|
Name |
Accession |
Description |
Interval |
E-value |
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
18-857 |
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: 1430.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 18 YDAAAIEGKWQRIWDEKGTYKTDEDPNKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGL 97
Cdd:COG0495 5 YNPKEIEKKWQKYWEENGTFKADEDSSKPKYYVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 98 PAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNT 177
Cdd:COG0495 85 PAENAAIKNGVHPAEWTYENIANMRRQLKRLGLSYDWSREIATCDPEYYKWTQWIFLQLYEKGLAYRKEAPVNWCPVDQT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 178 VLANEQVVEGRCWRCGSVPEKRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWIGRSEGAEIDFTLADkdgvtp 257
Cdd:COG0495 165 VLANEQVIDGRCWRCGAPVEKKELPQWFLKITDYADELLDDLDKLDGWPEKVKTMQRNWIGRSEGAEVDFPVEG------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 258 TDRKITVFTTRADTLFGVSFFLLPPESPLAAELVAgTECEAAFKELKEATEKVSSVDRQGSAREKHGVFTGRYVINPING 337
Cdd:COG0495 239 SDEKITVFTTRPDTLFGATFMVLAPEHPLVKELAT-PEQNAAVAAFIEEAKKKSEIERTSETKEKTGVFTGLYAINPLTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 338 RPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICEKDDPLYDElkderelkvtsvsWDHAMDAEGYLV 417
Cdd:COG0495 318 EKIPIWIADYVLMDYGTGAVMAVPAHDQRDFEFAKKYGLPIKQVIAPEDGDDPDI-------------LEEAYTGDGVLI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 418 QSGEFTGLkggKHSEAVDAIIGWLSERGLGRKKVQFRLRDWLISRQRYWGNPIPMIHCDCCGDVPVPYDQLPVTLPDNLD 497
Cdd:COG0495 385 NSGEFDGL---DSEEAKEAIIEWLEEKGLGKRKVNYRLRDWLISRQRYWGEPIPIIHCEDCGVVPVPEDQLPVELPEDVD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 498 L-GAGET-LAEYAPFYETTCPKCGRPAKRITDTMDTFTCSSWYYLRYCDPHNTELPFSKESVDRWMPVDNYIGGIEHAIL 575
Cdd:COG0495 462 FdPTGGSpLARAPEWVNVTCPKCGGPARRETDTMDTFVDSSWYYLRYTDPHNDEAPFDPEAANYWLPVDQYIGGIEHAIL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 576 HLLYSRFWTKVLRDLGMIDADEPFTNLLCQGMVKD--HNG------ETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAP 647
Cdd:COG0495 542 HLLYARFFTKVLRDLGLVSFDEPFKRLLTQGMVLEvgKDGvviggiEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGP 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 648 PEKDFDWDEKAVAGANRFIKRAWSIVWQLSAgahAGEFDARSLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEI 727
Cdd:COG0495 622 PERDLEWSDSGVEGAYRFLNRVWRLVVDEAE---ALKLDVADLSEADKELRRALHKTIKKVTEDIERLRFNTAIAALMEL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 728 VNAASKYLNETPAEDRVLEldfRVAHDIVAILAPICPHWAEELYHEaLHLEGSVYNEPWPEFDPELAKADTVEIAVQVMG 807
Cdd:COG0495 699 VNALYKAKDSGEADRAVLR---EALETLVLLLAPFAPHIAEELWER-LGHEGSVADAPWPEADEAALVEDEVTIVVQVNG 774
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1545248450 808 KVRGHATIAADATREQTEKAALA--AISEQLEGKTVRKVIVVPGKLVNVVAN 857
Cdd:COG0495 775 KVRGKIEVPADASKEELEAAALAdeKVQKFLEGKTIRKVIVVPGKLVNIVVK 826
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
18-857 |
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: 1068.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 18 YDAAAIEGKWQRIWDEKGTYKTDEDPNKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGL 97
Cdd:TIGR00396 1 YNHIEIEEKWQQKWDENKTFKVTDDSSKPKYYILSMFPYPSGALHMGHVRNYTITDVLSRYYRMKGYNVLHPIGWDAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 98 PAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNT 177
Cdd:TIGR00396 81 PAENAAIKRGIHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYKWTQWIFLELFEKGLAYVKEADVNWCPNDGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 178 VLANEQVV-EGRCWRCGSVPEKRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWIGRSEGAEIDFTLADkdgvt 256
Cdd:TIGR00396 161 VLANEQVDsDGRSWRGDTPVEKKELKQWFLKITAYAEELLNDLEELDHWPESVKEMQRNWIGKSEGVEITFKIAD----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 257 pTDRKITVFTTRADTLFGVSFFLLPPESPLaAELVAGTECE-AAFkeLKEATEKvSSVDRQGSAREKHGVFTGRYVINPI 335
Cdd:TIGR00396 236 -HDEKITVFTTRPDTIFGVTYLALAPEHPL-VEKAAENNPKvAAF--IKKILNK-TVAERTKATKEKKGVDTGIKAIHPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 336 NGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICekddplydelKDERELKVTSvswdhAMDAEGY 415
Cdd:TIGR00396 311 TGEKIPIWVANYVLMEYGTGAVMGVPAHDERDFEFAQKYGLPIKPVID----------PAEKDLSLTA-----AYTEDGV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 416 LVQSGEFTGLkggKHSEAVDAIIGWLSERGLGRKKVQFRLRDWLISRQRYWGNPIPMIHCDCCGDVPVPYDQLPVTLPD- 494
Cdd:TIGR00396 376 LVNSGEFNGL---NSSEARNAIIDMLEKEGKGKRKVNYRLRDWGFSRQRYWGEPIPIIHCEDGGVVPVPEEDLPVILPEd 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 495 -NLDLGAGETLAEYAPFYETTCPKCGRPAKRITDTMDTFTCSSWYYLRYCDPHNTELPFSKESVDRWMPVDNYIGGIEHA 573
Cdd:TIGR00396 453 vVYDGDGGSPLSRIPEWVNVTCPSCGKPALRETDTMDTFAGSSWYYLRYLDPKNTDGPFDKEKAEYWLPVDLYIGGIEHA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 574 ILHLLYSRFWTKVLRDLGMIDADEPFTNLLCQGMV--------------------------KDHN-----GETMSKSKGN 622
Cdd:TIGR00396 533 ILHLLYARFFHKFLRDIGYVNTKEPFKKLINQGMVlgfyyppngkvpadvlterdekgkdkAGGElvyvgYEKMSKSKGN 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 623 VVPPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKAVAGANRFIKRAWSIVWQLSAGAHAGEFDARSLKGQAGELFRTLN 702
Cdd:TIGR00396 613 GIDPQEIVESYGADALRLFIMFMGPIAASLEWNESGLEGARRFLDRVWNLVYEITGELDAASLTVTALEEAQKELRRDVH 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 703 GLGARCTSDYDRGQ-FNTAISAVMEIVNAASKYLNEtpaedrvlELDFRVAHDIVAILAPICPHWAEELYHEALHLEGSV 781
Cdd:TIGR00396 693 KFLKKVTEDLEKREsFNTAISAMMELLNKLYKAKKE--------ALMLEYLKGFVTVLSPFAPHLAEELWEKLGSEPFII 764
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545248450 782 YNEPWPEFDPELAKADTVEIAVQVMGKVRGHATIAADATREQTEKAALAA--ISEQLEGKTVRKVIVVPGKLVNVVAN 857
Cdd:TIGR00396 765 DNAKWPVVDETALVEDKTLIVVQVNGKFRAKITVPKDADEEQVEELAKQDpeVKKYLENKTIKKVIYVPGKLVNFVIK 842
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
1-856 |
0e+00 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 833.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 1 MSDVNDTNA-TQASRFPAYDAAAIEGKWQRIWDEKGTYKTDE--DPNKPKKYVLEMFPYPSG-DLHMGHARNYTIGDAMA 76
Cdd:PLN02563 62 PSALTSTTAkTTPAAKRAYPFHEIEPKWQRYWEENRTFRTPDdvDTSKPKFYVLDMFPYPSGaGLHVGHPEGYTATDILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 77 RQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKM 156
Cdd:PLN02563 142 RYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYDWDREISTTEPEYYKWTQWIFLQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 157 WEKGLAYRATSPVNWCPSCNTVLANEQVVEGRCWRCGSVPEKRELSQWYLKITDYAQELLDDLDKLTgWPENVKAQQRNW 236
Cdd:PLN02563 222 LKRGLAYQAEVPVNWCPALGTVLANEEVVDGLSERGGHPVIRKPMRQWMLKITAYADRLLEDLDDLD-WPESIKEMQRNW 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 237 IGRSEGAEIDFTLADKDGvTPTDRKITVFTTRADTLFGVSFFLLPPESPLAAELVAgTECEAAFKELKEATEKVSSVDRQ 316
Cdd:PLN02563 301 IGRSEGAELDFSVLDGEG-KERDEKITVYTTRPDTLFGATYLVVAPEHPLLSSLTT-AEQKEAVEEYVDAASRKSDLERT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 317 GSAREKHGVFTGRYVINPINGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICEKDDPLYDElkde 396
Cdd:PLN02563 379 ELQKEKTGVFTGSYAINPATGEAIPIWVADYVLGSYGTGAIMAVPAHDTRDFEFAQKFDLPIKWVVKPADGNEDDA---- 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 397 relkvtsvswDHAMDAEGYLVQSGEfTGLK--GGKHSEAVDAIIGWLSERGLGRKKVQFRLRDWLISRQRYWGNPIPMIH 474
Cdd:PLN02563 455 ----------EKAYTGEGVIVNSSS-SGLDinGLSSKEAAKKVIEWLEETGNGKKKVNYKLRDWLFARQRYWGEPIPVVF 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 475 CDCCGD-VPVPYDQLPVTLPDNLDL---GAGET-LAEYAPFYETTCPKCGRPAKRITDTMDTFTCSSWYYLRYCDPHNTE 549
Cdd:PLN02563 524 LEDSGEpVPVPESDLPLTLPELDDFtptGTGEPpLAKAVSWVNTVDPSSGKPARRETNTMPQWAGSCWYYLRFMDPKNSN 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 550 LPFSKESVDRWMPVDNYIGGIEHAILHLLYSRFWTKVLRDLGMIDADEPFTNLLCQGMV---------KDHNGE------ 614
Cdd:PLN02563 604 ALVDKEKEKYWMPVDLYVGGAEHAVLHLLYARFWHKVLYDIGVVSTKEPFQCLVNQGMIlgeveytafKDSDGEyvsadt 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 615 ---------------------------------------TMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDWD 655
Cdd:PLN02563 684 adrlgelqqekipeekviksgdsfvlkddpsirliarahKMSKSRGNVVNPDDVVSEYGADSLRLYEMFMGPLRDSKTWS 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 656 EKAVAGANRFIKRAWSIVwqLSAGAHAGEFDARSLKGQAG---ELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAAS 732
Cdd:PLN02563 764 TSGVEGVHRFLGRTWRLV--VGAPLPDGSFRDGTVVTDEEpslEQLRLLHKCIAKVTEEIESTRFNTAISAMMEFTNAAY 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 733 KYlNETPAEdrvleldfrVAHDIVAILAPICPHWAEELYHEALHlEGSVYNEPWPEFDPELAKADTVEIAVQVMGKVRGH 812
Cdd:PLN02563 842 KW-DKVPRE---------AIEPFVLLLSPYAPHLAEELWFRLGH-SNSLAYEPWPEANPSYLVDDTVVLPVQINGKTRGT 910
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 1545248450 813 ATIAADATREQTEKAAL--AAISEQLEGKTVRKVIVVPGKLVNVVA 856
Cdd:PLN02563 911 IEVEEGCSEDDAFALASqdEKLSKYLDGKEIKKRIYVPGKILNVIL 956
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
16-810 |
1.67e-95 |
|
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: 318.54 E-value: 1.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 16 PAYDAAAIEGKWQRIWDEKGTYKTDEDPNKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAF 95
Cdd:TIGR00422 3 KDYDPHEVEKKWYKKWEKSGFFKPDGNSNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 96 GLPAEN-----AAIKHNTQAAA-----------WTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEK 159
Cdd:TIGR00422 83 GIATQVkvekkLGAEGKTKHDLgreefrekiweWKEESGGTIKNQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 160 GLAYRATSPVNWCPSCNTVLANEQVVEgrcwrcgsvpEKRELSQWYlkitdyaqellddldkltgwpenvkaqqrnwigr 239
Cdd:TIGR00422 163 GLIYRGEYLVNWDPKLNTAISDIEVEY----------KEVKGKLYY---------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 240 segaeIDFTLADKDgvtptDRKITVFTTRADTLFGVSFFLLPPESPlaaelvagteceaafkelkeatekvssvdrqgsa 319
Cdd:TIGR00422 199 -----IRYPLANGS-----KDYLVVATTRPETMFGDTAVAVHPEDE---------------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 320 REKHgvFTGRYVINPINGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICEKDDpLYDELKDEREL 399
Cdd:TIGR00422 235 RYKH--LIGKKVILPLTGRKIPIIADEYVDMEFGTGAVKVTPAHDFNDYEWGKRHNLEFINILDEDGL-LNENAGKYQGL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 400 KVTS-----VSWdhaMDAEGYLVQSGEF-----TGLKGGKHSE-----------------AVDAI----IGWLSERglgR 448
Cdd:TIGR00422 312 TRFEarkkiVED---LKEEGLLVKIEPHthnvgTCWRSGTVVEpllskqwfvkvekladkALEAAeegeIKFVPKR---M 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 449 KKVQFR----LRDWLISRQRYWGNPIPMIHCDCCGDVPVPYDQLPVTLPDNldLGAGETLaeyapfyettcpkcgrpaKR 524
Cdd:TIGR00422 386 EKRYLNwlrnIKDWCISRQLIWGHRIPVWYCKECGEVYVAKEEPLPDDKTN--TGPSVEL------------------EQ 445
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 525 ITDTMDT-FTCSSWyylrycdphntelPFS-------KESVDRWMPVDNYIGGieHAILhllysRFWtkVLRdlgMIDAD 596
Cdd:TIGR00422 446 DTDVLDTwFSSSLW-------------PFStlgwpdeTKDLKKFYPTDLLVTG--YDII-----FFW--VAR---MIFRS 500
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 597 E------PFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKAVAGANRFIKRAW 670
Cdd:TIGR00422 501 LaltgqvPFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESARNFLNKLW 580
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 671 SI---VWQLSAGAHAGEFDARSLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIV--------NAASKYLNETP 739
Cdd:TIGR00422 581 NAsrfVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIwndfcdwyIELVKYRLYNG 660
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1545248450 740 AEDRVLELDFRVAH---DIVAILAPICPHWAEELYHEALHLEGSVYNEPWPEF-----DPELAKAdtVEIAVQVMGKVR 810
Cdd:TIGR00422 661 NEAEKKAARDTLYYvldKALRLLHPFMPFITEEIWQHFKEGADSIMLQSYPVVdaefvDEEAEKA--FELLKEIIVSIR 737
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
47-238 |
1.59e-86 |
|
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: 277.98 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 47 KKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMR 126
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 127 RMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCpscntvlaneqvvegrcwrcgsvpekRELSQWYL 206
Cdd:cd00812 81 RMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWC--------------------------KLLDQWFL 134
|
170 180 190
....*....|....*....|....*....|....
gi 1545248450 207 KI--TDYAQELLDDLDKLTGWPENVKAQQRNWIG 238
Cdd:cd00812 135 KYseTEWKEKLLKDLEKLDGWPEEVRAMQENWIG 168
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
18-828 |
5.42e-86 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 291.33 E-value: 5.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 18 YDAAAIEGKWQRIWDEKGTYKTDEDPNKPKkyvlemF------PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIG 91
Cdd:PRK13208 10 YDPEELEEKWQKIWEEEGTYKFDPDERKPV------YsidtppPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 92 FDAFGLPAE-----NAAIKHNTQAAA--------WTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWE 158
Cdd:PRK13208 84 WDDNGLPTErkvekYYGIRKDDISREefielcreLTDEDEKKFRELWRRLGLSVDWSLEYQTISPEYRRISQKSFLDLYK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 159 KGLAYRATSPVNWCPSCNTVLANEQVvegrcwrcgsvpEKRElsqwylKITDYAQellddldkltgwpenvkaqqrnwig 238
Cdd:PRK13208 164 KGLIYRAEAPVLWCPRCETAIAQAEV------------EYRE------REGKLNY------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 239 rsegaeIDFTLADkdgvtptDRKITVFTTRadtlfgvsffllpPESpLAAelvagteCEAAFkelkeatekVSSVDrqgs 318
Cdd:PRK13208 201 ------IKFPVED-------GEEIEIATTR-------------PEL-LPA-------CVAVV---------VHPDD---- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 319 AREKHgvFTGRYVINPINGRPAPIwVAD-YVLMDYGTGAVMgvpC---GDQRDFDFAKKYGLEIAPIICEKD--DPLYDE 392
Cdd:PRK13208 234 ERYKH--LVGKTAIVPLFGVEVPI-LADpLVDPDFGTGAVM---IctfGDKTDVTWWRELNLPTRIIIDEDGrmTEAAGK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 393 L-----KDERELKVTsvswdhAMDAEGYLVQSGEFT---GL--KGGKHSEAV-------------DAIIgwlsERGlgrK 449
Cdd:PRK13208 308 LagltiEEARKKIVE------DLKSGGLLGKQEPIKhnvKFceRCDTPLEILvtrqwfikvldlkEELL----ERG---K 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 450 KVQF-----RLR----------DWLISRQRYWGNPIPMIHCDCCGDVPVPYD-QLPVtlpdnldlgagETLAEYAPFYet 513
Cdd:PRK13208 375 EINWypehmRVRlenwieglnwDWCISRQRYFGTPIPVWYCKDCGHPILPDEeDLPV-----------DPTKDEPPGY-- 441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 514 TCPKCGrpAKRI---TDTMDT-FTCS-SWYYlrycdphNTELPFSKESVDRWMPVDNYIGGieHAILhllysRFW--TKV 586
Cdd:PRK13208 442 KCPQCG--SPGFegeTDVMDTwATSSiTPLI-------VTGWERDEDLFEKVFPMDLRPQG--HDII-----RTWlfYTI 505
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 587 LRDLgMIDADEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILfIAPPEKDFDWDEKAVAGANRFI 666
Cdd:PRK13208 506 LRAY-LLTGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDTPFDEKQVKIGRRLL 583
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 667 KRAWSI---VWQLSAGAHAGEFDA-----RSLKGQagelfrtLNGLGARCTSDYDRGQFNTAISAVMEIV--NAASKYL- 735
Cdd:PRK13208 584 TKLWNAsrfVLHFSADPEPDKAEVlepldRWILAK-------LAKVVEKATEALENYDFAKALEEIESFFwhVFCDDYLe 656
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 736 -------NETPAEDR-----VLeldFRVAHDIVAILAPICPHWAEELYHEaLHlEGSVYNEPWPEFDPELAK---ADTVE 800
Cdd:PRK13208 657 lvksrayGEDEEEEQksaryTL---YTVLDTLLRLLAPFLPFITEEVWSW-LY-GGSVHRASWPEPDEELIDeedEELGE 731
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1545248450 801 IAVQVMGKVRG--------------HATIAADATREQTEKAA 828
Cdd:PRK13208 732 LAKEILSAVRKykseaglslnaplkKVEVYGPADLELLEAAE 773
|
|
| tRNA-synt_1_2 |
pfam13603 |
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ... |
234-441 |
6.42e-77 |
|
Leucyl-tRNA synthetase, Domain 2; This is a family of the conserved region of Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4.
Pssm-ID: 433342 [Multi-domain] Cd Length: 185 Bit Score: 247.46 E-value: 6.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 234 RNWIGRSEGAEIDFTLADkdgvtpTDRKITVFTTRADTLFGVSFFLLPPESPLAAELvagTECEAAFKELKEATEKVSSV 313
Cdd:pfam13603 1 RNWIGRSEGAEITFPVEG------TDEKIEVFTTRPDTLMGVTFVALAPEHPLVEKL---AEKNPEVAAFIEECKNTSEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 314 DRQGSAREKHGVFTGRYVINPINGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICEKDDPLYDEL 393
Cdd:pfam13603 72 ERTSETKEKEGVFTGLYAIHPITGEKIPIWIANFVLMEYGTGAVMAVPAHDQRDFEFAKKYNLPIKPVIQPEDGDLDLDI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1545248450 394 KDErelkvtsvswdhAMDAEGYLVQSGEFTGLkggKHSEAVDAIIGWL 441
Cdd:pfam13603 152 MTE------------AYTEEGILVNSGEFDGL---DSEEAKEAIIKKL 184
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
26-655 |
1.65e-68 |
|
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: 238.46 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 26 KWQRIWDEKGTYKTDEDPNKPKK-YVLEMFP-YPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENA- 102
Cdd:pfam00133 1 QIYEFWDEQGYFKPELEKRKGKPsFTIHDGPpNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 103 ----------------AIKHNTQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRAT 166
Cdd:pfam00133 81 ekklgikekktrhkygREEFREKCREWKMEYADEIRKQFRRLGRSIDWDREYFTMDPELEAAVWEVFVRLHDKGLIYRGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 167 SPVNWCPSCNTVLANEQVVegrcwrcgsvpekrelsqwYLKITDYAqellddldkltgwpenvkaqqrnwigrsegAEID 246
Cdd:pfam00133 161 KLVNWSPALNTALSNLEVE-------------------YKDVKGPS------------------------------IHVA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 247 FTLADKDGVtptdrKITVFTTRADTLFGVSFFLLPPESPLAAELVAGTECEAAFKELkeaTEKVSSVDRQGSAREKHgvF 326
Cdd:pfam00133 192 FPLADDEGA-----SLVIWTTTPWTLPGNTAVAVNPEFDYVITGEGYILAEALLKSL---YKKGTDKKILEDFRGKE--L 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 327 TGRYVINPINGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIIceKDDPLYDE---------LKDER 397
Cdd:pfam00133 262 EGKEAIHPFVNREIPIITDDYVDMEFGTGAVHIAPAHGENDYEVGQRHNLEVINPV--DDDGTFTEeapdfqgvyRFDAR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 398 ELKVTsvswdhAMDAEGYLVQSGEFT-----GLKGGKHSE-----------------AVDAI--IGWLSERGLGRKKVQF 453
Cdd:pfam00133 340 KKIVE------LLTEKGLLLKIEPFThsypfCWRSGTPIIpratpqwfvrmdeladqALEAVekVQFVPKSGEKRYFNWL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 454 R-LRDWLISRQRYWGNPIPM--------IHCDCCGDVPVPYDQLPVTLPDNLDLGAGETLAEYAPFYEttcpkcgrpakR 524
Cdd:pfam00133 414 AnIQDWCISRQRWWGHPIPAwvskdteeVVCRGELFELVAGRFEEEGSIKWLHREAKDKLGYGKGTLE-----------Q 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 525 ITDTMDT-FTCSSWYYLRYCDPHNTELPFSKesvdrWMPVDNYIGGIEHailhllySRFWTKVLRDLGM-IDADEPFTNL 602
Cdd:pfam00133 483 DEDVLDTwFSSGSWPFSTLGWPFVNTEEFKK-----FFPADMLLEGSDQ-------TRGWFYRMIMLSTaLTGSVPFKNV 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1545248450 603 LCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFiAPPEKDFDWD 655
Cdd:pfam00133 551 LVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLAN-SDYGRDINLS 602
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
432-654 |
1.96e-60 |
|
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: 207.87 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 432 EAVDAIIGWLSERglgrKKVQfrlRDWL-ISRQRYWGNPIPMihcdccgdvpvpydqlpvtlpdnldlgagetlaeyapf 510
Cdd:cd00812 147 KDLEKLDGWPEEV----RAMQ---ENWIgCSRQRYWGTPIPW-------------------------------------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 511 yettcpkcgrpakriTDTMDTFTCSSWYYLRYCDPHNTELP------FSKESVDRWMPVDNYIGGIEHAILHLLYSRFWT 584
Cdd:cd00812 182 ---------------TDTMESLSDSTWYYARYTDAHNLEQPyegdleFDREEFEYWYPVDIYIGGKEHAPNHLLYSRFNH 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 585 KVLRDLGMIdADEPFTNLLCQGMVKdHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDW 654
Cdd:cd00812 247 KALFDEGLV-TDEPPKGLIVQGMVL-LEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDADFDW 314
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
14-809 |
2.00e-58 |
|
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: 214.93 E-value: 2.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 14 RFPA-YDAAAIEGKWQRIWDEKGTYKTDEDPNKPKK--YVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPI 90
Cdd:TIGR00392 1 KFPMrGNLSKREEKILAFWQENDIFEKVKKLNKGKPefIFHDGPPYANGSIHLGHALNKILKDIILRYKTMQGFNVTRKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 91 GFDAFGLPAENAAIKHN-------------------------TQAAAWTyqnmdnalATMRRMGFSYDYDRLVRTCDPEY 145
Cdd:TIGR00392 81 GWDTHGLPIEHKVEKKLgisgkkeissleieefrekcrefalKQIEEQR--------EQFQRLGVWGDWENPYKTMDPSY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 146 YKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVEGRCWRcgsvpEKRELSQwYLKITDYAQELLDDLDKL--- 222
Cdd:TIGR00392 153 EESQWWLFKEAHEKGLLYRGLKPVYWSPRCRTALAEAEVEYKENYK-----DVKDPSI-YVKFPVKKDKKTYLKVKLssl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 223 -----TGW--PENVKAqqrnwigrSEGAEIDFTLADKDGvtptdRKITVFttradtlfgvsffllppespLAAELVagte 295
Cdd:TIGR00392 227 liwttTPWtlPSNLAI--------AVHPDFEYALVQDNT-----KVEYFI--------------------LAKKLV---- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 296 cEAAFKELKEATEKVSSVdrQGSAREkhgvftGRYVINPINGR------PAPIWV-ADYVLMDYGTGAVMGVPCGDQRDF 368
Cdd:TIGR00392 270 -EKLYNKAGSDYEIIKTF--KGSDLE------GLEYEHPLYDFvsqlkeGAPVVIgGDHVTTEDGTGIVHTAPGHGEEDY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 369 DFAKKYGLEIAPIICEK---DDPLYDE----LKDErELKV--TSVSWDHAMDAEGYLVQSGE------------------ 421
Cdd:TIGR00392 341 EIGKKYGLEVLSPVDEKgvyTEGVNDFqgrfVKDA-DKDIikANKIIIEQLKDKGLLLKAEKithsyphcwrtktpviyr 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 422 -----FTGLKGGKhSEAVDAI--IGWLSERGLGRKK--VQFRlRDWLISRQRYWGNPIPMIHCDCCGDVpvpydqlpvtl 492
Cdd:TIGR00392 420 ateqwFIKTKDIK-DQMLEQIkkVNWVPEWGEGRFGnwLENR-PDWCISRQRYWGIPIPIWYCEDTGEP----------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 493 pdnLDLGAGETLAEYAPFYE----------------TTCPKCGRPAKRITDTMDTF--TCSSWYYLrycdphnTELPFSK 554
Cdd:TIGR00392 487 ---IVVGSIEELIELIELKGidawfedlhrdfldkiTLKSGDGGEYRRVPDVLDVWfdSGSMPYAS-------IHYPFEN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 555 ESVDRWMPVDNYIGGIEHailhllySRFWTKVLRDLGMIDADE-PFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPY 633
Cdd:TIGR00392 557 EKFKEVFPADFILEGSDQ-------TRGWFYSSLAIGTALFGQaPYKNVITHGFTLDEKGRKMSKSLGNVVDPLKVINKY 629
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 634 GADTMRLVILFIAPPE-KDFDWDEkaVAGANRFIKRawsIVWQLSAGAHA--------GEFDARSLKGQAGE---LFRTL 701
Cdd:TIGR00392 630 GADILRLYVASSDPWEdLRFSDEI--LKQVVEKYRK---IRWNTYRFLLTyanldkfdPLFNSVAVEKFPEEdrwILSRL 704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 702 NGLGARCTSDYDRGQFNTAISAVME-IVNAASK-YLN--------ETPAEDR--VLELDFRVAHDIVAILAPICPHWAEE 769
Cdd:TIGR00392 705 NSLVEEVNEALEKYNFHKVLRALQDfIVEELSNwYIRiirdrlycEAKDNDKraAQTTLYYALLTLVRLLAPFLPHTAEE 784
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1545248450 770 LYHEALHLEG--SVYNEPWPEFDPElAKADTVEIAVQVMGKV 809
Cdd:TIGR00392 785 IYQNLPGGEEeeSVHLNLWPEVDEE-FIDEALEANMAIVREI 825
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
15-823 |
5.42e-56 |
|
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: 208.40 E-value: 5.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 15 FPA-YDAAAIEGKWQRIWDEKGTY-KTDEDPNKPKKYVLemF---PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHP 89
Cdd:COG0060 12 FPMrANLPKREPEILKFWEENDIYeKSREARAGRPKFVL--HdgpPYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 90 IGFDAFGLPAENAAIKHN------------------------TQAAAWTYQnmdnalatMRRMGFSYDYDRLVRTCDPEY 145
Cdd:COG0060 90 PGWDCHGLPIELKVEKELgikkkdiekvgiaefrekcreyalKYVDEQRED--------FKRLGVWGDWDNPYLTMDPEY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 146 YK--WgqWMFLKMWEKGLAYRATSPVNWCPSCNTVLAN-EqvVEGRcwrcgsvpEKRELSQWY-LKITDYAQELLDDLDK 221
Cdd:COG0060 162 EEsiW--WALKKLYEKGLLYKGLKPVPWCPRCGTALAEaE--VEYK--------DVTSPSIYVkFPVKDEKALLLLEDAY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 222 L-----TGW--PENVkaqqrnwiGRSEGAEIDFTLADkdgVTPTDRKItvfttradtlfgvsffllppespLAAELVagt 294
Cdd:COG0060 230 LviwttTPWtlPANL--------AVAVHPDIDYVLVE---VTGGERLI-----------------------LAEALV--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 295 ecEAAFKELK-EATEKVSSVdrQGSAREkhgvftGRYVINPI-----NGRPAPIWVADYVLMDYGTGAVMGVP-CGdQRD 367
Cdd:COG0060 273 --EAVLKELGiEDYEVLATF--KGAELE------GLRYEHPFyyvvgYDRAHPVILGDYVTTEDGTGIVHTAPgHG-EDD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 368 FDFAKKYGLEIAPIIcekdDP---LYDELKDERELKVtsvsWD------HAMDAEGYLVQSGEFTglkggkHS------- 431
Cdd:COG0060 342 FEVGKKYGLPVLNPV----DDdgrFTEEAPLFAGLFV----KDanpaiiEDLKERGALLAREKIT------HSyphcwrc 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 432 ---------------------EAVDAI--IGWLSERGLGRkkvqFR-----LRDWLISRQRYWGNPIPMIHCDCCGDVPV 483
Cdd:COG0060 408 ktpliyratpqwfismdklrdRALEAIekVNWIPEWGEGR----FGnmlenRPDWCISRQRYWGVPIPIWVCEDCGELHR 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 484 PYD----------QLPVTLPDNLDLGA---GETLaeyapfyetTCPKCGRPAKRITDTMDtftC-----SSWYY-LRycd 544
Cdd:COG0060 484 TEEvigsvaelleEEGADAWFELDLHRpflDETL---------KCPKCGGTMRRVPDVLD---VwfdsgSMHFAvLE--- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 545 phNTElpfskesvDRWMPVDNYIGGI-EHailhllysR--FWTKVLrdLGMIDADE-PFTNLLCQGMVKDHNGETMSKSK 620
Cdd:COG0060 549 --NRE--------ELHFPADFYLEGSdQT--------RgwFYSSLL--TSTALFGRaPYKNVLTHGFVLDEDGRKMSKSL 608
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 621 GNVVPPSSVIEPYGADTMRlviLFIA--PPEKD--FDWDEkaVAGANRFIKRAWSIVWQLSAGAHagEFDARSLKGQAGE 696
Cdd:COG0060 609 GNVVDPQEVIDKYGADILR---LWVAssDYWGDlrFSDEI--LKEVRDVYRRLRNTYRFLLANLD--DFDPAEDAVPYED 681
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 697 --------LFRtLNGLGARCTSDYDRGQFNTAISAVMEIVNA--------ASK---YLNETPAEDR-----VLeldFRVA 752
Cdd:COG0060 682 lpeldrwiLSR-LNELIKEVTEAYDNYDFHRAYRALHNFCVEdlsnwyldISKdrlYTEAADSLDRraaqtTL---YEVL 757
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545248450 753 HDIVAILAPICPHWAEELYheaLHL----EGSVYNEPWPEFDPELAKADTVEiAVQVMGKVRGHATIAADATREQ 823
Cdd:COG0060 758 ETLVRLLAPILPFTAEEIW---QNLpgeaEESVHLADWPEVDEELIDEELEA-KWDLVREVRSAVLKALEAARKE 828
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
16-810 |
2.99e-53 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 199.95 E-value: 2.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 16 PAYDAAAIEGKWQRIWDEKGTYKTDEDPNKPkkYVLeMFPYP--SGDLHMGHARNYTIGDAMARQARMRGYDVL------ 87
Cdd:PRK05729 7 KTYDPKEVEAKWYQKWEEKGYFKPDDNSKKP--FSI-VIPPPnvTGSLHMGHALNNTLQDILIRYKRMQGYNTLwlpgtd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 88 ---------------------HPIGFDAFglpaenaaIKHntqAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYY 146
Cdd:PRK05729 84 hagiatqmvverqlaaegksrHDLGREKF--------LEK---VWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 147 KWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVegrcwrcgSVPEKRELsqWYLKitdYAqellddldkltgwp 226
Cdd:PRK05729 153 KAVREVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVE--------YKEVKGKL--WHIR---YP-------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 227 envkaqqrnwigrsegaeidftLADKDGVtptdrkITVFTTRADTLFG-----VSffllpPESPlaaelvagteceaafk 301
Cdd:PRK05729 206 ----------------------LADGSDY------LVVATTRPETMLGdtavaVN-----PEDE---------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 302 elkeatekvssvdrqgsaREKHgvFTGRYVINPINGRPAPIwVAD-YVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIap 380
Cdd:PRK05729 237 ------------------RYKH--LIGKTVILPLVGREIPI-IADeYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPM-- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 381 IICekddplydelkderelkvtsvswdhaMDAEGYLVQS-GEFTGLkggKHSEAVDAIIGWLSERGL-----------GR 448
Cdd:PRK05729 294 INI--------------------------MDEDGTINENpGEYQGL---DRFEARKAIVADLEELGLlvkiephthsvGH 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 449 ---------------------------------KKVQF--------------RLRDWLISRQRYWGNPIPMIHCDcCGDV 481
Cdd:PRK05729 345 sdrsgvviepylsdqwfvkmkplakpaleavenGEIKFvperwektyfhwmeNIQDWCISRQLWWGHRIPAWYDE-DGEV 423
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 482 PVpydqlpvtlpdnldlgagetlaeyAPFYETTCPKCgrPAKRITDTMDT-FtcSSWyylrycdphnteL-PFS------ 553
Cdd:PRK05729 424 YV------------------------GREEPEAREKA--LLTQDEDVLDTwF--SSA------------LwPFStlgwpe 463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 554 -KESVDRWMPVDNYIGGieHAILHllysrFWtkVLRdlgMIDA------DEPFTNLLCQGMVKDHNGETMSKSKGNVVPP 626
Cdd:PRK05729 464 kTEDLKRFYPTSVLVTG--FDIIF-----FW--VAR---MIMMglhftgQVPFKDVYIHGLVRDEQGRKMSKSKGNVIDP 531
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 627 SSVIEPYGADTMRLVILFIAPPEKDFDWDEKAVAGANRFIKRAWSI---VWQLSAGAHAGEFDARSLKGQAGELFRT-LN 702
Cdd:PRK05729 532 LDLIDKYGADALRFTLAALASPGRDIRFDEERVEGYRNFANKLWNAsrfVLMNLEGADVGELPDPEELSLADRWILSrLN 611
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 703 GLGARCTSDYDRGQFNTAISAV------------MEIV----NAASKylNETPAE-DRVLELDFRVAHdivailaPICPH 765
Cdd:PRK05729 612 RTVAEVTEALDKYRFDEAARALyefiwnefcdwyLELAkpvlQEAAK--RATRATlAYVLEQILRLLH-------PFMPF 682
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1545248450 766 WAEELYHEALHLEG--SVYNEPWPEFDPELAKADTVEIA--VQVMGKVR 810
Cdd:PRK05729 683 ITEELWQKLAPLGIeeSIMLAPWPEADEAIDEAAEAEFEwlKELITAIR 731
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
17-811 |
1.11e-52 |
|
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: 197.97 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 17 AYDAAAIEGKWQRIWDEKGTYKTDEDPNKPKkYVLeMFPYP--SGDLHMGHARNYTIGDAMARQARMRGYDVL------- 87
Cdd:COG0525 6 TYDPKEVEAKWYQYWEENGYFKADPDSDKEP-FTI-VIPPPnvTGSLHMGHALNNTLQDILIRYKRMQGYNTLwqpgtdh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 88 --------------------HPIGFDAFglpaenaaIKHntqAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYK 147
Cdd:COG0525 84 agiatqavverqlaeegksrHDLGREKF--------LER---VWEWKEESGGTITNQLRRLGASCDWSRERFTMDEGLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 148 WGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVegrcwrcgSVPEKRELsqWYLKitdYAqellddldkltgwpe 227
Cdd:COG0525 153 AVREVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVE--------HEEVKGHL--WHIR---YP--------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 228 nvkaqqrnwigrsegaeidftLADKDGvtptdrKITVFTTRADTLFG-----VSffllpPESPlaaelvagteceaafke 302
Cdd:COG0525 205 ---------------------LADGSG------YIVVATTRPETMLGdtavaVH-----PEDE----------------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 303 lkeatekvssvdrqgsaREKHgvFTGRYVINPINGRPAPIwVAD-YVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIapI 381
Cdd:COG0525 236 -----------------RYKH--LIGKTVILPLVGREIPI-IADeYVDPEFGTGAVKITPAHDPNDFEVGKRHNLPM--I 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 382 ICekddplydelkderelkvtsvswdhaMDAEGYLVQS-GEFTGLkggKHSEAVDAIIGWLSERGL-----------GR- 448
Cdd:COG0525 294 NI--------------------------LDEDGTINENaGKYRGL---DRFEARKAIVADLEELGLlvkvephkhsvGHs 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 449 --------------------------------KKVQF--------------RLRDWLISRQRYWGNPIPMIHCDcCGDVP 482
Cdd:COG0525 345 drsgtviepylsdqwfvkmkplakpaieavedGEIKFvperwektyfhwmeNIRDWCISRQLWWGHRIPAWYCP-DGEVY 423
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 483 VPYDQlpvtlpdnldlgagetlaeyapfyETTCPKCGrpAKRIT---DTMDT-FtcSSWyylrycdphnteL-PFS---- 553
Cdd:COG0525 424 VARTE------------------------PEACAKAG--SVNLTqdeDVLDTwF--SSA------------LwPFStlgw 463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 554 ---KESVDRWMPVDNYIGGieHAILHllysrFWtkVLRdlgMIDA------DEPFTNLLCQGMVKDHNGETMSKSKGNVV 624
Cdd:COG0525 464 pekTEDLKYFYPTSVLVTG--FDIIF-----FW--VAR---MIMMglhftgEVPFKDVYIHGLVRDEQGRKMSKSKGNVI 531
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 625 PPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKAVAGANRFIKRAWSI---VWQLSAGAHAGEFDARSLKGQAGELFRT- 700
Cdd:COG0525 532 DPLDLIDKYGADALRFTLAALASPGRDIKFDEERVEGYRNFANKLWNAsrfVLMNLEGFDPGLDPDPEELSLADRWILSr 611
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 701 LNGLGARCTSDYDRGQFNTAISAV------------MEIVNAAskYLNETPAEDR--------VLEldfrvahDIVAILA 760
Cdd:COG0525 612 LNKTIAEVTEALEKYRFDEAAQALydfvwnefcdwyLELAKPR--LYGGDEAAKRetratlvyVLE-------QILRLLH 682
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1545248450 761 PICPHWAEELYHE--ALHLEGSVYNEPWPEFDPELAKADTVEIAVQVMGKVRG 811
Cdd:COG0525 683 PFMPFITEEIWQKlpPRKEGESIMLAPWPEADEELIDEEAEAEFEWLKEVISA 735
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
61-809 |
1.11e-52 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 198.17 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 61 LHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLP----AEnaAIKHNTQAAAWTYQNM------------------ 118
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPilgiAE--RIARGDPETIELYKSLygipeeelekfkdpeyiv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 119 ----DNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNtvlaneQVVEgrcwrcgs 194
Cdd:PRK12300 79 eyfsEEAKEDMKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDN------NPVG-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 195 vpekrelsqwylkitdyAQELLDDldkltgwpenvkaqqrnwigrsEGAEI-DFTL----ADKDGVTPTdrkitvFTTRA 269
Cdd:PRK12300 145 -----------------DHDLLDG----------------------EEPEIvEYTLikfeESEDLILPA------ATLRP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 270 DTLFGVSFFLLPPESP-LAAElVAGTE---CEAAFKELKEATEKVsSVDRQGSAREkhgvFTGRYVINPINGRPAPIWVA 345
Cdd:PRK12300 180 ETIFGVTNLWVNPDATyVKAE-VDGEKwivSKEAAEKLSFQDRDV-EIIEEIKGSE----LIGKKVKNPVTGKEVPILPA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 346 DYVLMDYGTGAVMGVPCGDQRDF--------DFAKKYGLEIAPIIcekDDPLYDEL--KDE-RELKVTSVSwDHAMD--- 411
Cdd:PRK12300 254 DFVDPDNGTGVVMSVPAHAPYDYvalrdlkkNKELLDVIEPIPLI---EVEGYGEFpaKEVvEKLGIKSQE-DPELEeat 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 412 --------AEGYLVQS-GEFTGLkggKHSEAVDAIIGWLSERGLGRK--------------------------------- 449
Cdd:PRK12300 330 kevyraefHKGVLKENtGEYAGK---PVREAREKITKDLIEKGIADImyefsnrpvycrcgtecvvkvvkdqwfidysdp 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 450 --------------------KVQFR-----LRDWLISRQRYWGNPIP-----MIhcDCCGD----------------VPV 483
Cdd:PRK12300 407 ewkelahkaldnmeiipeeyRKEFEntidwLKDRACARRRGLGTRLPwdeewII--ESLSDstiymayytiahkireYGI 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 484 PYDQLPVTLPDNLDLGAG--ETLAEyapfyettcpKCGRPAKRItDTMdtftcsswyylrycdphntelpfsKESVDRWM 561
Cdd:PRK12300 485 KPEQLTPEFFDYVFLGKGdpEEVSK----------KTGIPKEIL-EEM------------------------REEFLYWY 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 562 PVDNYIGGIEHAILHLLYSRF----------WTKvlrdlGMIdadepfTNllcqGMVKdHNGETMSKSKGNVVPPSSVIE 631
Cdd:PRK12300 530 PVDWRHSGKDLIPNHLTFFIFnhvaifpeekWPR-----GIV------VN----GFVL-LEGKKMSKSKGNVIPLRKAIE 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 632 PYGADTMRLVILFIAPPEKDFDWDEKAVAGANRFIKRAWSIvwqlsagahagefdARSLKGQAGELFRT---------LN 702
Cdd:PRK12300 594 EYGADVVRLYLTSSAELLQDADWREKEVESVRRQLERFYEL--------------AKELIEIGGEEELRfidkwllsrLN 659
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 703 GLGARCTSDYDRGQFNTAI-SAVMEIVNAASKYLNETPAED-RVLEldfRVAHDIVAILAPICPHWAEELYHEALHlEGS 780
Cdd:PRK12300 660 RIIKETTEAMESFQTRDAVqEAFYELLNDLRWYLRRVGEANnKVLR---EVLEIWIRLLAPFTPHLAEELWHKLGG-EGF 735
|
890 900
....*....|....*....|....*....
gi 1545248450 781 VYNEPWPEFDPELAKaDTVEIAVQVMGKV 809
Cdd:PRK12300 736 VSLEKWPEPDESKID-EEAELAEEYVKRL 763
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
55-237 |
3.81e-45 |
|
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: 167.04 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAA----------------WTYQNM 118
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGKtrhdlgreeflekcweWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 119 DNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVvegrCWRCGSVPEK 198
Cdd:cd00817 90 GKIREQLKRLGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV----CSRSGDVIEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1545248450 199 RELSQWYLKITDYAQELLDDLDK--LTGWPENVKAQQRNWI 237
Cdd:cd00817 166 LLKPQWFVKVKDLAKKALEAVKEgdIKFVPERMEKRYENWL 206
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1-788 |
2.02e-44 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 173.64 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 1 MSDVN---DTNATQASRfpAYDAAAIEGKWQRIWDEKGTYKTDEDP-NKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMA 76
Cdd:PRK14900 1 MSNPNpieNENRTELAK--GYEHREVEARWYPFWQERGYFHGDEHDrTRPPFSIVLPPPNVTGSLHLGHALTATLQDVLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 77 RQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAA-----------------AWTYQNMDNALATMRRMGFSYDYDRLVR 139
Cdd:PRK14900 79 RWKRMSGFNTLWLPGTDHAGIATQMIVEKELKKTEkksrhdlgreaflervwAWKEQYGSRIGEQHKALGASLDWQRERF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 140 TCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVvegrcwrcgsvpEKRELSQWYLkitdyaqellddl 219
Cdd:PRK14900 159 TMDEGLSRAVREVFVRLHEEGLIYREKKLINWCPDCRTALSDLEV------------EHEEAHQGEL------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 220 dkltgWpenvkaqqrnwigrsegaEIDFTLADkdgvtpTDRKITVFTTRADTLFGVSFFLLPPESPLAAELVagteceaa 299
Cdd:PRK14900 214 -----W------------------SFAYPLAD------GSGEIVVATTRPETMLGDTAVAVHPLDPRYMALH-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 300 fkelkeatekvssvdrqgsarekhgvftGRYVINPINGRPAPIwVADYVLMD--YGTGAVMGVPCGDQRDFDFAKKYGLE 377
Cdd:PRK14900 257 ----------------------------GKKVRHPITGRTFPI-VADAILVDpkFGTGAVKVTPAHDFNDFEVGKRHGLE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 378 IAPII------CEKDDPL--YDELKDERELKvtsvswdhAMDAEGYLVQSGEFTGLKGGKHSEAVDAIIGWLSER----- 444
Cdd:PRK14900 308 MITVIgpdgrmTAEAGPLagLDRFEARKEVK--------RLLAEQGLDRGAKPHVLPLGRCQRSATILEPLLSDQwyvri 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 445 -GLGRKKV----QFRLR------------------DWLISRQRYWGNPIPMIHCdccgdvpvpydqlpvtlPDnldlgAG 501
Cdd:PRK14900 380 ePLARPAIeaveQGRTRfipeqwtntymawmrnihDWCISRQLWWGHQIPAWYC-----------------PD-----GH 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 502 ETLAEYAPfyeTTCPKCG-RPAKRITDTMDT-FTCSSWYYLRYCDPHNTelpfskESVDRWMPVDNYIGGieHAILHlly 579
Cdd:PRK14900 438 VTVARETP---EACSTCGkAELRQDEDVLDTwFSSGLWPFSTMGWPEQT------DTLRTFYPTSVMETG--HDIIF--- 503
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 580 srFWTKVLRDLGM-IDADEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKA 658
Cdd:PRK14900 504 --FWVARMMMMGLhFMGEVPFRTVYLHPMVRDEKGQKMSKTKGNVIDPLVITEQYGADALRFTLAALTAQGRDIKLAKER 581
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 659 VAGANRFIKRAW--SIVWQLSAGAHagEFDARSLKGQA---------GELFRTLNglgaRCTSDYDRGQFNTAISAVMEI 727
Cdd:PRK14900 582 IEGYRAFANKLWnaSRFALMNLSGY--QERGEDPARLArtpadrwilARLQRAVN----ETVEALEAFRFNDAANAVYAF 655
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1545248450 728 VNA-----------ASKYLNETPAEDRVLELDFRVAHDIVAILAPICPHWAEELYHEalhLEGSVYNEPWPE 788
Cdd:PRK14900 656 VWHelcdwyielakEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWHV---LRAQVGASAWAD 724
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
16-631 |
4.55e-38 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 153.62 E-value: 4.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 16 PAYDAAAIEGKWQRIWDEKGTYKTDEDP---NKPKKYVLeMFPYP--SGDLHMGHARNYTIGDAMARQARMRGYDVLHPI 90
Cdd:PTZ00419 26 ASYDPKEVESGWYEWWEKSGFFKPAEDAkslNSGKKFVI-VLPPPnvTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 91 GFDAFG----------LPAENAAIKHN-------TQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMF 153
Cdd:PTZ00419 105 GTDHAGiatqvvvekkLMKEENKTRHDlgreeflKKVWEWKDKHGNNICNQLRRLGSSLDWSREVFTMDEQRSKAVKEAF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 154 LKMWEKGLAYRATSPVNWCPSCNTVLANEQV----VEGrcwrcgsvPEKrelsqwyLKITDYAQELldDLDKLTgwpenv 229
Cdd:PTZ00419 185 VRLYEDGLIYRDTRLVNWCCYLKTAISDIEVefeeIEK--------PTK-------ITIPGYDKKV--EVGVLW------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 230 kaqqrnwigrsegaEIDFTLADKDgvtptDRKITVFTTRADTLFG-VSffllppesplaaelVAgteceaafkelkeate 308
Cdd:PTZ00419 242 --------------HFAYPLEDSG-----QEEIVVATTRIETMLGdVA--------------VA---------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 309 kVSSVDrqgsAREKHgvFTGRYVINP-INGRPAPIwVAD--YVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPIicek 385
Cdd:PTZ00419 273 -VHPKD----ERYKK--LHGKELIHPfIPDRKIPI-IADdeLVDMEFGTGAVKITPAHDPNDYEIAKRHNLPFINI---- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 386 ddplydelkderelkvtsvswdhaMDAEGYLVQ-SGEFTGLkggKHSEAVDAIIGWLSERGLGRKKV--QFRL------- 455
Cdd:PTZ00419 341 ------------------------FTLDGKINEnGGEFAGM---HRFDCRRKIEEELKEMGLLRDKVpnPMRLprcsrsg 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 456 -------------------------------------------------RDWLISRQRYWGNPIPMIHCDCCGDVPVPYD 486
Cdd:PTZ00419 394 divepmlipqwyvnckdmakraveavrngelkiipsshenvwyhwleniQDWCISRQLWWGHRIPAYRVISKGPETDPSD 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 487 QLPVTLPDNLDlgagETLAEYAPFYETTcpKCGRPAKRITDTMDTFTCSSWYylrycdphntelPFS-------KESVDR 559
Cdd:PTZ00419 474 EEPWVVARSEE----EALEKAKKKFGLS--EEDFELEQDEDVLDTWFSSGLF------------PFStlgwpdqTDDLQR 535
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545248450 560 WMPvdNYIGGIEHAILHllysrFWTK--VLRDLGMIDAdEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIE 631
Cdd:PTZ00419 536 FFP--TSLLETGSDILF-----FWVArmVMMSLHLTDK-LPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIE 601
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
24-841 |
1.49e-34 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 142.60 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 24 EGKWQRIWDEKGTYKTDEDPNKPKKYVL-EMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAE-- 100
Cdd:PLN02843 9 EPEIQKLWEENQVYKRVSDRNNGESFTLhDGPPYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIElk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 101 ------------NAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSP 168
Cdd:PLN02843 89 vlqsldqearkeLTPIKLRAKAAKFAKKTVDTQRESFKRYGVWGDWENPYLTLDPEYEAAQIEVFGQMFLNGYIYRGRKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 169 VNWCPSCNTVLAnEQVVEgrcwrcgsVPEKRELSQWY--LKITDYAQELLDDLDKL-----------TGW--PENVkAQQ 233
Cdd:PLN02843 169 VHWSPSSRTALA-EAELE--------YPEGHVSKSIYvaFPVVSPSETSPEELEEFlpglslaiwttTPWtmPANA-AVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 234 RNwigrsegAEIDFTLADKDGVTPTDRKITVFTTRAD---TLFGVSFFLLppespLAAELVAGTECeaafkelKEATEKV 310
Cdd:PLN02843 239 VN-------DKLQYSVVEVQSFSEDESTSGGNKKKRPgnvLKEQQKLFLI-----VATDLVPALEA-------KWGVKLV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 311 SSVDRQGSAREKhgvftGRYvINPINGRPAPIWVA-DYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLeiaPIICEKDDP- 388
Cdd:PLN02843 300 VLKTFPGSDLEG-----CRY-IHPLYNRESPVVIGgDYITTESGTGLVHTAPGHGQEDYITGLKYGL---PLLSPVDDAg 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 389 -LYDELKDERELKVTS---VSWDHAMDAEGYLVQSgEFTGLK-----------------------GGKHSEAVDAI--IG 439
Cdd:PLN02843 371 kFTEEAGQFSGLSVLGegnAAVVEALDEAGSLLME-EAYGHKypydwrtkkptifrateqwfasvEGFRQAALDAIdkVK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 440 WLSERGLGRKKVQFRLR-DWLISRQRYWGNPIPMIH-------------------------CDCCGDVPVPyDQLPvtlp 493
Cdd:PLN02843 450 WIPAQGENRIRAMVSGRsDWCISRQRTWGVPIPVFYhvetkeplmneetiahvksivaqkgSDAWWYMDVE-DLLP---- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 494 dnldlgagETLAEYAPFYEttcpkcgrpakRITDTMDTF--TCSSWYYLRYCDPhntELPFskesvdrwmPVDNYIGGIE 571
Cdd:PLN02843 525 --------EKYRDKASDYE-----------KGTDTMDVWfdSGSSWAGVLGSRE---GLSY---------PADLYLEGSD 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 572 HailHllysRFW------TKVlrdlgMIDADEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIE---------PYGAD 636
Cdd:PLN02843 574 Q---H----RGWfqssllTSV-----ATKGKAPYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVIEggknqkqepAYGAD 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 637 TMRLVIlfiappeKDFDWDEKAVAGANrfikrawsIVWQLSAGAHAGEFDARSLKGQAGE-------------------L 697
Cdd:PLN02843 642 VLRLWV-------ASVDYTGDVLIGPQ--------ILKQMSDIYRKLRGTLRYLLGNLHDwkpdnavpyedlpsidkyaL 706
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 698 FRTLNGLGARCTSdYDRGQFNTAISAVME--IVNAASKYLNEtpAEDRVL---ELDFR--------VAH--DIVAILAPI 762
Cdd:PLN02843 707 FQLENVVNEIEES-YDNYQFFKIFQILQRftIVDLSNFYLDV--AKDRLYvggTTSFTrrscqtvlAAHllSLLRAIAPI 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 763 CPHWAEEL-----YHEALHLEGSVYNEPWPEFDPELAKADTVEIAV-QVMGKVRGHATIAADATReqTEKaalaAISEQL 836
Cdd:PLN02843 784 LPHLAEDAwqnlpFQEDGSAAESVFEAGWPTPNEEWLSFPAEDVDFwSLLLEVRDEVNKVLESAR--NGK----LIGASL 857
|
....*
gi 1545248450 837 EGKTV 841
Cdd:PLN02843 858 EAKVY 862
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
49-237 |
4.18e-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: 127.15 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 49 YVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAA-----IKHNTQAAAWTYQ------- 116
Cdd:cd00668 3 YVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAerkggRKKKTIWIEEFREdpkefve 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 117 -NMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVnwcpscntvlaneqvvegrcwrcgsv 195
Cdd:cd00668 83 eMSGEHKEDFRRLGISYDWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV-------------------------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1545248450 196 pekRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWI 237
Cdd:cd00668 137 ---RITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAWL 175
|
|
| Anticodon_Ia_Leu_BEm |
cd07958 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial leucyl tRNA synthetases; ... |
654-773 |
9.63e-31 |
|
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: 116.94 E-value: 9.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 654 WDEKAVAGANRFIKRAWSIVWQLSAGAHAGEFDArSLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAASK 733
Cdd:cd07958 1 WSDSGVEGAYRFLNRVWRLVTELAEALAAPAAAA-ELSEEDKELRRKLHKTIKKVTEDIERLRFNTAIAALMELVNALYK 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1545248450 734 YLNETPAEDRVLEldfRVAHDIVAILAPICPHWAEELYHE 773
Cdd:cd07958 80 YKKKDAQHAAVLR---EALETLVLLLAPFAPHIAEELWEE 116
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
55-237 |
4.32e-29 |
|
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: 122.91 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDY 134
Cdd:COG0143 10 PYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFEKLGISFDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 135 drLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLAnEQVVEGRCWRC---------------------- 192
Cdd:COG0143 90 --FIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLP-DRYVEGTCPKCgaedaygdqcencgatleptel 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1545248450 193 --------GSVPEKRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWI 237
Cdd:COG0143 167 inprsaisGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEVRNEVLSWL 219
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
18-630 |
2.62e-28 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 122.70 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 18 YDAAAIEGKWQRIWDEKGTYKTDEDPNKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFG- 96
Cdd:PLN02381 100 YSPSAVEKSWYAWWEKSGYFGADAKSSKPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGi 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 97 ---------LPAENAAIKHN-------TQAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKG 160
Cdd:PLN02381 180 atqvvvekkLMRERHLTRHDigreefvSEVWKWKDEYGGTILNQLRRLGASLDWSRECFTMDEQRSKAVTEAFVRLYKEG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 161 LAYRATSPVNWCPSCNTVLANEQVvegrcwrcgsvpekrelsqwylkitDYAQELLDDLDKLTGWPENVKAqqrnwigrs 240
Cdd:PLN02381 260 LIYRDIRLVNWDCTLRTAISDVEV-------------------------DYIDIKERTLLKVPGYDKPVEF--------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 241 eGAEIDFTLADKDGVTptdrKITVFTTRADTLFGVSFFLLPPESPlaaelvagteceaafkelkeatekvssvdrqgsaR 320
Cdd:PLN02381 306 -GVLTSFAYPLEGGLG----EIVVATTRIETMLGDTAIAIHPDDE----------------------------------R 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 321 EKHgvFTGRYVINPINGRPAPIwVADYVLMD--YGTGAVMGVPCGDQRDFDFAKKYGLEIAPIICE-------------- 384
Cdd:PLN02381 347 YKH--LHGKFAVHPFNGRKLPI-ICDAILVDpnFGTGAVKITPAHDPNDFEVGKRHNLEFINIFTDdgkinsnggsefag 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 385 --------------KDDPLYDELK-DERELKVTSVSWD--HAMDAEGYLVQSGEFTglkggkhSEAVDAIIGWLSerglg 447
Cdd:PLN02381 424 mprfaareaviealQKKGLYRGAKnNEMRLGLCSRTNDvvEPMIKPQWFVNCSSMA-------KQALDAAIDGEN----- 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 448 rKKVQF--------------RLRDWLISRQRYWGNPIPMIHcdccgdvpvpydqlpVTLPDNLDLGAG------------ 501
Cdd:PLN02381 492 -KKLEFipkqylaewkrwleNIRDWCISRQLWWGHRIPAWY---------------VTLEDDQLKELGsyndhwvvarne 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 502 -ETLAEYAPFYettcpkcgrPAKRIT-----DTMDTFTCSSWYYLrycdphntelpfskeSVDRWmPVDN------YIGG 569
Cdd:PLN02381 556 sDALLEASQKF---------PGKKFElsqdpDVLDTWFSSGLFPL---------------SVLGW-PDDTddlkafYPTS 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1545248450 570 IEHAILHLLYsrFWTKVLRDLGM-IDADEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVI 630
Cdd:PLN02381 611 VLETGHDILF--FWVARMVMMGMqLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVI 670
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
54-237 |
6.42e-28 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 116.62 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 54 FPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYD 133
Cdd:pfam09334 7 LPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 134 YdrLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQV----------------------------- 184
Cdd:pfam09334 87 D--YGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVegtcphcgsedargdqcencgrhleptel 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1545248450 185 VEGRCWRCGSVPEKRELSQWYLKITDYAQELLDDLDK-LTGWPENVKAQQRNWI 237
Cdd:pfam09334 165 INPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEEnNPEWPENVKNMVLEWL 218
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
55-237 |
1.03e-27 |
|
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: 114.55 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSYDY 134
Cdd:cd00814 9 PYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 135 drLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLaneqvvegrcwrcgsvPEKRELSQWYLKITDYAQE 214
Cdd:cd00814 89 --FIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL----------------PEWREEEHYFFRLSKFQDR 150
|
170 180
....*....|....*....|....*
gi 1545248450 215 LLDDLDK--LTGWPENVKAQQRNWI 237
Cdd:cd00814 151 LLEWLEKnpDFIWPENARNEVLSWL 175
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
26-788 |
3.98e-26 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 115.42 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 26 KWqriWDEKGTYKTDEDPNKpKKYVLEMfPYP--SGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAE--- 100
Cdd:PLN02943 71 NW---WESQGYFKPNFDRGG-DPFVIPM-PPPnvTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQlvv 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 101 -----NAAIKHNTQA------AAWTYQNMDNALAT--MRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATS 167
Cdd:PLN02943 146 ekmlaSEGIKRTDLGrdeftkRVWEWKEKYGGTITnqIKRLGASCDWSRERFTLDEQLSRAVVEAFVRLHEKGLIYQGSY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 168 PVNWCPSCNTVLANEQVvegrcwrcgsvpekrelsqwylkitDYAQEllddldklTGWPENVKAqqrnwigRSEGAEIDF 247
Cdd:PLN02943 226 MVNWSPNLQTAVSDLEV-------------------------EYSEE--------PGTLYYIKY-------RVAGGSEDF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 248 tladkdgvtptdrkITVFTTRADTLFGVSFFLLPPESplaaelvagteceaafkelkeatekvssvdrqgsarEKHGVFT 327
Cdd:PLN02943 266 --------------LTIATTRPETLFGDVAIAVNPED------------------------------------DRYSKYI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 328 GRYVINPIN-GRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYGLEIAPII--------------CEKDDPLYDE 392
Cdd:PLN02943 296 GKMAIVPMTyGRHVPIIADRYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMnkdgtlnevaglywFEAREKLWSD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 393 L--------KDERELKV-------------TSVSWDHAMD--AEGYL--VQSGEFTGLkggkhSEAVDAIIG-WLSErgl 446
Cdd:PLN02943 376 LeetglavkKEPHTLRVprsqrggevieplVSKQWFVTMEplAEKALkaVENGELTII-----PERFEKIYNhWLSN--- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 447 grkkvqfrLRDWLISRQRYWGNPIPMIHC---DCCGDVPVPYDqlpvtlpdnldlgagetlAEYApfYETTCPKCGRPAK 523
Cdd:PLN02943 448 --------IKDWCISRQLWWGHRIPVWYIvgkDCEEDYIVARS------------------AEEA--LEKAREKYGKDVE 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 524 --RITDTMDT-FTCSSWYYLRYCDPHntelpFSKESVDRWMPVDNYIGGieHAILHllysrFWTKVLRDLGM-IDADEPF 599
Cdd:PLN02943 500 iyQDPDVLDTwFSSALWPFSTLGWPD-----VSAEDFKKFYPTTVLETG--HDILF-----FWVARMVMMGIeFTGTVPF 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 600 TNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILfIAPPEKDFDWDEKAVAGANRFIKRAWS---IVWQ- 675
Cdd:PLN02943 568 SYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLA-LGTAGQDLNLSTERLTSNKAFTNKLWNagkFVLQn 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 676 ------LSAGAH--AGEFDAR----SLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIV--NAASKYLNETPA- 740
Cdd:PLN02943 647 lpsqsdTSAWEHilACKFDKEesllSLPLPECWVVSKLHELIDSVTTSYDKYFFGDVGREIYDFFwsDFADWYIEASKTr 726
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1545248450 741 ----EDRVLELDFR-----VAHDIVAILAPICPHWAEELYHEALHLEGSVYNEPWPE 788
Cdd:PLN02943 727 lyhsGDNSALSRAQavllyVFENILKLLHPFMPFVTEELWQALPYRKEALIVSPWPQ 783
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
455-654 |
1.40e-25 |
|
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: 109.64 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 455 LRDWLISRQRYWGNPIPMIHCDCCGDVPVpydqlpvtlpdnldlGAGETLAEYAPFYETTCPKCGRPAKRITDTMDT-FT 533
Cdd:cd00817 209 IRDWCISRQLWWGHRIPAWYCKDGGHWVV---------------AREEDEAIDKAAPEACVPCGGEELKQDEDVLDTwFS 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 534 CSSWyylrycdphntelPFS-------KESVDRWMPVDNYIGGieHAILhllysRFW--TKVLRDLgMIDADEPFTNLLC 604
Cdd:cd00817 274 SSLW-------------PFStlgwpeeTKDLKKFYPTSLLVTG--HDII-----FFWvaRMIMRGL-KLTGKLPFKEVYL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1545248450 605 QGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDW 654
Cdd:cd00817 333 HGLVRDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
437-651 |
1.49e-23 |
|
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: 102.70 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 437 IIGWLSERglgrkkvqfrlRDWLISRQRYWGNPIPMIHCDCCGDVPVpydqlpvtlpdnldlgagetlaeyapfyettcp 516
Cdd:cd00818 182 FGNWLENR-----------RDWCISRQRYWGTPIPVWYCEDCGEVLV--------------------------------- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 517 kcgrpaKRITDTMDTF--TCSSWYY-LRYcdphntelPFSKESVDRWMPVDNYIGGIEHailhllySRFWTKVLRDLGMI 593
Cdd:cd00818 218 ------RRVPDVLDVWfdSGSMPYAqLHY--------PFENEDFEELFPADFILEGSDQ-------TRGWFYSLLLLSTA 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545248450 594 DADE-PFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKD 651
Cdd:cd00818 277 LFGKaPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
55-217 |
5.89e-23 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 103.42 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTYQNMDNALATMRRMGFSydY 134
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNIS--Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 135 DRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVEG--RCWRCGSVPEKRELSQWYLKITDYA 212
Cdd:PRK11893 88 DDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIEDgyRCPPTGAPVEWVEEESYFFRLSKYQ 167
|
....*
gi 1545248450 213 QELLD 217
Cdd:PRK11893 168 DKLLE 172
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
46-237 |
6.11e-22 |
|
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: 98.07 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 46 PKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKH-----------------NT 108
Cdd:cd00818 1 PEFVFHDGPPYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElgisgkkdiekmgiaefNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 109 QAAAWTYQNMDNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWcPscntVLAneqvvegr 188
Cdd:cd00818 81 KCREFALRYVDEQEEQFQRLGVWVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW-P----LIY-------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1545248450 189 cwrcgsvpekRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWI 237
Cdd:cd00818 148 ----------RATPQWFIRVTKIKDRLLEANDKVNWIPEWVKNRFGNWL 186
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
16-640 |
6.13e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 99.03 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 16 PAYDAAAIEGKWQRIWDEKGTYKTD--EDPNKPKKYVLEMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFD 93
Cdd:PLN02882 6 KDFSFPKQEEKILSLWSEIDAFKTQlkRTEGLPEYIFYDGPPFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 94 AFGLPAENA-----AIKHNTQ--------------------AAAWTyqnmdnalATMRRMG----FSYDYdrlvRTCDPE 144
Cdd:PLN02882 86 CHGLPVEYEidkklGIKRRDDvlkmgidkyneecrsivtrySKEWE--------KTVTRTGrwidFENDY----KTMDPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 145 YYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANeqvvegrcwrcgsvpekRELSQWYLKITDYAQ----ELLDDLD 220
Cdd:PLN02882 154 FMESVWWVFKQLFEKGLVYKGFKVMPYSTACKTPLSN-----------------FEAGLNYKDVSDPAVmvsfPIVGDPD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 221 K--LTGW-------PENVkAQQRNwigrsegAEIDFT-LADKDgvtpTDRKITVFTTRADTLfgvsffllPPESPLAael 290
Cdd:PLN02882 217 NasFVAWtttpwtlPSNL-ALCVN-------PNFTYVkVRNKY----TGKVYIVAESRLSAL--------PTAKPKS--- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 291 VAGTECEAAfKELKEATEKVSSVDRQGSarekhgvftgRY--VINPINGRPAPIW--VAD-YVLMDYGTGAVMGVPCGDQ 365
Cdd:PLN02882 274 KKGSKPENA-AEGYEVLAKVPGSSLVGK----------KYepLFDYFSEFSDTAFrvVADdYVTDDSGTGVVHCAPAFGE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 366 RDfdfakkYGLEIAPIICEKDDPLYDELKDEREL--KVTSVSWDHAMDAE----------GYLVQSGEFTglkggkHSEA 433
Cdd:PLN02882 343 DD------YRVCLANGIIEKGGNLPVPVDDDGCFteKVTDFSGRYVKDADkdiiaaikakGRLVKSGSIT------HSYP 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 434 V----------DAIIGW------LSERGLGR-----------KKVQFR-----LRDWLISRQRYWGNPIPmIHCDCCGDV 481
Cdd:PLN02882 411 FcwrsdtpliyRAVPSWfvkveeIKDRLLENnkqtywvpdyvKEKRFHnwlenARDWAVSRSRFWGTPLP-IWISDDGEE 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 482 PVPYDQLpvtlpDNLDLGAGETLAEYAPFY--ETTCPKCGRPA----KRITDTMDT-FTCSS--WYYLRYcdphntelPF 552
Cdd:PLN02882 490 VVVIGSI-----AELEKLSGVKVTDLHRHFidHITIPSSRGPEfgvlRRVDDVFDCwFESGSmpYAYIHY--------PF 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 553 -SKESVDRWMPVDNYIGGIEHailhllySRFWTKVLRDLGMIDADEP-FTNLLCQGMVKDHNGETMSKSKGNVVPPSSVI 630
Cdd:PLN02882 557 eNKELFEKNFPADFVAEGLDQ-------TRGWFYTLMVLSTALFDKPaFKNLICNGLVLAEDGKKMSKSLKNYPDPNEVI 629
|
730
....*....|
gi 1545248450 631 EPYGADTMRL 640
Cdd:PLN02882 630 DKYGADALRL 639
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
438-654 |
3.06e-19 |
|
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: 89.40 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 438 IGWLSERGlgRKKVQFRLR---DWLISRQRYWGNPIPmihcdccgdvpvpydqlpvtlpdnldlgagetlaeyapfyett 514
Cdd:cd00668 160 GKIVPEHV--KNRMEAWLEsllDWAISRQRYWGTPLP------------------------------------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 515 cpkcgrpakriTDTMDTFTCSSWYYLRYCDphnteLPFSKESVDRWMPVDNYIGGIEHAILHLLYSRFWTKvlrdlgMID 594
Cdd:cd00668 195 -----------EDVFDVWFDSGIGPLGSLG-----YPEEKEWFKDSYPADWHLIGKDILRGWANFWITMLV------ALF 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 595 ADEPFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDW 654
Cdd:cd00668 253 GEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
24-667 |
4.07e-19 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 93.11 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 24 EGKWQRIWDEKGTYKTDEDPNKPKK-YVL-EMFPYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAEN 101
Cdd:PTZ00427 78 EEKVLKYWKSIDAFNTSNKLAKNKKaYIFyDGPPFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLPIEY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 102 AAIKHNTQAAAWTYQNM-----------------DNALATMRRMGFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYR 164
Cdd:PTZ00427 158 EIEKENNINKKEDILKMgidvynekcrgivlkysNEWVKTVERIGRWIDFKNDYKTMDKTFMESVWWVFSELYKNNYVYK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 165 ATSPVNWCPSCNTVLANEQV-----------VEGRCWRCGSVPEKRELSQwylkitdyaqelLDDLDKLTGWPENVKAQQ 233
Cdd:PTZ00427 238 SFKVMPYSCKCNTPISNFELnlnykdtpdpsIIISFVLCSDFPKVEEECN------------IEEDKQLLGEKYSVLYNN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 234 RnwigRSEGAEIDFTlaDKDGVTPT-DRKITVFTTRADTL-------FGVSFFLLPPESPLAAELVAGTEC--EAAFKEL 303
Cdd:PTZ00427 306 K----RENSNNGNNN--STNNVCYAqHSEILAWTTTPWTLpsnlalcVNEHFTYLRIHHVKSNRVVIVGECrlEWIMKEL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 304 KEATEKVSSVDRQGSAREK----HGVFTGRYVINPINGRPAPIWVADYVLMDYGTGAVMGVPCGDQRDFDFAKKYG---- 375
Cdd:PTZ00427 380 KWNVEDLKIVNRFKGKELKglryKPLFTNFYEKYNFKERAYKILADDFVTDDAGTGIVHCAPTYGEDDFRVCKKNGvidp 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 376 ---LEIAPI-----------------ICEKDDPLYDELKDERELKVTSV-------SWD-------HAMDAEGYLVQSGE 421
Cdd:PTZ00427 460 eknIFIDPLdangyftneveevqnlyIKEADNVIKKKLKNENRLLSNNTivhsypfCWRsdtpliyRAIPAWFIRVSNST 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 422 FTGLKGGKHSEAVDAII------GWLSERglgrkkvqfrlRDWLISRQRYWGNPIPmIHCD------CCGDVPVPYDQLP 489
Cdd:PTZ00427 540 NELVKNNETTYWIPAHIkekkfhNWIKDA-----------KDWCISRNRYWGTPIP-IWADekmetvICVESIKHLEELS 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 490 vTLPDNLDLGAgetlaEYAPFYETTCPKcGR---PAKRITDTMDT-FTCSSWYYLRYCDPHNTElpfsKESVDRWMPVDN 565
Cdd:PTZ00427 608 -GVKNINDLHR-----HFIDHIEIKNPK-GKtypKLKRIPEVFDCwFESGSMPYAKVHYPFSTE----KEDFHKIFPADF 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 566 YIGGIEHailhllySRFWTKVLRDLGMIDADE-PFTNLLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRL-VIL 643
Cdd:PTZ00427 677 IAEGLDQ-------TRGWFYTLLVISTLLFDKaPFKNLICNGLVLASDGKKMSKRLKNYPDPLYILDKYGADSLRLyLIN 749
|
730 740
....*....|....*....|....
gi 1545248450 644 FIAPPEKDFDWDEKavaGANRFIK 667
Cdd:PTZ00427 750 SVAVRAENLKFQEK---GVNEVVK 770
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
55-237 |
3.68e-17 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 85.97 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNT--QAAAWTYQNMDnaLATMRRMGFSY 132
Cdd:PRK00133 11 PYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGItpEELIARYHAEH--KRDFAGFGISF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 133 D-YDrlvRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLAnEQVVEGRCWRC------------------- 192
Cdd:PRK00133 89 DnYG---STHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLP-DRFVKGTCPKCgaedqygdncevcgatysp 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1545248450 193 -----------GSVPEKRELSQWYLKITDYAQELLDDLDKLTGWPENVKAQQRNWI 237
Cdd:PRK00133 165 telinpksaisGATPVLKESEHFFFKLPRFEEFLKEWITRSGELQPNVANKMKEWL 220
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
701-819 |
2.17e-16 |
|
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: 76.67 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 701 LNGLGARCTSDYDRGQFNTAISAVME-IVNAASKY--------LNETPAEDRVLELDFRVAHDIVAILAPICPHWAEELY 771
Cdd:pfam08264 8 LNKLIKEVTEAYENYRFNTAAQALYEfFWNDLSDWylelikdrLYGEEPDSRAQTTLYEVLETLLRLLAPFMPFITEELW 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1545248450 772 HealhlEGSVYNEPWPE----FDPELAKA-DTVEIAVQVMGKVRGHATIAADA 819
Cdd:pfam08264 88 Q-----KESIHLAPWPEdaelEEAELEEAfELRQEIVQAIRKLRSELKIKKSL 135
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
56-217 |
8.36e-16 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 81.77 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 56 YPSGDLHMGHArnYT--IGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAAWTyqnmDNALATMR----RMG 129
Cdd:PRK12267 14 YPNGKPHIGHA--YTtiAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYV----DEISAGFKelwkKLD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 130 FSYDYdrLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVE-GRCWRCGSVPEKRELSQWYLKI 208
Cdd:PRK12267 88 ISYDK--FIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVDgGKCPDCGREVELVKEESYFFRM 165
|
....*....
gi 1545248450 209 TDYAQELLD 217
Cdd:PRK12267 166 SKYQDRLLE 174
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
612-771 |
3.42e-12 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 69.91 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 612 NGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKAVAG------ANRF---IKRAWSIVWQLSAGA-- 680
Cdd:PRK11893 296 DGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINrinadlANDLgnlAQRTLSMIAKNFDGKvp 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 681 HAGEFDArslkgQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAASKYLNET-P------AEDRVLELDFRVAH 753
Cdd:PRK11893 376 EPGALTE-----ADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQaPwslaktDPERLATVLYTLLE 450
|
170 180
....*....|....*....|.
gi 1545248450 754 DI--VAILA-PICPHWAEELY 771
Cdd:PRK11893 451 VLrgIAVLLqPVMPELAAKIL 471
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
612-838 |
3.48e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 63.94 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 612 NGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDW-DEKAVAGANRFIKRawsIVWQLSAGAHAGEFDARSL 690
Cdd:PLN02959 715 NSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGDGVDDANFvFETANAAILRLTKE---IAWMEEVLAAESSLRTGPP 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 691 KGQAGELFRT-LNGLGARCTSDYDRGQFNTAI-SAVMEIVNAASKYLNETPAEDRVLELDFRVAHDIVAILAPICPHWAE 768
Cdd:PLN02959 792 STYADRVFENeINIAIAETEKNYEAMMFREALkSGFYDLQAARDEYRLSCGSGGMNRDLVWRFMDVQTRLITPICPHYAE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 769 ELYHEALHLEGSVYNEPWP---EFDPELAKA-----DTVE-----IAVQVMGKVRGHATIAAdATREQTEKAALAAISEQ 835
Cdd:PLN02959 872 HVWREILKKEGFAVTAGWPvagEPDLTLKRAnkylqDSIVsfrklLQKQLAGSKKAKKGGAP-VTLPEKKLAGLIYVAEK 950
|
...
gi 1545248450 836 LEG 838
Cdd:PLN02959 951 YDG 953
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
22-105 |
1.03e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 59.31 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 22 AIEGKWQRIWDEKGTYKTD--EDPNKPKKYVLEMFPYP--SGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGL 97
Cdd:PLN02959 17 EIEVAVQKWWEEEKVFEAEagDEPPKPGEKFFGNFPYPymNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGM 96
|
....*...
gi 1545248450 98 PAENAAIK 105
Cdd:PLN02959 97 PIKASADK 104
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
701-814 |
1.28e-07 |
|
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. This family includes bacterial and eukaryotic mitochondrial members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153414 [Multi-domain] Cd Length: 180 Bit Score: 52.53 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 701 LNGLGARCTSDYDRGQFNTAISAVMEIVNA--------ASK---YLNETPAEDR-----VLeldFRVAHDIVAILAPICP 764
Cdd:cd07960 53 LNELIKEVREAYENYEFHKVYQALNNFCTVdlsafyldIIKdrlYCDAKDSLERrsaqtVL---YHILDALLKLLAPILP 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1545248450 765 HWAEELYHE--ALHLEGSVYNEPWPEFDPELAKADTVEIAVQVMgKVRGHAT 814
Cdd:cd07960 130 FTAEEVWEHlpGEKKEESVFLEDWPELPEEWKDEELEEKWEKLL-ALRDEVN 180
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
55-237 |
1.45e-07 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 55.17 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 55 PYPSGDLHMGHarnyTIG-----DAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAawtyQNMDNALATMRRM- 128
Cdd:PLN02610 26 PYVNNVPHLGN----IIGcvlsaDVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK----EICDKYHAIHKEVy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 129 -GFSYDYDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLAnEQVVEG-------------------- 187
Cdd:PLN02610 98 dWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLA-DRLVEGtcptegcnydsargdqcekc 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545248450 188 ------------RCWRCGSVPEKRELSQWYL---KITDYAQELLDDLDKLTGWPENVKAQQRNWI 237
Cdd:PLN02610 177 gkllnptelidpKCKVCKNTPRIRDTDHLFLelpLLKDKLVEYINETSVAGGWSQNAIQTTNAWL 241
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
572-653 |
2.63e-07 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 53.30 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 572 HAIlhllysrFWTKVLRDLGMidadEPFTNLLCQGMVKDhNGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKD 651
Cdd:cd00814 249 HAI-------YWPAMLLGAGL----PLPTRIVAHGYLTV-EGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKD 316
|
..
gi 1545248450 652 FD 653
Cdd:cd00814 317 SD 318
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
612-783 |
3.35e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 54.04 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 612 NGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEKDFDWDEKAvaganrFIKRAWS------------IV------ 673
Cdd:PRK12267 296 KDGKMSKSKGNVVDPEELVDRYGLDALRYYLLREVPFGSDGDFSPEA------LVERINSdlandlgnllnrTVaminky 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 674 --WQLSAGAHAGEFDArSLKGQAGELFRTLNGLgarctsdYDRGQFNTAISAVMEIVNAASKYLNET-P-----AEDRVL 745
Cdd:PRK12267 370 fdGEIPAPGNVTEFDE-ELIALAEETLKNYEEL-------MEELQFSRALEEVWKLISRANKYIDETaPwvlakDEGKKE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1545248450 746 ELDFRVAH-----DIVAIL-APICPHWAEELYhEALHLEGSVYN 783
Cdd:PRK12267 442 RLATVMYHlaeslRKVAVLlSPFMPETSKKIF-EQLGLEEELTS 484
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
701-773 |
8.00e-07 |
|
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: 48.74 E-value: 8.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545248450 701 LNGLGARCTSDYDRGQFNTAI-SAVMEIVNAASKYLNETPAEDRVlELDFRVAHDIVAILAPICPHWAEELYHE 773
Cdd:cd07959 44 LNRLIKETTEAYENMQFREALkEGLYELQNDLDWYRERGGAGMNK-DLLRRFIEVWTRLLAPFAPHLAEEIWHE 116
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
55-87 |
8.79e-07 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) 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. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 50.64 E-value: 8.79e-07
10 20 30
....*....|....*....|....*....|...
gi 1545248450 55 PYPSGDLHMGHARNYTIGDAMARQARMRGYDVL 87
Cdd:cd00671 9 ANPTGPLHVGHLRNAIIGDSLARILEFLGYDVT 41
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
42-86 |
1.15e-06 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 52.08 E-value: 1.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1545248450 42 DPNKPKKYVLEmF--PYPSGDLHMGHARNYTIGDAMARQARMRGYDV 86
Cdd:PRK01611 106 DIGKGKKVVVE-YvsANPTGPLHVGHLRSAVIGDALARILEFAGYDV 151
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
28-87 |
2.08e-06 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 51.19 E-value: 2.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545248450 28 QRIWDEKGTYKTDedPNKPKKYVLEMF-PYPSGDLHMGHARNYTIGDAMARQARMRGYDVL 87
Cdd:TIGR00456 95 QKILTQKEKYGSK--KLKNKKIIIEFSsANPAGPLHVGHLRNAIIGDSLARILEFLGYDVI 153
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
606-747 |
3.28e-06 |
|
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: 50.49 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 606 GMVKDhNGETMSKSKGNVVPPSSVIEPYGADTMRLVILfIAPPEKDFDWDEKAVAGANRFIKRawsivwqLSAGAHagef 685
Cdd:COG0215 257 GFLTV-NGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLL-SAHYRSPLDFSEEALEEAEKALER-------LYNALR---- 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545248450 686 DARSLKGQAGELFRTLNGLGARCTS--DYDrgqFNT--AISAVMEIVNAASKYLNETPAEDRVLEL 747
Cdd:COG0215 324 RLEEALGAADSSAEEIEELREEFIAamDDD---FNTpeALAVLFELVREINKALDEGEDKAALAAL 386
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
56-265 |
6.83e-06 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 49.71 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 56 YPSGDLHMGHARNYTIGDAMARQARMRGYDVLHPIGFDAFGLPAENAAIKHNTQAAawtyQNMDNALATMRRMGFSYD-- 133
Cdd:PLN02224 79 YVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPP----EHCDIISQSYRTLWKDLDia 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 134 YDRLVRTCDPEYYKWGQWMFLKMWEKGLAYRATSPVNWCPSCNTVLANEQVVEGRCWRCGSVP-EKRELSQWYLKITDYa 212
Cdd:PLN02224 155 YDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLENNCCPVHQMPcVARKEDNYFFALSKY- 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545248450 213 QELLDDLdkLTGWPENVKAQQR-----NWIGRS-EGAEIDFTLADKDGVTPTDRKITVF 265
Cdd:PLN02224 234 QKPLEDI--LAQNPRFVQPSYRlnevqSWIKSGlRDFSISRALVDWGIPVPDDDKQTIY 290
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
612-772 |
7.42e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 49.76 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 612 NGETMSKSKGNVVPPSSVIEPYGADTMRLVILFIAPPEK---DFDWDE-----------KAVAGANR---FIKRawsivw 674
Cdd:PRK00133 326 EGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIddlDFNWEDfqqrvnselvgKVVNFASRtagFINK------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 675 qlsagahagEFDAR-SLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAASKYLNE--------TPAED--R 743
Cdd:PRK00133 400 ---------RFDGKlPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDnepwklakQDGERlqA 470
|
170 180
....*....|....*....|....*....
gi 1545248450 744 VLELDFRVAHDIVAILAPICPHWAEELYH 772
Cdd:PRK00133 471 VCSVGLNLFRALAIYLKPVLPELAERAEA 499
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
41-86 |
9.83e-06 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 48.99 E-value: 9.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1545248450 41 EDPNKPKKYVLEmF--PYPSGDLHMGHARNYTIGDAMARQARMRGYDV 86
Cdd:COG0018 110 SDAGKGKKVVVE-YvsANPTKPLHVGHLRGAVIGDALARILEAAGYDV 156
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
696-771 |
1.54e-04 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 42.48 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 696 ELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAASKYLNET--------PAEDRV-------LELdFRvahdIVAI-L 759
Cdd:cd07957 40 ELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYIDETapwklakeEDPERLatvlyvlLEL-LR----ILAIlL 114
|
90
....*....|..
gi 1545248450 760 APICPHWAEELY 771
Cdd:cd07957 115 SPFMPETAEKIL 126
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
656-748 |
6.16e-04 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 40.18 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 656 EKAVAGANRFIKRAWSIVWQ--LSAGAHAGEFDARSLKGQAGELFRTLNGLGARCTSDYDRGQFNTAISAVMEIVNAASK 733
Cdd:cd07375 1 EERLKQARAFLNRLYRLLSFfrKALGGTQPKWDNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELNW 80
|
90
....*....|....*
gi 1545248450 734 YLNETPAEDRVLELD 748
Cdd:cd07375 81 YLDELKPALQTEELR 95
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
502-657 |
1.73e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 41.54 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 502 ETLAEYAPFyETTCPKCGrpaKRITdTMDTFTCSSWYyLRYCDP--HNTELPFSKES------VD---RWM--PVDNYIG 568
Cdd:cd00674 160 ELQETWYPF-MPYCEKCG---KDTT-TVEAYDAKAGT-VTYKCEcgHEETVDIRTGRgkltwrVDwpmRWAilGVDFEPF 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 569 GIEHAILHLLYsrfwtkvlrDLGMIDADE------PFTnlLCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLVI 642
Cdd:cd00674 234 GKDHASAGGSY---------DTGKEIAREifggepPVP--VMYEFIGLKGGGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
170
....*....|....*
gi 1545248450 643 LFIAPPEKDFDWDEK 657
Cdd:cd00674 303 ARRKNPEKHIGFDLD 317
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
505-655 |
8.50e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 39.80 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 505 AEYAPF--YettCPKCGRPAKRITDTMDtftcSSWYYLRYCDP--HNTELPFSKES------VD---RWMP--VDNYIGG 569
Cdd:PRK00750 169 ATYSPFlpI---CPKCGKVLTTPVISYD----AEAGTVTYDCEcgHEGEVPVTGGHgklqwkVDwpmRWAAlgVDFEPFG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545248450 570 IEHAilhllySRFWT---KVLRD-LGmIDADEPFtnllCQGMVKDHNGETMSKSKGNVVPPSSVIEPYGADTMRLvILFI 645
Cdd:PRK00750 242 KDHA------SASYDtskKIAREiLG-GEPPEPF----VYELFLDKKGEKISKSKGNVITIEDWLEYAPPESLRL-FMFA 309
|
170
....*....|.
gi 1545248450 646 AP-PEKDFDWD 655
Cdd:PRK00750 310 RPkPAKRLDFD 320
|
|
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