTEEIESTRFNTAI-SAMMEFTNAAYKWDKVPRE---------AIEPFVLLLSPYAPHLAEELWFRLGHSN 877
|
330
....*....|..
gi 48428689 879 SIMNASWPVAGP 890
Cdd:PLN02563 878 SLAYEPWPEANP 889
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
716-924 |
4.40e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 63.97 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 716 KMSKSTGNF---LTLtqaIDKFSADGMRLALAdagdtvedanfveAMADAGI-LRL-YTWVE---------W-----VKE 776
Cdd:PRK05729 520 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIRFdEERVEgyrnfanklWnasrfVLM 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 777 MVANWDSLRSGPASTFN--DRVFASELNAGIIKTDQNYEKMMFKEALKT--GFF--EF-----QAAKDKYRELAVEGMHR 845
Cdd:PRK05729 584 NLEGADVGELPDPEELSlaDRWILSRLNRTVAEVTEALDKYRFDEAARAlyEFIwnEFcdwylELAKPVLQEAAKRATRA 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 846 ELVfRFIEvQTL-LLAPFCPHLCEHIWTLL---GKPDSIMNASWPVAGPV-NEVLIHSSQYLMEVTHDLRlRLKNYMMPA 920
Cdd:PRK05729 664 TLA-YVLE-QILrLLHPFMPFITEELWQKLaplGIEESIMLAPWPEADEAiDEAAEAEFEWLKELITAIR-NIRAEMNIP 740
|
....
gi 48428689 921 KGKK 924
Cdd:PRK05729 741 PSKK 744
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
716-910 |
1.03e-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: 62.76 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 716 KMSKSTGNF---LTLtqaIDKFSADGMRLALAdagdtvedanfveAMADAGI-LRLYT-WVE------------------ 772
Cdd:COG0525 522 KMSKSKGNVidpLDL---IDKYGADALRFTLA-------------ALASPGRdIKFDEeRVEgyrnfanklwnasrfvlm 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 773 WVKEMVANWDSLRSgpASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKT--GFF--EFQaakDKYRELA-------VE 841
Cdd:COG0525 586 NLEGFDPGLDPDPE--ELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQAlyDFVwnEFC---DWYLELAkprlyggDE 660
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48428689 842 GMHRELVFRFIEV--QTL-LLAPFCPHLCEHIWTLLGKP---DSIMNASWPVAGP--VNEVLIHSSQYLMEVTHDLR 910
Cdd:COG0525 661 AAKRETRATLVYVleQILrLLHPFMPFITEEIWQKLPPRkegESIMLAPWPEADEelIDEEAEAEFEWLKEVISAIR 737
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
637-755 |
1.68e-09 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 61.15 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 637 YVFFkEAPFPKTQIAKEkLDQLKQEFEFWYPVDLRVS-----GKDLVpnhlsyylYNHVAMWP----EQSDKWPTAVRAN 707
Cdd:pfam09334 246 YVWL-DAPIGYISATKE-LSGNEEKWKEWWPNDPDTElvhfiGKDII--------YFHTIFWPamllGAGYRLPTTVFAH 315
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 48428689 708 GHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANF 755
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDF 363
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
664-880 |
2.39e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 61.44 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 664 FWyPVDLRVSGKDLVPNHLSYylynhvamWPEQ--SD--KWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGM 739
Cdd:PRK11893 252 YW-PADVHLIGKDILRFHAVY--------WPAFlmAAglPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 740 RLALA-------DaGDTVED----------ANFVEAMADAgilrlytwvewVKEMVANW--DSLRSGPASTFNDRVFASE 800
Cdd:PRK11893 323 RYFLLreipfgqD-GDFSREafinrinadlANDLGNLAQR-----------TLSMIAKNfdGKVPEPGALTEADEALLEA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 801 LNAGIIKTDQNYEKMMFKEALK---------TGFFEFQA----AKDKYRELAVEGMHRELVFRFIevqTLLLAPFCPHLC 867
Cdd:PRK11893 391 AAALLERVRAAMDNLAFDKALEailalvraaNKYIDEQApwslAKTDPERLATVLYTLLEVLRGI---AVLLQPVMPELA 467
|
250
....*....|...
gi 48428689 868 EHIWTLLGKPDSI 880
Cdd:PRK11893 468 AKILDQLGVEEDE 480
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
693-893 |
6.91e-09 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 60.39 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 693 WPEQSDK----WPTAVRANGHLLL--------------------------------NSEKMSKSTGNFLTLTQAIDKFSA 736
Cdd:PRK14900 479 WPEQTDTlrtfYPTSVMETGHDIIffwvarmmmmglhfmgevpfrtvylhpmvrdeKGQKMSKTKGNVIDPLVITEQYGA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 737 DGMRLALAD----------AGDTVEDAN-FVEAMADAGILRLYTWVEWVKEMVanwDSLRSgpASTFNDRVFASELNAGI 805
Cdd:PRK14900 559 DALRFTLAAltaqgrdiklAKERIEGYRaFANKLWNASRFALMNLSGYQERGE---DPARL--ARTPADRWILARLQRAV 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 806 IKTDQNYEKMMFKEALKTGF-FEFQAAKDKYRELAVEGMH----------RELVFRFIEVQTLLLAPFCPHLCEHIWTLL 874
Cdd:PRK14900 634 NETVEALEAFRFNDAANAVYaFVWHELCDWYIELAKEALAsedpearrsvQAVLVHCLQTSYRLLHPFMPFITEELWHVL 713
|
250 260
....*....|....*....|....*.
gi 48428689 875 -------GKPDSIMNASWPVAGPVNE 893
Cdd:PRK14900 714 raqvgasAWADSVLAAEYPRKGEADE 739
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
637-755 |
1.30e-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: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 637 YVFFkEAPFPKTQIAKEKLDQLKQEFEFWY--PVDLRVSGKDLVPNHlsyylynhVAMWP---EQSDKW-PTAVRANGHL 710
Cdd:cd00814 204 YVWF-DALIGYISATGYYNEEWGNSWWWKDgwPELVHFIGKDIIRFH--------AIYWPamlLGAGLPlPTRIVAHGYL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 48428689 711 LLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANF 755
Cdd:cd00814 275 TVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
707-743 |
2.13e-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: 2.13e-08
10 20 30
....*....|....*....|....*....|....*..
gi 48428689 707 NGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 743
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
707-743 |
1.91e-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: 1.91e-07
10 20 30
....*....|....*....|....*....|....*..
gi 48428689 707 NGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 743
Cdd:cd00672 165 TGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
44-245 |
6.16e-07 |
|
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: 53.02 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 44 GKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPikacadklkreielygcppdfpdeeee 123
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 124 eeeTSVKTEDIIIKDkakgkkskaaakagsskyqwGIMKSlGLSDEEIVKfsEAEHWLDYFPPLAIQDLKRMGLKVDWRR 203
Cdd:cd00817 54 ---TQVVVEKKLGIE--------------------GKTRH-DLGREEFLE--KCWEWKEESGGKIREQLKRLGASVDWSR 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 48428689 204 SFITTDvnPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDG 245
Cdd:cd00817 108 EYFTMD--PGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLR 147
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
666-746 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 666 YPVDLRVSGKDLV-PNHlsyylYNHVAMWPEQSDK-WPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 743
Cdd:pfam01406 206 DQIDIHGGGIDLAfPHH-----ENEIAQSEAAFDKqLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFL 280
|
...
gi 48428689 744 ADA 746
Cdd:pfam01406 281 LSV 283
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
13-97 |
1.35e-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: 49.69 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 13 LKKIEKEIQQKWDTERVFEvnasNLEKQTSKGKYFVtF---PyPYMNGRLHLGHTfsLSKC--EFAVGYQRLKGKCCLFP 87
Cdd:COG0060 18 LPKREPEILKFWEENDIYE----KSREARAGRPKFV-LhdgP-PYANGDIHIGHA--LNKIlkDIIVRYKTMRGFDVPYV 89
|
90
....*....|
gi 48428689 88 FGLHCTGMPI 97
Cdd:COG0060 90 PGWDCHGLPI 99
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
657-755 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 657 QLKQEFEFWYPVDLRVSGKDLvpnhLSYYLYNHVAMWPEQSDKWP-TAVRANGhLLLNSE--KMSKSTGNFLTLTQAIDK 733
Cdd:cd00817 286 EETKDLKKFYPTSLLVTGHDI----IFFWVARMIMRGLKLTGKLPfKEVYLHG-LVRDEDgrKMSKSLGNVIDPLDVIDG 360
|
90 100
....*....|....*....|..
gi 48428689 734 FSADGMRLALADAGDTVEDANF 755
Cdd:cd00817 361 YGADALRFTLASAATQGRDINL 382
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
708-741 |
2.27e-05 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 48.49 E-value: 2.27e-05
10 20 30
....*....|....*....|....*....|....
gi 48428689 708 GHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRL 741
Cdd:PTZ00399 307 GHLHIKGLKMSKSLKNFITIRQALSKYTARQIRL 340
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
716-932 |
2.95e-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: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 716 KMSKSTGNFLTLTQAIDKFSADGMRLALAdAGDTVEDANF----VEAMADAgILRLY-TWV---------EWVKEMVA-- 779
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVA-SSDYWGDLRFsdeiLKEVRDV-YRRLRnTYRfllanlddfDPAEDAVPye 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 780 NWDSLrsgpastfnDRVFASELNAGIIKTDQNYEKMMFKEALKT--GF-------FEFQAAKD---------KYRELAVE 841
Cdd:COG0060 681 DLPEL---------DRWILSRLNELIKEVTEAYDNYDFHRAYRAlhNFcvedlsnWYLDISKDrlyteaadsLDRRAAQT 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 842 GMHRELvfrfiEVQTLLLAPFCPHLCEHIWTLL--GKPDSIMNASWPVA--GPVNEVLIHSSQYLMEVTHDLRLRLKNym 917
Cdd:COG0060 752 TLYEVL-----ETLVRLLAPILPFTAEEIWQNLpgEAEESVHLADWPEVdeELIDEELEAKWDLVREVRSAVLKALEA-- 824
|
250
....*....|....*
gi 48428689 918 mpAKGKKTDKQPLQK 932
Cdd:COG0060 825 --ARKEKLIRQPLEA 837
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
17-97 |
9.39e-05 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 46.69 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 17 EKEIQQKWDTERVFEVNASNlekqtSKGKYFVTF--PyPYMNGRLHLGHtfSLSKC--EFAVGYQRLKGKCCLFPFGLHC 92
Cdd:PLN02843 9 EPEIQKLWEENQVYKRVSDR-----NNGESFTLHdgP-PYANGDLHIGH--ALNKIlkDFINRYQLLQGKKVHYVPGWDC 80
|
....*
gi 48428689 93 TGMPI 97
Cdd:PLN02843 81 HGLPI 85
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
835-874 |
3.77e-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: 3.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 48428689 835 YRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLL 874
Cdd:cd07958 78 YKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
666-743 |
5.76e-04 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 44.15 E-value: 5.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48428689 666 YPVDLRVSGKDLV-PNHLSYYLYNHVAMWPEQSDKWPtavrANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLAL 743
Cdd:PLN02946 276 HSFDIHGGGMDLVfPHHENEIAQSCAACCDSNISYWI----HNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL 350
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
46-105 |
1.08e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 42.66 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 46 YFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLK 105
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEG 60
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
716-890 |
1.45e-03 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 42.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 716 KMSKSTGNFLTLTQAID---------KFSADGMRLALAD---AGDTVEDANFVEAMADA-----GILR--LYTWVEWVKE 776
Cdd:PLN02843 611 KMSKSLGNVVDPRLVIEggknqkqepAYGADVLRLWVASvdyTGDVLIGPQILKQMSDIyrklrGTLRylLGNLHDWKPD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 777 MVANWDSLrsgPAStfnDRVFASELNAGIIKTDQNYEKMMFKEALKT---------GFFEFQAAKDKyreLAVEGMHRel 847
Cdd:PLN02843 691 NAVPYEDL---PSI---DKYALFQLENVVNEIEESYDNYQFFKIFQIlqrftivdlSNFYLDVAKDR---LYVGGTTS-- 759
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 48428689 848 vFRFIEVQTLL----------LAPFCPHLCEHIWTLL------GKPDSIMNASWPVAGP 890
Cdd:PLN02843 760 -FTRRSCQTVLaahllsllraIAPILPHLAEDAWQNLpfqedgSAAESVFEAGWPTPNE 817
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
654-752 |
1.58e-03 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 42.78 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428689 654 KLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYlynhVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDK 733
Cdd:PLN02224 308 KQQNLETAVSFGWPASLHLIGKDILRFHAVYW----PAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQK 383
|
90 100
....*....|....*....|....*
gi 48428689 734 FSADGMR------LALADAGDTVED 752
Cdd:PLN02224 384 FGPDAVRyfflreVEFGNDGDYSED 408
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
45-86 |
1.99e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 42.18 E-value: 1.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 48428689 45 KYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLF 86
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFF 43
|
|
| |
