|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
3-1086 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 2267.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 3 TNPDEPKSRARTDFLLNNELEVQKFWDENKVFQADPGNDSPSPGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRL 82
Cdd:PLN02959 1 MMAEGGKSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPKPGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 83 RGSNVLLPFAFHCTGMPIKASADKLAREIQQYGYPPVFPVA-EGSSAAVADATQADQVDVVAPDKFKGKKSKATAKAGAQ 161
Cdd:PLN02959 81 RGANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEdEDEAAAVAAAKAEAEAAAAPPDKFKGKKSKAVAKSGTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 162 KYQWEIMKSFGLDDEEIARFQDPYHWLTHFPPLAKEVLKKFGLGCDWRRSFITTDMNPYYDAFVKWQMRKLKKLGKVVKD 241
Cdd:PLN02959 161 KYQWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTDVNPYYDAFVRWQFRKLKKKGKIVKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 242 MRYTIYSPLDGQPCADHDRATGEGVQPQEYVLIKMEVISPFPPKLKSLEGRKVYLAAATLRPETMYGQTNCWVLPDGMYG 321
Cdd:PLN02959 241 KRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPPFPGKLKALEGKKVFLAAATLRPETMYGQTNCWVLPDGKYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 322 AFEINDTDVFILTARSAFNLAYQHLSRVPEKPTCLCELSGSDLIGLPLKSPLAFNETIYALPMLTVLTDKGTGIVTSVPS 401
Cdd:PLN02959 321 AYEINDTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSVPS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 402 DSPDDFMALQDLVTKPALRAKYGVKDEWVLPYEIIPIIHIPEFGDKSAEKVCHDLKIKSQNDKEKLAEAKRMTYLKGFTD 481
Cdd:PLN02959 401 DSPDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGFTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 482 GTMIVGEFSGRKVQEAKPLIKSKLLEEGTAVLYSEPEKKVMSRSGDECVVALTDQWYITYGEAEWKQKAVKCLDHMNTFS 561
Cdd:PLN02959 481 GTMLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNLYS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 562 TETRNGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLVESLSDSTLYMAYYTVAHLLQNGNMYGKEISSVRPEEMTDEVWD 641
Cdd:PLN02959 561 DETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGKDKSSIKPEQMTDEVWD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 642 FVFCDGPAPK-SEIPAALLNKMKHEFKYWYPFDIRVSGKDLIQNHLTFCIYNHTALLPEHHWPIGFRCNGHLMLNSEKMS 720
Cdd:PLN02959 641 FVFCGGPLPKsSDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAEEHWPRGFRCNGHLMLNSEKMS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 721 KSTGNFLTLEDAIKKYSSDATRFALADAGDGMDDANFVTETANSAVMRLTKEISWMEEVTAAESKLRTGPPTTYADRVFS 800
Cdd:PLN02959 721 KSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLTKEIAWMEEVLAAESSLRTGPPSTYADRVFE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 801 NEMNIAIKETEKSYNAFMFRDALKSGFYDLQLARDEYRLSCGAAGMNRDLLWRFMDVQTRLITPICPHYAEHVWQKIMKK 880
Cdd:PLN02959 801 NEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRLSCGSGGMNRDLVWRFMDVQTRLITPICPHYAEHVWREILKK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 881 EGFAIKAGWPAADTPDPTLRIANKYLQDSIVLMRKLLQKQESGSKKPKKGAAPAPPseEKKMSIGLIYVNEHYSGWKEQC 960
Cdd:PLN02959 881 EGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKGGAPVTL--PEKKLAGLIYVAEKYDGWKEEC 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 961 LKVLQSKFDSQSRSFSPDQEIAEALKECPIGQEMNLKQVQKLCMPFIKLKKDEAREVGPQALDLKLPFGEMDVLRENLEL 1040
Cdd:PLN02959 959 LRILQSKFDSQSRTFAPDAEILEALKESSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQALDLKLPFDEIEVLQENLEL 1038
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 1162454698 1041 IKRQLGLEQVEVLSASDEAARAKAGEHASLLEKNPPSPGDPIAIFL 1086
Cdd:PLN02959 1039 IKRQLGLEEVEILSASDPDAVAKAGAHASLLKQNPPSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
25-1063 |
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: 786.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 25 QKFWDENKVFQADPGNDspspgEKFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPIKASA 104
Cdd:TIGR00395 8 QKRWEEAHIFEADPDDR-----EKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVTGTPILGLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 105 DKLAREiqqygyppvfpvaegssaavadatqadqvdvvapdkfkgkkskatakagAQKYQWEIMKSFGLDDEEIARFQDP 184
Cdd:TIGR00395 83 ELIKRR-------------------------------------------------DELTIKNYTEVHAIPREELLKFTDP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 185 YHWLTHFPPLAKEVLKKFGLGCDWRRSFITTDmnPYYDAFVKWQMRKLKKLGKVVKDMRYTIYSPLDGQPCADHDRATGE 264
Cdd:TIGR00395 114 EYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDHDLLSGE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 265 GVQPQEYVLIKMEvispfppklksLEGRKVYLAAATLRPETMYGQTNCWVLPDGMYGAFEINDTDvFILTARSAFNLAYQ 344
Cdd:TIGR00395 192 GVTIVEYILIKFE-----------LEDGAFYFVAATLRPETVYGVTNCWVNPTITYVIAEVGGEK-WITSKEAFENLSYQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 345 HLSRVPekptcLCELSGSDLIGLPLKSPLAFNEtIYALPMLTVLTDKGTGIVTSVPSDSPDDFMALQDLVTKPALrakYG 424
Cdd:TIGR00395 260 KLKYKP-----IEEVPGKQFIGKKVHNPVVGPE-VPILPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDPEY---LG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 425 VKDEWVlPYEIIPIIHIPEFGDKSAEKVCHDLKIKSQNDKEKLAEAKRMTYLKGFTDGTMIVG--EFSGRKVQEAKPLIK 502
Cdd:TIGR00395 331 IKPVVI-DIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIYNipPYKGMKVSEAKEKVK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 503 SKLLEEGTAVLYSEP-EKKVMSRSGDECVV-ALTDQWYITYGEAEWKQKAVKCLDHMNTFSTETRNGFEHTLGWLNQWAC 580
Cdd:TIGR00395 410 ADLIDAGLADVMYEFsESPVICRCGTDCIVkVVEDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDWLKDWAC 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 581 SRSFGLGTRIPWDEQFLVESLSDSTLYMAYYTVAHLLQNGNmygkeissVRPEEMTDEVWDFVFC-DGPAPKSEIPAALL 659
Cdd:TIGR00395 490 CRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDY--------YGNEQMTDEFFDYIFLgKGDVKNTNIPLPAI 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 660 NKMKHEFKYWYPFDIRVSGKDLIQNHLTFCIYNHTALLPEHHWPIGFRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSD 739
Cdd:TIGR00395 562 QKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPEKFWPRGIVVNGYVMLEGKKMSKSKGNVLTLEQAVEKFGAD 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 740 ATRFALADAGDGMDDANFVTETANSAVMRLTKEISWMEEVTaAESKLRTGPPTTYADRVFSNEMNIAIKETEKSYNAFMF 819
Cdd:TIGR00395 642 VARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEEIT-KESNLETGEETSFIDRWLESRMNAAIKETYEAMENFQT 720
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 820 RDALKSGFYDLQLARDEYRLSCGaaGMNRDLLWRFMDVQTRLITPICPHYAEHVWQkIMKKEGFAIKAGWPAADTP--DP 897
Cdd:TIGR00395 721 RKAVKYALFDLQADVDWYRRRGG--VNHKDVLARYLETWIKLLAPFAPHFAEEMWE-EVGNEGFVSLAKFPEASEPavDK 797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 898 TLRIANKYLQDsivLMRKLLQKQESGSKKPKKGAapappseekkmsiglIYVNEHysgWKEQCLKVLQSKFDSQsrsfsp 977
Cdd:TIGR00395 798 EVEAAEEYLRN---LVRDIQEIAKIDASKPKRVY---------------LYTSED---WKSQCLKIVAELFGED------ 850
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 978 dqeIAEALKecpigQEMNLKQVQKLCMPFIKLKKDEAREVGPQALDLklpFGEMDVLRENLELIKRQLGLEQVEVLSASD 1057
Cdd:TIGR00395 851 ---TGEDMK-----KVMEEPEERKRGKEVISLVKQIIKDEKKEDELQ---ISEIEVLKAAARFIKKEVGALVIIEFSADS 919
|
....*.
gi 1162454698 1058 EAARAK 1063
Cdd:TIGR00395 920 FPENKK 925
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
62-1086 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 687.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 62 LHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPIKASADKLAReiqqygyppvfpvaegssaavadatqadqvdv 141
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 142 vapdkfkgkkskatakaGAQKYQWEIMKSFGLDDEEIARFQDPYHWLTHFPPLAKEVLKKFGLGCDWRRSFITTDmnPYY 221
Cdd:PRK12300 49 -----------------GDPETIELYKSLYGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--PEY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 222 DAFVKWQMRKLKKLGKVVKDMRYTIYSPLDGQPCADHDRATGEGVQPQEYVLIKMEvispfppklkslEGRKVYLAAATL 301
Cdd:PRK12300 110 SKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFE------------ESEDLILPAATL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 302 RPETMYGQTNCWVLPDGMYGAFEINDtDVFILTARSAFNLAYQHLSRVPEKptclcELSGSDLIGLPLKSPLAfNETIYA 381
Cdd:PRK12300 178 RPETIFGVTNLWVNPDATYVKAEVDG-EKWIVSKEAAEKLSFQDRDVEIIE-----EIKGSELIGKKVKNPVT-GKEVPI 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 382 LPMLTVLTDKGTGIVTSVPSDSPDDFMALQDLVTKPALRAKYG----VKDEwvlpyeiipiihipEFGDKSAEKVCHDLK 457
Cdd:PRK12300 251 LPADFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNKELLDVIEpiplIEVE--------------GYGEFPAKEVVEKLG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 458 IKSQNDkEKLAEAKRMTYLKGFTDGTMI--VGEFSGRKVQEAKPLIKSKLLEEGTA-VLYSEPEKKVMSRSGDECVVA-L 533
Cdd:PRK12300 317 IKSQED-PELEEATKEVYRAEFHKGVLKenTGEYAGKPVREAREKITKDLIEKGIAdIMYEFSNRPVYCRCGTECVVKvV 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 534 TDQWYITYGEAEWKQKAVKCLDHMNTFSTETRNGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLVESLSDSTLYMAYYTV 613
Cdd:PRK12300 396 KDQWFIDYSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTI 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 614 AHLLQNGNMygkeissvRPEEMTDEVWDFVF-----CDGPAPKSEIPAALLNKMKHEFKYWYPFDIRVSGKDLIQNHLTF 688
Cdd:PRK12300 476 AHKIREYGI--------KPEQLTPEFFDYVFlgkgdPEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTF 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 689 CIYNHTALLPEHHWPIGFRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALADAGDGMDDANFVTETANSAVMR 768
Cdd:PRK12300 548 FIFNHVAIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQ 627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 769 LTKEISWMEEVTAAESKlrtgPPTTYADRVFSNEMNIAIKETEKSYNAFMFRDALKSGFYDLQLARDEYRLSCGAAgmNR 848
Cdd:PRK12300 628 LERFYELAKELIEIGGE----EELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRRVGEA--NN 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 849 DLLWRFMDVQTRLITPICPHYAEHVWQKiMKKEGFAIKAGWPAAD--TPDPTLRIANKYLQDSIVLMRKLLQKqesGSKK 926
Cdd:PRK12300 702 KVLREVLEIWIRLLAPFTPHLAEELWHK-LGGEGFVSLEKWPEPDesKIDEEAELAEEYVKRLIEDIREILKV---AKIK 777
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 927 PKKgaapappseekkmsiGLIYVNEhysGWKEQCLKVLQSKFDSQS--RSFSPDQEIAEALKECPigqemnlKQVQKLCM 1004
Cdd:PRK12300 778 PKK---------------VYIYVAP---DWKYEVLEIAAENGDVKEaiKELMKDEELRKHGKEVA-------KLAQKIVK 832
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 1005 PFIKLKKDEARevgpqalDLKLPFGEMDVLRENLELIKRQLGLEqVEVLSASDEAARAKAGEhaslleknpPSPGDPiAI 1084
Cdd:PRK12300 833 EVLKLDKEVRK-------LILKNIDEEEVLEEAKDFLEKELGVE-VEIYGADDPGKKKKKKK---------ALPLKP-AI 894
|
..
gi 1162454698 1085 FL 1086
Cdd:PRK12300 895 YI 896
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
532-758 |
2.18e-70 |
|
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: 237.53 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 532 ALTDQWYITYGEAEWKQKAVKCLDHMNTFSTETRNGFEHTLGwlnqwaCSRSFGLGTRIPWdeQFLVESLSDSTLYMAYY 611
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 612 TVAHLLQNGNMYgkeissvrpeemtdevwdfvfcdgpapkseipaaLLNKMKHEFKYWYPFDIRVSGKDLIQNHLTFCIY 691
Cdd:cd00812 199 TDAHNLEQPYEG----------------------------------DLEFDREEFEYWYPVDIYIGGKEHAPNHLLYSRF 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162454698 692 NHTALLPE----HHWPIGFRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALADAGDgmDDANFV 758
Cdd:cd00812 245 NHKALFDEglvtDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFD 313
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
757-877 |
2.48e-44 |
|
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: 155.83 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 757 FVTETANSAVMRLTKEISWMEEVTAAESKLrtgPPTTYADRVFSNEMNIAIKETEKSYNAFMFRDALKSGFYDLQLARDE 836
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1162454698 837 YRLSCGaAGMNRDLLWRFMDVQTRLITPICPHYAEHVWQKI 877
Cdd:cd07959 78 YRERGG-AGMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
19-929 |
1.92e-31 |
|
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: 133.26 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 19 NNELEVQKFWDENKVFQADPGndspSPGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGM 98
Cdd:TIGR00422 9 EVEKKWYKKWEKSGFFKPDGN----SNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 99 pikasadklareiqqygyppvfpvaegssaavadATQAdqvdVVapDKFKGKKSKATAKAGAQKYQWEIMKsfgLDDEEI 178
Cdd:TIGR00422 85 ----------------------------------ATQV----KV--EKKLGAEGKTKHDLGREEFREKIWE---WKEESG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 179 ARFqdpyhwlthfpplaKEVLKKFGLGCDWRRSFITTD---MNPYYDAFVKWqmrklkklgkVVKDMRYTIYSPLDGQPC 255
Cdd:TIGR00422 122 GTI--------------KNQIKRLGASLDWSRERFTMDeglSKAVKEAFVRL----------YEKGLIYRGEYLVNWDPK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 256 ADHDRATGEgVQPQEyVLIKMEVIspfppKLKSLEGRKVYLAAATLRPETMYGQTNCWVLPDgmygafeindtdvfilta 335
Cdd:TIGR00422 178 LNTAISDIE-VEYKE-VKGKLYYI-----RYPLANGSKDYLVVATTRPETMFGDTAVAVHPE------------------ 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 336 rsafNLAYQHLsrvpekptclcelsgsdlIGLPLKSPLaFNETIyalPMLT---VLTDKGTGIVTSVPSDSPDDFmalqd 412
Cdd:TIGR00422 233 ----DERYKHL------------------IGKKVILPL-TGRKI---PIIAdeyVDMEFGTGAVKVTPAHDFNDY----- 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 413 lvtkpalrakygvkdEWvlpyeiipiihipefGDKsaekvcHDLKIKSQNDKeklaeakrmtylkgftDGTM--IVGEFS 490
Cdd:TIGR00422 282 ---------------EW---------------GKR------HNLEFINILDE----------------DGLLneNAGKYQ 309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 491 GRKVQEAKPLIKSKLLEEGTAVLYSEPEKKV--MSRSGDECVVALTDQWYITYgeAEWKQKAVKCLD---------HMNt 559
Cdd:TIGR00422 310 GLTRFEARKKIVEDLKEEGLLVKIEPHTHNVgtCWRSGTVVEPLLSKQWFVKV--EKLADKALEAAEegeikfvpkRME- 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 560 fstetrNGFEHTLGWLNQWACSRSFGLGTRIP-WdeqFLVEslsDSTLYMAYYTVAHLLQNGNMYGKEIssvRPEE---- 634
Cdd:TIGR00422 387 ------KRYLNWLRNIKDWCISRQLIWGHRIPvW---YCKE---CGEVYVAKEEPLPDDKTNTGPSVEL---EQDTdvld 451
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 635 --MTDEVWDFVFCDGPapkseipaallnKMKHEFKYWYPFDIRVSGKDLIQNHLTFCIYNHTALLPEhhwpIGFR---CN 709
Cdd:TIGR00422 452 twFSSSLWPFSTLGWP------------DETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQ----VPFKevyIH 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 710 GhlMLNSE---KMSKSTGNFLTLEDAIKKYSSDATRFALADAGDGMDDANFVTETANSA---------VMRLT-KEISWM 776
Cdd:TIGR00422 516 G--LVRDEqgrKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESArnflnklwnASRFVlMNLSDD 593
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 777 EEVTAAESKLRTgppttyADRVFSNEMNIAIKETEKSYNAFMFRDALKS-------GFYDLQLARDEYRLSCGAAG---M 846
Cdd:TIGR00422 594 LELSGGEEKLSL------ADRWILSKLNRTIKEVRKALDKYRFAEAAKAlyefiwnDFCDWYIELVKYRLYNGNEAekkA 667
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 847 NRDLLWRFMDVQTRLITPICPHYAEHVWQKIMKKEGFAIKAGWPAADTP--DPTLRIANKYLQDSIVLMRKLlqKQESGS 924
Cdd:TIGR00422 668 ARDTLYYVLDKALRLLHPFMPFITEEIWQHFKEGADSIMLQSYPVVDAEfvDEEAEKAFELLKEIIVSIRNL--KAESNI 745
|
....*
gi 1162454698 925 KKPKK 929
Cdd:TIGR00422 746 PPNAP 750
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
48-210 |
1.39e-28 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 117.35 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 48 KFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPIKASADKLAREIQQYgyppvfpvaegss 127
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 128 aavadatqadqvdvvapDKFKGKKSKATAKAGAQKYQWEIMksFGLDDEEIARFQdpyHWLTHFPPLaKEVLKKFGLGCD 207
Cdd:cd00812 68 -----------------TEYNIKKMKEQLKRMGFSYDWRRE--FTTCDPEYYKFT---QWLFLKLYE-KGLAYKKEAPVN 124
|
...
gi 1162454698 208 WRR 210
Cdd:cd00812 125 WCK 127
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
453-757 |
1.42e-27 |
|
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: 114.44 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 453 CHDLKIKSQNDKEKLAEAKRMTYLKGFTDGTMIVGEFSGRKVQEAKPLIKSKLLEEGTAVLYSEPEKKV------MSRSG 526
Cdd:cd00668 48 THGLPIELKAERKGGRKKKTIWIEEFREDPKEFVEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVelifsrLYEKG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 527 ----DECVVALTDQWYITYGEaeWKQKAVKCLDHMNTFSTETRNGFEHTLGWLNQWACSRSFGLGTRIPWDeqfLVESLS 602
Cdd:cd00668 128 liyrGTHPVRITEQWFFDMPK--FKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLPED---VFDVWF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 603 DSTLYMAYYTVAhllqngnmygkeissvrPEEmtdevwdfvfcdgpapkseipaallnkmKHEFKYWYPFDIRVSGKDLI 682
Cdd:cd00668 203 DSGIGPLGSLGY-----------------PEE----------------------------KEWFKDSYPADWHLIGKDIL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162454698 683 QNHLTFCIYNHTALLPEhHWPIGFRCNGHLMLN-SEKMSKSTGNFLTLEDAIKKYSSDATRFALADAGDGMDDANF 757
Cdd:cd00668 238 RGWANFWITMLVALFGE-IPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
24-757 |
9.30e-26 |
|
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: 113.66 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 24 VQKFWDENKVFQADPGNDSPSPgeKFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPIKAS 103
Cdd:pfam00133 2 IYEFWDEQGYFKPELEKRKGKP--SFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 104 ADKlareiqqygyppvfpvaegssaavadatqadqvdvvapdKFKGKKSKATAKAGAQKYQ---WEIMksfglddEEIAR 180
Cdd:pfam00133 80 VEK---------------------------------------KLGIKEKKTRHKYGREEFRekcREWK-------MEYAD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 181 FQdpyhwlthfpplaKEVLKKFGLGCDWRRSFITtdMNPYYDAFVKWQMRKLKKLGKVVKDMRYTIYSPLDGQPCADHDR 260
Cdd:pfam00133 114 EI-------------RKQFRRLGRSIDWDREYFT--MDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 261 ATGEGVQPQEYVlikmevisPFPPKlkslEGRKVYLAAATLRPETMYGQTNCWVLPDGMYGafeINDTDVFILTARSafn 340
Cdd:pfam00133 179 EYKDVKGPSIHV--------AFPLA----DDEGASLVIWTTTPWTLPGNTAVAVNPEFDYV---ITGEGYILAEALL--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 341 layQHLSRVPEKPTCLCELSGSDLIGLPLKSPlaFNETiyALPMLT---VLTDKGTGIVTSVPSDSPDDFMALQdlvtkp 417
Cdd:pfam00133 241 ---KSLYKKGTDKKILEDFRGKELEGKEAIHP--FVNR--EIPIITddyVDMEFGTGAVHIAPAHGENDYEVGQ------ 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 418 alraKYGVkdEWVLPyeiipiihipefgdksaekvchdlkiksqndkeklaeakrMTYLKGFTDGtmiVGEFSGRKVQEA 497
Cdd:pfam00133 308 ----RHNL--EVINP----------------------------------------VDDDGTFTEE---APDFQGVYRFDA 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 498 KPLIkSKLLEEGTAVLYSEPEKkvMS-----RSGDECVVALTDQWYITYgeAEWKQKAVKCLDHMNTFSTETRNGFEHTL 572
Cdd:pfam00133 339 RKKI-VELLTEKGLLLKIEPFT--HSypfcwRSGTPIIPRATPQWFVRM--DELADQALEAVEKVQFVPKSGEKRYFNWL 413
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 573 GWLNQWACSRSFGLGTRIP-W-DEQFLVESLSDSTLYMAYYTVAHLLQNGNMYGKEISSVRPEEMT----DEVWDFVFCD 646
Cdd:pfam00133 414 ANIQDWCISRQRWWGHPIPaWvSKDTEEVVCRGELFELVAGRFEEEGSIKWLHREAKDKLGYGKGTleqdEDVLDTWFSS 493
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 647 GPAPKSEIPAALLNkmKHEFKYWYPFDIRVSGKDLIQNHLTFCIYNHTALLPEHhwPigFR---CNGhLMLNSE--KMSK 721
Cdd:pfam00133 494 GSWPFSTLGWPFVN--TEEFKKFFPADMLLEGSDQTRGWFYRMIMLSTALTGSV--P--FKnvlVHG-LVRDEQgrKMSK 566
|
730 740 750
....*....|....*....|....*....|....*.
gi 1162454698 722 STGNFLTLEDAIKKYSSDATRFALADAgDGMDDANF 757
Cdd:pfam00133 567 SLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
20-893 |
8.00e-17 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 85.63 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 20 NELEVQKFWDENKVFQADPGNDSPSpgekFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMP 99
Cdd:PRK13208 15 LEEKWQKIWEEEGTYKFDPDERKPV----YSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 100 IKasadklaREIQ-QYGYPPvfpvaegssaavadatqadqvDVVAPDKFKGKKSKATakagaqkyqweimksfgldDEEI 178
Cdd:PRK13208 91 TE-------RKVEkYYGIRK---------------------DDISREEFIELCRELT-------------------DEDE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 179 ARFqdpyhwlthfpplaKEVLKKFGLGCDWRRSFITtdMNPYY-----DAFVK-WQMrklkklgkvvkDMRY-----TIY 247
Cdd:PRK13208 124 KKF--------------RELWRRLGLSVDWSLEYQT--ISPEYrrisqKSFLDlYKK-----------GLIYraeapVLW 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 248 SPLDGQPCA-----DHDRATgegvqpqEYVLIKmevispFPPKlkslEGRKVYLAaaTLRPETMYGqtnC---WVLPDgm 319
Cdd:PRK13208 177 CPRCETAIAqaeveYREREG-------KLNYIK------FPVE----DGEEIEIA--TTRPELLPA---CvavVVHPD-- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 320 ygafeindtDvfiltARsafnlaYQHLsrvpekptclcelsgsdlIGLPLKSPLaFNETIYALPMLTVLTDKGTGIV--- 396
Cdd:PRK13208 233 ---------D-----ER------YKHL------------------VGKTAIVPL-FGVEVPILADPLVDPDFGTGAVmic 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 397 TsvpsdspddFMALQDLvtkpalrakygvkdEWVLPyeiipiihipefgdksaekvcHDLKIKSQNDKeklaeakrmtyl 476
Cdd:PRK13208 274 T---------FGDKTDV--------------TWWRE---------------------LNLPTRIIIDE------------ 297
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 477 kgftDGTM--IVGEFSGRKVQEAKPLIKSKLLEEGtaVLYsEPEK-----KVMSRSGD--ECVValTDQWYITYgeAEWK 547
Cdd:PRK13208 298 ----DGRMteAAGKLAGLTIEEARKKIVEDLKSGG--LLG-KQEPikhnvKFCERCDTplEILV--TRQWFIKV--LDLK 366
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 548 QKAVKCLDHMNtFSTET-RNGFEHtlgWLNQ----WACSRSFGLGTRIP-W------------DEQFLVESLSDStlyMA 609
Cdd:PRK13208 367 EELLERGKEIN-WYPEHmRVRLEN---WIEGlnwdWCISRQRYFGTPIPvWyckdcghpilpdEEDLPVDPTKDE---PP 439
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 610 YYTVAHLLQNGNMYGKEI------SSVRPEEMTDEVWDfvfcdgpapkseipaallnkmKHEFKYWYPFDIRVSGKDLIQ 683
Cdd:PRK13208 440 GYKCPQCGSPGFEGETDVmdtwatSSITPLIVTGWERD---------------------EDLFEKVFPMDLRPQGHDIIR 498
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 684 NHLTFCI---YNHTALLPEHHWPIgfrcNGH-LMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALADAGDGMDDA---- 755
Cdd:PRK13208 499 TWLFYTIlraYLLTGKLPWKNIMI----SGMvLDPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASARLGSDTPfdek 574
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 756 ------NFVTETANSAvmrltKEISWMEEVTAAESKlrtgPPTTYADRVFSNEMNIAIKETEKSYNAFMF---RDALKSG 826
Cdd:PRK13208 575 qvkigrRLLTKLWNAS-----RFVLHFSADPEPDKA----EVLEPLDRWILAKLAKVVEKATEALENYDFakaLEEIESF 645
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162454698 827 FYDLqLArDEY------RLScGAAGMNRDL-----LWRFMDVQTRLITPICPHYAEHVWQKImkKEGFAIKAGWPAAD 893
Cdd:PRK13208 646 FWHV-FC-DDYlelvksRAY-GEDEEEEQKsarytLYTVLDTLLRLLAPFLPFITEEVWSWL--YGGSVHRASWPEPD 718
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
796-929 |
1.65e-14 |
|
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: 71.67 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 796 DRVFSNEMNIAIKETEKSYNAFMFRDALKSGFYDLQLAR-DEY------RLSCGAAGMN-RDLLWRFMDVQTRLITPICP 867
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLsDWYlelikdRLYGEEPDSRaQTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1162454698 868 HYAEHVWQKimkkeGFAIKAGWPA-ADTPDPTLRIANKYLQDSIVLMRKLLQKQESGSKKPKK 929
Cdd:pfam08264 81 FITEELWQK-----ESIHLAPWPEdAELEEAELEEAFELRQEIVQAIRKLRSELKIKKSLPLE 138
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
521-757 |
2.52e-11 |
|
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: 66.89 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 521 VMSRSGDECVVALTDQWYITYGEAewKQKAVKCL--DHMNTFSTETRNGFEHtlgWLNQ---WACSRSFGLGTRIP-WDE 594
Cdd:cd00817 155 VCSRSGDVIEPLLKPQWFVKVKDL--AKKALEAVkeGDIKFVPERMEKRYEN---WLENirdWCISRQLWWGHRIPaWYC 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 595 QFLVESLSDSTLYMAYYTVAHLLQNGnmYGKEisSVRPEE------MTDEVWDFVFCDGPapkseipaallnKMKHEFKY 668
Cdd:cd00817 230 KDGGHWVVAREEDEAIDKAAPEACVP--CGGE--ELKQDEdvldtwFSSSLWPFSTLGWP------------EETKDLKK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 669 WYPFDIRVSGKDLIQNHLT---FCIYNHTALLPehhwpigFRcngHLMLNS-------EKMSKSTGNFLTLEDAIKKYSS 738
Cdd:cd00817 294 FYPTSLLVTGHDIIFFWVArmiMRGLKLTGKLP-------FK---EVYLHGlvrdedgRKMSKSLGNVIDPLDVIDGYGA 363
|
250
....*....|....*....
gi 1162454698 739 DATRFALADAGDGMDDANF 757
Cdd:cd00817 364 DALRFTLASAATQGRDINL 382
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
671-745 |
2.99e-11 |
|
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: 67.05 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 671 PFDIRVSGKDLI---------QNHltfCIYNHTallPEHHWpigfrcNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDAT 741
Cdd:COG0215 219 TFDIHGGGIDLIfphheneiaQSE---AATGKP---FARYWm----hNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVL 288
|
....
gi 1162454698 742 RFAL 745
Cdd:COG0215 289 RFFL 292
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
678-824 |
4.33e-11 |
|
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: 66.68 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 678 GKDLIQNHltfCIYnhtallpehhWPI-----GFR------CNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALA 746
Cdd:COG0143 289 GKDIIRFH---AII----------WPAmlmaaGLPlpkkvfAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 747 DAGDGMDDANF-----VT----ETAN--------SAVMrLTKEIswmeevtaaESKLRTGPPTTYADRVFSNEMNIAIKE 809
Cdd:COG0143 356 REVPFGQDGDFswedfVArvnsDLANdlgnlasrTLSM-IHKYF---------DGKVPEPGELTEADEELLAEAEAALEE 425
|
170
....*....|....*
gi 1162454698 810 TEKSYNAFMFRDALK 824
Cdd:COG0143 426 VAEAMEAFEFRKALE 440
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
672-745 |
7.83e-11 |
|
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: 62.98 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 672 FDIRVSGKDLIQNH------LTFCIYNHTallPEHHWpigfRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFAL 745
Cdd:cd00672 129 FDIHGGGVDLIFPHheneiaQSEAATGKP---FARYW----LHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
48-228 |
4.80e-10 |
|
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: 62.05 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 48 KFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPIKASADKLareiqqygyppvfpvaegss 127
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERK-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 128 aavadatqadqvdvvapdkfKGKKSKatakagaqkyqweimksfgldDEEIARF-QDPYHWLTHFPPLAKEVLKKFGLGC 206
Cdd:cd00668 61 --------------------GGRKKK---------------------TIWIEEFrEDPKEFVEEMSGEHKEDFRRLGISY 99
|
170 180
....*....|....*....|..
gi 1162454698 207 DWRRSFITTDmnPYYDAFVKWQ 228
Cdd:cd00668 100 DWSDEYITTE--PEYSKAVELI 119
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
670-748 |
5.51e-10 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 62.00 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 670 YPFDIRVSGKDLIQNHLTFCIYNHTALL---PEHHWpigfRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALA 746
Cdd:pfam01406 206 DQIDIHGGGIDLAFPHHENEIAQSEAAFdkqLANYW----LHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLL 281
|
..
gi 1162454698 747 DA 748
Cdd:pfam01406 282 SV 283
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
708-899 |
1.33e-09 |
|
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: 62.41 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 708 CNGH-LMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALAdAGDGMDDanfvtetansavMRLTKEIswMEEVTAAESKL 786
Cdd:COG0060 592 THGFvLDEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVA-SSDYWGD------------LRFSDEI--LKEVRDVYRRL 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 787 RTgpptTY-------------ADRVFSNEM-----------NIAIKETEKSYNAFMFRDALK----------SGFYdLQL 832
Cdd:COG0060 657 RN----TYrfllanlddfdpaEDAVPYEDLpeldrwilsrlNELIKEVTEAYDNYDFHRAYRalhnfcvedlSNWY-LDI 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162454698 833 ARDeyRLSCGAAGMNRDL-----LWRFMDVQTRLITPICPHYAEHVWQKIMKKEG---FAikAGWPAADTP--DPTL 899
Cdd:COG0060 732 SKD--RLYTEAADSLDRRaaqttLYEVLETLVRLLAPILPFTAEEIWQNLPGEAEesvHL--ADWPEVDEEliDEEL 804
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
666-757 |
8.27e-09 |
|
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: 58.31 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 666 FKYWYPFDIRVSGKDLIQNHltfCIYnhtallpehhWPI-----GFR------CNGHLMLNSEKMSKSTGNFLTLEDAIK 734
Cdd:cd00814 230 WKDGWPELVHFIGKDIIRFH---AIY----------WPAmllgaGLPlptrivAHGYLTVEGKKMSKSRGNVVDPDDLLE 296
|
90 100
....*....|....*....|...
gi 1162454698 735 KYSSDATRFALADAGDGMDDANF 757
Cdd:cd00814 297 RYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
665-757 |
8.71e-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: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 665 EFKYWYPFDIRVS-----GKDLIQNHltfCIYnhtallpehhWPI-----GFR------CNGHLMLNSEKMSKSTGNFLT 728
Cdd:pfam09334 268 KWKEWWPNDPDTElvhfiGKDIIYFH---TIF----------WPAmllgaGYRlpttvfAHGYLTYEGGKMSKSRGNVVW 334
|
90 100
....*....|....*....|....*....
gi 1162454698 729 LEDAIKKYSSDATRFALADAGDGMDDANF 757
Cdd:pfam09334 335 PSEALDRFPPDALRYYLARNRPETKDTDF 363
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
718-916 |
1.00e-08 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 59.73 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 718 KMSKSTGNFLTLEDAIKKYSSDATRFALAD-AGDGMD--------DA--NFVTETANSA--VMrltkeiswMEEVTAAES 784
Cdd:PRK05729 520 KMSKSKGNVIDPLDLIDKYGADALRFTLAAlASPGRDirfdeervEGyrNFANKLWNASrfVL--------MNLEGADVG 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 785 KLRTGPPTTYADRVFSNEMNIAIKETEKSYNAFMFRDALKSgFYDlqLARDEY----------RLSCGAAGMNRDLLWRF 854
Cdd:PRK05729 592 ELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARA-LYE--FIWNEFcdwylelakpVLQEAAKRATRATLAYV 668
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162454698 855 MDVQTRLITPICPHYAEHVWQKIMKKEGFA--IKAGWPAAD-TPDPTLRIANKYLQDSIVLMRKL 916
Cdd:PRK05729 669 LEQILRLLHPFMPFITEELWQKLAPLGIEEsiMLAPWPEADeAIDEAAEAEFEWLKELITAIRNI 733
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
718-916 |
1.32e-08 |
|
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: 59.29 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 718 KMSKSTGNFLTLEDAIKKYSSDATRFALAD-AGDGMD--------DA--NFVTETANSAvmRLTKeiSWMEEVTAAESKL 786
Cdd:COG0525 522 KMSKSKGNVIDPLDLIDKYGADALRFTLAAlASPGRDikfdeervEGyrNFANKLWNAS--RFVL--MNLEGFDPGLDPD 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 787 RTgpPTTYADRVFSNEMNIAIKETEKSYNAFMFRDALKSgFYDlqLARDEY----------RLSCG---AAGMNRDLLWR 853
Cdd:COG0525 598 PE--ELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQA-LYD--FVWNEFcdwylelakpRLYGGdeaAKRETRATLVY 672
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162454698 854 FMDVQTRLITPICPHYAEHVWQKI--MKKEGFAIKAGWPAADTP--DPTLRIANKYLQDSIVLMRKL 916
Cdd:COG0525 673 VLEQILRLLHPFMPFITEEIWQKLppRKEGESIMLAPWPEADEEliDEEAEAEFEWLKEVISAIRNI 739
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
481-897 |
5.74e-08 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 57.31 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 481 DGTMI--VGEFSGRKVQEAKPLIKSKLLEEGTaVLYSEPEKKVMSRSGDECVVA---LTDQWYITYgeAEWKQKAVKCLD 555
Cdd:PRK14900 315 DGRMTaeAGPLAGLDRFEARKEVKRLLAEQGL-DRGAKPHVLPLGRCQRSATILeplLSDQWYVRI--EPLARPAIEAVE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 556 HMNT-FSTET-RNGFEHTLGWLNQWACSRSFGLGTRIPwdeqflveslsdstlymAYY-TVAHLLqngnmYGKEISSVRP 632
Cdd:PRK14900 392 QGRTrFIPEQwTNTYMAWMRNIHDWCISRQLWWGHQIP-----------------AWYcPDGHVT-----VARETPEACS 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 633 -----EEMTDE-VWDFVFCDGPAPKSEI--PaallnKMKHEFKYWYPFDIRVSGKDLIqnhltFCIYNHTALLPEHHW-P 703
Cdd:PRK14900 450 tcgkaELRQDEdVLDTWFSSGLWPFSTMgwP-----EQTDTLRTFYPTSVMETGHDII-----FFWVARMMMMGLHFMgE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 704 IGFR-CNGHLMLNSEK---MSKSTGNFLTLEDAIKKYSSDATRFALA-------DAGDGMDD-------ANFVTETANSA 765
Cdd:PRK14900 520 VPFRtVYLHPMVRDEKgqkMSKTKGNVIDPLVITEQYGADALRFTLAaltaqgrDIKLAKERiegyrafANKLWNASRFA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 766 VMRLtkeiswmeevtaAESKLRTGPPT----TYADRVFSNEMNIAIKETEKSYNAFMFRDALKSGF---------YDLQL 832
Cdd:PRK14900 600 LMNL------------SGYQERGEDPArlarTPADRWILARLQRAVNETVEALEAFRFNDAANAVYafvwhelcdWYIEL 667
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 833 ARDE-YRLSCGAAGMNRDLLWRFMDVQTRLITPICPHYAEHVWQKIMKKEGfaiKAGWP----AADTPDP 897
Cdd:PRK14900 668 AKEAlASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLRAQVG---ASAWAdsvlAAEYPRK 734
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
678-943 |
9.88e-08 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 56.31 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 678 GKDLIQNHltfCIYnhtallpehhWPI-----GFR------CNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALA 746
Cdd:PRK00133 291 GKDIIYFH---TLF----------WPAmlegaGYRlptnvfAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLA 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 747 -DAGDGMDDANFvtetansavmrltkeiSW---MEEVTA----------------AESKLRTGPPTTYADRVFSNEMNIA 806
Cdd:PRK00133 358 aKLPETIDDLDF----------------NWedfQQRVNSelvgkvvnfasrtagfINKRFDGKLPDALADPELLEEFEAA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 807 IKETEKSYNAFMFRDALKSGfydLQLAR--DEY---------------------RLSCGAAgmnRDLlwrfmdvqTRLIT 863
Cdd:PRK00133 422 AEKIAEAYEAREFRKALREI---MALADfaNKYvddnepwklakqdgerlqavcSVGLNLF---RAL--------AIYLK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 864 PICPHYAEHVWqKIMKKEGFAikagWPAADTPdptlrIANKYLQDSIVLMRK--------LLQKQESGSKKPKKGAAPAP 935
Cdd:PRK00133 488 PVLPELAERAE-AFLNLEELT----WDDAQQP-----LAGHPINKFKILFTRiedkqieaLIEASKEAAAAKAAAAAAAA 557
|
....*...
gi 1162454698 936 PSEEKKMS 943
Cdd:PRK00133 558 PLAEEPIA 565
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
25-99 |
3.61e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 54.44 E-value: 3.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162454698 25 QKFWDENKVFQADPGNDSPSPGEKFFGNFPYPYMNGlLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMP 99
Cdd:PLN02563 90 QRYWEENRTFRTPDDVDTSKPKFYVLDMFPYPSGAG-LHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLP 163
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
54-227 |
3.06e-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: 50.71 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 54 PYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLLPFAFHCTGMPikasadklareiqqygyppvfpvaegssaavada 133
Cdd:cd00817 8 PPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA---------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 134 TQAdqvdVVapDKFKGKKSKATAKAGAQKYQWEIMKsfgLDDEEIARFqdpyhwlthfpplaKEVLKKFGLGCDWRRSFI 213
Cdd:cd00817 54 TQV----VV--EKKLGIEGKTRHDLGREEFLEKCWE---WKEESGGKI--------------REQLKRLGASVDWSREYF 110
|
170
....*....|....*....
gi 1162454698 214 TtdMNPYY-----DAFVKW 227
Cdd:cd00817 111 T--MDPGLsravqEAFVRL 127
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
21-408 |
3.39e-06 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 51.31 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 21 ELEVQKFWDENKVFQA-DPGNDspspGEKFFGNFPYPYMNGLLHLGHAfsLSKL--EFGAAYHRLRGSNVLLPFAFHCTG 97
Cdd:PLN02843 9 EPEIQKLWEENQVYKRvSDRNN----GESFTLHDGPPYANGDLHIGHA--LNKIlkDFINRYQLLQGKKVHYVPGWDCHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 98 MPIK----ASADKLAREiqqygyppvfpvaegssaavadatqadqvdVVAPDKFKgKKSKATAKAGAQKYqweiMKSFgl 173
Cdd:PLN02843 83 LPIElkvlQSLDQEARK------------------------------ELTPIKLR-AKAAKFAKKTVDTQ----RESF-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 174 ddeeiarfqdpyhwlthfpplakevlKKFGLGCDWRRSFITTDmnPYYDAF---VKWQMRklkklgkvvkdMRYTIY--- 247
Cdd:PLN02843 126 --------------------------KRYGVWGDWENPYLTLD--PEYEAAqieVFGQMF-----------LNGYIYrgr 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 248 -----SPLDGQPCADHDRATGEG-VQPQEYVLIKMEVIS-PFPPKLKS-LEGrkVYLAAATLRPETMYGQTNCWVLPDGM 319
Cdd:PLN02843 167 kpvhwSPSSRTALAEAELEYPEGhVSKSIYVAFPVVSPSeTSPEELEEfLPG--LSLAIWTTTPWTMPANAAVAVNDKLQ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 320 YGAFEINDTDVFILTARSAFNLAYQHLSRVPEKPT--------------------CLCELSGSDLIGLPLKSPLAFNETI 379
Cdd:PLN02843 245 YSVVEVQSFSEDESTSGGNKKKRPGNVLKEQQKLFlivatdlvpaleakwgvklvVLKTFPGSDLEGCRYIHPLYNRESP 324
|
410 420
....*....|....*....|....*....
gi 1162454698 380 YALPMLTVLTDKGTGIVTSVPSDSPDDFM 408
Cdd:PLN02843 325 VVIGGDYITTESGTGLVHTAPGHGQEDYI 353
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
670-794 |
1.06e-05 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 49.64 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 670 YPFDIRVSGKDLI----QNHLTFC-IYNHTallpeHHWPIGFRCNGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATR-- 742
Cdd:PTZ00399 267 DPIDIHSGGIDLKfphhDNELAQSeAYFDK-----HQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRll 341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1162454698 743 FALADAGDGMddaNFVTETANSAVmrlTKEISWMEEVTAAESKLRTGPPTTY 794
Cdd:PTZ00399 342 FLLHKWDKPM---NYSDESMDEAI---EKDKVFFNFFANVKIKLRESELTSP 387
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
667-746 |
3.97e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 47.57 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 667 KYWyPFDIRVSGKDLIQNHltfCIYnhtallpehhWPI-----GFR------CNGHLMLNSEKMSKSTGNFLTLEDAIKK 735
Cdd:PRK11893 251 KYW-PADVHLIGKDILRFH---AVY----------WPAflmaaGLPlpkrvfAHGFLTLDGEKMSKSLGNVIDPFDLVDE 316
|
90
....*....|.
gi 1162454698 736 YSSDATRFALA 746
Cdd:PRK11893 317 YGVDAVRYFLL 327
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
26-90 |
9.49e-05 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 46.54 E-value: 9.49e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162454698 26 KFWDENKVFQADPGNDSPSPGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVL-LP 90
Cdd:PTZ00419 39 EWWEKSGFFKPAEDAKSLNSGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLwVP 104
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
670-745 |
1.76e-04 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 45.69 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 670 YPFDIRVSGKDLIqnhltfciynhtalLPEHHWPIGFRC-------------NGHLMLNSEKMSKSTGNFLTLEDAIKKY 736
Cdd:PLN02946 276 HSFDIHGGGMDLV--------------FPHHENEIAQSCaaccdsnisywihNGFVTVDSEKMSKSLGNFFTIRQVIDLY 341
|
....*....
gi 1162454698 737 SSDATRFAL 745
Cdd:PLN02946 342 HPLALRLFL 350
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
667-745 |
4.56e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 44.41 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 667 KYWyPFDIRVSGKDLIQNHltfCIYNHTAL------LPEH---HwpigfrcnGHLMLNSEKMSKSTGNFLTLEDAIKKYS 737
Cdd:PRK12267 251 KFW-PADVHLVGKDILRFH---AIYWPIMLmalglpLPKKvfaH--------GWWLMKDGKMSKSKGNVVDPEELVDRYG 318
|
....*...
gi 1162454698 738 SDATRFAL 745
Cdd:PRK12267 319 LDALRYYL 326
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
793-894 |
7.61e-04 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153414 [Multi-domain] Cd Length: 180 Bit Score: 41.74 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 793 TYADRVFSNEMNIAIKETEKSYNAFMFRDALK----------SGFYdLQLARD---------EYRLSCGAAgmnrdlLWR 853
Cdd:cd07960 43 LELDRYALHRLNELIKEVREAYENYEFHKVYQalnnfctvdlSAFY-LDIIKDrlycdakdsLERRSAQTV------LYH 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1162454698 854 FMDVQTRLITPICPHYAEHVWQkIMKKEGFAI---KAGWPAADT 894
Cdd:cd07960 116 ILDALLKLLAPILPFTAEEVWE-HLPGEKKEEsvfLEDWPELPE 158
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
54-114 |
1.92e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 41.89 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162454698 54 PYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVLlpfafHCTGM-----PIKASADKLAREIQQY 114
Cdd:pfam09334 6 ALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVL-----FVCGTdehgtPIELKAEKEGITPEEL 66
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
672-787 |
3.76e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 41.06 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162454698 672 FDIRVSGKDLIQNHLTFCIYNHTALLPEHhWPIGFRCNGHLMLNSEKMSKSTGNFLTLEDAIKK-YSSDATRFALAdAGD 750
Cdd:PRK14536 234 CDIHIGGVDHIRVHHTNEIAQCEAATGKP-WVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLL-GGH 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1162454698 751 GMDDANF---VTETANSAVMRLTKEIS-WMEEVTAAESKLR 787
Cdd:PRK14536 312 YRSQLAFsweALKTAKAARRSLVRRVArVVDAARATTGSVR 352
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
709-748 |
6.02e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 40.47 E-value: 6.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1162454698 709 NGHLMLNSEKMSKSTGNFLTLEDAIKKYSSDATRFALADA 748
Cdd:PRK14535 499 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRA 538
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
56-106 |
7.12e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 39.91 E-value: 7.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1162454698 56 PYMNGLLHLGHAfsLSKL--EFGAAYHRLRGSNVLLPFAFHCTGMPIKASADK 106
Cdd:cd00818 10 PYANGLPHYGHA--LNKIlkDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEK 60
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
54-114 |
7.79e-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: 39.82 E-value: 7.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162454698 54 PYPYMNGLLHLGHAFSLSKLEFGAAYHRLRGSNVllpfaFHCTGM-----PIKASADKLAREIQQY 114
Cdd:cd00814 7 ALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDV-----LFVTGTdehgtKIEQKAEEEGVTPQEL 67
|
|
| |
