|
Name |
Accession |
Description |
Interval |
E-value |
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
40-848 |
0e+00 |
|
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: 749.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 40 HRIEA----HWREQlsgGQFNPKD--SQDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGL 113
Cdd:COG0495 8 KEIEKkwqkYWEEN---GTFKADEdsSKPKYYVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 114 PAENAANQRGVEPASWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKT 193
Cdd:COG0495 85 PAENAAIKNGVHPAEWTYENIANMRRQLKRLGLSYDWSREIATCDPEYYKWTQWIFLQLYEKGLAYRKEAPVNWCPVDQT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 194 VLADEQVDaNGCSWRSGAKVEKKLLRQWFIRTSAYAKQLLDGLEdpTLRDWRD-IINLQRHWIGECDG--YAFNlLTSAS 270
Cdd:COG0495 165 VLANEQVI-DGRCWRCGAPVEKKELPQWFLKITDYADELLDDLD--KLDGWPEkVKTMQRNWIGRSEGaeVDFP-VEGSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 271 GLLRVWTTHPEHLkdphaFLVLRSNHHLSKL--------------------------------KGADS-LSAANPFAGTT 317
Cdd:COG0495 241 EKITVFTTRPDTLfg-atFMVLAPEHPLVKElatpeqnaavaafieeakkkseiertsetkekTGVFTgLYAINPLTGEK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 318 MPV--------------VFS----DEVTF--------PPKsdvylaaPSFRGEDKDLWDSYGLAFTSNGK--DEESLSPA 369
Cdd:COG0495 320 IPIwiadyvlmdygtgaVMAvpahDQRDFefakkyglPIK-------QVIAPEDGDDPDILEEAYTGDGVliNSGEFDGL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 370 NWEMLRKEVLQAATRLNVGGYRVSSKLKDWLISRQRYWGTPIPIVHCQKCGAVPVPEEQLPVSLPPKDSPK--------- 440
Cdd:COG0495 393 DSEEAKEAIIEWLEEKGLGKRKVNYRLRDWLISRQRYWGEPIPIIHCEDCGVVPVPEDQLPVELPEDVDFDptggsplar 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 441 -EAFL-CDCPKCGeKDARRETDTMDTFVDSSWYYLRYLDAQNSERIFDTALTKKFMPVDLYIGGKEHAVLHLYYARFINH 518
Cdd:COG0495 473 aPEWVnVTCPKCG-GPARRETDTMDTFVDSSWYYLRYTDPHNDEAPFDPEAANYWLPVDQYIGGIEHAILHLLYARFFTK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 519 FLHSCGLSPTSEPFSRLLVQGMVMGrsfrvkgsgryVPETEVEIVNakknqavlketkepvvmtWEKMSKSKLNGVEPSD 598
Cdd:COG0495 552 VLRDLGLVSFDEPFKRLLTQGMVLE-----------VGKDGVVIGG------------------IEKMSKSKGNVVDPDE 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 599 MFNEYGTDTTRLIILADVAPTSHRNWSSATFPGILNWQKRLWLTLQDFqqarEDQTASDVVPTSEeflaEDAKLFDARNF 678
Cdd:COG0495 603 IIEKYGADTLRLFEMFAGPPERDLEWSDSGVEGAYRFLNRVWRLVVDE----AEALKLDVADLSE----ADKELRRALHK 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 679 YVKGATFNYRhAQQLSVAISKMQGLTNSLRRTPKHVLRHGKQFERALAAQIIMLAPMAPHFASELWskfvaipgrlnpas 758
Cdd:COG0495 675 TIKKVTEDIE-RLRFNTAIAALMELVNALYKAKDSGEADRAVLREALETLVLLLAPFAPHIAEELW-------------- 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 759 QELQWSEDVLAQRWPDIDPAY----NLDLSIKVNGfencviKVqRTHLD---KVTHSDALDIAFNTESVTSYLIDKKIRT 831
Cdd:COG0495 740 ERLGHEGSVADAPWPEADEAAlvedEVTIVVQVNG------KV-RGKIEvpaDASKEELEAAALADEKVQKFLEGKTIRK 812
|
890
....*....|....*..
gi 19528361 832 TNFVlyPGieAILNIYV 848
Cdd:COG0495 813 VIVV--PG--KLVNIVV 825
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
42-835 |
0e+00 |
|
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 683.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 42 IEAHWREQ-LSGGQFNPKD--SQDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENA 118
Cdd:TIGR00396 6 IEEKWQQKwDENKTFKVTDdsSKPKYYILSMFPYPSGALHMGHVRNYTITDVLSRYYRMKGYNVLHPIGWDAFGLPAENA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 119 ANQRGVEPASWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADE 198
Cdd:TIGR00396 86 AIKRGIHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQWIFLELFEKGLAYVKEADVNWCPNDGTVLANE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 199 QVDANGCSWRSGAKVEKKLLRQWFIRTSAYAKQLLDGLEdpTLRDWRD-IINLQRHWIGECDGYAFNL-LTSASGLLRVW 276
Cdd:TIGR00396 166 QVDSDGRSWRGDTPVEKKELKQWFLKITAYAEELLNDLE--ELDHWPEsVKEMQRNWIGKSEGVEITFkIADHDEKITVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 277 TTHPEHLKDPhAFLVLRSNHHLSKL------------------------------KGADSLS-AANPFAGTTMPVVFSDE 325
Cdd:TIGR00396 244 TTRPDTIFGV-TYLALAPEHPLVEKaaennpkvaafikkilnktvaertkatkekKGVDTGIkAIHPLTGEKIPIWVANY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 326 VTFPPKSDVYLAAPSFRGEDKDLWDSYGL-----------------AFTSNGKDEES--LSPANWEMLRKEVLQAATRLN 386
Cdd:TIGR00396 323 VLMEYGTGAVMGVPAHDERDFEFAQKYGLpikpvidpaekdlsltaAYTEDGVLVNSgeFNGLNSSEARNAIIDMLEKEG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 387 VGGYRVSSKLKDWLISRQRYWGTPIPIVHCQKCGAVPVPEEQLPVSLPPKD-------SP----KEAFLCDCPKCGeKDA 455
Cdd:TIGR00396 403 KGKRKVNYRLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDLPVILPEDVvydgdggSPlsriPEWVNVTCPSCG-KPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 456 RRETDTMDTFVDSSWYYLRYLDAQNSERIFDTALTKKFMPVDLYIGGKEHAVLHLYYARFINHFLHSCGLSPTSEPFSRL 535
Cdd:TIGR00396 482 LRETDTMDTFAGSSWYYLRYLDPKNTDGPFDKEKAEYWLPVDLYIGGIEHAILHLLYARFFHKFLRDIGYVNTKEPFKKL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 536 LVQGMVMGrsFRVKGSGRYVPETEVEivnaKKNQAVLKETKEPVVMTWEKMSKSKLNGVEPSDMFNEYGTDTTRLIILAD 615
Cdd:TIGR00396 562 INQGMVLG--FYYPPNGKVPADVLTE----RDEKGKDKAGGELVYVGYEKMSKSKGNGIDPQEIVESYGADALRLFIMFM 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 616 VAPTSHRNWSSATFPGILNWQKRLW-LTLQDfqQAREDQTASDVVPTSEeflaEDAKLFDARNFYVKGATFNYRHAQQLS 694
Cdd:TIGR00396 636 GPIAASLEWNESGLEGARRFLDRVWnLVYEI--TGELDAASLTVTALEE----AQKELRRDVHKFLKKVTEDLEKRESFN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 695 VAISKMQGLTNSLRRTPKHVLrhgkqFERALAAQIIMLAPMAPHFASELWSKFVAIPGrlnpasqelqwseDVLAQRWPD 774
Cdd:TIGR00396 710 TAISAMMELLNKLYKAKKEAL-----MLEYLKGFVTVLSPFAPHLAEELWEKLGSEPF-------------IIDNAKWPV 771
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19528361 775 IDPAYNLDLSIKVNGFENCVIKVQRTHLDKVTHSDALDIAFNTESVTSYLIDKKIRTTNFV 835
Cdd:TIGR00396 772 VDETALVEDKTLIVVQVNGKFRAKITVPKDADEEQVEELAKQDPEVKKYLENKTIKKVIYV 832
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
10-854 |
6.80e-166 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 507.44 E-value: 6.80e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 10 WGAVYWNSWRRLLTQSCTRNDNPELTSDVK-----------HRIEAHWREQLSGGQ-FNPKDSQD----KYYVLSMFPYP 73
Cdd:PLN02563 42 FRRSRRGGVSRSLTRRAFAAPSALTSTTAKttpaakraypfHEIEPKWQRYWEENRtFRTPDDVDtskpKFYVLDMFPYP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 74 SG-NLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLKRLGCSFDWNH 152
Cdd:PLN02563 122 SGaGLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYDWDR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 153 ELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVdANGCSWRSGAKVEKKLLRQWFIRTSAYAKQL 232
Cdd:PLN02563 202 EISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV-VDGLSERGGHPVIRKPMRQWMLKITAYADRL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 233 LDGLEDptlRDWRD-IINLQRHWIGECDG--YAFNLL----TSASGLLRVWTTHP------------------------E 281
Cdd:PLN02563 281 LEDLDD---LDWPEsIKEMQRNWIGRSEGaeLDFSVLdgegKERDEKITVYTTRPdtlfgatylvvapehpllsslttaE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 282 HLKDPHAFLVLRSNH------HLSKLK-GADSLS-AANPFAGTTMPVVFSDEVTFPPKSDVYLAAPSFRGEDKDLWDSYG 353
Cdd:PLN02563 358 QKEAVEEYVDAASRKsdlertELQKEKtGVFTGSyAINPATGEAIPIWVADYVLGSYGTGAIMAVPAHDTRDFEFAQKFD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 354 L------------------AFTSNGKDEESLSPA------NWEMLRKEVLQAATRLNVGGYRVSSKLKDWLISRQRYWGT 409
Cdd:PLN02563 438 LpikwvvkpadgneddaekAYTGEGVIVNSSSSGldinglSSKEAAKKVIEWLEETGNGKKKVNYKLRDWLFARQRYWGE 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 410 PIPIVHCQKCG-AVPVPEEQLPVSLP------PKDSPkEAFLCDC--------PKCGeKDARRETDTMDTFVDSSWYYLR 474
Cdd:PLN02563 518 PIPVVFLEDSGePVPVPESDLPLTLPelddftPTGTG-EPPLAKAvswvntvdPSSG-KPARRETNTMPQWAGSCWYYLR 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 475 YLDAQNSERIFDTALTKKFMPVDLYIGGKEHAVLHLYYARFINHFLHSCGLSPTSEPFSRLLVQGMVMGR----SFRvKG 550
Cdd:PLN02563 596 FMDPKNSNALVDKEKEKYWMPVDLYVGGAEHAVLHLLYARFWHKVLYDIGVVSTKEPFQCLVNQGMILGEveytAFK-DS 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 551 SGRYVPETEV-------------EIVNAKKNQAVLKET-KEPVVMTWEKMSKSKLNGVEPSDMFNEYGTDTTRLI----- 611
Cdd:PLN02563 675 DGEYVSADTAdrlgelqqekipeEKVIKSGDSFVLKDDpSIRLIARAHKMSKSRGNVVNPDDVVSEYGADSLRLYemfmg 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 612 ILADVAPtshrnWSSATFPGILNWQKRLWLTLQDFQQA----REDQTASDVVPtSEEFLAEDAKLFDARNFYVKGATFNy 687
Cdd:PLN02563 755 PLRDSKT-----WSTSGVEGVHRFLGRTWRLVVGAPLPdgsfRDGTVVTDEEP-SLEQLRLLHKCIAKVTEEIESTRFN- 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 688 rhaqqlsVAISKMQGLTNslrrtpkHVLRHGKQFERALAAQIIMLAPMAPHFASELWSKfvaipgrlnpasqeLQWSEDV 767
Cdd:PLN02563 828 -------TAISAMMEFTN-------AAYKWDKVPREAIEPFVLLLSPYAPHLAEELWFR--------------LGHSNSL 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 768 LAQRWPDIDPAYNLD----LSIKVNGFENCVIKVQRThldkVTHSDALDIAFNTESVTSYLIDKKIRTTNFVlyPGieAI 843
Cdd:PLN02563 880 AYEPWPEANPSYLVDdtvvLPVQINGKTRGTIEVEEG----CSEDDAFALASQDEKLSKYLDGKEIKKRIYV--PG--KI 951
|
970
....*....|.
gi 19528361 844 LNIYVDKAKMK 854
Cdd:PLN02563 952 LNVILKQQNVK 962
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
63-624 |
8.30e-129 |
|
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: 388.91 E-value: 8.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 63 KYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLK 142
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 143 RLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDpvdktvladeqvdangcswrsgakvekKLLRQWF 222
Cdd:cd00812 81 RMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWC---------------------------KLLDQWF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 223 IRTS--AYAKQLLDGLEDPTLRdWRDIINLQRHWIGecdgyafnlltsasgllrvwtthpehlkdphaflvlrsnhhlsk 300
Cdd:cd00812 134 LKYSetEWKEKLLKDLEKLDGW-PEEVRAMQENWIG-------------------------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 301 lkgadslsaanpfagttmpvvfsdevtfppksdvylaapsfrgedkdlwdsyglaftsngkdeeslspanwemlrkevlq 380
Cdd:cd00812 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 381 aatrlnvggyrvssklkdwlISRQRYWGTPIPIvhcqkcgavpvpeeqlpvslppkdspkeaflcdcpkcgekdarreTD 460
Cdd:cd00812 169 --------------------CSRQRYWGTPIPW---------------------------------------------TD 183
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 461 TMDTFVDSSWYYLRYLDAQNSER------IFDTALTKKFMPVDLYIGGKEHAVLHLYYARFINHFLHSCGLSpTSEPFSR 534
Cdd:cd00812 184 TMESLSDSTWYYARYTDAHNLEQpyegdlEFDREEFEYWYPVDIYIGGKEHAPNHLLYSRFNHKALFDEGLV-TDEPPKG 262
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 535 LLVQGMVMGRSfrvkgsgryvpeteveivnakknqavlketkepvvmtwEKMSKSKLNGVEPSDMFNEYGTDTTRLIILA 614
Cdd:cd00812 263 LIVQGMVLLEG--------------------------------------EKMSKSKGNVVTPDEAIKKYGADAARLYILF 304
|
570
....*....|
gi 19528361 615 DVAPTSHRNW 624
Cdd:cd00812 305 AAPPDADFDW 314
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
71-610 |
1.59e-67 |
|
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: 229.83 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAA-NQRGVEPAS---------------WTEQNI 134
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVeKKLGIEGKTrhdlgreeflekcweWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 135 AQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVdangcSWRSGAKVE 214
Cdd:cd00817 90 GKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV-----CSRSGDVIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 215 KKLLRQWFIRTSAYAKQLLDGLEDPTLRdWrdiinlqrhwigecdgyafnlltsasgllrvwttHPEHLKdphaflvlrs 294
Cdd:cd00817 165 PLLKPQWFVKVKDLAKKALEAVKEGDIK-F----------------------------------VPERME---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 295 nhhlsklkgadslsaanpfagttmpvvfsdevtfppksDVYLaapsfrgedkdlwdsyglaftsngkdeeslspaNWeml 374
Cdd:cd00817 200 --------------------------------------KRYE---------------------------------NW--- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 375 rkevlqaatrLNvggyrvssKLKDWLISRQRYWGTPIPIVHCQKCGAVPV-PEEQLPVslppkdspKEAFLCDCPKCGEK 453
Cdd:cd00817 206 ----------LE--------NIRDWCISRQLWWGHRIPAWYCKDGGHWVVaREEDEAI--------DKAAPEACVPCGGE 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 454 DARRETDTMDTFVDSS-W--YYLRYLDaqnserifDTALTKKFMPVDLYIGGkeHAVLHLYYARFInhflhSCGLSPTSE 530
Cdd:cd00817 260 ELKQDEDVLDTWFSSSlWpfSTLGWPE--------ETKDLKKFYPTSLLVTG--HDIIFFWVARMI-----MRGLKLTGK 324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 531 -PFSRLLVQGMVMGrsfrvkgsgryvpeteveivnakknqavlketkepvvMTWEKMSKSKLNGVEPSDMFNEYGTDTTR 609
Cdd:cd00817 325 lPFKEVYLHGLVRD-------------------------------------EDGRKMSKSLGNVIDPLDVIDGYGADALR 367
|
.
gi 19528361 610 L 610
Cdd:cd00817 368 F 368
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
71-789 |
3.10e-64 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 230.85 E-value: 3.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAA-NQRGV--EPAS----------WTEQNIAQM 137
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLPTERKVeKYYGIrkDDISreefielcreLTDEDEKKF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 138 KEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADeqvdangcswrsgAKVEKKl 217
Cdd:PRK13208 127 RELWRRLGLSVDWSLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQ-------------AEVEYR- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 218 lrqwfIRTSAYakqlldgledptlrdwrdiinlqrHWIgecdgyAFNllTSASGLLRVWTTHPE----------HLKDPh 287
Cdd:PRK13208 193 -----EREGKL------------------------NYI------KFP--VEDGEEIEIATTRPEllpacvavvvHPDDE- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 288 aflvlRSNHhlskLKGadsLSAANPFAGTTMPVVFSDEV------------TFPPKSDVYLaapsFR----------GED 345
Cdd:PRK13208 235 -----RYKH----LVG---KTAIVPLFGVEVPILADPLVdpdfgtgavmicTFGDKTDVTW----WRelnlptriiiDED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 346 KDLWDSYGL---------------AFTSNGKDEES-------------------LSPANW----EMLRKEVLQAATRLNV 387
Cdd:PRK13208 299 GRMTEAAGKlagltieearkkiveDLKSGGLLGKQepikhnvkfcercdtpleiLVTRQWfikvLDLKEELLERGKEINW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 388 GGYRVSSKLK--------DWLISRQRYWGTPIPIVHCQKCGAVPVP-EEQLPVSlPPKDSPKEaflCDCPKCGEKDARRE 458
Cdd:PRK13208 379 YPEHMRVRLEnwieglnwDWCISRQRYFGTPIPVWYCKDCGHPILPdEEDLPVD-PTKDEPPG---YKCPQCGSPGFEGE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 459 TDTMDTFVDSS---WYYLRYLDaqnserifDTALTKKFMPVDLYIGGkehavlH------LYYARFINHFLHSCglspts 529
Cdd:PRK13208 455 TDVMDTWATSSitpLIVTGWER--------DEDLFEKVFPMDLRPQG------HdiirtwLFYTILRAYLLTGK------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 530 EPFSRLLVQGMVMGRsfrvKGsgryvpeteveivnakknqavlketkepvvmtwEKMSKSKLNGVEPSDMFNEYGTDTTR 609
Cdd:PRK13208 515 LPWKNIMISGMVLDP----DG---------------------------------KKMSKSKGNVVTPEELLEKYGADAVR 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 610 LiiladvaptshrnWSSATFPG---ILNWQK---------RLW----LTLQdFQQAREDQTASDVVPTSEEFLAEDAKL- 672
Cdd:PRK13208 558 Y-------------WAASARLGsdtPFDEKQvkigrrlltKLWnasrFVLH-FSADPEPDKAEVLEPLDRWILAKLAKVv 623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 673 ------FDARNFY---------------------VKGATFNYRHAqqlsvaiskmqgltnSLRRTPKHVLRHgkqferAL 725
Cdd:PRK13208 624 ekateaLENYDFAkaleeiesffwhvfcddylelVKSRAYGEDEE---------------EEQKSARYTLYT------VL 682
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19528361 726 AAQIIMLAPMAPHFASELWSKFvaipgrlnpasqelqWSEDVLAQRWPDIDPAYN-------LDLSIKVNG 789
Cdd:PRK13208 683 DTLLRLLAPFLPFITEEVWSWL---------------YGGSVHRASWPEPDEELIdeedeelGELAKEILS 738
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
40-747 |
3.74e-59 |
|
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: 217.23 E-value: 3.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 40 HRIEAHWREQ-LSGGQFNPKDSQDK--YYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAE 116
Cdd:TIGR00422 8 HEVEKKWYKKwEKSGFFKPDGNSNKppFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 117 NAAN-QRGVEPAS---------------WTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQ 180
Cdd:TIGR00422 88 VKVEkKLGAEGKTkhdlgreefrekiweWKEESGGTIKNQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLIYR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 181 NEALVNWDPVDKTVLADEQVDANgcswrsgaKVEKKLlrqWFIRtsayakqlldgledptlrdwrdiinlqrhwigecdg 260
Cdd:TIGR00422 168 GEYLVNWDPKLNTAISDIEVEYK--------EVKGKL---YYIR------------------------------------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 261 yaFNLLTSASGLLRVWTTHPE----------HLKDPHaflvlrsNHHLSKLKgadslsAANPFAGTTMPVVFSDEVTFPP 330
Cdd:TIGR00422 201 --YPLANGSKDYLVVATTRPEtmfgdtavavHPEDER-------YKHLIGKK------VILPLTGRKIPIIADEYVDMEF 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 331 KSDVYLAAPSFRGEDKDLWDSYGL----AFTSNGK-DEESLSPANWEML--RKEVLQA-----------ATRLNVG-GYR 391
Cdd:TIGR00422 266 GTGAVKVTPAHDFNDYEWGKRHNLefinILDEDGLlNENAGKYQGLTRFeaRKKIVEDlkeegllvkiePHTHNVGtCWR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 392 --------------VS--------------------------------SKLKDWLISRQRYWGTPIPIVHCQKCGAVPVP 425
Cdd:TIGR00422 346 sgtvvepllskqwfVKvekladkaleaaeegeikfvpkrmekrylnwlRNIKDWCISRQLIWGHRIPVWYCKECGEVYVA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 426 EEQLPVSLPPKDSPKEAFlcdcpkcgekdaRRETDTMDTFVDSSWYYLRYLDAQNserifDTALTKKFMPVDLYIGGkeH 505
Cdd:TIGR00422 426 KEEPLPDDKTNTGPSVEL------------EQDTDVLDTWFSSSLWPFSTLGWPD-----ETKDLKKFYPTDLLVTG--Y 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 506 AVLHLYYARFInhflhSCGLSPTSE-PFSRLLVQGMVMGrsfrvkgsgryvpeteveivnaKKNQavlketkepvvmtwe 584
Cdd:TIGR00422 487 DIIFFWVARMI-----FRSLALTGQvPFKEVYIHGLVRD----------------------EQGR--------------- 524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 585 KMSKSKLNGVEPSDMFNEYGTDTTRLIILADVAPTSHRNWSSATFPGILNWQKRLW----LTLQ------DFQQAREDQT 654
Cdd:TIGR00422 525 KMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESARNFLNKLWnasrFVLMnlsddlELSGGEEKLS 604
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 655 ASDVVPTSE--EFLAEDAKLFDARNFYVKGA---TFNYRHAQQLSVAISK--MQGLTNSLRRTPKHVLRHgkqferALAA 727
Cdd:TIGR00422 605 LADRWILSKlnRTIKEVRKALDKYRFAEAAKalyEFIWNDFCDWYIELVKyrLYNGNEAEKKAARDTLYY------VLDK 678
|
810 820
....*....|....*....|
gi 19528361 728 QIIMLAPMAPHFASELWSKF 747
Cdd:TIGR00422 679 ALRLLHPFMPFITEEIWQHF 698
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
42-616 |
2.97e-35 |
|
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: 142.55 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 42 IEAHWREQlsgGQFNPKDSQDK----YYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNV-FQPmGWDSFGLPAE 116
Cdd:pfam00133 2 IYEFWDEQ---GYFKPELEKRKgkpsFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVlWVP-GWDHHGLPTE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 117 NAANQR------------GVEP-----ASWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAY 179
Cdd:pfam00133 78 QVVEKKlgikekktrhkyGREEfrekcREWKMEYADEIRKQFRRLGRSIDWDREYFTMDPELEAAVWEVFVRLHDKGLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 180 QNEALVNWDPVDKTVLADEQV---DANGCSwrsgakvekkllrqWFIrtsayakqlldgledptlrdwrdiinlqrhwig 256
Cdd:pfam00133 158 RGKKLVNWSPALNTALSNLEVeykDVKGPS--------------IHV--------------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 257 ecdgyAFNLLTSASGLLRVWTTHPEHLK-------DPHAFLVLRSNHH-------------------LSKLKGAD--SLS 308
Cdd:pfam00133 191 -----AFPLADDEGASLVIWTTTPWTLPgntavavNPEFDYVITGEGYilaeallkslykkgtdkkiLEDFRGKEleGKE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 309 AANPFAGTTMPVVFSDEVTFPPKSDVYLAAPSFRGEDKDLWDSYGLAF----TSNGKDEESLSP--------AN------ 370
Cdd:pfam00133 266 AIHPFVNREIPIITDDYVDMEFGTGAVHIAPAHGENDYEVGQRHNLEVinpvDDDGTFTEEAPDfqgvyrfdARkkivel 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 371 ----------------------------------WEMLRKEVLQAATRLNVGGY--------RVSSKLK---DWLISRQR 405
Cdd:pfam00133 346 ltekglllkiepfthsypfcwrsgtpiipratpqWFVRMDELADQALEAVEKVQfvpksgekRYFNWLAniqDWCISRQR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 406 YWGTPIPI--------VHCQKCGAVPVPEEQLPVSlppKDSPKEAFLCDCPKCGEKDARRETDTMDTFVDS-SWYY--LR 474
Cdd:pfam00133 426 WWGHPIPAwvskdteeVVCRGELFELVAGRFEEEG---SIKWLHREAKDKLGYGKGTLEQDEDVLDTWFSSgSWPFstLG 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 475 YLDAQNSERifdtaltKKFMPVDLYIGGKEhaVLHLYYARFINHFLHSCGlsptSEPFSRLLVQGMVMgrsfrvKGSGRy 554
Cdd:pfam00133 503 WPFVNTEEF-------KKFFPADMLLEGSD--QTRGWFYRMIMLSTALTG----SVPFKNVLVHGLVR------DEQGR- 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19528361 555 vpeteveivnakknqavlketkepvvmtweKMSKSKLNGVEPSDMFNEYGTDTTRL-IILADV 616
Cdd:pfam00133 563 ------------------------------KMSKSLGNVIDPLDVIDKYGADALRLwLANSDY 595
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
71-744 |
1.61e-32 |
|
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273054 [Multi-domain] Cd Length: 861 Bit Score: 135.58 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQR-------GVEPASWTE----------QN 133
Cdd:TIGR00392 45 PYANGSIHLGHALNKILKDIILRYKTMQGFNVTRKPGWDTHGLPIEHKVEKKlgisgkkEISSLEIEEfrekcrefalKQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 134 IAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVDANGCSWrsgakv 213
Cdd:TIGR00392 125 IEEQREQFQRLGVWGDWENPYKTMDPSYEESQWWLFKEAHEKGLLYRGLKPVYWSPRCRTALAEAEVEYKENYK------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 214 EKKllrqwfiRTSAYAKQLLDGLEDPtlrdwrdiinlqrhwigecdgyafNLLTSASGLLrVWTTHP------------- 280
Cdd:TIGR00392 199 DVK-------DPSIYVKFPVKKDKKT------------------------YLKVKLSSLL-IWTTTPwtlpsnlaiavhp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 281 --EHLK-----DPHAFLVLRSNHH------------LSKLKGAD--SLSAANPFAG------TTMPVVFSDE-VTFPPKS 332
Cdd:TIGR00392 247 dfEYALvqdntKVEYFILAKKLVEklynkagsdyeiIKTFKGSDleGLEYEHPLYDfvsqlkEGAPVVIGGDhVTTEDGT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 333 DVYLAAPSFRGEDKDLWDSYGL----------AFTSNGKDEESLS----------------------------------- 367
Cdd:TIGR00392 327 GIVHTAPGHGEEDYEIGKKYGLevlspvdekgVYTEGVNDFQGRFvkdadkdiikankiiieqlkdkglllkaekithsy 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 368 PANW------------------EMLRKEVLQAATRLNVGGYRVSSKLK-------DWLISRQRYWGTPIPIVHCQKCG-- 420
Cdd:TIGR00392 407 PHCWrtktpviyrateqwfiktKDIKDQMLEQIKKVNWVPEWGEGRFGnwlenrpDWCISRQRYWGIPIPIWYCEDTGep 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 421 -----------AVPVPEEQLPVSLPPKDSPKEAFLCdCPKCGEkdARRETDTMDTFVDS--SWYylryldAQNSERiFDT 487
Cdd:TIGR00392 487 ivvgsieelieLIELKGIDAWFEDLHRDFLDKITLK-SGDGGE--YRRVPDVLDVWFDSgsMPY------ASIHYP-FEN 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 488 ALTKKFMPVDLYIGGKEHavlhlYYARFINHFLHSCGLSPTSePFSRLLVQGmvmgrsFRVKGSGRyvpeteveivnakk 567
Cdd:TIGR00392 557 EKFKEVFPADFILEGSDQ-----TRGWFYSSLAIGTALFGQA-PYKNVITHG------FTLDEKGR-------------- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 568 nqavlketkepvvmtweKMSKSKLNGVEPSDMFNEYGTDTTRLI---------------ILADVApTSHRN--WSSATF- 629
Cdd:TIGR00392 611 -----------------KMSKSLGNVVDPLKVINKYGADILRLYvassdpwedlrfsdeILKQVV-EKYRKirWNTYRFl 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 630 --PGILNWQKRLWLTLQDFQQAREDQTasdVVPTSEEFLAEDAKLFDARNFYVKGATFNYRHAQQLS---VAISKMQ--- 701
Cdd:TIGR00392 673 ltYANLDKFDPLFNSVAVEKFPEEDRW---ILSRLNSLVEEVNEALEKYNFHKVLRALQDFIVEELSnwyIRIIRDRlyc 749
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 19528361 702 GLTNSLRRTPKHVLRHgkqferALAAQIIMLAPMAPHFASELW 744
Cdd:TIGR00392 750 EAKDNDKRAAQTTLYY------ALLTLVRLLAPFLPHTAEEIY 786
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
63-624 |
3.95e-32 |
|
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: 127.53 E-value: 3.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 63 KYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVE-------------PASW 129
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRkkktiwieefredPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 130 TEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEalvnwdpvdKTVLADEqvdangcswrs 209
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGT---------HPVRITE----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 210 gakvekkllrQWFIRTSAYAKQLLDGLEdptlrdwrdiinlQRHWIgecdgyafnlltsasgllrvwtthPEHLKDphaf 289
Cdd:cd00668 141 ----------QWFFDMPKFKEKLLKALR-------------RGKIV------------------------PEHVKN---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 290 lvlrsnhhlsklkgadslsaanpfagttmpvvfsdevtfppksdvylaapsfrgedkdlwdsyglaftsngkdeeslspA 369
Cdd:cd00668 170 -------------------------------------------------------------------------------R 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 370 NWEMLRkevlqaatrlnvggyrvssKLKDWLISRQRYWGTPIPivhcqkcgavpvpeeqlpvslppkdspkeaflcdcpk 449
Cdd:cd00668 171 MEAWLE-------------------SLLDWAISRQRYWGTPLP------------------------------------- 194
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 450 cgekdarreTDTMDTFVDSSWYYLRYLDAQnseriFDTALTKKFMPVDLYIGGKEHAVLHLYYarFINHFLHSCGlsptS 529
Cdd:cd00668 195 ---------EDVFDVWFDSGIGPLGSLGYP-----EEKEWFKDSYPADWHLIGKDILRGWANF--WITMLVALFG----E 254
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 530 EPFSRLLVQGMVMGrsfrvkGSGRyvpeteveivnakknqavlketkepvvmtweKMSKSKLNGVEPSDMFNEYGTDTTR 609
Cdd:cd00668 255 IPPKNLLVHGFVLD------EGGQ-------------------------------KMSKSKGNVIDPSDVVEKYGADALR 297
|
570
....*....|....*
gi 19528361 610 LIILADVAPTSHRNW 624
Cdd:cd00668 298 YYLTSLAPYGDDIRL 312
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
71-610 |
9.07e-29 |
|
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: 124.04 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNV-FQPmGWDSFGLPAENAANQR-GVEPASWTE---------------QN 133
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVpYVP-GWDCHGLPIELKVEKElGIKKKDIEKvgiaefrekcreyalKY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 134 IAQMKEQLKRLGCSFDWNHELSTCSPKYYK--WtqHLFLMLHRHGLAYQNEALVNWDPVDKTVLADeqvdangcswrsgA 211
Cdd:COG0060 134 VDEQREDFKRLGVWGDWDNPYLTMDPEYEEsiW--WALKKLYEKGLLYKGLKPVPWCPRCGTALAE-------------A 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 212 KVEKKLLRQwfirTSAYAK-QLLDGLEDPTLRDwrdiinlqrhwigecdgyafnlltsASGLlrVWTT------------ 278
Cdd:COG0060 199 EVEYKDVTS----PSIYVKfPVKDEKALLLLED-------------------------AYLV--IWTTtpwtlpanlava 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 279 -HPE------HLKDPHAFLV-----------LRSNHH--LSKLKGAD--SLSAANPFAGttmpvVFSDEVTFPpksdVYL 336
Cdd:COG0060 248 vHPDidyvlvEVTGGERLILaealveavlkeLGIEDYevLATFKGAEleGLRYEHPFYY-----VVGYDRAHP----VIL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 337 A--------------APSFRGEDKDLWDSYGLAFTS----NGKDEESLSP--------ANWEMLRKevLQAATRL-NVGG 389
Cdd:COG0060 319 GdyvttedgtgivhtAPGHGEDDFEVGKKYGLPVLNpvddDGRFTEEAPLfaglfvkdANPAIIED--LKERGALlAREK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 390 YRVS-----------------------SKLK-----------------------------DWLISRQRYWGTPIPIVHCQ 417
Cdd:COG0060 397 ITHSyphcwrcktpliyratpqwfismDKLRdraleaiekvnwipewgegrfgnmlenrpDWCISRQRYWGVPIPIWVCE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 418 KCGAVPVPE----------EQLPVSLPPKDSPKEAFL---CDCPKCGeKDARRETDTMDTFVDS--SWYylryldAQNSE 482
Cdd:COG0060 477 DCGELHRTEevigsvaellEEEGADAWFELDLHRPFLdetLKCPKCG-GTMRRVPDVLDVWFDSgsMHF------AVLEN 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 483 RifdtalTKKFMPVDLYI-GGKEHavlhlyyaR--FinHFLH--SCGLSPTSePFSRLLVQGMVMGrsfrvkGSGRyvpe 557
Cdd:COG0060 550 R------EELHFPADFYLeGSDQT--------RgwF--YSSLltSTALFGRA-PYKNVLTHGFVLD------EDGR---- 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 19528361 558 teveivnakknqavlketkepvvmtweKMSKSKLNGVEPSDMFNEYGTDTTRL 610
Cdd:COG0060 603 ---------------------------KMSKSLGNVVDPQEVIDKYGADILRL 628
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
63-245 |
9.18e-27 |
|
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: 115.60 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 63 KYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLK 142
Cdd:COG0143 2 KFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 143 RLGCSFDWNHelSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVD--------------------- 201
Cdd:COG0143 82 KLGISFDNFI--RTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEgtcpkcgaedaygdqcencga 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19528361 202 -------ANGCSWRSGAKVEKKLLRQWFIRTSAYAKQLLDGLEdpTLRDWR 245
Cdd:COG0143 160 tleptelINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIE--ENPDIQ 208
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
64-257 |
1.84e-26 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 112.38 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 64 YYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLKR 143
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 144 LGCSFDwnHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQV----------DANG-----C--- 205
Cdd:pfam09334 81 FNISFD--DYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVegtcphcgseDARGdqcenCgrh 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19528361 206 ----------SWRSGAKVEKKLLRQWFIRTSAYAKQLLDGLEDPTLRdWRD-IINLQRHWIGE 257
Cdd:pfam09334 159 leptelinpkCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNPE-WPEnVKNMVLEWLKE 220
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
63-257 |
2.75e-25 |
|
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: 107.62 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 63 KYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLK 142
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 143 RLGCSFDwnHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLAdeqvdangcSWRSgakvEKkllrQWF 222
Cdd:cd00814 81 WLNISFD--YFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------EWRE----EE----HYF 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 19528361 223 IRTSAYAKQLLDGLEDPTLRDWRD-IINLQRHWIGE 257
Cdd:cd00814 142 FRLSKFQDRLLEWLEKNPDFIWPEnARNEVLSWLKE 177
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
29-778 |
9.03e-25 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 111.24 E-value: 9.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 29 NDNPELTSDVKHR-IEAHWRE-QLSGGQFNPKDSQDKYYVLSM-FPYP--SGNLHMGHVRVYTIADSVARFQRMCGKNVF 103
Cdd:PRK14900 10 ENRTELAKGYEHReVEARWYPfWQERGYFHGDEHDRTRPPFSIvLPPPnvTGSLHLGHALTATLQDVLIRWKRMSGFNTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 104 QPMGWDSFGLPAENAANQ--RGVEPAS---------------WTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQ 166
Cdd:PRK14900 90 WLPGTDHAGIATQMIVEKelKKTEKKSrhdlgreaflervwaWKEQYGSRIGEQHKALGASLDWQRERFTMDEGLSRAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 167 HLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVD----ANGCSWrSGAKVEKKLLRQWFIRTSAYAKQLLDGL-----E 237
Cdd:PRK14900 170 EVFVRLHEEGLIYREKKLINWCPDCRTALSDLEVEheeaHQGELW-SFAYPLADGSGEIVVATTRPETMLGDTAvavhpL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 238 DPTlrdWRDIINlqRHWIGECDGYAFNLLTSA--------SGLLRVWTTHpehlkDPHAFLV-LRSNHHLSKLKGADS-- 306
Cdd:PRK14900 249 DPR---YMALHG--KKVRHPITGRTFPIVADAilvdpkfgTGAVKVTPAH-----DFNDFEVgKRHGLEMITVIGPDGrm 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 307 LSAANPFAGTtmpvvfsDEVTFPPKSDVYLAAPSF-RGEDKDLWdSYGLAFTSNGKDEESLSPaNW----EMLRKEVLQA 381
Cdd:PRK14900 319 TAEAGPLAGL-------DRFEARKEVKRLLAEQGLdRGAKPHVL-PLGRCQRSATILEPLLSD-QWyvriEPLARPAIEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 382 A----TRLNVGGYRVS-----SKLKDWLISRQRYWGTPIPIVHCQKcGAVPVPEEQlPVSlppkdspkeaflcdCPKCGE 452
Cdd:PRK14900 390 VeqgrTRFIPEQWTNTymawmRNIHDWCISRQLWWGHQIPAWYCPD-GHVTVARET-PEA--------------CSTCGK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 453 KDARRETDTMDTFVDSSWYYLRYLDAQNserifDTALTKKFMPVDLYIGGkeHAVLHLYYARFINHFLHSCGlsptSEPF 532
Cdd:PRK14900 454 AELRQDEDVLDTWFSSGLWPFSTMGWPE-----QTDTLRTFYPTSVMETG--HDIIFFWVARMMMMGLHFMG----EVPF 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 533 SRLLVQGMVMGRsfrvKGsgryvpeteveivnakknqavlketkepvvmtwEKMSKSKLNGVEPSDMFNEYGTDTTRLII 612
Cdd:PRK14900 523 RTVYLHPMVRDE----KG---------------------------------QKMSKTKGNVIDPLVITEQYGADALRFTL 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 613 LADVAPTSHRNWSSATFPGILNWQKRLW-------LTLQDFQQAREDQTASDVVPTSEEFLA-------EDAKLFDARNF 678
Cdd:PRK14900 566 AALTAQGRDIKLAKERIEGYRAFANKLWnasrfalMNLSGYQERGEDPARLARTPADRWILArlqravnETVEALEAFRF 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 679 YVKGAT---FNYRHAQQLSVAISK--MQGLTNSLRRTPKHVLRHgkqferALAAQIIMLAPMAPHFASELWSKFvaipgr 753
Cdd:PRK14900 646 NDAANAvyaFVWHELCDWYIELAKeaLASEDPEARRSVQAVLVH------CLQTSYRLLHPFMPFITEELWHVL------ 713
|
810 820
....*....|....*....|....*.
gi 19528361 754 lnPASQELQ-WSEDVLAQRWPDIDPA 778
Cdd:PRK14900 714 --RAQVGASaWADSVLAAEYPRKGEA 737
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
63-238 |
1.04e-21 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 99.96 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 63 KYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLK 142
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 143 RLGCSFDwnHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEAL--------VNWDPvdktvlaDEQVDANGCSWRSGAKVE 214
Cdd:PRK11893 82 ALNISYD--DFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEgwycvrceEFYTE-------SELIEDGYRCPPTGAPVE 152
|
170 180
....*....|....*....|....
gi 19528361 215 KKLLRQWFIRTSAYAKQLLDGLED 238
Cdd:PRK11893 153 WVEEESYFFRLSKYQDKLLELYEA 176
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
71-614 |
1.66e-21 |
|
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: 96.92 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQ-----------------N 133
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIEkmgiaefnakcrefalrY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 134 IAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWdPVdktvladeqvdangcswrsgakv 213
Cdd:cd00818 90 VDEQEEQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW-PL----------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 214 ekkLLR---QWFIRTSAYAKQLLDGLEdptlrdwrdiinlQRHWIgecdgyafnlltsasgllrvwtthPEHLKDphafl 290
Cdd:cd00818 146 ---IYRatpQWFIRVTKIKDRLLEAND-------------KVNWI------------------------PEWVKN----- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 291 vlrsnhhlsklkgadslsaanpfagttmpvvfsdevtfppksdvylaapSFRgedkdlwdsyglaftsngkdeeslspan 370
Cdd:cd00818 181 -------------------------------------------------RFG---------------------------- 183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 371 wEMLRkevlqaatrlnvggyrvssKLKDWLISRQRYWGTPIPIVHCQkcgavpvpeeqlpvslppkdspkeaflcdcpKC 450
Cdd:cd00818 184 -NWLE-------------------NRRDWCISRQRYWGTPIPVWYCE-------------------------------DC 212
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 451 GEKDARRETDTMDTFVDS--SWYylryldAQNSERiFDTALTKKFMPVDLYIGGKE------HAVLHLYYARFinhflhs 522
Cdd:cd00818 213 GEVLVRRVPDVLDVWFDSgsMPY------AQLHYP-FENEDFEELFPADFILEGSDqtrgwfYSLLLLSTALF------- 278
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 523 cglspTSEPFSRLLVQGMVMGrsfrvkGSGRyvpeteveivnakknqavlketkepvvmtweKMSKSKLNGVEPSDMFNE 602
Cdd:cd00818 279 -----GKAPYKNVIVHGFVLD------EDGR-------------------------------KMSKSLGNYVDPQEVVDK 316
|
570
....*....|..
gi 19528361 603 YGTDTTRLIILA 614
Cdd:cd00818 317 YGADALRLWVAS 328
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
42-201 |
2.22e-21 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 100.18 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 42 IEAHWREQ-LSGGQFNPKDSQDKYYVLsMFPYP--SGNLHMGHVRVYTIADSVARFQRMCGKNV-FQPmGWDSFGLpA-- 115
Cdd:PRK05729 14 VEAKWYQKwEEKGYFKPDDNSKKPFSI-VIPPPnvTGSLHMGHALNNTLQDILIRYKRMQGYNTlWLP-GTDHAGI-Atq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 116 ---ENAANQRGV---------------EpasWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGL 177
Cdd:PRK05729 91 mvvERQLAAEGKsrhdlgrekflekvwE---WKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAVREVFVRLYEKGL 167
|
170 180
....*....|....*....|....
gi 19528361 178 AYQNEALVNWDPVDKTVLADEQVD 201
Cdd:PRK05729 168 IYRGKRLVNWDPKLQTALSDLEVE 191
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
42-201 |
4.88e-21 |
|
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: 98.97 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 42 IEAHWREQ-LSGGQFNPK-DSQDKYYVLsMFPYP--SGNLHMGHVRVYTIADSVARFQRMCGKNV-FQPmGWDSFGLpA- 115
Cdd:COG0525 12 VEAKWYQYwEENGYFKADpDSDKEPFTI-VIPPPnvTGSLHMGHALNNTLQDILIRYKRMQGYNTlWQP-GTDHAGI-At 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 116 ----ENAANQRG-----------VEPA-SWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAY 179
Cdd:COG0525 89 qavvERQLAEEGksrhdlgrekfLERVwEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSKAVREVFVRLYEKGLIY 168
|
170 180
....*....|....*....|..
gi 19528361 180 QNEALVNWDPVDKTVLADEQVD 201
Cdd:COG0525 169 RGKRLVNWDPKLKTALSDLEVE 190
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
42-201 |
3.50e-19 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 93.15 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 42 IEAHWRE-QLSGGQFNP------KDSQDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLp 114
Cdd:PTZ00419 33 VESGWYEwWEKSGFFKPaedaksLNSGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGI- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 115 aenaANQRGVEPASWTEQNI----------------------AQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLML 172
Cdd:PTZ00419 112 ----ATQVVVEKKLMKEENKtrhdlgreeflkkvwewkdkhgNNICNQLRRLGSSLDWSREVFTMDEQRSKAVKEAFVRL 187
|
170 180
....*....|....*....|....*....
gi 19528361 173 HRHGLAYQNEALVNWDPVDKTVLADEQVD 201
Cdd:PTZ00419 188 YEDGLIYRDTRLVNWCCYLKTAISDIEVE 216
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
77-197 |
1.41e-16 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 84.53 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 77 LHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLP----AENAANQ--------RGV--EPASWTEQ-----NIA-- 135
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPilgiAERIARGdpetielyKSLygIPEEELEKfkdpeYIVey 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19528361 136 ---QMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLAD 197
Cdd:PRK12300 81 fseEAKEDMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNPVGD 145
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
41-612 |
6.11e-16 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 82.68 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 41 RIEAHWREQlsgGQFNPK-DSQDKYYVLSMfPYP--SGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFG----L 113
Cdd:PLN02943 68 RIYNWWESQ---GYFKPNfDRGGDPFVIPM-PPPnvTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGiatqL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 114 PAENAANQRGVEPA------------SWTEQNIAQMKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQN 181
Cdd:PLN02943 144 VVEKMLASEGIKRTdlgrdeftkrvwEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVRLHEKGLIYQG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 182 EALVNWDPVDKTVLADEQVDANgcswrsgakvekkllrqwfirtsayakqlldglEDPtlrdwrdiinlqrhwiGECDGY 261
Cdd:PLN02943 224 SYMVNWSPNLQTAVSDLEVEYS---------------------------------EEP----------------GTLYYI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 262 AFNLLTSASGLLRVWTTHPEHLKDPHAFLVLRSNHHLSKLKGAdslSAANPFAGTTMPVVFSDEVTFPP----------- 330
Cdd:PLN02943 255 KYRVAGGSEDFLTIATTRPETLFGDVAIAVNPEDDRYSKYIGK---MAIVPMTYGRHVPIIADRYVDKDfgtgvlkispg 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 331 --KSDVYLA--------------------APSFRGE-DKDLW---DSYGLAFTSN------------GKDEESLSPANW- 371
Cdd:PLN02943 332 hdHNDYLLArklglpilnvmnkdgtlnevAGLYWFEaREKLWsdlEETGLAVKKEphtlrvprsqrgGEVIEPLVSKQWf 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 372 ---EMLRKEVLQAATR--LNVGGYRVS-------SKLKDWLISRQRYWGTPIPI--VHCQKCgavpvpEEQLPVSLPPKD 437
Cdd:PLN02943 412 vtmEPLAEKALKAVENgeLTIIPERFEkiynhwlSNIKDWCISRQLWWGHRIPVwyIVGKDC------EEDYIVARSAEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 438 SPKEAFlcdcPKCGEK-DARRETDTMDTFVDSSWYYLRYLDAQN-SERIFdtaltKKFMPVDLYIGGkeHAVLHLYYARF 515
Cdd:PLN02943 486 ALEKAR----EKYGKDvEIYQDPDVLDTWFSSALWPFSTLGWPDvSAEDF-----KKFYPTTVLETG--HDILFFWVARM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 516 INHFLHSCGlsptSEPFSRLLVQGMVMgrsfrvKGSGRyvpeteveivnakknqavlketkepvvmtweKMSKSKLNGVE 595
Cdd:PLN02943 555 VMMGIEFTG----TVPFSYVYLHGLIR------DSQGR-------------------------------KMSKTLGNVID 593
|
650
....*....|....*..
gi 19528361 596 PSDMFNEYGTDTTRLII 612
Cdd:PLN02943 594 PLDTIKEFGTDALRFTL 610
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
19-640 |
2.05e-15 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 81.10 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 19 RRLLTQSCTRNDNPeltSDVKHRIEAHWReqlSGGQF--NPKDSQDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQR 96
Cdd:PLN02381 89 KKRLSSQMAKQYSP---SAVEKSWYAWWE---KSGYFgaDAKSSKPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 97 MCGKNVFQPMGWDSFGLPAE-----NAANQRGV------------EPASWTEQNIAQMKEQLKRLGCSFDWNHELSTCSP 159
Cdd:PLN02381 163 MSGYNALWVPGVDHAGIATQvvvekKLMRERHLtrhdigreefvsEVWKWKDEYGGTILNQLRRLGASLDWSRECFTMDE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 160 KYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQVDANGCSwrsgakvEKKLLrqwfiRTSAYAKQLldgledp 239
Cdd:PLN02381 243 QRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISDVEVDYIDIK-------ERTLL-----KVPGYDKPV------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 240 tlrdwrdiinlqrhwigecdgyAFNLLTSAS-------GLLRVWTTHPEHLKDPHAFLVLRSNHHLSKLKGAdslSAANP 312
Cdd:PLN02381 304 ----------------------EFGVLTSFAyplegglGEIVVATTRIETMLGDTAIAIHPDDERYKHLHGK---FAVHP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 313 FAGTTMPVVFSDEVTFP----------PKSDV------------------------------YLAAPSFRG--------E 344
Cdd:PLN02381 359 FNGRKLPIICDAILVDPnfgtgavkitPAHDPndfevgkrhnlefiniftddgkinsnggseFAGMPRFAAreaviealQ 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 345 DKDLWD-------SYGLAFTSNGKDEESLSP---ANWEMLRKEVLQAAT-----RLNV-------GGYRVSSKLKDWLIS 402
Cdd:PLN02381 439 KKGLYRgaknnemRLGLCSRTNDVVEPMIKPqwfVNCSSMAKQALDAAIdgenkKLEFipkqylaEWKRWLENIRDWCIS 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 403 RQRYWGTPIP----IVHCQKCGAVPVPEEQLPVSLPPKDSPKEAFLcdcPKCGEK-DARRETDTMDTFVDSSWYYLRYLD 477
Cdd:PLN02381 519 RQLWWGHRIPawyvTLEDDQLKELGSYNDHWVVARNESDALLEASQ---KFPGKKfELSQDPDVLDTWFSSGLFPLSVLG 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 478 AQNserifDTALTKKFMPVDLYIGGkeHAVLHLYYARFINHFLHSCGlsptSEPFSRLLVQGMVM---GRSFRvKGSGRY 554
Cdd:PLN02381 596 WPD-----DTDDLKAFYPTSVLETG--HDILFFWVARMVMMGMQLGG----DVPFRKVYLHPMIRdahGRKMS-KSLGNV 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 555 VpeTEVEIVNAKKNQAVLKETKE------PVVMTWEKMSKSKLNGVEpsdmfnEYGTDTTRLIILADVAPTSHRNWSSAT 628
Cdd:PLN02381 664 I--DPLEVINGISLEGLHKRLEEgnldpkELVVAKEGQKKDFPNGIA------ECGTDALRFALVSYTAQSDKINLDILR 735
|
730
....*....|..
gi 19528361 629 FPGILNWQKRLW 640
Cdd:PLN02381 736 VVGYRQWCNKLW 747
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
624-747 |
5.62e-15 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes bacterial and eukaryotic mitochondrial members, as well as LeuRS from the archaeal Halobacteria. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.
Pssm-ID: 153412 [Multi-domain] Cd Length: 117 Bit Score: 71.87 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 624 WSSATFPGILNWQKRLWltlqdfQQAREDQTASDVVPTSEEFLAEDAKLFDARNFYVKGATFNYRHaQQLSVAISKMQGL 703
Cdd:cd07958 1 WSDSGVEGAYRFLNRVW------RLVTELAEALAAPAAAAELSEEDKELRRKLHKTIKKVTEDIER-LRFNTAIAALMEL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19528361 704 TNSLRRTPKHVLRHGKQFERALAAQIIMLAPMAPHFASELWSKF 747
Cdd:cd07958 74 VNALYKYKKKDAQHAAVLREALETLVLLLAPFAPHIAEELWEEL 117
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
61-234 |
4.15e-14 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 76.34 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 61 QDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPaswtEQNIAQMKEQ 140
Cdd:PRK00133 1 MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITP----EELIARYHAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 141 ----LKRLGCSFDWNHelSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLADEQV----------DANG-- 204
Cdd:PRK00133 77 hkrdFAGFGISFDNYG--STHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVkgtcpkcgaeDQYGdn 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19528361 205 C----------------SWRSGAKVEKKLLRQWFIRTSAYAKQLLD 234
Cdd:PRK00133 155 CevcgatysptelinpkSAISGATPVLKESEHFFFKLPRFEEFLKE 200
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
59-238 |
7.58e-13 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 72.14 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 59 DSQDKYYVLSMFPYPSGNLHMGHVrvYT--IADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQ 136
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHA--YTtiAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 137 MKEQLKRLGCSFDwnHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEaLVNWDPV-DKTVLADEQVDANGCSWRSGAKVEk 215
Cdd:PRK12267 79 FKELWKKLDISYD--KFIRTTDERHKKVVQKIFEKLYEQGDIYKGE-YEGWYCVsCETFFTESQLVDGGKCPDCGREVE- 154
|
170 180
....*....|....*....|....*
gi 19528361 216 kLLRQ--WFIRTSAYAKQLLDGLED 238
Cdd:PRK12267 155 -LVKEesYFFRMSKYQDRLLEYYEE 178
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
71-197 |
1.70e-10 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 64.79 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAE-------NAANQRGVEP-------ASWTEQNIAQ 136
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIElkvlqslDQEARKELTPiklrakaAKFAKKTVDT 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19528361 137 MKEQLKRLGCSFDWNHELSTCSPKYYKWTQHLFLMLHRHGLAYQNEALVNWDPVDKTVLAD 197
Cdd:PLN02843 121 QRESFKRYGVWGDWENPYLTLDPEYEAAQIEVFGQMFLNGYIYRGRKPVHWSPSSRTALAE 181
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
584-779 |
9.34e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 59.11 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 584 EKMSKSKLNGVEPSDMFNEYGTDTTRLIILADVAPTSHRNWSSATFPGILNWQKRLWLTLQDFQQAREDqtasdvvptsE 663
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQLERFYELAKELIEIGGE----------E 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 664 EFLAEDAKLFDARNFYVKGATFNYRHAQQLSVAISKMQGLTNSLR----RTPKHVlrhGKQFERALAAQIIMLAPMAPHF 739
Cdd:PRK12300 646 ELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELLNDLRwylrRVGEAN---NKVLREVLEIWIRLLAPFTPHL 722
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19528361 740 ASELWSKFvaipGRLNPASQElqwsedvlaqRWPDIDPAY 779
Cdd:PRK12300 723 AEELWHKL----GGEGFVSLE----------KWPEPDESK 748
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
71-117 |
4.08e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 50.88 E-value: 4.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAEN 117
Cdd:PLN02882 47 PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEY 93
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
71-156 |
9.77e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which 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.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 46.32 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 71 PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWTEQNIAQMKEQLK-RLGCSFD 149
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEyMFLQAAD 85
|
....*..
gi 19528361 150 WNHELST 156
Cdd:cd00802 86 FLLLYET 92
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
29-116 |
1.71e-05 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 48.81 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 29 NDNPELTSDvKHRIEAHWReqlSGGQFNPKDSQDKYYVLSMF----PYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQ 104
Cdd:PTZ00427 69 SENPNIVEE-EEKVLKYWK---SIDAFNTSNKLAKNKKAYIFydgpPFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVER 144
|
90
....*....|..
gi 19528361 105 PMGWDSFGLPAE 116
Cdd:PTZ00427 145 KFGWDCHGLPIE 156
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
62-121 |
4.66e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 47.37 E-value: 4.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 62 DKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQ 121
Cdd:PLN02959 45 EKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGMPIKASADK 104
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
397-413 |
2.97e-04 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 44.57 E-value: 2.97e-04
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
697-746 |
6.69e-04 |
|
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: 40.85 E-value: 6.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19528361 697 ISKMQGLTNSLRRTPKHVLRHgkqferALAAQIIMLAPMAPHFASELWSK 746
Cdd:pfam08264 46 LIKDRLYGEEPDSRAQTTLYE------VLETLLRLLAPFMPFITEELWQK 89
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
51-180 |
1.29e-03 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 42.39 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19528361 51 SGGQFNPKDSQDKYYVLSMFPYPSGNLHMGHVRVYTIADSVARFQRMCGKNVFQPMGWDSFGLPAENAANQRGVEPASWT 130
Cdd:PLN02224 58 SSSQESTVDEADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHC 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 19528361 131 EQNIAQMKEQLKRLGCSFDwnHELSTCSPKYYKWTQHLFLMLHRHGLAYQ 180
Cdd:PLN02224 138 DIISQSYRTLWKDLDIAYD--KFIRTTDPKHEAIVKEFYARVFANGDIYR 185
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
397-413 |
1.34e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 42.40 E-value: 1.34e-03
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
78-146 |
1.92e-03 |
|
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: 41.63 E-value: 1.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19528361 78 HMGHVRVYTIADSVARFQRMCGKNVFQpmgwdsfglpAEN----------AANQRGVEPASWTEQNIAQMKEQLKRLGC 146
Cdd:COG0215 37 HIGHARTFVVFDVLRRYLRYLGYKVTY----------VRNitdvddkiikRAAEEGESIWELAERYIAAFHEDMDALGV 105
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
717-747 |
2.46e-03 |
|
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: 38.73 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|.
gi 19528361 717 HGKQFERALAAQIIMLAPMAPHFASELWSKF 747
Cdd:cd07959 87 NKDLLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
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