|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
1-1044 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 1897.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 1 MATARRDTLLELQARAQKKWADEKTFEVSAPKDGSKP-PKFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETL 79
Cdd:PLN02959 7 KSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPKPgEKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 80 FPFAFHCTGMPIKASADKIKNEIAKYGNPPVFPVIDEAAEAAAAAAAAAQKAADAknaDPTKFAAKKSKASAKAGTQTYQ 159
Cdd:PLN02959 87 LPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEDEDEAAAVAAAKAEAEAAAA---PPDKFKGKKSKAVAKSGTQKYQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 160 WDIMKSSGIGDSEIPPFADPYHWLDYFPPLAKRDVAAMGCQarsishrspydrvgvvnaVDWRRSFTTTDHNPFYDAFVR 239
Cdd:PLN02959 164 WEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLG------------------CDWRRSFITTDVNPYYDAFVR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 240 WQFNTLKKIGKVIKAKRMAVYSPLDGQPCADHDRASGEGVGPQEYVLIKMRVYDEcLVGELAPLAGKNVFLAAATLRPET 319
Cdd:PLN02959 226 WQFRKLKKKGKIVKDKRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPP-FPGKLKALEGKKVFLAAATLRPET 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 320 MYGQTNCWILPDGDYGAFEMANGDVMVMCDRAARNLSYQERTKAEGDTGKILSFKGAALIGCAVKSPLAILEKIYCLPML 399
Cdd:PLN02959 305 MYGQTNCWVLPDGKYGAYEINDTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPML 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 400 TILMGKGTGVVTSVPSDSPDDFMALSDLKAKKALREKFGVLDEWVLPFDVVPCVRIPEFGDACAPIVCEQLKIQSQNDKA 479
Cdd:PLN02959 385 TILTDKGTGVVTSVPSDSPDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 480 KLEEAKHRTYLKGFTDGVMLRGVYEGEPVKIVKPKIRDLMLESGDAIVYSEPEKQVMSRSGDECVVALTDQWYLEYGEEG 559
Cdd:PLN02959 465 KLAEAKRLTYLKGFTDGTMLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 560 WREKAEKCLAGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGS 639
Cdd:PLN02959 545 WKKKAEKCLSKMNLYSDETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGK 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 640 ARPSVEPSAMTDEVWDAVFLGVPLPAGSDFPKELLKEMKTEFEFWYPFDLRVSGKDLIQNHLTFSIYNHVALWAEDEskW 719
Cdd:PLN02959 625 DKSSIKPEQMTDEVWDFVFCGGPLPKSSDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAEEH--W 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 720 PRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAGDTIEDANF------------------------- 774
Cdd:PLN02959 703 PRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFvfetanaailrltkeiawmeevlaa 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 775 ---------------------------------------ALKCGYYDLQSARDAYRLQCGGlgeeGNMHAELVKRFIEVS 815
Cdd:PLN02959 783 esslrtgppstyadrvfeneiniaiaeteknyeammfreALKSGFYDLQAARDEYRLSCGS----GGMNRDLVWRFMDVQ 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 816 TLLLAPFCPHTCEHVWGALLGKPGTVTKAGFPTYVEPDKALMAAARYLDDLVSSIRKGVAKATAPPKKKGAGPPP--PIK 893
Cdd:PLN02959 859 TRLITPICPHYAEHVWREILKKEGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKGGAPvtLPE 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 894 TCDAAHVFVAEKFGGWQEVCLGILAEKYDASANAFPPVNEVLDAVKASELSKDANFKNVMKMVMPFIKFKQDEAKAVGED 973
Cdd:PLN02959 939 KKLAGLIYVAEKYDGWKEECLRILQSKFDSQSRTFAPDAEILEALKESSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQ 1018
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 303277431 974 ALSVRLIFDEAGVLNENAAFIAKACGLKAFAVFSSagdalDGAAAESVAAATSGGVKVDAATPGAPAVYYI 1044
Cdd:PLN02959 1019 ALDLKLPFDEIEVLQENLELIKRQLGLEEVEILSA-----SDPDAVAKAGAHASLLKQNPPSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
11-1043 |
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: 735.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 11 ELQARAQKKWADEKTFEVsapkDGSKPPKFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMP 90
Cdd:TIGR00395 2 AIEKKWQKRWEEAHIFEA----DPDDREKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVTGTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 91 IKASADKIKNEIAKYGnppvfpvideaaeaaaaaaaaaqkaadaknadptkfaakkskasakagtqtyqWDIMKSSGIGD 170
Cdd:TIGR00395 78 ILGLAELIKRRDELTI-----------------------------------------------------KNYTEVHAIPR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 171 SEIPPFADPYHWLDYFPPLAKRDVAAMGCqarsishrspydrvgvvnAVDWRRSFTTTDhnPFYDAFVRWQFNTLKKIGK 250
Cdd:TIGR00395 105 EELLKFTDPEYIVEYFSREAESACKSMGY------------------SIDWRRSFKTTD--PYYDRFIEWQMNKLKELGL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 251 VIKAKRMAVYSPLDGQPCADHDRASGEGVGPQEYVLIKMRVYDECLvgelaplagknvFLAAATLRPETMYGQTNCWILP 330
Cdd:TIGR00395 165 IVKGEHPVRYCPKDGNPVEDHDLLSGEGVTIVEYILIKFELEDGAF------------YFVAATLRPETVYGVTNCWVNP 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 331 DGDYGAFEmANGDVMVMCDRAARNLSYQERtkaegDTGKILSFKGAALIGCAVKSPLaILEKIYCLPMLTILMGKGTGVV 410
Cdd:TIGR00395 233 TITYVIAE-VGGEKWITSKEAFENLSYQKL-----KYKPIEEVPGKQFIGKKVHNPV-VGPEVPILPAEFVDTTKGTGVV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 411 TSVPSDSPDDFMALSDLKAKKalrEKFGVLDEWVlPFDVVPCVRIPEFGDACAPIVCEQLKIQSQNDKAKLEEAKHRTYL 490
Cdd:TIGR00395 306 MSVPAHAPDDYIALEDLLHDP---EYLGIKPVVI-DIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYK 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 491 KGFTDGVMLRG--VYEGEPVKIVKPKIRDLMLESGDAIVYSEP-EKQVMSRSGDECVV-ALTDQWYLEYGEEGWREKAEK 566
Cdd:TIGR00395 382 EEYHTGVMIYNipPYKGMKVSEAKEKVKADLIDAGLADVMYEFsESPVICRCGTDCIVkVVEDQWFVKYSDESWKELAHE 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 567 CLAGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDmygsarpsVEP 646
Cdd:TIGR00395 462 CLEGMRIIPEEVKNAFEGKIDWLKDWACCRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDY--------YGN 533
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 647 SAMTDEVWDAVFLGVPLPAGSDFPKELLKEMKTEFEFWYPFDLRVSGKDLIQNHLTFSIYNHVALWAEDesKWPRGFRTN 726
Cdd:TIGR00395 534 EQMTDEFFDYIFLGKGDVKNTNIPLPAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPEK--FWPRGIVVN 611
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 727 GHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAGDTIEDANF-------------------------------- 774
Cdd:TIGR00395 612 GYVMLEGKKMSKSKGNVLTLEQAVEKFGADVARLYIADAAETVQDADWkesevegtilrlerlyefaeeitkesnletge 691
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 775 -------------------------------ALKCGYYDLQSARDAYRLQcgglgeEGNMHAELVKRFIEVSTLLLAPFC 823
Cdd:TIGR00395 692 etsfidrwlesrmnaaiketyeamenfqtrkAVKYALFDLQADVDWYRRR------GGVNHKDVLARYLETWIKLLAPFA 765
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 824 PHTCEHVWgALLGKPGTVTKAGFPTYVEP--DKALMAAARYLDDLVSSIRKGVAKATAPPKKkgagppppiktcdaAHVF 901
Cdd:TIGR00395 766 PHFAEEMW-EEVGNEGFVSLAKFPEASEPavDKEVEAAEEYLRNLVRDIQEIAKIDASKPKR--------------VYLY 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 902 VAEKfggWQEVCLGILAEKYDasanafppvNEVLDAVKasELSKDANFknvMKMVMPFIKFKQDEAKAVGEDALsvrLIF 981
Cdd:TIGR00395 831 TSED---WKSQCLKIVAELFG---------EDTGEDMK--KVMEEPEE---RKRGKEVISLVKQIIKDEKKEDE---LQI 890
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303277431 982 DEAGVLNENAAFIAKACGLKAFAVFSSAGDALDgaaaesvaaatsggvKVDAATPGAPAVYY 1043
Cdd:TIGR00395 891 SEIEVLKAAARFIKKEVGALVIIEFSADSFPEN---------------KKRNAVPGKPAIYL 937
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
53-1001 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 653.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 53 LHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMPIKASADKIKNeiakygnppvfpvideaaeaaaaaaaaaqkaa 132
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 133 daknADPTkfaakkskasakagtqtyQWDIMKS-SGIGDSEIPPFADPYHWLDYFPPLAKRDVAAMGCqarSIshrspyd 211
Cdd:PRK12300 49 ----GDPE------------------TIELYKSlYGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGY---SI------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 212 rvgvvnavDWRRSFTTTDhnPFYDAFVRWQFNTLKKIGKVIKAKRMAVYSPLDGQPCADHDRASGEGVGPQEYVLIKMRV 291
Cdd:PRK12300 97 --------DWRREFTTTD--PEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFEE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 292 YDEClvgelaplagknvFLAAATLRPETMYGQTNCWILPDGDYGAFEMaNGDVMVMCDRAARNLSYQERT-KAEGDtgki 370
Cdd:PRK12300 167 SEDL-------------ILPAATLRPETIFGVTNLWVNPDATYVKAEV-DGEKWIVSKEAAEKLSFQDRDvEIIEE---- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 371 lsFKGAALIGCAVKSPLAiLEKIYCLPMLTILMGKGTGVVTSVPSDSPDDFMALSDLKAKKALREKFGVldewvlpfdvV 450
Cdd:PRK12300 229 --IKGSELIGKKVKNPVT-GKEVPILPADFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNKELLDVIEP----------I 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 451 PCVRIPEFGDACAPIVCEQLKIQSQNDKaKLEEAKHRTYLKGFTDGVML--RGVYEGEPVKIVKPKIRDLMLESGDAIVY 528
Cdd:PRK12300 296 PLIEVEGYGEFPAKEVVEKLGIKSQEDP-ELEEATKEVYRAEFHKGVLKenTGEYAGKPVREAREKITKDLIEKGIADIM 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 529 SE-PEKQVMSRSGDECVVA-LTDQWYLEYGEEGWREKAEKCLAGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVPW 606
Cdd:PRK12300 375 YEfSNRPVYCRCGTECVVKvVKDQWFIDYSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPW 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 607 DEQFLIESLSDSTIYMAYYTVAHLLQGGDMygsarpsvEPSAMTDEVWDAVFLGVPLPA----GSDFPKELLKEMKTEFE 682
Cdd:PRK12300 455 DEEWIIESLSDSTIYMAYYTIAHKIREYGI--------KPEQLTPEFFDYVFLGKGDPEevskKTGIPKEILEEMREEFL 526
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 683 FWYPFDLRVSGKDLIQNHLTFSIYNHVALWaeDESKWPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFAL 762
Cdd:PRK12300 527 YWYPVDWRHSGKDLIPNHLTFFIFNHVAIF--PEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYL 604
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 763 ADAGDTIEDANF------------------------------------------------------------ALKCGYYD 782
Cdd:PRK12300 605 TSSAELLQDADWrekevesvrrqlerfyelakelieiggeeelrfidkwllsrlnriiketteamesfqtrdAVQEAFYE 684
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 783 LQSARDAYRlqcgGLGEEGNmhAELVKRFIEVSTLLLAPFCPHTCEHVWgALLGKPGTVTKAGFPTYVE--PDKALMAAA 860
Cdd:PRK12300 685 LLNDLRWYL----RRVGEAN--NKVLREVLEIWIRLLAPFTPHLAEELW-HKLGGEGFVSLEKWPEPDEskIDEEAELAE 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 861 RYLDDLVSSIR--KGVAKATapPKKkgagppppiktcdaAHVFVAEKfggWQEVCLGILAEKYDasanafppVNEVLDAV 938
Cdd:PRK12300 758 EYVKRLIEDIReiLKVAKIK--PKK--------------VYIYVAPD---WKYEVLEIAAENGD--------VKEAIKEL 810
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 303277431 939 KASELSKDANfKNVMKMVMPFIKFKQDEAKAVGEDALSVrliFDEAGVLNENAAFIAKACGLK 1001
Cdd:PRK12300 811 MKDEELRKHG-KEVAKLAQKIVKEVLKLDKEVRKLILKN---IDEEEVLEEAKDFLEKELGVE 869
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
546-774 |
1.84e-68 |
|
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: 232.14 E-value: 1.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 546 ALTDQWYLEYGEEGWREKAEKCLAGMRTYHDEARKAFEHTLGwlrqwaCSRAFGLGTRVPWdeQFLIESLSDSTIYMAYY 625
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 626 TVAHLLQGGDmygsarpsvepsamtdevwdavflgvplpagsdfpKELLKEMKTEFEFWYPFDLRVSGKDLIQNHLTFSI 705
Cdd:cd00812 199 TDAHNLEQPY-----------------------------------EGDLEFDREEFEYWYPVDIYIGGKEHAPNHLLYSR 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 303277431 706 YNHVALWAED--ESKWPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAGDtiEDANF 774
Cdd:cd00812 244 FNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADF 312
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
541-771 |
5.34e-24 |
|
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: 104.04 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 541 DECVVALTDQWYLEYGEegWREKAEKCLAGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVPWDeqfLIESLSDSTI 620
Cdd:cd00668 132 GTHPVRITEQWFFDMPK--FKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLPED---VFDVWFDSGI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 621 YMAYYTvahllqggdmygsarpsvepsamtdevwdavflgvplpagsDFPKEllkemKTEFEFWYPFDLRVSGKDLIQNH 700
Cdd:cd00668 207 GPLGSL-----------------------------------------GYPEE-----KEWFKDSYPADWHLIGKDILRGW 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303277431 701 LTFSIYNHVALWAEdesKWPRGFRTNGHLLLNN-EKMSKSTGNFKTLKAAIEAYSSDAMRFALAdAGDTIED 771
Cdd:cd00668 241 ANFWITMLVALFGE---IPPKNLLVHGFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLT-SLAPYGD 308
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
39-266 |
3.51e-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: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 39 KFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMPIKASADKIKNeiakygnppvfpvideaa 118
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 119 eaaaaaaaaaqkaadaknadptkfaakkskasakagtqtyqwdimkssgigdseippfaDPYHWLDYFPPLAKRDVAAMG 198
Cdd:cd00812 63 -----------------------------------------------------------DPEDWTEYNIKKMKEQLKRMG 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303277431 199 CqarsishrspydrvgvvnAVDWRRSFTTTDhnPFYDAFVRWQFNTLKKIGKVIKAKRMAVYSPLDGQ 266
Cdd:cd00812 84 F------------------SYDWRREFTTCD--PEYYKFTQWLFLKLYEKGLAYKKEAPVNWCKLLDQ 131
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
734-834 |
2.31e-20 |
|
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: 87.65 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 734 EKMSKSTGNFKTLKAAIEAYSSDaMRFALADAGDTIEDANF--ALKCGYYDLQSARDAYRLQCGGlgeegNMHAELVKRF 811
Cdd:cd07959 21 EELIETEGELEELTFIDRWLLSR-LNRLIKETTEAYENMQFreALKEGLYELQNDLDWYRERGGA-----GMNKDLLRRF 94
|
90 100
....*....|....*....|...
gi 303277431 812 IEVSTLLLAPFCPHTCEHVWGAL 834
Cdd:cd07959 95 IEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
17-774 |
1.56e-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: 84.38 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 17 QKKWADEKTFEVSAPKDGSKPPKFFGNFPyPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMPIKASAD 96
Cdd:pfam00133 3 YEFWDEQGYFKPELEKRKGKPSFTIHDGP-PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 97 KiknEIAKYGNPPVFpvideaaeaaaaaaaaaqkaadaknadptkfaakkskasaKAGTQTYQWDIMKssgigdseippf 176
Cdd:pfam00133 82 K---KLGIKEKKTRH----------------------------------------KYGREEFREKCRE------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 177 adpyhWLDYFPPLAKRDVAAMGcqarsishrspydrvgvvNAVDWRRSFTTTDhnPFYDAFVRWQFNTLKKIGKVIKAKR 256
Cdd:pfam00133 107 -----WKMEYADEIRKQFRRLG------------------RSIDWDREYFTMD--PELEAAVWEVFVRLHDKGLIYRGKK 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 257 MAVYSPLDGQPCADHDRASGEGVGPQEYVLIkmrvydeclvgelaPLAG-KNVFLAAATLRPETMYGQTNCWILPDGDYG 335
Cdd:pfam00133 162 LVNWSPALNTALSNLEVEYKDVKGPSIHVAF--------------PLADdEGASLVIWTTTPWTLPGNTAVAVNPEFDYV 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 336 afemANGDVMVMCDraARNLSYQERtkaeGDTGKILS-FKGAALIGCAVKSPLAilekIYCLPMLT---ILMGKGTGVVT 411
Cdd:pfam00133 228 ----ITGEGYILAE--ALLKSLYKK----GTDKKILEdFRGKELEGKEAIHPFV----NREIPIITddyVDMEFGTGAVH 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 412 SVPSDSPDDFmalsdlkakkALREKFGVldEWVLPFDvvpcvripefGDACapivceqlkiqsqndkakleeakhrtylk 491
Cdd:pfam00133 294 IAPAHGENDY----------EVGQRHNL--EVINPVD----------DDGT----------------------------- 322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 492 gFTDGVmlrGVYEGEPVKIVKPKIRDLMLESGdaiVYSEPEKQVMS-----RSGDECVVALTDQWYLEYGEegWREKAEK 566
Cdd:pfam00133 323 -FTEEA---PDFQGVYRFDARKKIVELLTEKG---LLLKIEPFTHSypfcwRSGTPIIPRATPQWFVRMDE--LADQALE 393
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 567 CLAGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVP-W-----DEQFLIESLSD----------STIYMAYYTVAHL 630
Cdd:pfam00133 394 AVEKVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPaWvskdtEEVVCRGELFElvagrfeeegSIKWLHREAKDKL 473
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 631 LQGGDMYgsarpsvepsAMTDEVWDAVFLGVPLPAGS-DFPKELLKEMKTEFefwyPFDLRVSGKDLIQNHLTFSIYNHV 709
Cdd:pfam00133 474 GYGKGTL----------EQDEDVLDTWFSSGSWPFSTlGWPFVNTEEFKKFF----PADMLLEGSDQTRGWFYRMIMLST 539
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 710 ALWAEdeskwpRGFR---TNGhLLLNNE--KMSKSTGNFKTLKAAIEAYSSDAMRFALADAgDTIEDANF 774
Cdd:pfam00133 540 ALTGS------VPFKnvlVHG-LVRDEQgrKMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
17-884 |
6.88e-14 |
|
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: 76.25 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 17 QKKWADEKTFEvsaPKDGSKPPKFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMPIKASAD 96
Cdd:TIGR00422 15 YKKWEKSGFFK---PDGNSNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 97 KIKNEIAKygnppvfpvideaaeaaaaaaaaaqkaadaknadptkfaakkskasakagtqtyqwdimKSSGIGDSEippf 176
Cdd:TIGR00422 92 KKLGAEGK-----------------------------------------------------------TKHDLGREE---- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 177 adpyhWLDYFPPLAKRDVAAMGCQARsishrspydRVGVvnAVDWRRSFTTTD---HNPFYDAFVRWQFNtlkkiGKVIK 253
Cdd:TIGR00422 109 -----FREKIWEWKEESGGTIKNQIK---------RLGA--SLDWSRERFTMDeglSKAVKEAFVRLYEK-----GLIYR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 254 AKRMAVYSPLDGQPCADHDRASGEGVGPQEYVlikmrVYdeclvgelaPLA-GKNVFLAAATLRPETMYGQTNCWILPDg 332
Cdd:TIGR00422 168 GEYLVNWDPKLNTAISDIEVEYKEVKGKLYYI-----RY---------PLAnGSKDYLVVATTRPETMFGDTAVAVHPE- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 333 dygafemangdvmvmcdraarnlsyQERTKaegdtgkilsfkgaALIGCAVKSPLAILEkiycLPMLT---ILMGKGTGV 409
Cdd:TIGR00422 233 -------------------------DERYK--------------HLIGKKVILPLTGRK----IPIIAdeyVDMEFGTGA 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 410 VTSVPSDSPDDFmalsdlkakkalrekfgvldEWV----LPFdvvpcvripefgdacapivceqlkIQSQNDKAKLEEAK 485
Cdd:TIGR00422 270 VKVTPAHDFNDY--------------------EWGkrhnLEF------------------------INILDEDGLLNENA 305
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 486 hrtylkgftdgvmlrGVYEGEPVKIVKPKI-RDLMLESgdAIVYSEPEKQ---VMSRSGDECVVALTDQWY--LEYGEEG 559
Cdd:TIGR00422 306 ---------------GKYQGLTRFEARKKIvEDLKEEG--LLVKIEPHTHnvgTCWRSGTVVEPLLSKQWFvkVEKLADK 368
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 560 WREKAEKCLagMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVP-W----DEQFLIESLSDSTIYMAYYTVAHLLQGg 634
Cdd:TIGR00422 369 ALEAAEEGE--IKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPvWyckeCGEVYVAKEEPLPDDKTNTGPSVELEQ- 445
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 635 dmygsaRPSVEPSAMTDEVWDAVFLGVPlpagsdfpkellkEMKTEFEFWYPFDLRVSGKDLIQNHLTFSIYNHVALwae 714
Cdd:TIGR00422 446 ------DTDVLDTWFSSSLWPFSTLGWP-------------DETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLAL--- 503
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 715 dESKWPrgFRT---NGhlLL---NNEKMSKSTGNFKTLKAAIEAYSSDAMRFALA-----------DAGDTIEDANFALK 777
Cdd:TIGR00422 504 -TGQVP--FKEvyiHG--LVrdeQGRKMSKSLGNVIDPLDVIEKYGADALRFTLAslvtpgddinfDWKRVESARNFLNK 578
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 778 C------------GYYDLQ-------------------------SARDAYRLQ--------------C------------ 794
Cdd:TIGR00422 579 LwnasrfvlmnlsDDLELSggeeklsladrwilsklnrtikevrKALDKYRFAeaakalyefiwndfCdwyielvkyrly 658
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 795 GGLGEEGNMHAELVKRFIEVSTLLLAPFCPHTCEHVWGALLGKPGTVTKAGFPTYVEP--DKALMAAARYLDDLVSSIRK 872
Cdd:TIGR00422 659 NGNEAEKKAARDTLYYVLDKALRLLHPFMPFITEEIWQHFKEGADSIMLQSYPVVDAEfvDEEAEKAFELLKEIIVSIRN 738
|
970
....*....|..
gi 303277431 873 GVAKATAPPKKK 884
Cdd:TIGR00422 739 LKAESNIPPNAP 750
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
687-762 |
3.87e-10 |
|
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: 60.67 E-value: 3.87e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303277431 687 FDLRVSGKDLIQNHLTFSIYNHVALWAEdesKWPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFAL 762
Cdd:cd00672 129 FDIHGGGVDLIFPHHENEIAQSEAATGK---PFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
726-813 |
1.02e-09 |
|
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: 62.04 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 726 NGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAG---------DTIEDAnfalKCGYYDLQSARDAYRLQCGG 796
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHyrspldfseEALEEA----EKALERLYNALRRLEEALGA 331
|
90
....*....|....*..
gi 303277431 797 LGEEGNMHAELVKRFIE 813
Cdd:COG0215 332 ADSSAEEIEELREEFIA 348
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
39-104 |
7.54e-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: 7.54e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303277431 39 KFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMPIKASADKIKNEIAK 104
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRKKK 66
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
550-774 |
9.19e-09 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 58.84 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 550 QWYLEyGEEGWREKAEkclagmrtyhdearkafEHTLGWLRQ----WACSRAFGLGTRVPWDEqflieslsDSTIYmayy 625
Cdd:pfam09334 197 EWIEE-NNPEWPENVK-----------------NMVLEWLKEglkdRAISRDLDWGIPVPGAE--------GKVFY---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 626 tvahllqggdmygsarpsvepsamtdeVW-DAV-----FLGVPLPAGSDFPKELLKEMKTEFefwYPFdlrvSGKDLIQN 699
Cdd:pfam09334 247 ---------------------------VWlDAPigyisATKELSGNEEKWKEWWPNDPDTEL---VHF----IGKDIIYF 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303277431 700 HltfSIYNHVALWAEDESKwPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAGDTIEDANF 774
Cdd:pfam09334 293 H---TIFWPAMLLGAGYRL-PTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDF 363
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
11-91 |
9.63e-09 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 59.44 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 11 ELQARAQKKWADEKTFevsAPKDGSKPPKFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMP 90
Cdd:PRK13208 14 ELEEKWQKIWEEEGTY---KFDPDERKPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLP 90
|
.
gi 303277431 91 I 91
Cdd:PRK13208 91 T 91
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
535-774 |
1.16e-08 |
|
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: 58.41 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 535 VMSRSGDECVVALTDQWYLEYGEEGwrEKAEKCL--AGMRTYHDEARKAFEHTLGWLRQWACSRAFGLGTRVP-Wdeqfl 611
Cdd:cd00817 155 VCSRSGDVIEPLLKPQWFVKVKDLA--KKALEAVkeGDIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIPaW----- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 612 iESLSDSTIYMAYYTVAHLLQGGDMYGSARPSVEPSAMTDeVWDAVFlgvplpAGSDFPKELLK--EMKTEFEFWYPFDL 689
Cdd:cd00817 228 -YCKDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDED-VLDTWF------SSSLWPFSTLGwpEETKDLKKFYPTSL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 690 RVSGKDLIqnhltFsiynhvaLWAedeskwprgFRT--NGHLLLNN-----------------EKMSKSTGNFKTLKAAI 750
Cdd:cd00817 300 LVTGHDII-----F-------FWV---------ARMimRGLKLTGKlpfkevylhglvrdedgRKMSKSLGNVIDPLDVI 358
|
250 260
....*....|....*....|....
gi 303277431 751 EAYSSDAMRFALADAGDTIEDANF 774
Cdd:cd00817 359 DGYGADALRFTLASAATQGRDINL 382
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
693-777 |
2.10e-08 |
|
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: 58.20 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 693 GKDLIQNHltfSIYnhvalwaedeskWP-----RGFRT------NGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFA 761
Cdd:COG0143 289 GKDIIRFH---AII------------WPamlmaAGLPLpkkvfaHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYY 353
|
90
....*....|....*.
gi 303277431 762 LADAGDTIEDANFALK 777
Cdd:COG0143 354 LLREVPFGQDGDFSWE 369
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
685-765 |
3.35e-08 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 56.22 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 685 YPFDLRVSGKDLIQNHLTFSIYNHVALWaedESKWPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALAD 764
Cdd:pfam01406 206 DQIDIHGGGIDLAFPHHENEIAQSEAAF---DKQLANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLS 282
|
.
gi 303277431 765 A 765
Cdd:pfam01406 283 V 283
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
744-872 |
1.31e-07 |
|
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: 51.64 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 744 KTLKAAIEAYssDAMRFAlaDAGDTIEDanFALK--CGYYdLQSARDayRLQCGglgEEGNMHAELVKRFIEVSTLLLAP 821
Cdd:pfam08264 10 KLIKEVTEAY--ENYRFN--TAAQALYE--FFWNdlSDWY-LELIKD--RLYGE---EPDSRAQTTLYEVLETLLRLLAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 303277431 822 FCPHTCEHVWgallgKPGTVTKAGFP-TYVEPDKALMAAARYLDDLVSSIRK 872
Cdd:pfam08264 78 FMPFITEELW-----QKESIHLAPWPeDAELEEAELEEAFELRQEIVQAIRK 124
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
585-774 |
4.79e-07 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 52.92 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 585 TLGWLRQ----WACSR-AFGLGTRVPWDEqflieslsDSTIYmayytvahllqggdmygsarpsvepsamtdeVW-DAVF 658
Cdd:cd00814 171 VLSWLKEglkdLSITRdLFDWGIPVPLDP--------GKVIY-------------------------------VWfDALI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 659 --LGvplpagsdFPKELLKEMKTEFEFWYPF--DLRVSGKDLIQNHltfSIYnhvalwaedeskWP-----RGFRT---- 725
Cdd:cd00814 212 gyIS--------ATGYYNEEWGNSWWWKDGWpeLVHFIGKDIIRFH---AIY------------WPamllgAGLPLptri 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 303277431 726 --NGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADAGDTIEDANF 774
Cdd:cd00814 269 vaHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
11-90 |
1.65e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 52.52 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 11 ELQARAQKKWADEKTFEVSAPKDGSKPPKF-FGNFPYPYMNGmLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGM 89
Cdd:PLN02563 84 EIEPKWQRYWEENRTFRTPDDVDTSKPKFYvLDMFPYPSGAG-LHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGL 162
|
.
gi 303277431 90 P 90
Cdd:PLN02563 163 P 163
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
681-879 |
3.12e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 51.35 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 681 FEFWYPFDLRVSGKDLIQNHLTFSIYNHVALwaEDESKWpRGFRTNGHLL-LNNEKMSKSTGNFKTLKAAIEAYSSDAMR 759
Cdd:PRK13208 481 FEKVFPMDLRPQGHDIIRTWLFYTILRAYLL--TGKLPW-KNIMISGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVR 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 760 FALADA--GDTI---ED---------------ANFALKCGY----------------------------------YDLQS 785
Cdd:PRK13208 558 YWAASArlGSDTpfdEKqvkigrrlltklwnaSRFVLHFSAdpepdkaevlepldrwilaklakvvekatealenYDFAK 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 786 ARDA------------------YRLQcGGLGEEGNMHAELVKRF-IEVSTLLLAPFCPHTCEHVWGALLGkpGTVTKAGF 846
Cdd:PRK13208 638 ALEEiesffwhvfcddylelvkSRAY-GEDEEEEQKSARYTLYTvLDTLLRLLAPFLPFITEEVWSWLYG--GSVHRASW 714
|
250 260 270
....*....|....*....|....*....|....*
gi 303277431 847 PTYVEP--DKALMAAARYLDDLVSSIRKgvAKATA 879
Cdd:PRK13208 715 PEPDEEliDEEDEELGELAKEILSAVRK--YKSEA 747
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
45-90 |
5.80e-06 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 49.94 E-value: 5.80e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 303277431 45 PYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFPFAFHCTGMP 90
Cdd:cd00817 8 PPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA 53
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
693-777 |
6.32e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 50.15 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 693 GKDLIQNHLTFsiynhvalwaedeskWP-----RGFRT------NGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFA 761
Cdd:PRK00133 291 GKDIIYFHTLF---------------WPamlegAGYRLptnvfaHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYY 355
|
90
....*....|....*..
gi 303277431 762 LA-DAGDTIEDANFALK 777
Cdd:PRK00133 356 LAaKLPETIDDLDFNWE 372
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
685-760 |
1.08e-05 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 49.64 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 685 YPFDLRVSGKDLI----QNHLTFS-IYNhvalwaeDESKWPRGFRTNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMR 759
Cdd:PTZ00399 267 DPIDIHSGGIDLKfphhDNELAQSeAYF-------DKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIR 339
|
.
gi 303277431 760 F 760
Cdd:PTZ00399 340 L 340
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
520-777 |
7.23e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 46.86 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 520 LESGDAIVYSEPEKQVMSRS--GDECVVAL-TDQWYLEYgeEGWREKAEKCLAG--MRTYHDEARKAFEHTLGWLRQWAC 594
Cdd:PLN02943 376 LEETGLAVKKEPHTLRVPRSqrGGEVIEPLvSKQWFVTM--EPLAEKALKAVENgeLTIIPERFEKIYNHWLSNIKDWCI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 595 SRAFGLGTRVP-W-------DEQFLIESLSDSTiymayYTVAHLLQGGDMYGSARPSVEPSAMTDEVWDAVFLGVPLPAG 666
Cdd:PLN02943 454 SRQLWWGHRIPvWyivgkdcEEDYIVARSAEEA-----LEKAREKYGKDVEIYQDPDVLDTWFSSALWPFSTLGWPDVSA 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 667 SDFPKellkemktefefWYPFDLRVSGKDLiqnhLTFSIYNHVALWAEDESKWPRGFRTNGHLLLNNE--KMSKSTGNFK 744
Cdd:PLN02943 529 EDFKK------------FYPTTVLETGHDI----LFFWVARMVMMGIEFTGTVPFSYVYLHGLIRDSQgrKMSKTLGNVI 592
|
250 260 270
....*....|....*....|....*....|...
gi 303277431 745 TLKAAIEAYSSDAMRFALAdAGDTIEDANFALK 777
Cdd:PLN02943 593 DPLDTIKEFGTDALRFTLA-LGTAGQDLNLSTE 624
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
685-788 |
9.22e-05 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 46.46 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 685 YPFDLRVSGKDLIQNHLTFSIYNHVALWAEDE-SKWPRgfrtNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFAL- 762
Cdd:PLN02946 276 HSFDIHGGGMDLVFPHHENEIAQSCAACCDSNiSYWIH----NGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLl 351
|
90 100 110
....*....|....*....|....*....|.
gi 303277431 763 -----ADAGDTIEDANFALKCGYYDLQSARD 788
Cdd:PLN02946 352 gthyrSPINYSDVQLESASERIFYIYQTLHD 382
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
797-834 |
5.18e-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: 40.67 E-value: 5.18e-04
10 20 30
....*....|....*....|....*....|....*...
gi 303277431 797 LGEEGNMHAELVKRFIEVSTLLLAPFCPHTCEHVWGAL 834
Cdd:cd07958 80 YKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
17-91 |
9.55e-04 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 43.22 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 17 QKKWADEKTFE-VSAPKDGskppkffGNF-----PyPYMNGMLHLGHAfsLSKL--EFASAYHRLKGDETLFPFAFHCTG 88
Cdd:PLN02843 13 QKLWEENQVYKrVSDRNNG-------ESFtlhdgP-PYANGDLHIGHA--LNKIlkDFINRYQLLQGKKVHYVPGWDCHG 82
|
...
gi 303277431 89 MPI 91
Cdd:PLN02843 83 LPI 85
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
20-80 |
2.19e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 42.30 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303277431 20 WADEKTFE-VSAPKDGSKPPKFFGNFPYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLF 80
Cdd:PTZ00419 41 WEKSGFFKpAEDAKSLNSGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLW 102
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
45-97 |
3.46e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 41.12 E-value: 3.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 303277431 45 PYPYMNGMLHLGHAFSLSKLEFASAYHRLKGDETLFpfafhCTGM-----PIKASADK 97
Cdd:pfam09334 6 ALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLF-----VCGTdehgtPIELKAEK 58
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
653-762 |
3.62e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 41.32 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 653 VW-DAVF-----LGVPLPAGSDFPKellkemktefeFWyPFDLRVSGKDLIQNHltfSIYnhvalwaedeskWP------ 720
Cdd:PRK12267 227 VWiDALLnyitaLGYGSDDDELFKK-----------FW-PADVHLVGKDILRFH---AIY------------WPimlmal 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 303277431 721 -----RGFRTNGHLLLNNEKMSKSTGNF---KTLkaaIEAYSSDAMRFAL 762
Cdd:PRK12267 280 glplpKKVFAHGWWLMKDGKMSKSKGNVvdpEEL---VDRYGLDALRYYL 326
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
698-765 |
3.94e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 41.24 E-value: 3.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303277431 698 QNHLTFSIYNHVALWAEdeskwprgfrtNGHLLLNNEKMSKSTGNFKTLKAAIEAYSSDAMRFALADA 765
Cdd:PRK14535 482 QTHHGQSIASHVKYWLH-----------NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 538
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
812-877 |
6.76e-03 |
|
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: 40.45 E-value: 6.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303277431 812 IEVSTLLLAPFCPHTCEHVWGAL-LGKPGTVTKAGFPTYVEP--DKAL---MAAARyldDLVSSIRKGVAKA 877
Cdd:COG0060 757 LETLVRLLAPILPFTAEEIWQNLpGEAEESVHLADWPEVDEEliDEELeakWDLVR---EVRSAVLKALEAA 825
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
683-763 |
8.25e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 39.87 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303277431 683 FWyPFDLRVSGKDLIQNHltfSIYnhvalW-----AEDESKwPRGFRTNGHLLLNNEKMSKSTGNfkTL--KAAIEAYSS 755
Cdd:PRK11893 252 YW-PADVHLIGKDILRFH---AVY-----WpaflmAAGLPL-PKRVFAHGFLTLDGEKMSKSLGN--VIdpFDLVDEYGV 319
|
....*...
gi 303277431 756 DAMRFALA 763
Cdd:PRK11893 320 DAVRYFLL 327
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
17-58 |
8.79e-03 |
|
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: 40.06 E-value: 8.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 303277431 17 QKKWADEKTFE--VSAPKDGskpPKFF---GnfPyPYMNGMLHLGHA 58
Cdd:COG0060 26 LKFWEENDIYEksREARAGR---PKFVlhdG--P-PYANGDIHIGHA 66
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
45-89 |
9.48e-03 |
|
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: 39.44 E-value: 9.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 303277431 45 PYPYMNGMLHLGHAFS--LSKLeFASaYHRLKGDETLFpfafhCTGM 89
Cdd:cd00814 7 ALPYVNGVPHLGHLYGtvLADV-FAR-YQRLRGYDVLF-----VTGT 46
|
|
| |
