|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
1-1068 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 1476.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 1 MATTERKGTFKVEYLQKIEREVQQRWEAERVHESDAPTAPKKrQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHR 80
Cdd:PLN02959 1 MMAEGGKSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPK-PGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 81 LKGRRVLWPFGFHCTGMPIKACADKLTRELEQFGFPPQFPETEEVVPVAAEAASE------VPKDKSKGKKSKAVAKTGA 154
Cdd:PLN02959 80 LRGANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEDEDEAAAVAAAKAeaeaaaAPPDKFKGKKSKAVAKSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 155 AKYQWQIMQSLGLKDEEIKDFANAEHWLNYFPPLAVQDLKRIGVHVDWRRTFITTDANPYFDSFVRWQFNHLKERGKIMY 234
Cdd:PLN02959 160 QKYQWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTDVNPYYDAFVRWQFRKLKKKGKIVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 235 GKRYTIYSPKDGQPCMDHDRSSGEGVGPQEYTLIKMKVL-EVPKALSSIK-QPIFMVAATLRPETMYGQTNCWLHPDIKY 312
Cdd:PLN02959 240 DKRYTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLpPFPGKLKALEgKKVFLAAATLRPETMYGQTNCWVLPDGKY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 313 IAWQANkNNEVWVSTRRAARNMTYQGFTAVEGEIKVLAEVTGQDLLGVPLSAPLTKHKVVYSLPMLSIKEDKGTGVVTSV 392
Cdd:PLN02959 320 GAYEIN-DTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 393 PSDSPDDYAALVDLQKKEAFRQKYGLKDEMVLPYEPIPIIEVPTLGKLSAVHAYETLKIQSQNDKDKLAEAKEMCYLKSF 472
Cdd:PLN02959 399 PSDSPDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 473 YDGVMLVGAFAGRKIQDVKKDLQKRLVDANEADVYYEPEKTIMSRSADECVVALCNQWYLNYGEPEWQAQATKILHGMET 552
Cdd:PLN02959 479 TDGTMLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 553 FHEEARNNFEACLNWLHEYACSRTYGLGTKLPWDDKWLIESLSDSTIYMAFYTVVHLLQGG-TFRGEKPgpfGIKPSDMT 631
Cdd:PLN02959 559 YSDETRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGdMYGKDKS---SIKPEQMT 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 632 GEIWDYIFFKeTPLPKKTAIKQEHLAVLRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAIWPNDEnkWPKGMRVNGHL 711
Cdd:PLN02959 636 DEVWDFVFCG-GPLPKSSDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAEEH--WPRGFRCNGHL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 712 LLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDSVEDANFVESTADAGILRLYTFIEWVKEMLENRSSLRKGTDK 791
Cdd:PLN02959 713 MLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLTKEIAWMEEVLAAESSLRTGPPS 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 792 TFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLARDKYRELCGANGMHEDLVLEFIRRQALLVSPICPHMAEH 871
Cdd:PLN02959 793 TYADRVFENEINIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRLSCGSGGMNRDLVWRFMDVQTRLITPICPHYAEH 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 872 VWG-LLGNKESIVHARWPEVGAINEVDILCSEYLMEAAHSFRlnlkNLLQiKGKAGKDKSVNVQAA-----KPNRGLVWV 945
Cdd:PLN02959 873 VWReILKKEGFAVTAGWPVAGEPDLTLKRANKYLQDSIVSFR----KLLQ-KQLAGSKKAKKGGAPvtlpeKKLAGLIYV 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 946 AKTYPPWQCCVLDTMKELFNKSQAL--PDNKVIAA----TLQQKAELKKFMKRVMPFAQMIREKVESgKGVAALAVTLEF 1019
Cdd:PLN02959 948 AEKYDGWKEECLRILQSKFDSQSRTfaPDAEILEAlkesSVGQEANFKQVQKLCMPFVKFKKDEAIA-VGPQALDLKLPF 1026
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574733 1020 DERQVLISNLEYLKNTLDLDVLEIKYTDDPSAPEKTREE--------VRPGSPFISF 1068
Cdd:PLN02959 1027 DEIEVLQENLELIKRQLGLEEVEILSASDPDAVAKAGAHasllkqnpPSPGNPVAIF 1083
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
18-1068 |
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: 840.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 18 IEREVQQRWEAERVHESDaptaPKKRqaEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGM 97
Cdd:TIGR00395 3 IEKKWQKRWEEAHIFEAD----PDDR--EKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVTGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 98 PIKACADKLTRELEQFGfppqfpeteevvpvaaEAASEVPkdkskgkkskavaktgaakyqwqimqslGLKDEEIKDFAN 177
Cdd:TIGR00395 77 PILGLAELIKRRDELTI----------------KNYTEVH----------------------------AIPREELLKFTD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 178 AEHWLNYFPPLAVQDLKRIGVHVDWRRTFITTDanPYFDSFVRWQFNHLKERGKIMYGKRYTIYSPKDGQPCMDHDRSSG 257
Cdd:TIGR00395 113 PEYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVEDHDLLSG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 258 EGVGPQEYTLIKMKVLEvpkalssikQPIFMVAATLRPETMYGQTNCWLHPDIKYIawQANKNNEVWVSTRRAARNMTYQ 337
Cdd:TIGR00395 191 EGVTIVEYILIKFELED---------GAFYFVAATLRPETVYGVTNCWVNPTITYV--IAEVGGEKWITSKEAFENLSYQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 338 gftavEGEIKVLAEVTGQDLLGVPLSAPLTKHKVVYsLPMLSIKEDKGTGVVTSVPSDSPDDYAALVDLQKKEafrQKYG 417
Cdd:TIGR00395 260 -----KLKYKPIEEVPGKQFIGKKVHNPVVGPEVPI-LPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDP---EYLG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 418 LKDEmVLPYEPIPIIEVPTLGKLSAVHAYETLKIQSQNDKDKLAEAKEMCYLKSFYDGVMLVGA--FAGRKIQDVKKDLQ 495
Cdd:TIGR00395 331 IKPV-VIDIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIYNIppYKGMKVSEAKEKVK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 496 KRLVDANEADVYYEP-EKTIMSRSADECVVALC-NQWYLNYGEPEWQAQATKILHGMETFHEEARNNFEACLNWLHEYAC 573
Cdd:TIGR00395 410 ADLIDAGLADVMYEFsESPVICRCGTDCIVKVVeDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKIDWLKDWAC 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 574 SRTYGLGTKLPWDDKWLIESLSDSTIYMAFYTVVHLLQGGTfrgekpgpfgIKPSDMTGEIWDYIFFKETPLpKKTAIKQ 653
Cdd:TIGR00395 490 CRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDY----------YGNEQMTDEFFDYIFLGKGDV-KNTNIPL 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 654 EHLAVLRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAIWPndENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVD 733
Cdd:TIGR00395 559 PAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFP--EKFWPRGIVVNGYVMLEGKKMSKSKGNVLTLEQAVE 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 734 KFSADGMRLCLADAGDSVEDANFVESTADAGILRLYTFIEWVKEMLEnRSSLRKGTDKTFNDQVFLSELNLKTQQTDENY 813
Cdd:TIGR00395 637 KFGADVARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEEITK-ESNLETGEETSFIDRWLESRMNAAIKETYEAM 715
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 814 RKMLFKEALRSGFYELQLARDKYRELCGanGMHEDLVLEFIRRQALLVSPICPHMAEHVWGLLGNKESIVHARWPEVG-- 891
Cdd:TIGR00395 716 ENFQTRKAVKYALFDLQADVDWYRRRGG--VNHKDVLARYLETWIKLLAPFAPHFAEEMWEEVGNEGFVSLAKFPEASep 793
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 892 AINEVDILCSEYlmeaahsfrlnLKNLLQ-IKgkagkdKSVNVQAAKPNRGLVWVAktyPPWQCCVLDTMKELFNKsQAL 970
Cdd:TIGR00395 794 AVDKEVEAAEEY-----------LRNLVRdIQ------EIAKIDASKPKRVYLYTS---EDWKSQCLKIVAELFGE-DTG 852
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 971 PDNKVIaatlqqkAELKKFMKRVMPFAQMIREKVESGKGVAAlavtLEFDERQVLISNLEYLKNtlDLDVLEIKYTDDPS 1050
Cdd:TIGR00395 853 EDMKKV-------MEEPEERKRGKEVISLVKQIIKDEKKEDE----LQISEIEVLKAAARFIKK--EVGALVIIEFSADS 919
|
1050
....*....|....*...
gi 28574733 1051 APEKTREEVRPGSPFISF 1068
Cdd:TIGR00395 920 FPENKKRNAVPGKPAIYL 937
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
61-1066 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 736.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 61 LHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKACADKLTReleqfgfppqfpeteevvpvaaeaasevpkdk 140
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIAR-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 141 skgkkskavaktGAAKYQWQIMQSLGLKDEEIKDFANAEHWLNYFPPLAVQDLKRIGVHVDWRRTFITTDanPYFDSFVR 220
Cdd:PRK12300 49 ------------GDPETIELYKSLYGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--PEYSKFIE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 221 WQFNHLKERGKIMYGKRYTIYSPKDGQPCMDHDRSSGEGVGPQEYTLIKMKVLEVpkalssikqpIFMVAATLRPETMYG 300
Cdd:PRK12300 115 WQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFEESED----------LILPAATLRPETIFG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 301 QTNCWLHPDIKYIawQANKNNEVWVSTRRAARNMTYQGFtavegEIKVLAEVTGQDLLGVPLSAPLTKHKVVySLPMLSI 380
Cdd:PRK12300 185 VTNLWVNPDATYV--KAEVDGEKWIVSKEAAEKLSFQDR-----DVEIIEEIKGSELIGKKVKNPVTGKEVP-ILPADFV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 381 KEDKGTGVVTSVPSDSPDDYAALVDLQKKEafrqkyglkdEMVLPYEPIPIIEVPTLGKLSAVHAYETLKIQSQNDKdKL 460
Cdd:PRK12300 257 DPDNGTGVVMSVPAHAPYDYVALRDLKKNK----------ELLDVIEPIPLIEVEGYGEFPAKEVVEKLGIKSQEDP-EL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 461 AEAKEMCYLKSFYDGVML--VGAFAGRKIQDVKKDLQKRLVDANEADVYYE-PEKTIMSRSADECVVA-LCNQWYLNYGE 536
Cdd:PRK12300 326 EEATKEVYRAEFHKGVLKenTGEYAGKPVREAREKITKDLIEKGIADIMYEfSNRPVYCRCGTECVVKvVKDQWFIDYSD 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 537 PEWQAQATKILHGMETFHEEARNNFEACLNWLHEYACSRTYGLGTKLPWDDKWLIESLSDSTIYMAFYTVVHLLQGGtfr 616
Cdd:PRK12300 406 PEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAHKIREY--- 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 617 gekpgpfGIKPSDMTGEIWDYIFF-KETP--LPKKTAIKQEHLAVLRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAI 693
Cdd:PRK12300 483 -------GIKPEQLTPEFFDYVFLgKGDPeeVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFIFNHVAI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 694 WPndENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDSVEDANFVESTADAGILRLYTFIE 773
Cdd:PRK12300 556 FP--EEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQLERFYE 633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 774 WVKEMLEnrssLRKGTDKTFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLARDKYRELCGANGmhEDLVLEF 853
Cdd:PRK12300 634 LAKELIE----IGGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRRVGEAN--NKVLREV 707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 854 IRRQALLVSPICPHMAEHVWGLLGNKESIVHARWPEVGA--INEVDILCSEY---LMEaahsfrlNLKNLLQIKGKagkd 928
Cdd:PRK12300 708 LEIWIRLLAPFTPHLAEELWHKLGGEGFVSLEKWPEPDEskIDEEAELAEEYvkrLIE-------DIREILKVAKI---- 776
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 929 ksvnvqaaKPNRGLVWVAktyPPWQCCVLDTMKELFNKSQALPDnkviaatLQQKAELKKFMKRVMPFAQMIREKVESGK 1008
Cdd:PRK12300 777 --------KPKKVYIYVA---PDWKYEVLEIAAENGDVKEAIKE-------LMKDEELRKHGKEVAKLAQKIVKEVLKLD 838
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574733 1009 GVAALAVTLEFDERQVLISNLEYLKNTLDLDVlEIKYTDDPSAPEKTREEVrPGSPFI 1066
Cdd:PRK12300 839 KEVRKLILKNIDEEEVLEEAKDFLEKELGVEV-EIYGADDPGKKKKKKKAL-PLKPAI 894
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
525-758 |
6.54e-69 |
|
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: 234.06 E-value: 6.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 525 ALCNQWYLNYGEPEWQAQATKILHGMETFHEEARNNFEaclNWLheyACSRTYGLGTKLPWddKWLIESLSDSTIYMAFY 604
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQE---NWI---GCSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 605 TVVHLLQGgtfrgekpgpfgikpsdmtgeiwdyiffketplPKKTAIKQehlavLRREFEYWYPMDLRVSGKDLIQNHLT 684
Cdd:cd00812 199 TDAHNLEQ---------------------------------PYEGDLEF-----DREEFEYWYPVDIYIGGKEHAPNHLL 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574733 685 FCLYNHAAIWPND--ENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDsvEDANFVE 758
Cdd:cd00812 241 YSRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFDW 314
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
756-876 |
5.02e-39 |
|
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: 140.80 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 756 FVESTADAGILRLYTFIEWVKEMLENRSSLrkgTDKTFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLARDK 835
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 28574733 836 YRELCGAnGMHEDLVLEFIRRQALLVSPICPHMAEHVWGLL 876
Cdd:cd07959 78 YRERGGA-GMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
47-204 |
2.47e-29 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 119.66 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 47 KFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKACADKLTRELEQFgfppqfpeTEEvv 126
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW--------TEY-- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574733 127 pvaaeaasevpkdksKGKKSKAVAKTGAAKYQWQIMQSLGlkdeeIKDFANAEHWLNYFPPLAvQDLKRIGVHVDWRR 204
Cdd:cd00812 71 ---------------NIKKMKEQLKRMGFSYDWRREFTTC-----DPEYYKFTQWLFLKLYEK-GLAYKKEAPVNWCK 127
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
22-756 |
1.12e-21 |
|
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: 100.95 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 22 VQQRWEAERVHEsdaPTAPKKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKA 101
Cdd:pfam00133 2 IYEFWDEQGYFK---PELEKRKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 102 CADKltreleqfgfppQFPETEEvvpvaaeaasevpkdkskgkksKAVAKTGAAKYQwqimqslglkdEEIKDfanaehW 181
Cdd:pfam00133 79 VVEK------------KLGIKEK----------------------KTRHKYGREEFR-----------EKCRE------W 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 182 LNYFPPLAVQDLKRIGVHVDWRRTFITTDanPYFDSFVRWQFNHLKERGKIMYGKRYTIYSPKDGQPCMDHDRSSGEGVG 261
Cdd:pfam00133 108 KMEYADEIRKQFRRLGRSIDWDREYFTMD--PELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVEYKDVKG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 262 PqeYTLIKMKVLEVPKAlssikqpiFMVAATLRPETMYGQTNCWLHPDIKYIAWQANKNNEVWVSTRRAARNMTYqgfta 341
Cdd:pfam00133 186 P--SIHVAFPLADDEGA--------SLVIWTTTPWTLPGNTAVAVNPEFDYVITGEGYILAEALLKSLYKKGTDK----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 342 vegeiKVLAEVTGQDLLGVPLSAPLTKHKVvyslPMLS---IKEDKGTGVVTSVPSDSPDDYAAlvdlqkkeafRQKYGL 418
Cdd:pfam00133 251 -----KILEDFRGKELEGKEAIHPFVNREI----PIITddyVDMEFGTGAVHIAPAHGENDYEV----------GQRHNL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 419 kdEMVLPYEPipiievptlgklsavhayetlkiqsqndkdklaeakemcylksfyDGVML--VGAFAGRKIQDVKKDLQK 496
Cdd:pfam00133 312 --EVINPVDD---------------------------------------------DGTFTeeAPDFQGVYRFDARKKIVE 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 497 RLvdaNEADVYYEPEKTIMS-----RSADECVVALCNQWYLNYgePEWQAQATKILHGMETFHEEARNNFEaclNWL--- 568
Cdd:pfam00133 345 LL---TEKGLLLKIEPFTHSypfcwRSGTPIIPRATPQWFVRM--DELADQALEAVEKVQFVPKSGEKRYF---NWLani 416
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 569 HEYACSRTYGLGTKLP-WDDKWLIESLSDSTIymaFYTVVHLLQGGtfrgekpgpfgikpsdmTGEIWDYIFFKETPLPK 647
Cdd:pfam00133 417 QDWCISRQRWWGHPIPaWVSKDTEEVVCRGEL---FELVAGRFEEE-----------------GSIKWLHREAKDKLGYG 476
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 648 KTAIKQE-------------HLAVL------RREFEYWYPMDLRVSGKDLIQnhltFCLYNHAAIWPNDENKWP-KGMRV 707
Cdd:pfam00133 477 KGTLEQDedvldtwfssgswPFSTLgwpfvnTEEFKKFFPADMLLEGSDQTR----GWFYRMIMLSTALTGSVPfKNVLV 552
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 28574733 708 NGhLLLNS--AKMSKSDGNFLTLTEAVDKFSADGMRLCLADAgDSVEDANF 756
Cdd:pfam00133 553 HG-LVRDEqgRKMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
481-745 |
4.45e-20 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 92.48 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 481 AFAGRKIQDVKKDLqKRL---VDANEADVYYEPEKT-----IMSRSADEC-------VVALCNQWYLNYgePEWQAQATK 545
Cdd:cd00668 79 EFVEEMSGEHKEDF-RRLgisYDWSDEYITTEPEYSkavelIFSRLYEKGliyrgthPVRITEQWFFDM--PKFKEKLLK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 546 ILHGMETFHEEARNNFEACLNWLHEYACSRTYGLGTKLPwddKWLIESLSDSTIYMAFYTvvhllqggtfrgekpgpfgI 625
Cdd:cd00668 156 ALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLP---EDVFDVWFDSGIGPLGSL-------------------G 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 626 KPSDmtgeiwdyiffketplpkktaikqehlavlRREFEYWYPMDLRVSGKDLIQNHLTFCLYNHAAIwpnDENKWPKGM 705
Cdd:cd00668 214 YPEE------------------------------KEWFKDSYPADWHLIGKDILRGWANFWITMLVAL---FGEIPPKNL 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28574733 706 RVNGHLLLN-SAKMSKSDGNFLTLTEAVDKFSADGMRLCLA 745
Cdd:cd00668 261 LVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLT 301
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
16-937 |
1.23e-17 |
|
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: 88.58 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 16 QKIEREVQQRWEAERVHESDaPTAPKkrqaEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCT 95
Cdd:TIGR00422 8 HEVEKKWYKKWEKSGFFKPD-GNSNK----PPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 96 GMPIKACADKLTREleqfgfppQFPETEEVvpvaaeaasevpkdkskgkkskavaktGAAKYQWQIMQslgLKDEEIKdf 175
Cdd:TIGR00422 83 GIATQVKVEKKLGA--------EGKTKHDL---------------------------GREEFREKIWE---WKEESGG-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 176 anaehwlnyfppLAVQDLKRIGVHVDWRRTFITTDANPYF---DSFVRWQfnhlkERGKIMYGKRYTIYSPKDGQPCMDh 252
Cdd:TIGR00422 123 ------------TIKNQIKRLGASLDWSRERFTMDEGLSKavkEAFVRLY-----EKGLIYRGEYLVNWDPKLNTAISD- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 253 drssgegvgpqeytlIKMKVLEVPKALSSIKQPI------FMVAATLRPETMYGQTNCWLHPDIKyiawqanknnevwvs 326
Cdd:TIGR00422 185 ---------------IEVEYKEVKGKLYYIRYPLangskdYLVVATTRPETMFGDTAVAVHPEDE--------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 327 trraaRNmtyqgftavegeikvlaevtgQDLLGVPLSAPLTKHKVvyslPMLS---IKEDKGTGVVTSVPSDSPDDYAal 403
Cdd:TIGR00422 235 -----RY---------------------KHLIGKKVILPLTGRKI----PIIAdeyVDMEFGTGAVKVTPAHDFNDYE-- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 404 vdLQKKeafrqkyglkdemvlpyepipiievptlgklsavHAYETLKIqsQNDKDKLAEAkemcylksfydgvmlVGAFA 483
Cdd:TIGR00422 283 --WGKR----------------------------------HNLEFINI--LDEDGLLNEN---------------AGKYQ 309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 484 GRKIQDVKKDLQKRLvdanEADVYYEPEKTIMS------RSADECVVALCNQWYLNYGEPEWQAQATKILHGMETFHEEA 557
Cdd:TIGR00422 310 GLTRFEARKKIVEDL----KEEGLLVKIEPHTHnvgtcwRSGTVVEPLLSKQWFVKVEKLADKALEAAEEGEIKFVPKRM 385
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 558 RNNFEACLNWLHEYACSRTYGLGTKLPwddkwlieslsdstiymAFYtvvhllqggtfrgekpgpfgikpSDMTGEIWDY 637
Cdd:TIGR00422 386 EKRYLNWLRNIKDWCISRQLIWGHRIP-----------------VWY-----------------------CKECGEVYVA 425
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 638 iffKETPLPKK-------TAIKQEH-------------LAVL-----RREFEYWYPMDLRVSGKDLI----------QNH 682
Cdd:TIGR00422 426 ---KEEPLPDDktntgpsVELEQDTdvldtwfssslwpFSTLgwpdeTKDLKKFYPTDLLVTGYDIIffwvarmifrSLA 502
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 683 LTFCL-----YNHAAIwpNDEnkwpkgmrvNGHlllnsaKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGDSVEDANFV 757
Cdd:TIGR00422 503 LTGQVpfkevYIHGLV--RDE---------QGR------KMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFD 565
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 758 ESTADAG---ILRLYTFIEWVKEMLENRSSLRKGTDK-TFNDQVFLSELNLKTQQTDENYRKMLFKEALRSgFYE----- 828
Cdd:TIGR00422 566 WKRVESArnfLNKLWNASRFVLMNLSDDLELSGGEEKlSLADRWILSKLNRTIKEVRKALDKYRFAEAAKA-LYEfiwnd 644
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 829 -----LQLArdKYRelcgANGMHEDL------VLEFIRRQAL-LVSPICPHMAEHVWGLLGNK-ESIVHARWPEVGA-IN 894
Cdd:TIGR00422 645 fcdwyIELV--KYR----LYNGNEAEkkaardTLYYVLDKALrLLHPFMPFITEEIWQHFKEGaDSIMLQSYPVVDAeFV 718
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 28574733 895 EVDILCS-EYLMEAAHSFRlNLKNLLQIKGKAGKDKSVNVQAAK 937
Cdd:TIGR00422 719 DEEAEKAfELLKEIIVSIR-NLKAESNIPPNAPLKVLLIYTEAE 761
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
47-243 |
2.96e-17 |
|
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: 84.01 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 47 KFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKacadkltreleqfgfppqfpeteevv 126
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIE-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 127 pVAAEAASEVPKdkskgkkskavaktgaakyqwqimqslglKDEEIKDFANA-EHWLNYFPPLAVQDLKRIGVHVDWRRT 205
Cdd:cd00668 55 -LKAERKGGRKK-----------------------------KTIWIEEFREDpKEFVEEMSGEHKEDFRRLGISYDWSDE 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 28574733 206 FITTDanPYFDSFVRWQFNHLKERGKIMYGKRYTIYSP 243
Cdd:cd00668 105 YITTE--PEYSKAVELIFSRLYEKGLIYRGTHPVRITE 140
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
15-912 |
1.57e-13 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 75.23 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 15 LQKIEREVQQRWEAERVHESDaPTAPKKRqaekFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHC 94
Cdd:PRK13208 12 PEELEEKWQKIWEEEGTYKFD-PDERKPV----YSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 95 TGMPIkacadkltrEL---EQFGFPPQ------FPE-TEEVVpvaaeaasevpkdkskgkkskavaktgaakyqwqimqs 164
Cdd:PRK13208 87 NGLPT---------ERkveKYYGIRKDdisreeFIElCRELT-------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 165 lglkDEEIKDFanaehwlnyfpplaVQDLKRIGVHVDWRRTFITTDANpYFD----SFVRwqfnhLKERGKIMYGKRYTI 240
Cdd:PRK13208 120 ----DEDEKKF--------------RELWRRLGLSVDWSLEYQTISPE-YRRisqkSFLD-----LYKKGLIYRAEAPVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 241 YSPKDG----QPcmdhdrssgEgvgpQEYTlikmkvlEVPKALSSIKqpiFMVA-------ATLRPETM-------Ygqt 302
Cdd:PRK13208 176 WCPRCEtaiaQA---------E----VEYR-------EREGKLNYIK---FPVEdgeeieiATTRPELLpacvavvV--- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 303 ncwlHP-DIKYiawqanknnevwvstrraarnmtyqgftavegeikvlaevtgQDLLGVPLSAPLTKHKVvyslPML--- 378
Cdd:PRK13208 230 ----HPdDERY------------------------------------------KHLVGKTAIVPLFGVEV----PILadp 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 379 SIKEDKGTGVV---TsvpsdspddYAALVDLQkkeaFRQKYGLkdemvlpyEPIPIIevptlgklsavhayetlkiqsqn 455
Cdd:PRK13208 260 LVDPDFGTGAVmicT---------FGDKTDVT----WWRELNL--------PTRIII----------------------- 295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 456 DKD-KLAEAKemcylksfydgvmlvGAFAGRKIQDVKkdlqKRLVDA-NEADVYYEPEKTimSRSADEC---------VV 524
Cdd:PRK13208 296 DEDgRMTEAA---------------GKLAGLTIEEAR----KKIVEDlKSGGLLGKQEPI--KHNVKFCercdtpleiLV 354
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 525 AlcNQWYLNYgePEWQAQATKILHGMEtFH-EEARNNFEaclNWLH----EYACSRTYGLGTKLP-W-----------DD 587
Cdd:PRK13208 355 T--RQWFIKV--LDLKEELLERGKEIN-WYpEHMRVRLE---NWIEglnwDWCISRQRYFGTPIPvWyckdcghpilpDE 426
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 588 KWL-IESLSDStiyMAFYTVVHLLQGGtFRGEKpgpfgikpsD-----MTGEIwdyiffkeTPLPKKTAIKQEHLavlrr 661
Cdd:PRK13208 427 EDLpVDPTKDE---PPGYKCPQCGSPG-FEGET---------DvmdtwATSSI--------TPLIVTGWERDEDL----- 480
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 662 eFEYWYPMDLRVSGKDLIQNHL--TF--CLYNHAAI-WpndenkwpKGMRVNGHLL-LNSAKMSKSDGNFLTLTEAVDKF 735
Cdd:PRK13208 481 -FEKVFPMDLRPQGHDIIRTWLfyTIlrAYLLTGKLpW--------KNIMISGMVLdPDGKKMSKSKGNVVTPEELLEKY 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 736 SADGMRLCLADA--GDsveDANFVESTADAG------ILRLYTFIewvkEMLENRSSLRKGTDKTFNDQVFLSELNLKTQ 807
Cdd:PRK13208 552 GADAVRYWAASArlGS---DTPFDEKQVKIGrrlltkLWNASRFV----LHFSADPEPDKAEVLEPLDRWILAKLAKVVE 624
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 808 QTDENYRKMLFKEAL---RSGFYE------LQLArdKYReLCGANGMHEDL----VLEF-IRRQALLVSPICPHMAEHVW 873
Cdd:PRK13208 625 KATEALENYDFAKALeeiESFFWHvfcddyLELV--KSR-AYGEDEEEEQKsaryTLYTvLDTLLRLLAPFLPFITEEVW 701
|
970 980 990 1000
....*....|....*....|....*....|....*....|.
gi 28574733 874 GLLGNKeSIVHARWPEVG--AINEVDILCSEYLMEAAHSFR 912
Cdd:PRK13208 702 SWLYGG-SVHRASWPEPDeeLIDEEDEELGELAKEILSAVR 741
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
675-899 |
9.78e-13 |
|
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: 72.07 E-value: 9.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 675 GKDLIqnhltfclYNHAAIWP-----NDENKwPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAGD 749
Cdd:COG0143 289 GKDII--------RFHAIIWPamlmaAGLPL-PKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 750 SVEDANFveSTAD---------AGIL-----RLYTFIEwvKEMlENRssLRKGTDKTFNDQVFLSELNLKTQQTDENYRK 815
Cdd:COG0143 360 FGQDGDF--SWEDfvarvnsdlANDLgnlasRTLSMIH--KYF-DGK--VPEPGELTEADEELLAEAEAALEEVAEAMEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 816 MLFKEALRSGFyEL--------------QLARDKYRELCgANGMHedLVLEFIRRQALLVSPICPHMAEHVWGLLG---N 878
Cdd:COG0143 433 FEFRKALEEIM-ALaraankyidetapwKLAKDEDPERL-ATVLY--TLLEALRILAILLKPFLPETAEKILEQLGlegD 508
|
250 260
....*....|....*....|...
gi 28574733 879 KESIVHARWP-EVG-AINEVDIL 899
Cdd:COG0143 509 ELTWEDAGWPlPAGhKIGKPEPL 531
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
795-925 |
1.48e-12 |
|
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: 66.27 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 795 DQVFLSELNLKTQQTDENYRKMLFKEALRSGFYELQLAR-DKYRELC-------GANGMHEDLVLEFIRRQALLVSPICP 866
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLsDWYLELIkdrlygeEPDSRAQTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 867 HMAEHVWgllgNKESIVHARWPEVGAINEVDILCS-EYLMEAAHSFRlNLKNLLQIKGKA 925
Cdd:pfam08264 81 FITEELW----QKESIHLAPWPEDAELEEAELEEAfELRQEIVQAIR-KLRSELKIKKSL 135
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
708-890 |
3.10e-12 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 71.24 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 708 NGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCL------------ADAGdsVEDAN-FVEstadagilRLYTFIEW 774
Cdd:COG0495 580 DGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEmfagpperdlewSDSG--VEGAYrFLN--------RVWRLVVD 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 775 VKEMLENRSSLRKGTDKtfndqvflsELNLKTQQT----DENYRKMLFKEALrSGFYELQLARDKYRELCGANGmheDLV 850
Cdd:COG0495 650 EAEALKLDVADLSEADK---------ELRRALHKTikkvTEDIERLRFNTAI-AALMELVNALYKAKDSGEADR---AVL 716
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 28574733 851 LEFIRRQALLVSPICPHMAEHVWGLLGNKESIVHARWPEV 890
Cdd:COG0495 717 REALETLVLLLAPFAPHIAEELWERLGHEGSVADAPWPEA 756
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
659-882 |
1.62e-10 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 64.90 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 659 LRREFEYWYPMDLRVSGKDliqnhltfCLYNHAAIWP----NDENKWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDK 734
Cdd:PRK11893 245 LAELFNKYWPADVHLIGKD--------ILRFHAVYWPaflmAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 735 FSADGMRLCLADagDSVE--DANFVEstaDAgilrlytFIEWVKEMLEN-------RSS----------LRKGTDKTFND 795
Cdd:PRK11893 317 YGVDAVRYFLLR--EIPFgqDGDFSR---EA-------FINRINADLANdlgnlaqRTLsmiaknfdgkVPEPGALTEAD 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 796 QVFLSELNLKTQQTDENYRKMLFKEALrsgFYELQLARDkyrelcgANG-----------------MHEDL--VLEFIRR 856
Cdd:PRK11893 385 EALLEAAAALLERVRAAMDNLAFDKAL---EAILALVRA-------ANKyideqapwslaktdperLATVLytLLEVLRG 454
|
250 260
....*....|....*....|....*.
gi 28574733 857 QALLVSPICPHMAEHVWGLLGNKESI 882
Cdd:PRK11893 455 IAVLLQPVMPELAAKILDQLGVEEDE 480
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
16-98 |
9.64e-10 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 63.15 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 16 QKIEREVQQRWEAERVHEsdAPTAPKKrqaEKFFVTFPFPYMNGRLHLGHTFSlskaeYSM-----RYHRLKGRRVLWPF 90
Cdd:COG0495 8 KEIEKKWQKYWEENGTFK--ADEDSSK---PKYYVLDMFPYPSGRLHMGHVRN-----YTIgdvvaRYKRMQGYNVLHPM 77
|
....*...
gi 28574733 91 GFHCTGMP 98
Cdd:COG0495 78 GWDAFGLP 85
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
46-246 |
9.91e-10 |
|
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: 61.88 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 46 EKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPikacadkltreleqfgfppqfpeTEEV 125
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA-----------------------TQVV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 126 VpvaaeaasevpkdkskgkkSKAVAKTGAAKYQ----------WQImqslglKDEEIKDFANAehwlnyfpplavqdLKR 195
Cdd:cd00817 58 V-------------------EKKLGIEGKTRHDlgreeflekcWEW------KEESGGKIREQ--------------LKR 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574733 196 IGVHVDWRRTFITTDANPYF---DSFVRwqfnhLKERGKIMYGKRYTIYSPKDG 246
Cdd:cd00817 99 LGASVDWSREYFTMDPGLSRavqEAFVR-----LYEKGLIYRDNRLVNWCPKLR 147
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
675-880 |
5.10e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 60.55 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 675 GKDLIqnhltfclYNHAAIWP-----NDENKwPKGMRVNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLA-DAG 748
Cdd:PRK00133 291 GKDII--------YFHTLFWPamlegAGYRL-PTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAaKLP 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 749 DSVEDANFveSTAD---------AGIL-----RLYTFIEwvkemlenrsslRKGTDK---TFNDQVFLSELNLKTQQTDE 811
Cdd:PRK00133 362 ETIDDLDF--NWEDfqqrvnselVGKVvnfasRTAGFIN------------KRFDGKlpdALADPELLEEFEAAAEKIAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 812 NYRKMLFKEALRSGfyeLQLAR--DKY-----------------RELCgANGmhedlvLEFIRRQALLVSPICPHMAEHV 872
Cdd:PRK00133 428 AYEAREFRKALREI---MALADfaNKYvddnepwklakqdgerlQAVC-SVG------LNLFRALAIYLKPVLPELAERA 497
|
....*...
gi 28574733 873 WGLLGNKE 880
Cdd:PRK00133 498 EAFLNLEE 505
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
15-425 |
9.43e-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: 59.71 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 15 LQKIEREVQQRWEAERVHEsdaptapKKRQA----EKFfvTF---PfPYMNGRLHLGHTfsLSKaeYS----MRYHRLKG 83
Cdd:COG0060 18 LPKREPEILKFWEENDIYE-------KSREAragrPKF--VLhdgP-PYANGDIHIGHA--LNK--ILkdiiVRYKTMRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 84 RRVLWPFGFHCTGMPIkacadkltrEleqfgfppqfpeteevvpvaaeaasevpkdkskgkkskavaktgaakyqWQIMQ 163
Cdd:COG0060 84 FDVPYVPGWDCHGLPI---------E-------------------------------------------------LKVEK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 164 SLGLKDEEIKDF----------ANAEHWLNyfpplaVQ--DLKRIGVHVDWrrtfittdANPYF---DSF---VRWQFNH 225
Cdd:COG0060 106 ELGIKKKDIEKVgiaefrekcrEYALKYVD------EQreDFKRLGVWGDW--------DNPYLtmdPEYeesIWWALKK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 226 LKERGKIMYGKRYTIYSPKDGQPCMDH-----DRSSgegvgPQEYtlIKMKVLEVPKALssIKQPIFMVAATlrpetmyg 300
Cdd:COG0060 172 LYEKGLLYKGLKPVPWCPRCGTALAEAeveykDVTS-----PSIY--VKFPVKDEKALL--LLEDAYLVIWT-------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 301 qTNCW---------LHPDIKYIAWQANKNNEVWVSTRRAARNMTYQGFTAVEgeikVLAEVTGQDLLGVPLSAPLT---- 367
Cdd:COG0060 235 -TTPWtlpanlavaVHPDIDYVLVEVTGGERLILAEALVEAVLKELGIEDYE----VLATFKGAELEGLRYEHPFYyvvg 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574733 368 ---KHKVV---YslpmlsIKEDKGTGVVTSVPSDSPDDYAALvdlqkkeafrQKYGLkdEMVLP 425
Cdd:COG0060 310 ydrAHPVIlgdY------VTTEDGTGIVHTAPGHGEDDFEVG----------KKYGL--PVLNP 355
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
717-889 |
1.75e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 59.07 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 717 KMSKSDGNFLTLTEAVDKFSADGMRLCLADAGdSVEDANFVESTADAGILRlytFIEWVKEMLE----NRSSLRKGTDKT 792
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRLYEMFMG-PLRDSKTWSTSGVEGVHR---FLGRTWRLVVgaplPDGSFRDGTVVT 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 793 FN--DQVFLSELNLKTQQTDENYRKMLFKEALrSGFYELQLARDKYrelcgangmhEDLVLEFIRRQALLVSPICPHMAE 870
Cdd:PLN02563 799 DEepSLEQLRLLHKCIAKVTEEIESTRFNTAI-SAMMEFTNAAYKW----------DKVPREAIEPFVLLLSPYAPHLAE 867
|
170
....*....|....*....
gi 28574733 871 HVWGLLGNKESIVHARWPE 889
Cdd:PLN02563 868 ELWFRLGHSNSLAYEPWPE 886
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
696-812 |
2.92e-08 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 58.12 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 696 NDENKWpkgmrVN-----GHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMR-LCLADAGDSVedANFVESTADAGILRLY 769
Cdd:PTZ00399 294 FDKHQW-----VNyflhsGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRlLFLLHKWDKP--MNYSDESMDEAIEKDK 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 28574733 770 TFIEW---VKEMLenRSSLRKGTDKTFNDQVflsELNLKTQQTDEN 812
Cdd:PTZ00399 367 VFFNFfanVKIKL--RESELTSPQKWTQHDF---ELNELFEETKSA 407
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
661-756 |
6.07e-08 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 56.53 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 661 REFEYWYPMDLRVS-----GKDLIqnhltfclYNHAAIWP---NDEN-KWPKGMRVNGHLLLNSAKMSKSDGNFLTLTEA 731
Cdd:pfam09334 267 EKWKEWWPNDPDTElvhfiGKDII--------YFHTIFWPamlLGAGyRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEA 338
|
90 100
....*....|....*....|....*
gi 28574733 732 VDKFSADGMRLCLADAGDSVEDANF 756
Cdd:pfam09334 339 LDRFPPDALRYYLARNRPETKDTDF 363
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
19-401 |
2.10e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 55.33 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 19 EREVQQRWEAERVHESDAptapkKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMP 98
Cdd:PLN02943 66 EERIYNWWESQGYFKPNF-----DRGGDPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 99 IKACADKLtreleqfgfppqfpeteevvpVAAEAASEVPkdkskgkkskaVAKTGAAKYQWQimqslglkdeeikdfana 178
Cdd:PLN02943 141 TQLVVEKM---------------------LASEGIKRTD-----------LGRDEFTKRVWE------------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 179 ehWLNYFPPLAVQDLKRIGVHVDWRRTFITTD---ANPYFDSFVRwqfnhLKERGKIMYGKRYTIYSPKDGQPCMDHDrs 255
Cdd:PLN02943 171 --WKEKYGGTITNQIKRLGASCDWSRERFTLDeqlSRAVVEAFVR-----LHEKGLIYQGSYMVNWSPNLQTAVSDLE-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 256 sgegvgpQEYTlikmkvlEVPKALSSIKQPI------FMVAATLRPETMYGQTNCWLHPDIKyiawqanknnevwvstrr 329
Cdd:PLN02943 242 -------VEYS-------EEPGTLYYIKYRVaggsedFLTIATTRPETLFGDVAIAVNPEDD------------------ 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574733 330 aaRNMTYQGFTAVegeikvlaevtgqdllgVPLSAplTKHkvvysLPMLS---IKEDKGTGVVTSVPSDSPDDYA 401
Cdd:PLN02943 290 --RYSKYIGKMAI-----------------VPMTY--GRH-----VPIIAdryVDKDFGTGVLKISPGHDHNDYL 338
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
708-781 |
6.26e-07 |
|
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: 53.57 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 708 NGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGMRLCLADAG---------DSVEDanfvestADAGILRLYTFIEWVKEM 778
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHyrspldfseEALEE-------AEKALERLYNALRRLEEA 328
|
...
gi 28574733 779 LEN 781
Cdd:COG0215 329 LGA 331
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
55-237 |
3.49e-06 |
|
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: 50.69 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 55 PYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMPIKACADKltreleQFGFPpqfpeteevvpvaaeaas 134
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEK------ELGIS------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 135 evpkdkskgkKSKAVAKTGAAKYQwqimqslglkdEEIKDFA--NAEHWLNYFpplavqdlKRIGVHVDWRRTFITTDan 212
Cdd:cd00818 66 ----------GKKDIEKMGIAEFN-----------AKCREFAlrYVDEQEEQF--------QRLGVWVDWENPYKTMD-- 114
|
170 180
....*....|....*....|....*
gi 28574733 213 PYFDSFVRWQFNHLKERGKIMYGKR 237
Cdd:cd00818 115 PEYMESVWWVFKQLHEKGLLYRGYK 139
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
19-99 |
4.94e-06 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 50.93 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 19 EREVQQRWEAERVHEsdapTAPKKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHCTGMP 98
Cdd:PLN02843 9 EPEIQKLWEENQVYK----RVSDRNNGESFTLHDGPPYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLP 84
|
.
gi 28574733 99 I 99
Cdd:PLN02843 85 I 85
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
36-88 |
1.16e-05 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 49.62 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 28574733 36 APTAPKKRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLW 88
Cdd:PTZ00419 50 AEDAKSLNSGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLW 102
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
48-113 |
2.42e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 48.06 E-value: 2.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574733 48 FFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLwpfgfHCTGM-----PIKACADKLTRELEQF 113
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVL-----FVCGTdehgtPIELKAEKEGITPEEL 66
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
669-742 |
3.00e-05 |
|
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: 46.42 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 669 MDLRVSGKDLIQNH------LTFCLYNH--AAIWpndenkwpkgMRvNGHLLLNSAKMSKSDGNFLTLTEAVDKFSADGM 740
Cdd:cd00672 129 FDIHGGGVDLIFPHheneiaQSEAATGKpfARYW----------LH-TGHLTIDGEKMSKSLGNFITVRDALKKYDPEVL 197
|
..
gi 28574733 741 RL 742
Cdd:cd00672 198 RL 199
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
20-895 |
3.85e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 48.06 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 20 REVQQRWEA---ER--VHESDAPtapkkRQAEKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHC 94
Cdd:PRK14900 22 REVEARWYPfwqERgyFHGDEHD-----RTRPPFSIVLPPPNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLPGTDH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 95 TGMPIKACADKltrELEQfgfppqfpeteevvpvaAEAASEvpkdkskgkksKAVAKTGAAKYQWQIMQSLGLKDEEikd 174
Cdd:PRK14900 97 AGIATQMIVEK---ELKK-----------------TEKKSR-----------HDLGREAFLERVWAWKEQYGSRIGE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 175 fanaEHwlnyfpplavqdlKRIGVHVDWRRTFITTDANpyFDSFVRWQFNHLKERGKIMYGKRYTIYSPKdgqpCmdHDR 254
Cdd:PRK14900 143 ----QH-------------KALGASLDWQRERFTMDEG--LSRAVREVFVRLHEEGLIYREKKLINWCPD----C--RTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 255 SSGEGVGPQEYTlikmkvlevPKALSSIKQPIF-----MVAATLRPETMYGQTNCWLHP-DIKYiawqanknnevwvstr 328
Cdd:PRK14900 198 LSDLEVEHEEAH---------QGELWSFAYPLAdgsgeIVVATTRPETMLGDTAVAVHPlDPRY---------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 329 raarnmtyqgftavegeikvlaevtgQDLLGVPLSAPLTKHKVVYSLPMLSIKEDKGTGVVTSVPSDSPDDYaalvdlqk 408
Cdd:PRK14900 253 --------------------------MALHGKKVRHPITGRTFPIVADAILVDPKFGTGAVKVTPAHDFNDF-------- 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 409 keafrqKYGLKdemvlpyepipiievptlgklsavHAYETLKIqsqndkdkLAEAKEMCYLKSFYDGvmlVGAFAGRKiq 488
Cdd:PRK14900 299 ------EVGKR------------------------HGLEMITV--------IGPDGRMTAEAGPLAG---LDRFEARK-- 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 489 DVKKDLQKRLVDANEadvyyEPEKTIMSRSADECVVA---LCNQWYLNYgEPEWQAQATKILHGMETF-HEEARNNFEAC 564
Cdd:PRK14900 336 EVKRLLAEQGLDRGA-----KPHVLPLGRCQRSATILeplLSDQWYVRI-EPLARPAIEAVEQGRTRFiPEQWTNTYMAW 409
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 565 LNWLHEYACSRTYGLGTKLPwddKWLIeslSDSTIYMAFYT--VVHLLQGGTFRGEKpgpfGIKPSDMTGEIWDyifFKE 642
Cdd:PRK14900 410 MRNIHDWCISRQLWWGHQIP---AWYC---PDGHVTVARETpeACSTCGKAELRQDE----DVLDTWFSSGLWP---FST 476
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 643 TPLPKKTAikqehlavlrrEFEYWYPMDLRVSGKDLI--------------QNHLTF-CLYNHAAIwpNDEnkwpKGmrv 707
Cdd:PRK14900 477 MGWPEQTD-----------TLRTFYPTSVMETGHDIIffwvarmmmmglhfMGEVPFrTVYLHPMV--RDE----KG--- 536
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 708 nghlllnsAKMSKSDGNFLTLTEAVDKFSADGMRLCLAD----------AGDSVEDAN-FVESTADAGILRLYTFIEWVK 776
Cdd:PRK14900 537 --------QKMSKTKGNVIDPLVITEQYGADALRFTLAAltaqgrdiklAKERIEGYRaFANKLWNASRFALMNLSGYQE 608
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 777 EMLENRSSLRkgtdkTFNDQVFLSELNLKTQQTDENYRKMLFKEALRSGF---------YELQLARDK-YRELCGANGMH 846
Cdd:PRK14900 609 RGEDPARLAR-----TPADRWILARLQRAVNETVEALEAFRFNDAANAVYafvwhelcdWYIELAKEAlASEDPEARRSV 683
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574733 847 EDLVLEFIRRQALLVSPICPHMAEHVWGLL-------GNKESIVHARWPEVGAINE 895
Cdd:PRK14900 684 QAVLVHCLQTSYRLLHPFMPFITEELWHVLraqvgasAWADSVLAAEYPRKGEADE 739
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
46-87 |
1.80e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 45.64 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 28574733 46 EKFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRVL 87
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVF 42
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
17-98 |
2.74e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 45.20 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 17 KIEREVQQRWEAERV-HESDAPTAPKKrqaeKFFVTFPFPYMNGR-LHLGHTFSLSKAEYSMRYHRLKGRRVLWPFGFHC 94
Cdd:PLN02563 84 EIEPKWQRYWEENRTfRTPDDVDTSKP----KFYVLDMFPYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDA 159
|
....
gi 28574733 95 TGMP 98
Cdd:PLN02563 160 FGLP 163
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
662-756 |
4.17e-04 |
|
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: 44.16 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 662 EFEYWYPMDLRVSGKDLIQnhltFclynhaaiwpndenkWPKGMRVNGHLLLNSA-----------------KMSKSDGN 724
Cdd:cd00817 290 DLKKFYPTSLLVTGHDIIF----F---------------WVARMIMRGLKLTGKLpfkevylhglvrdedgrKMSKSLGN 350
|
90 100 110
....*....|....*....|....*....|..
gi 28574733 725 FLTLTEAVDKFSADGMRLCLADAGDSVEDANF 756
Cdd:cd00817 351 VIDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
47-86 |
9.17e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 43.25 E-value: 9.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 28574733 47 KFFVTFPFPYMNGRLHLGHTFSLSKAEYSMRYHRLKGRRV 86
Cdd:PRK12267 5 TFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDV 44
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
667-747 |
1.76e-03 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 41.97 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 667 YPMDLRVSGKDLIQNH------LTFCLYNH--AAIWPNdenkwpkgmrvNGHLLLNSAKMSKSDGNFLTLTEAVDKFSAD 738
Cdd:pfam01406 206 DQIDIHGGGIDLAFPHheneiaQSEAAFDKqlANYWLH-----------NGHVMIDGEKMSKSLGNFFTIRDVLKRYDPE 274
|
....*....
gi 28574733 739 GMRLCLADA 747
Cdd:pfam01406 275 ILRYFLLSV 283
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
16-88 |
4.95e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 41.24 E-value: 4.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574733 16 QKIEREVQQRWEAERVHESDAPTApkkrqaEKFFVTFPFPYMNGRLHLGHTF------SLskaeysMRYHRLKGRRVLW 88
Cdd:PRK05729 12 KEVEAKWYQKWEEKGYFKPDDNSK------KPFSIVIPPPNVTGSLHMGHALnntlqdIL------IRYKRMQGYNTLW 78
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
795-890 |
5.31e-03 |
|
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: 39.43 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574733 795 DQVFLSELNLKTQQTDENYRKMLFKEALR----------SGFYeLQLARDK-YrelCGANGMHEdlvlefiRRQAL---- 859
Cdd:cd07960 46 DRYALHRLNELIKEVREAYENYEFHKVYQalnnfctvdlSAFY-LDIIKDRlY---CDAKDSLE-------RRSAQtvly 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 28574733 860 --------LVSPICPHMAEHVWGLLG---NKESIVHARWPEV 890
Cdd:cd07960 115 hildallkLLAPILPFTAEEVWEHLPgekKEESVFLEDWPEL 156
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
16-88 |
7.28e-03 |
|
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: 40.42 E-value: 7.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574733 16 QKIEREVQQRWEAERVHESDAptAPKKrqaEKFFVTFPFPYMNGRLHLGHTF------SLskaeysMRYHRLKGRRVLW 88
Cdd:COG0525 10 KEVEAKWYQYWEENGYFKADP--DSDK---EPFTIVIPPPNVTGSLHMGHALnntlqdIL------IRYKRMQGYNTLW 77
|
|
| |
