|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
1-1083 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 2322.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 1 MEGSKSFARRDRLLEIEVKVRNWWEEKDVFRAEAGEKPPEPGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRG 80
Cdd:PLN02959 3 AEGGKSTARRDRLLEIEVAVQKWWEEEKVFEAEAGDEPPKPGEKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 81 ANVLLPFGFHCTGMPIKASADKLAWEIQQFGDPPVFPTEVEEQPGEEPEPEDPNGGAPALPDKFKGKKSKAASKSSGQMY 160
Cdd:PLN02959 83 ANVLLPFAFHCTGMPIKASADKLAREIQQYGNPPVFPEEDEDEAAAVAAAKAEAEAAAAPPDKFKGKKSKAVAKSGTQKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 161 QWEIMRSFGLSDSEISKFQNPYNWLSFFPPLAMEDLKAFGLGCDWRRSFITTDMNPYYDNFIKWQMRKLKAIGKIVKDVR 240
Cdd:PLN02959 163 QWEIMRSFGLPDSEIAKFQDPYHWLSYFPPLAKEDLKAFGLGCDWRRSFITTDVNPYYDAFVRWQFRKLKKKGKIVKDKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 241 YTIYSPLDGQPCADHDRASGEGVQPQEYTLIKMEVVSPYPPKLSSLEGKKVYLAAATLRPETMYGQTNAWVLPDGKYGAF 320
Cdd:PLN02959 243 YTIYSPLDGQPCADHDRASGEGVGPQEYVLIKMEVLPPFPGKLKALEGKKVFLAAATLRPETMYGQTNCWVLPDGKYGAY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 321 EINDDEVFIITQRAALNLAYQNFSKVPEKPTCLVELTGYDLIGLPLKSPLSFNEIIYSLPMLSILTDKGTGIVTSVPSDA 400
Cdd:PLN02959 323 EINDTEVFILTARAALNLAYQNFSKVPGKPTCLVELTGYDLIGLPLKSPLAFNEVIYALPMLTILTDKGTGVVTSVPSDS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 401 PDDYMALHDLKSKPAFRAKYGVKDEWIMPFEIIPIIDIPEYGDRSAEKVCNDLKIKSQNEKEKLAEAKRLTYLRGFTEGT 480
Cdd:PLN02959 403 PDDYMALSDLKAKPALRAKYGVKDEWVLPFEVVPIINIPEFGDKSAEKVCEDLKIKSQNDKEKLAEAKRLTYLKGFTDGT 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 481 MLVGEFAGRKVQEAKPLIRSKLIEIGQAIVYSEPEKRVMSRSGDECVVALTDQWYIIYGEPEWKKLAEDCLSNMNLYSDE 560
Cdd:PLN02959 483 MLVGEYAGRKVQEAKPLIKKKLIEAGQAILYSEPEKKVMSRSGDECVVALTDQWYLTYGEEEWKKKAEKCLSKMNLYSDE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 561 TRHGFEHTLSWLNQWACSRSFGLGTRFPWDEEFLVESLSDSTIYMAYYTVAHILQNGDLYGSGTSSVKPEQMTDEVWDFL 640
Cdd:PLN02959 563 TRHGFEHTLGWLNQWACSRSFGLGTRIPWDEQFLIESLSDSTIYMAYYTVAHLLQGGDMYGKDKSSIKPEQMTDEVWDFV 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 641 FSGGPYPTSSDIPSSILNKMKQEFEYWYPFDLRVSGKDLIQNHLTFCIYNHTAIMSKNHWPRGFRCNGHIMLNSEKMSKS 720
Cdd:PLN02959 643 FCGGPLPKSSDIPAELLEKMKQEFEYWYPFDLRVSGKDLIQNHLTFAIYNHTAIWAEEHWPRGFRCNGHLMLNSEKMSKS 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 721 TGNFRTLRQAIEEFSADATRFSLADAGDGVDDANFVFETANAAILRLTKELSWMEEVLEAEASLRTGALSTYADQVFANE 800
Cdd:PLN02959 723 TGNFLTLRQAIEEFSADATRFALADAGDGVDDANFVFETANAAILRLTKEIAWMEEVLAAESSLRTGPPSTYADRVFENE 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 801 INIAVTLTEQHYRNCMFREALKTGFYDLQAARDEYRFSCGAGGMNHDLVWRFMDVQTCLITPICPHYAEYVRREILKKDG 880
Cdd:PLN02959 803 INIAIAETEKNYEAMMFREALKSGFYDLQAARDEYRLSCGSGGMNRDLVWRFMDVQTRLITPICPHYAEHVWREILKKEG 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 881 FAVHAGWPTADSPDLTLKAANKYLQDSIVLMRKLLQKQILGSKKANKKGAPVTsLTESNLKGLIYVNEQYDGWKEECLRI 960
Cdd:PLN02959 883 FAVTAGWPVAGEPDLTLKRANKYLQDSIVSFRKLLQKQLAGSKKAKKGGAPVT-LPEKKLAGLIYVAEKYDGWKEECLRI 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 961 LQSKFDSRNRTFAADKEILEALQRSSVGQATNSKQVQKLCMPFLRFKKDEAVALGPQALDLRLPFGEIEVLRGNLDLIKR 1040
Cdd:PLN02959 962 LQSKFDSQSRTFAPDAEILEALKESSVGQEANFKQVQKLCMPFVKFKKDEAIAVGPQALDLKLPFDEIEVLQENLELIKR 1041
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 225465204 1041 QLGLEQVEILSGTDPDALAKAGNLVSLLNQNPPSPGNPTAIFL 1083
Cdd:PLN02959 1042 QLGLEEVEILSASDPDAVAKAGAHASLLKQNPPSPGNPVAIFV 1084
|
|
| leuS_arch |
TIGR00395 |
leucyl-tRNA synthetase, archaeal and cytosolic family; The leucyl-tRNA synthetases belong to ... |
15-1083 |
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: 802.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRAEagekpPEPGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGM 94
Cdd:TIGR00395 2 AIEKKWQKRWEEAHIFEAD-----PDDREKFFLTMAYPYLNGVMHAGHCRTFTIPEVSARFERMKGKNVLFPLGFHVTGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 95 PIKASADKLAWEIQQFGdppvfpteveeqpgeepepedpnggapalpdkfkgkkskaaskssgqmyqWEIMRSFGLSDSE 174
Cdd:TIGR00395 77 PILGLAELIKRRDELTI--------------------------------------------------KNYTEVHAIPREE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 175 ISKFQNPYNWLSFFPPLAMEDLKAFGLGCDWRRSFITTDmnPYYDNFIKWQMRKLKAIGKIVKDVRYTIYSPLDGQPCAD 254
Cdd:TIGR00395 107 LLKFTDPEYIVEYFSREAESACKSMGYSIDWRRSFKTTD--PYYDRFIEWQMNKLKELGLIVKGEHPVRYCPKDGNPVED 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 255 HDRASGEGVQPQEYTLIKMEvvspyppklssLEGKKVYLAAATLRPETMYGQTNAWVLPDGKYGAFEInDDEVFIITQRA 334
Cdd:TIGR00395 185 HDLLSGEGVTIVEYILIKFE-----------LEDGAFYFVAATLRPETVYGVTNCWVNPTITYVIAEV-GGEKWITSKEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 335 ALNLAYQnfsKVPEKPtcLVELTGYDLIGLPLKSPLSFNEIIYsLPMLSILTDKGTGIVTSVPSDAPDDYMALHDLKSKP 414
Cdd:TIGR00395 253 FENLSYQ---KLKYKP--IEEVPGKQFIGKKVHNPVVGPEVPI-LPAEFVDTTKGTGVVMSVPAHAPDDYIALEDLLHDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 415 AFrakYGVKDEWImPFEIIPIIDIPEYGDRSAEKVCNDLKIKSQNEKEKLAEAKRLTYLRGFTEGTMLVG--EFAGRKVQ 492
Cdd:TIGR00395 327 EY---LGIKPVVI-DIEPVPLIHTDGYGDLPAKEIVEEKGIKSQKDKNLLEEATKILYKEEYHTGVMIYNipPYKGMKVS 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 493 EAKPLIRSKLIEIGQAIVYSEP-EKRVMSRSGDECVV-ALTDQWYIIYGEPEWKKLAEDCLSNMNLYSDETRHGFEHTLS 570
Cdd:TIGR00395 403 EAKEKVKADLIDAGLADVMYEFsESPVICRCGTDCIVkVVEDQWFVKYSDESWKELAHECLEGMRIIPEEVKNAFEGKID 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 571 WLNQWACSRSFGLGTRFPWDEEFLVESLSDSTIYMAYYTVAHILQNGDLygsgtssvKPEQMTDEVWDFLFSGGPYPTSS 650
Cdd:TIGR00395 483 WLKDWACCRRYGLGTRLPWDEKWLIESLSDSTIYMAYYTIAHYLNKDYY--------GNEQMTDEFFDYIFLGKGDVKNT 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 651 DIPSSILNKMKQEFEYWYPFDLRVSGKDLIQNHLTFCIYNHTAIMSKNHWPRGFRCNGHIMLNSEKMSKSTGNFRTLRQA 730
Cdd:TIGR00395 555 NIPLPAIQKLRREFEYWYPLDWRISGKDLIPNHLTFYIFHHVAIFPEKFWPRGIVVNGYVMLEGKKMSKSKGNVLTLEQA 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 731 IEEFSADATRFSLADAGDGVDDANFVFETANAAILRLTKELSWMEEVLEaEASLRTGALSTYADQVFANEINIAVTLTEQ 810
Cdd:TIGR00395 635 VEKFGADVARLYIADAAETVQDADWKESEVEGTILRLERLYEFAEEITK-ESNLETGEETSFIDRWLESRMNAAIKETYE 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 811 HYRNCMFREALKTGFYDLQAARDEYRFScgAGGMNHDLVWRFMDVQTCLITPICPHYAEYVrREILKKDGFAVHAGWPTA 890
Cdd:TIGR00395 714 AMENFQTRKAVKYALFDLQADVDWYRRR--GGVNHKDVLARYLETWIKLLAPFAPHFAEEM-WEEVGNEGFVSLAKFPEA 790
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 891 DSP--DLTLKAANKYLQDsivLMRKLLQ-KQILGSKkankkgaPVtsltesnlKGLIYVNEQydgWKEECLRILQSKFds 967
Cdd:TIGR00395 791 SEPavDKEVEAAEEYLRN---LVRDIQEiAKIDASK-------PK--------RVYLYTSED---WKSQCLKIVAELF-- 847
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 968 rnrtfaaDKEILEALqrssvGQATNSKQVQKLCMPFLRFKKDEAVALGPQALDLrlpFGEIEVLRGNLDLIKRQLGLEQV 1047
Cdd:TIGR00395 848 -------GEDTGEDM-----KKVMEEPEERKRGKEVISLVKQIIKDEKKEDELQ---ISEIEVLKAAARFIKKEVGALVI 912
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 225465204 1048 eILSGTDPDALAKAGNLVsllnqnppsPGNPtAIFL 1083
Cdd:TIGR00395 913 -IEFSADSFPENKKRNAV---------PGKP-AIYL 937
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
58-1083 |
0e+00 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 708.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 58 LHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGMPIKASADKLAweiqqFGDPpvfpteveeqpgeepepedpngga 137
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIA-----RGDP------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 138 palpdkfkgkkskaaskssgqmYQWEIMRSF-GLSDSEISKFQNPYNWLSFFPPLAMEDLKAFGLGCDWRRSFITTDmnP 216
Cdd:PRK12300 52 ----------------------ETIELYKSLyGIPEEELEKFKDPEYIVEYFSEEAKEDMKRIGYSIDWRREFTTTD--P 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 217 YYDNFIKWQMRKLKAIGKIVKDVRYTIYSPLDGQPCADHDRASGEGVQPQEYTLIKMEvvspyppklsslEGKKVYLAAA 296
Cdd:PRK12300 108 EYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGDHDLLDGEEPEIVEYTLIKFE------------ESEDLILPAA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 297 TLRPETMYGQTNAWVLPDGKYGAFEInDDEVFIITQRAALNLAYQNFSKVPEKptclvELTGYDLIGLPLKSPLSFNEII 376
Cdd:PRK12300 176 TLRPETIFGVTNLWVNPDATYVKAEV-DGEKWIVSKEAAEKLSFQDRDVEIIE-----EIKGSELIGKKVKNPVTGKEVP 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 377 ySLPMLSILTDKGTGIVTSVPSDAPDDYMALHDLKSKPafrakygvkdEWIMPFEIIPIIDIPEYGDRSAEKVCNDLKIK 456
Cdd:PRK12300 250 -ILPADFVDPDNGTGVVMSVPAHAPYDYVALRDLKKNK----------ELLDVIEPIPLIEVEGYGEFPAKEVVEKLGIK 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 457 SQNEkEKLAEAKRLTYLRGFTEGTML--VGEFAGRKVQEAKPLIRSKLIEIGQAIVYSE-PEKRVMSRSGDECVVA-LTD 532
Cdd:PRK12300 319 SQED-PELEEATKEVYRAEFHKGVLKenTGEYAGKPVREAREKITKDLIEKGIADIMYEfSNRPVYCRCGTECVVKvVKD 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 533 QWYIIYGEPEWKKLAEDCLSNMNLYSDETRHGFEHTLSWLNQWACSRSFGLGTRFPWDEEFLVESLSDSTIYMAYYTVAH 612
Cdd:PRK12300 398 QWFIDYSDPEWKELAHKALDNMEIIPEEYRKEFENTIDWLKDRACARRRGLGTRLPWDEEWIIESLSDSTIYMAYYTIAH 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 613 ILQNGDLygsgtssvKPEQMTDEVWDFLFSG----GPYPTSSDIPSSILNKMKQEFEYWYPFDLRVSGKDLIQNHLTFCI 688
Cdd:PRK12300 478 KIREYGI--------KPEQLTPEFFDYVFLGkgdpEEVSKKTGIPKEILEEMREEFLYWYPVDWRHSGKDLIPNHLTFFI 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 689 YNHTAIMSKNHWPRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSLADAGDGVDDANFVFETANAAILRLT 768
Cdd:PRK12300 550 FNHVAIFPEEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQLE 629
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 769 KELSWMEEVLEAEAslrtGALSTYADQVFANEINIAVTLTEQHYRNCMFREALKTGFYDLQAARDEYRFSCgaGGMNHDL 848
Cdd:PRK12300 630 RFYELAKELIEIGG----EEELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRWYLRRV--GEANNKV 703
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 849 VWRFMDVQTCLITPICPHYAEyvrrEI---LKKDGFAVHAGWPTADSpdltlKAANKYLQDSIVLMRKLLQ--KQILGSK 923
Cdd:PRK12300 704 LREVLEIWIRLLAPFTPHLAE----ELwhkLGGEGFVSLEKWPEPDE-----SKIDEEAELAEEYVKRLIEdiREILKVA 774
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 924 KANKKgapvtsltesnlKGLIYVNEQydgWKEECLRILQSKFDSRNrtfaADKEILEALQRSSVGQATnSKQVQKLcmpf 1003
Cdd:PRK12300 775 KIKPK------------KVYIYVAPD---WKYEVLEIAAENGDVKE----AIKELMKDEELRKHGKEV-AKLAQKI---- 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 1004 lrfkKDEAVALGPQALDLR-LPFGEIEVLRGNLDLIKRQLGLEqVEILSGTDPDALAKAGNLVsllnqnppsPGNPtAIF 1082
Cdd:PRK12300 831 ----VKEVLKLDKEVRKLIlKNIDEEEVLEEAKDFLEKELGVE-VEIYGADDPGKKKKKKKAL---------PLKP-AIY 895
|
.
gi 225465204 1083 L 1083
Cdd:PRK12300 896 I 896
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
529-757 |
6.36e-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: 236.38 E-value: 6.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 529 ALTDQWYIIYGEPEWKKLAEDCLSNMNLYSDETRHGFEHTLSwlnqwaCSRSFGLGTRFPWdeEFLVESLSDSTIYMAYY 608
Cdd:cd00812 127 KLLDQWFLKYSETEWKEKLLKDLEKLDGWPEEVRAMQENWIG------CSRQRYWGTPIPW--TDTMESLSDSTWYYARY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 609 TVAHILQNGDLYgsgtssvkpeqmtdevwdflfsggpyptssdipssILNKMKQEFEYWYPFDLRVSGKDLIQNHLTFCI 688
Cdd:cd00812 199 TDAHNLEQPYEG-----------------------------------DLEFDREEFEYWYPVDIYIGGKEHAPNHLLYSR 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225465204 689 YNHTAIMSKNH----WPRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSLADAGDgvDDANFVF 757
Cdd:cd00812 244 FNHKALFDEGLvtdePPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAP--PDADFDW 314
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
755-875 |
1.45e-36 |
|
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: 133.87 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 755 FVFETANAAILRLTKELSWMEEVLEAEASLrtgALSTYADQVFANEINIAVTLTEQHYRNCMFREALKTGFYDLQAARDE 834
Cdd:cd07959 1 FREEEANSAILRLERFYELAEELIETEGEL---EELTFIDRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLDW 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 225465204 835 YRFSCGAgGMNHDLVWRFMDVQTCLITPICPHYAEYVRREI 875
Cdd:cd07959 78 YRERGGA-GMNKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
23-755 |
1.10e-27 |
|
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: 119.82 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 23 WWEEKDVFRAEAGEKPPEPgeKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGMPIKASADK 102
Cdd:pfam00133 5 FWDEQGYFKPELEKRKGKP--SFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 103 LAWEiqqfgdppvfpteveeqpgeEPEPEDPNGGAPALPDKFkgkkskaaskssgqmyqWEIMRSFGlsdSEISKfqnpy 182
Cdd:pfam00133 83 KLGI--------------------KEKKTRHKYGREEFREKC-----------------REWKMEYA---DEIRK----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 183 nwlsffpplameDLKAFGLGCDWRRSFITtdMNPYYDNFIKWQMRKLKAIGKIVKDVRYTIYSPLDGQPCADHDrasgeg 262
Cdd:pfam00133 118 ------------QFRRLGRSIDWDREYFT--MDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLE------ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 263 vqpQEYTlikmEVVSP-----YPPKlsslEGKKVYLAAATLRPETMYGQTNAWVLPDGKYGAfeinDDEVFIITQRAALN 337
Cdd:pfam00133 178 ---VEYK----DVKGPsihvaFPLA----DDEGASLVIWTTTPWTLPGNTAVAVNPEFDYVI----TGEGYILAEALLKS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 338 LAyqnfsKVPEKPTCLVELTGYDLIGLPLKSPLSFNEIiyslPMLS---ILTDKGTGIVTSVPSDAPDDYMAlhdlkskp 414
Cdd:pfam00133 243 LY-----KKGTDKKILEDFRGKELEGKEAIHPFVNREI----PIITddyVDMEFGTGAVHIAPAHGENDYEV-------- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 415 afRAKYGVkdEWIMPfeiipiidipeygdrsaekvcndlkiksqnekeklaeakrLTYLRGFTEGtmlVGEFAGRKVQEA 494
Cdd:pfam00133 306 --GQRHNL--EVINP----------------------------------------VDDDGTFTEE---APDFQGVYRFDA 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 495 KPLIRSKLIEIGqaiVYSEPEKRVMS-----RSGDECVVALTDQWYIiygepEWKKLAEDCL-SNMNLY----SDETRhg 564
Cdd:pfam00133 339 RKKIVELLTEKG---LLLKIEPFTHSypfcwRSGTPIIPRATPQWFV-----RMDELADQALeAVEKVQfvpkSGEKR-- 408
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 565 FEHTLSWLNQWACSRSFGLGTRFP-W-DEEFLVESLSDSTIYMAYYTVAHILQNGDLYGSGTSSVKPEQMT----DEVWD 638
Cdd:pfam00133 409 YFNWLANIQDWCISRQRWWGHPIPaWvSKDTEEVVCRGELFELVAGRFEEEGSIKWLHREAKDKLGYGKGTleqdEDVLD 488
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 639 FLFSGGPYPTSS-DIPssilNKMKQEFEYWYPFDLRVSGKDLIQNHLTFCIYNHTAIMSKNHWpRGFRCNGhIMLNSE-- 715
Cdd:pfam00133 489 TWFSSGSWPFSTlGWP----FVNTEEFKKFFPADMLLEGSDQTRGWFYRMIMLSTALTGSVPF-KNVLVHG-LVRDEQgr 562
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 225465204 716 KMSKSTGNFRTLRQAIEEFSADATRFSLADAgDGVDDANF 755
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
44-244 |
2.05e-25 |
|
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: 108.10 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 44 KFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGMPIKASADKLAweiqqfgdppvfpteveeq 123
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 124 pgeepepedpnggapalpdkfkgkkskaaskssgqmyqweimrsfglsdseiskfQNPYNWLSFFPPLAMEDLKAFGLGC 203
Cdd:cd00812 62 -------------------------------------------------------RDPEDWTEYNIKKMKEQLKRMGFSY 86
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 225465204 204 DWRRSFITTDmnPYYDNFIKWQMRKLKAIGKIVKD---VRYTIY 244
Cdd:cd00812 87 DWRREFTTCD--PEYYKFTQWLFLKLYEKGLAYKKeapVNWCKL 128
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
524-755 |
2.42e-24 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 104.81 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 524 DECVVALTDQWYIIYgePEWKKLAEDCLSNMNLYSDETRHGFEHTLSWLNQWACSRSFGLGTRFPwdeEFLVESLSDSTI 603
Cdd:cd00668 132 GTHPVRITEQWFFDM--PKFKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLP---EDVFDVWFDSGI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 604 YMAYYTVahilqngdlygsgtssvkpeqmtdevwdflfsggpYPtssdipssilnKMKQEFEYWYPFDLRVSGKDLIQNH 683
Cdd:cd00668 207 GPLGSLG-----------------------------------YP-----------EEKEWFKDSYPADWHLIGKDILRGW 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225465204 684 LTFCIYNHTAIMSKnHWPRGFRCNGHIMLN-SEKMSKSTGNFRTLRQAIEEFSADATRFSLADAGDGVDDANF 755
Cdd:cd00668 241 ANFWITMLVALFGE-IPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
15-948 |
3.04e-22 |
|
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: 103.60 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRAEagekPPEPGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGM 94
Cdd:TIGR00422 9 EVEKKWYKKWEKSGFFKPD----GNSNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 95 PIKASADKLAW-EIQQFGDPPvfpteveeqpgeepepedpnggapalPDKFKGKKskaaskssgqmyqWEimrsfgLSDS 173
Cdd:TIGR00422 85 ATQVKVEKKLGaEGKTKHDLG--------------------------REEFREKI-------------WE------WKEE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 174 EISKFQNpynwlsffpplameDLKAFGLGCDWRRSFITtdMNPYYDNFIKWQMRKLKAIGKIVKDVRYTIYSPLDGQPCA 253
Cdd:TIGR00422 120 SGGTIKN--------------QIKRLGASLDWSRERFT--MDEGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAIS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 254 DhdrasgegvqpqeytlikMEVVspYPPKLSSL--------EGKKVYLAAATLRPETMYGQTNAWVLPdgkygafeinDD 325
Cdd:TIGR00422 184 D------------------IEVE--YKEVKGKLyyiryplaNGSKDYLVVATTRPETMFGDTAVAVHP----------ED 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 326 EvfiitqraalnlAYQNfskvpekptclveltgydLIGLPLKSPLSFNEIiyslpmlSILTD------KGTGIVTSVPSD 399
Cdd:TIGR00422 234 E------------RYKH------------------LIGKKVILPLTGRKI-------PIIADeyvdmeFGTGAVKVTPAH 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 400 APDDYmalhdlkskpafrakygvkdEWimpfeiipiidipeyGDRSaekvcNDLKIKSQNEKEKLAEAkrltylrgfteg 479
Cdd:TIGR00422 277 DFNDY--------------------EW---------------GKRH-----NLEFINILDEDGLLNEN------------ 304
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 480 tmlVGEFAGRKVQEAkpliRSKLIEIGQA---IVYSEPEKR---VMSRSGDECVVALTDQWYIiyGEPEWKKLAEDCLSN 553
Cdd:TIGR00422 305 ---AGKYQGLTRFEA----RKKIVEDLKEeglLVKIEPHTHnvgTCWRSGTVVEPLLSKQWFV--KVEKLADKALEAAEE 375
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 554 --MNLYSDEtrhgFEHTL-SWLNQ---WACSRSFGLGTRFPwdeeflveslsdstiymAYYTVahilQNGDLYGSGT--- 624
Cdd:TIGR00422 376 geIKFVPKR----MEKRYlNWLRNikdWCISRQLIWGHRIP-----------------VWYCK----ECGEVYVAKEepl 430
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 625 --------SSVKPEQMTDeVWDFLFSggpyptSSDIPSSILN--KMKQEFEYWYPFDLRVSGKDLIQNHLTFCIYNHTAI 694
Cdd:TIGR00422 431 pddktntgPSVELEQDTD-VLDTWFS------SSLWPFSTLGwpDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLAL 503
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 695 MSKNHWPRGFrCNGHIM-LNSEKMSKSTGNFRTLRQAIEEFSADATRFSLADAGDGVDDANF--------------VFET 759
Cdd:TIGR00422 504 TGQVPFKEVY-IHGLVRdEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFdwkrvesarnflnkLWNA 582
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 760 ANAAILRLT--KELSWMEEVLE-----AEASLR------TGALSTYAdqvFANEINIAVTLTEQHYRNcMFREALKTGFY 826
Cdd:TIGR00422 583 SRFVLMNLSddLELSGGEEKLSladrwILSKLNrtikevRKALDKYR---FAEAAKALYEFIWNDFCD-WYIELVKYRLY 658
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 827 D-----LQAARDEYRFscgaggmnhdlvwrFMDVQTCLITPICPHYAEYVrREILKKDGFAVH-AGWPTADSPDLTLKAA 900
Cdd:TIGR00422 659 NgneaeKKAARDTLYY--------------VLDKALRLLHPFMPFITEEI-WQHFKEGADSIMlQSYPVVDAEFVDEEAE 723
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 225465204 901 NKY--LQDSIVLMRKLL-QKQILGSKK-------ANKKGAPVTSLTESNLKGLIYVNE 948
Cdd:TIGR00422 724 KAFelLKEIIVSIRNLKaESNIPPNAPlkvlliyTEAETAERLKLNAVDIKGAINFSE 781
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
15-96 |
1.95e-12 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 71.76 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRaeagEKPPEPGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGM 94
Cdd:PRK13208 14 ELEEKWQKIWEEEGTYK----FDPDERKPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGL 89
|
..
gi 225465204 95 PI 96
Cdd:PRK13208 90 PT 91
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
489-755 |
5.63e-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: 65.73 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 489 RKVQEA-KPLIRSKLIEIGQAIVYSEPEKR-------VMSRSGDECVVALTDQWYIIYGEpewkkLAEDCLSN-----MN 555
Cdd:cd00817 118 RAVQEAfVRLYEKGLIYRDNRLVNWCPKLRtaisdieVCSRSGDVIEPLLKPQWFVKVKD-----LAKKALEAvkegdIK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 556 LYSDETRHGFEHtlsWLNQ---WACSRSFGLGTRFP-WDEEFlveslsDSTIYMAYYTVAHILQNGDLYGSGTSSVKPEQ 631
Cdd:cd00817 193 FVPERMEKRYEN---WLENirdWCISRQLWWGHRIPaWYCKD------GGHWVVAREEDEAIDKAAPEACVPCGGEELKQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 632 MTDeVWDFLFSggpyptSSDIPSSILN--KMKQEFEYWYPFDLRVSGKDLIQNHLTFCIYNHTAIMSKNHWPRgfrcngh 709
Cdd:cd00817 264 DED-VLDTWFS------SSLWPFSTLGwpEETKDLKKFYPTSLLVTGHDIIFFWVARMIMRGLKLTGKLPFKE------- 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 225465204 710 IMLNS-------EKMSKSTGNFRTLRQAIEEFSADATRFSLADAGDGVDDANF 755
Cdd:cd00817 330 VYLHGlvrdedgRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
676-822 |
1.25e-09 |
|
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: 62.05 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 676 GKDLIQNHltfCIYnhtaimsknhWP-----RGFR------CNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSLA 744
Cdd:COG0143 289 GKDIIRFH---AII----------WPamlmaAGLPlpkkvfAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 745 DAGDGVDDANFVFEtanAAILRLTKEL----------------SWMEEVLEAEASLrtgalsTYADQVFANEINIAVTLT 808
Cdd:COG0143 356 REVPFGQDGDFSWE---DFVARVNSDLandlgnlasrtlsmihKYFDGKVPEPGEL------TEADEELLAEAEAALEEV 426
|
170
....*....|....
gi 225465204 809 EQHYRNCMFREALK 822
Cdd:COG0143 427 AEAMEAFEFRKALE 440
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
670-743 |
1.77e-09 |
|
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: 58.74 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 670 FDLRVSGKDLIQNH------LTFCIYNHtaimsknHWPRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSL 743
Cdd:cd00672 129 FDIHGGGVDLIFPHheneiaQSEAATGK-------PFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
707-743 |
2.70e-09 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 60.89 E-value: 2.70e-09
10 20 30
....*....|....*....|....*....|....*..
gi 225465204 707 NGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSL 743
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
568-755 |
1.73e-08 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 57.54 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 568 TLSWLNQ----WACSR-SFGLGTRFPWDEeflveslsDSTIYmayytvahilqngdlygsgtssvkpeqmtdeVW-DFLF 641
Cdd:cd00814 171 VLSWLKEglkdLSITRdLFDWGIPVPLDP--------GKVIY-------------------------------VWfDALI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 642 SggpYPTSSDIPssilNKMKQEFEYWYPFDLRVS---GKDLIQNHltfCIYNHTAIMSKNHW-PRGFRCNGHIMLNSEKM 717
Cdd:cd00814 212 G---YISATGYY----NEEWGNSWWWKDGWPELVhfiGKDIIRFH---AIYWPAMLLGAGLPlPTRIVAHGYLTVEGKKM 281
|
170 180 190
....*....|....*....|....*....|....*...
gi 225465204 718 SKSTGNFRTLRQAIEEFSADATRFSLADAGDGVDDANF 755
Cdd:cd00814 282 SKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
668-746 |
8.25e-08 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 55.07 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 668 YPFDLRVSGKDLIQNHLTFCIYNHTAIMSK---NHWPRgfrcNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSLA 744
Cdd:pfam01406 206 DQIDIHGGGIDLAFPHHENEIAQSEAAFDKqlaNYWLH----NGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLL 281
|
..
gi 225465204 745 DA 746
Cdd:pfam01406 282 SV 283
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
661-771 |
1.31e-07 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 54.99 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 661 KQEFEYWYPFDLRVS-----GKDLIQNHltfCIYnHTAIMSKNHW--PRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEE 733
Cdd:pfam09334 266 EEKWKEWWPNDPDTElvhfiGKDIIYFH---TIF-WPAMLLGAGYrlPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDR 341
|
90 100 110
....*....|....*....|....*....|....*...
gi 225465204 734 FSADATRFSLADAGDGVDDANFVFETanaAILRLTKEL 771
Cdd:pfam09334 342 FPPDALRYYLARNRPETKDTDFSWED---FVERVNSEL 376
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
15-95 |
5.18e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 54.06 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRAEAGEKPPEPGEKFFGNFPYPYMNGfLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGM 94
Cdd:PLN02563 84 EIEPKWQRYWEENRTFRTPDDVDTSKPKFYVLDMFPYPSGAG-LHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGL 162
|
.
gi 225465204 95 P 95
Cdd:PLN02563 163 P 163
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
50-95 |
7.08e-07 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 52.63 E-value: 7.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 225465204 50 PYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGMP 95
Cdd:cd00817 8 PPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIA 53
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
794-924 |
1.22e-06 |
|
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: 48.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 794 DQVFANEINIAVTLTEQHYRNCMFREALKTGFYDLQAAR-DEY------RFSCGAGGMNH-DLVWRFMDVQTCLITPICP 865
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLsDWYlelikdRLYGEEPDSRAqTTLYEVLETLLRLLAPFMP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 866 HYAEyvrrEILKKDgFAVHAGWP-TADSPDLTLKAANKYLQDSIVLMRKLLQKQILGSKK 924
Cdd:pfam08264 81 FITE----ELWQKE-SIHLAPWPeDAELEEAELEEAFELRQEIVQAIRKLRSELKIKKSL 135
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
1-763 |
1.44e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 52.64 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 1 MEGSKSFArrdrlLEIEVKVRNWWEEKDVFRAEAGEKppepGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRG 80
Cdd:PLN02943 55 PETAKSFD-----FTSEERIYNWWESQGYFKPNFDRG----GDPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 81 ANVLLPFGFHCTGMpikasADKLAWEiqqfgdppvfpteveeqpgeepepedpnggapalpdkfkgkkskaaskssgQMY 160
Cdd:PLN02943 126 RPTLWIPGTDHAGI-----ATQLVVE---------------------------------------------------KML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 161 QWEIMRSFGLSDSEISKfqNPYNWLSFFPPLAMEDLKAFGLGCDWRRSFITTDMN---PYYDNFIkwqmrKLKAIGKIVK 237
Cdd:PLN02943 150 ASEGIKRTDLGRDEFTK--RVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQlsrAVVEAFV-----RLHEKGLIYQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 238 DVRYTIYSPLDGQPCADHDRASGEgvQPQEYTLIKMEVVSpyppklssleGKKVYLAAATLRPETMYGQTNAWVLPDgky 317
Cdd:PLN02943 223 GSYMVNWSPNLQTAVSDLEVEYSE--EPGTLYYIKYRVAG----------GSEDFLTIATTRPETLFGDVAIAVNPE--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 318 gafeinDDEvfiitqraalnlaYQNFskvpekptclveltgydlIGLPLKSPLSFNEiiySLPMLS---ILTDKGTGIVT 394
Cdd:PLN02943 288 ------DDR-------------YSKY------------------IGKMAIVPMTYGR---HVPIIAdryVDKDFGTGVLK 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 395 SVPSDAPDDYmalhdlkskpAFRAKYGvkdewiMPFeiipiidipeygdrsaekvcndLKIKSQnekeklaeakrltylr 474
Cdd:PLN02943 328 ISPGHDHNDY----------LLARKLG------LPI----------------------LNVMNK---------------- 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 475 gftEGTMlvGEFAGRKVQEAKPLIRSKLIEIGQAiVYSEPEKRVMSRS--GDECVVAL-TDQWYIIYgEPewkkLAEDCL 551
Cdd:PLN02943 354 ---DGTL--NEVAGLYWFEAREKLWSDLEETGLA-VKKEPHTLRVPRSqrGGEVIEPLvSKQWFVTM-EP----LAEKAL 422
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 552 -----SNMNLYSDETRHGFEHTLSWLNQWACSRSFGLGTRFP-W-------DEEFLVESLSDSTIYMAYytvahilqngD 618
Cdd:PLN02943 423 kavenGELTIIPERFEKIYNHWLSNIKDWCISRQLWWGHRIPvWyivgkdcEEDYIVARSAEEALEKAR----------E 492
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 619 LYGsgtSSVKPEQMTDeVWDFLFSGGPYPTSS-DIPssilNKMKQEFEYWYPFDLRVSGKDLIqnhltFCIYNHTAIMsk 697
Cdd:PLN02943 493 KYG---KDVEIYQDPD-VLDTWFSSALWPFSTlGWP----DVSAEDFKKFYPTTVLETGHDIL-----FFWVARMVMM-- 557
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 698 nhwprGFRCNG-----HIMLN-------SEKMSKSTGNFRTLRQAIEEFSADATRFSLAdAGDGVDDANFVFE--TANAA 763
Cdd:PLN02943 558 -----GIEFTGtvpfsYVYLHglirdsqGRKMSKTLGNVIDPLDTIKEFGTDALRFTLA-LGTAGQDLNLSTErlTSNKA 631
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
15-86 |
2.54e-06 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 51.93 E-value: 2.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225465204 15 EIEVKVRNWWEEKDVFRAEAGEKPPEPGEKFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVL-LP 86
Cdd:PTZ00419 32 EVESGWYEWWEKSGFFKPAEDAKSLNSGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLwVP 104
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
676-758 |
3.49e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 51.31 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 676 GKDLIQNHltfciynhtAIMsknhWP-----RGFR------CNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSLA 744
Cdd:PRK00133 291 GKDIIYFH---------TLF----WPamlegAGYRlptnvfAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLA 357
|
90
....*....|....*
gi 225465204 745 -DAGDGVDDANFVFE 758
Cdd:PRK00133 358 aKLPETIDDLDFNWE 372
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
668-743 |
9.46e-06 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 49.54 E-value: 9.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225465204 668 YPFDLRVSGKDLIQNHLTFCIYNHTAIM---SKNHWPRgfrcNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRFSL 743
Cdd:PLN02946 276 HSFDIHGGGMDLVFPHHENEIAQSCAACcdsNISYWIH----NGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL 350
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
668-741 |
1.50e-04 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 45.79 E-value: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225465204 668 YPFDLRVSGKDLI----QNHLTFCiynhTAIMSKNHWPRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRF 741
Cdd:PTZ00399 267 DPIDIHSGGIDLKfphhDNELAQS----EAYFDKHQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRL 340
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
17-96 |
5.20e-04 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 44.38 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 17 EVKVRNWWEEKDVFRAEAGEkppEPGEKFFGNFPYPYMNGFLHLGHAfsLSKL--EFAAAFHRLRGANVLLPFGFHCTGM 94
Cdd:PLN02843 9 EPEIQKLWEENQVYKRVSDR---NNGESFTLHDGPPYANGDLHIGHA--LNKIlkDFINRYQLLQGKKVHYVPGWDCHGL 83
|
..
gi 225465204 95 PI 96
Cdd:PLN02843 84 PI 85
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
15-84 |
5.92e-04 |
|
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: 43.89 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRAEA-GEKPPepgekffgnF----PYPYMNGFLHLGHAF------SLSKlefaaaFHRLRGANV 83
Cdd:COG0525 11 EVEAKWYQYWEENGYFKADPdSDKEP---------FtiviPPPNVTGSLHMGHALnntlqdILIR------YKRMQGYNT 75
|
.
gi 225465204 84 L 84
Cdd:COG0525 76 L 76
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
15-86 |
6.64e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 43.94 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 15 EIEVKVRNWWEEKDVFRAEAGEKPPepgekffgnF----PYPYMNGFLHLGHAF------SLSKlefaaaFHRLRGANVL 84
Cdd:PRK05729 13 EVEAKWYQKWEEKGYFKPDDNSKKP---------FsiviPPPNVTGSLHMGHALnntlqdILIR------YKRMQGYNTL 77
|
...
gi 225465204 85 -LP 86
Cdd:PRK05729 78 wLP 80
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
6-96 |
8.69e-04 |
|
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: 43.53 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 6 SFARRDRLLEIEVKVRNWWEEKDVFRA--EAGEKppepGEKFF---GnfPyPYMNGFLHLGHAfsLSKL--EFAAAFHRL 78
Cdd:COG0060 11 DFPMRANLPKREPEILKFWEENDIYEKsrEARAG----RPKFVlhdG--P-PYANGDIHIGHA--LNKIlkDIIVRYKTM 81
|
90
....*....|....*...
gi 225465204 79 RGANVLLPFGFHCTGMPI 96
Cdd:COG0060 82 RGFDVPYVPGWDCHGLPI 99
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
23-84 |
1.80e-03 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 42.58 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225465204 23 WWEEKDVFRAEA-GEKPPepgekFFGNFPYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVL 84
Cdd:PLN02381 112 WWEKSGYFGADAkSSKPP-----FVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNAL 169
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
52-102 |
2.38e-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: 41.45 E-value: 2.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 225465204 52 PYMNGFLHLGHAfsLSKL--EFAAAFHRLRGANVLLPFGFHCTGMPIKASADK 102
Cdd:cd00818 10 PYANGLPHYGHA--LNKIlkDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEK 60
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
663-744 |
3.57e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 41.41 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 663 EFEYWYPFDLRVSGKDLIQNHltfCIYNHTAIMSKN-HWPRGFRCNGHIMLNSEKMSKSTGNfrTL--RQAIEEFSADAT 739
Cdd:PRK11893 248 LFNKYWPADVHLIGKDILRFH---AVYWPAFLMAAGlPLPKRVFAHGFLTLDGEKMSKSLGN--VIdpFDLVDEYGVDAV 322
|
....*
gi 225465204 740 RFSLA 744
Cdd:PRK11893 323 RYFLL 327
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
50-112 |
6.57e-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: 6.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225465204 50 PYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLLPFGFHCTGMPIKASADKLAWEIQQFGD 112
Cdd:cd00814 7 ALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCD 69
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
670-785 |
6.71e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 40.29 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225465204 670 FDLRVSGKDLIQNHLTFCIYNHTAIMSKNhWPRGFRCNGHIMLNSEKMSKSTGNFRTLRQAIEE-FSADATRFSLAdAGD 748
Cdd:PRK14536 234 CDIHIGGVDHIRVHHTNEIAQCEAATGKP-WVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLL-GGH 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 225465204 749 GVDDANFVFE---TANAAILRLTKELS-WMEEVLEAEASLR 785
Cdd:PRK14536 312 YRSQLAFSWEalkTAKAARRSLVRRVArVVDAARATTGSVR 352
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
50-112 |
7.48e-03 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 39.97 E-value: 7.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225465204 50 PYPYMNGFLHLGHAFSLSKLEFAAAFHRLRGANVLlpfgfHCTGM-----PIKASADKLAWEIQQFGD 112
Cdd:pfam09334 6 ALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVL-----FVCGTdehgtPIELKAEKEGITPEELVD 68
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
707-741 |
8.70e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 40.09 E-value: 8.70e-03
10 20 30
....*....|....*....|....*....|....*
gi 225465204 707 NGHIMLNSEKMSKSTGNFRTLRQAIEEFSADATRF 741
Cdd:PRK14535 499 NGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRF 533
|
|
| |
