|
Name |
Accession |
Description |
Interval |
E-value |
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
2-327 |
1.35e-74 |
|
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: 252.31 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWkSSPIEPLNFStKELMSRPYQVISTLYHLHTF 81
Cdd:COG0060 585 APYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS-SDYWGDLRFS-DEILKEVRDVYRRLRNTYRF 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 82 YRQNseYDKFDINETTIEWAKknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSEL 161
Cdd:COG0060 663 LLAN--LDDFDPAEDAVPYED----LPELDRWILSRLNELIKEVTEAYDNYDFHRAYRALHNFCVEDLSNWYLDISKDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 162 WDEDDSQKNRRStIYAILAKTLKTIDILIHPFSPFTTQYLYSTIFGEK-ENILLETWPKQDTSLIDEKIEESFDLLKDVV 240
Cdd:COG0060 737 YTEAADSLDRRA-AQTTLYEVLETLVRLLAPILPFTAEEIWQNLPGEAeESVHLADWPEVDEELIDEELEAKWDLVREVR 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 241 SVAA----ASRMKGKLkrRWPLNEAIICLEKGQ-KNILESLSELVKSQMNIQNYKIFEIESSEGIEQYLELKQNGLPVvp 315
Cdd:COG0060 816 SAVLkaleAARKEKLI--RQPLEAAVVLYADEElAAALESLGDLLAEELNVSEVELVDDAEDLGKDALKALDVEGISV-- 891
|
330
....*....|..
gi 663503655 316 KIELERSAiGPK 327
Cdd:COG0060 892 TVEVEKAD-GEK 902
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
2-263 |
1.96e-46 |
|
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: 172.94 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWkSSPIEPLNFSTKELMSRPYQVISTLYHLHTF 81
Cdd:TIGR00392 593 APYKNVITHGFTLDEKGRKMSKSLGNVVDPLKVINKYGADILRLYVAS-SDPWEDLRFSDEILKQVVEKYRKIRWNTYRF 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 82 YRQNSEYDKFDINETTIEWAKKNNLltppDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSEL 161
Cdd:TIGR00392 672 LLTYANLDKFDPLFNSVAVEKFPEE----DRWILSRLNSLVEEVNEALEKYNFHKVLRALQDFIVEELSNWYIRIIRDRL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 162 WDEDDSQKNRrsTIYAILAKTLKTIDILIHPFSPFTTQ--YLYSTIFGEKENILLETWPKQDTSLIDEKIEESFDLLKDV 239
Cdd:TIGR00392 748 YCEAKDNDKR--AAQTTLYYALLTLVRLLAPFLPHTAEeiYQNLPGGEEEESVHLNLWPEVDEEFIDEALEANMAIVREI 825
|
250 260
....*....|....*....|....
gi 663503655 240 VSVAAASRMKGKLKRRWPLNEAII 263
Cdd:TIGR00392 826 VEAFLALRDAANKKLRQPLKELVI 849
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
3-371 |
5.33e-39 |
|
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: 150.98 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSRpYQVISTLYHLHTFY 82
Cdd:TIGR00422 508 PFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESA-RNFLNKLWNASRFV 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 83 RQNSEYDKfdinettiEWAKKNNLLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSELW 162
Cdd:TIGR00422 587 LMNLSDDL--------ELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIWNDFCDWYIELVKYRLY 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 163 -DEDDSQKNRRSTIYAILAKTLKtidiLIHPFSPFTTQYLYSTIFGEKENILLETWPKQDTSLIDEKIEESFDLLKDVVS 241
Cdd:TIGR00422 659 nGNEAEKKAARDTLYYVLDKALR----LLHPFMPFITEEIWQHFKEGADSIMLQSYPVVDAEFVDEEAEKAFELLKEIIV 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 242 VAAASRMKGKLKRRWPLNEAIICLEKGQKNILESLSELVKSQMNIQNYKIfeiessegIEQYLELKQNGLPVVPKIELer 321
Cdd:TIGR00422 735 SIRNLKAESNIPPNAPLKVLLIYTEAETAERLKLNAVDIKGAINFSEVEV--------VIEKPEVTEAVVELVPGFEI-- 804
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 663503655 322 saIGP-----KAKQDMGKLLKMFSETDPETIITE--LNSNGsftFQIDQNSIVLDKE 371
Cdd:TIGR00422 805 --IIPvkgliNKAKELARLQKQLDKEKKEVIRIEgkLENEG---FVKKAPKEVIEKE 856
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
3-301 |
8.03e-36 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 141.48 E-value: 8.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFyfmW--KSSPIEPLNFSTKElMSRPYQVISTLYHLHT 80
Cdd:PRK13208 516 PWKNIMISGMVLDPDGKKMSKSKGNVVTPEELLEKYGADAVRY---WaaSARLGSDTPFDEKQ-VKIGRRLLTKLWNASR 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 81 FYRQNSEYDKFDINETTiewakknnllTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSE 160
Cdd:PRK13208 592 FVLHFSADPEPDKAEVL----------EPLDRWILAKLAKVVEKATEALENYDFAKALEEIESFFWHVFCDDYLELVKSR 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 161 LWDEDDSqKNRRSTIYAiLAKTLKTIDILIHPFSPFTTQYLYSTIFGEKenILLETWPKQDTSLIDEKIEESFDLLKDVV 240
Cdd:PRK13208 662 AYGEDEE-EEQKSARYT-LYTVLDTLLRLLAPFLPFITEEVWSWLYGGS--VHRASWPEPDEELIDEEDEELGELAKEIL 737
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663503655 241 SV--AAASRMKGKLKRrwPLNEAIICLEKGQKnILESLSELVKSQMNIQNYKIFEIESSEGIE 301
Cdd:PRK13208 738 SAvrKYKSEAGLSLNA--PLKKVEVYGPADLE-LLEAAEEDLKAAGNIEELELVEGDPELEVE 797
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
3-299 |
2.01e-33 |
|
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: 134.41 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSrpyqvistlyhlhtfY 82
Cdd:COG0525 505 PFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIKFDEERVEG---------------Y 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 83 R--------------QNSEYDKFDINETTIEwakknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINS 148
Cdd:COG0525 570 RnfanklwnasrfvlMNLEGFDPGLDPDPEE-------LSLADRWILSRLNKTIAEVTEALEKYRFDEAAQALYDFVWNE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 149 LSQIYIPITKSELWDEDDSQKNrrsTIYAILAKTLKTIDILIHPFSPFTTQYLYSTI--FGEKENILLETWPKQDTSLID 226
Cdd:COG0525 643 FCDWYLELAKPRLYGGDEAAKR---ETRATLVYVLEQILRLLHPFMPFITEEIWQKLppRKEGESIMLAPWPEADEELID 719
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663503655 227 EKIEESFDLLKDVVSV--AAASRMKGKLKRRWPLneAIICLEKGQKNILESLSELVKSQMNIQNYKIFEIESSEG 299
Cdd:COG0525 720 EEAEAEFEWLKEVISAirNIRAEMNIPPSKKLPL--LLKGADEADRARLEENAAYIKRLARLEEITILVDEKPEG 792
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
3-241 |
3.52e-32 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 130.61 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSrpyqvistlyhlhtfY 82
Cdd:PRK05729 503 PFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFDEERVEG---------------Y 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 83 R--------------QNSEYDKFDINEttiewakKNNLLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINS 148
Cdd:PRK05729 568 RnfanklwnasrfvlMNLEGADVGELP-------DPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARALYEFIWNE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 149 LSQIYIPITKSELWDEDdsqknRRSTIYaILAKTLKTIDILIHPFSPFTTQYLYSTI--FGEKENILLETWPKQDTSLiD 226
Cdd:PRK05729 641 FCDWYLELAKPVLQEAA-----KRATRA-TLAYVLEQILRLLHPFMPFITEELWQKLapLGIEESIMLAPWPEADEAI-D 713
|
250
....*....|....*
gi 663503655 227 EKIEESFDLLKDVVS 241
Cdd:PRK05729 714 EAAEAEFEWLKELIT 728
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
70-244 |
6.03e-30 |
|
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic 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, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 115.34 E-value: 6.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 70 QVISTLYHLHTFYRQNSEYDKFDINETTIEWAKKNNLltppDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINsL 149
Cdd:cd07961 12 KVLLPLWNAYRFFVTYANLDGFDPGKDDDAVASLNVL----DRWILSRLNSLIKEVTEEMEAYDLYTAVRALLEFIDE-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 150 SQIYIPITKSELWDEDDSQKNRRStiYAILAKTLKTIDILIHPFSPFTTQYLYSTIFGE----KENILLETWPKQDTSLI 225
Cdd:cd07961 87 TNWYIRRNRKRFWGEEGDDDKLAA--YATLYEVLLTLSRLMAPFTPFITEEIYQNLRRElgdaPESVHLLDWPEVDESLI 164
|
170
....*....|....*....
gi 663503655 226 DEKIEESFDLLKDVVSVAA 244
Cdd:cd07961 165 DEELEEAMELVREIVELGR 183
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
111-262 |
2.98e-27 |
|
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: 106.33 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 111 DIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSELWDEDDSqknrrSTIYAILAKTLKTIDILI 190
Cdd:pfam08264 1 DRWILSRLNKLIKEVTEAYENYRFNTAAQALYEFFWNDLSDWYLELIKDRLYGEEPD-----SRAQTTLYEVLETLLRLL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663503655 191 HPFSPFTTQYLYstifgEKENILLETWPKqDTSLIDEKIEESFDLLKDVVSVAAASRMKGKLKRRWPLNEAI 262
Cdd:pfam08264 76 APFMPFITEELW-----QKESIHLAPWPE-DAELEEAELEEAFELRQEIVQAIRKLRSELKIKKSLPLEVVI 141
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
4-429 |
1.22e-26 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 114.05 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 4 YKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMwkSSPI---EPLNFSTKELMSRPYQVISTLYHLHT 80
Cdd:PLN02882 598 FKNLICNGLVLAEDGKKMSKSLKNYPDPNEVIDKYGADALRLYLI--NSPVvraEPLRFKEEGVFGVVKDVFLPWYNAYR 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 81 FYRQNSE------YDKFdineTTIEWAKKNNLLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFlINSLSQIYI 154
Cdd:PLN02882 676 FLVQNAKrlevegGAPF----VPLDLAKLQNSANVLDRWINSATQSLVKFVREEMGAYRLYTVVPYLVKF-IDNLTNIYV 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 155 PITKSEL---WDEDDSqKNRRSTIYAILAKTLKTidilIHPFSPFTTQYLYS----TIFGEKENILLETWPKQDTSLIDE 227
Cdd:PLN02882 751 RFNRKRLkgrTGEEDC-RTALSTLYNVLLTSCKV----MAPFTPFFTEVLYQnlrkVLPGSEESIHYCSFPQVDEGELDE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 228 KIEESFDLLKDVVSVAAASRMKGKLKRRWPLNEAIICLEKGQ--KNILESLSELVKSQMNIQNykifeIESSEGIEQYLE 305
Cdd:PLN02882 826 RIEQSVSRMQTVIELARNIRERHNKPLKTPLKEMVVVHPDAEflDDITGKLKEYVLEELNVRS-----LVPCNDPLKYAS 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 306 LkqnglpvvpKIELERSAIGPKAKQDMGKLLKMFSETDPETIItELNSNGSFTFQ---IDQNSIVLDKEDFIVDFDVDEK 382
Cdd:PLN02882 901 L---------RAEPNFSVLGKRLGKSMGLVAKEVKAMSQDDIL-EFEKAGEVTIAghtLKAGDIKVVRDFKRPEGVSKED 970
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 663503655 383 YQFAKRQNLVVMISLERDNEMMAKGLIKDLARRLQTLRKERGYNPTD 429
Cdd:PLN02882 971 IDAAGDGDVLVILDLRVDESLLEAGVAREVVNRIQKLRKKAGLEPTD 1017
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
17-240 |
6.28e-23 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 102.64 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSrpyqVISTLYHLHTFYRQNSEYdkfdinet 96
Cdd:PRK12300 574 EGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVES----VRRQLERFYELAKELIEI-------- 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 97 tiewaKKNNLLTPPDIWLLSKLQRMVQKTTDANNECKFHEsgKAIEDF--LINSLSqiyipitkselWDEDDSQKNRRST 174
Cdd:PRK12300 642 -----GGEEELRFIDKWLLSRLNRIIKETTEAMESFQTRD--AVQEAFyeLLNDLR-----------WYLRRVGEANNKV 703
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663503655 175 IYAILAKTLKtidiLIHPFSPFTTQYLYSTIfGEKENILLETWPKQDTSLIDEKIEESFDLLKDVV 240
Cdd:PRK12300 704 LREVLEIWIR----LLAPFTPHLAEELWHKL-GGEGFVSLEKWPEPDESKIDEEAELAEEYVKRLI 764
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
3-233 |
1.99e-22 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 101.22 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFStKELMSRPYQVISTLYHLHTFY 82
Cdd:PRK14900 521 PFRTVYLHPMVRDEKGQKMSKTKGNVIDPLVITEQYGADALRFTLAALTAQGRDIKLA-KERIEGYRAFANKLWNASRFA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 83 RQN---SEYDKFDINETTiewakknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKS 159
Cdd:PRK14900 600 LMNlsgYQERGEDPARLA---------RTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFVWHELCDWYIELAKE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 160 ELWDEDDSQKnrrSTIYAILAKTLKTIDILIHPFSPFTTQYLYSTI------FGEKENILLETWPKQDTslIDEKIEESF 233
Cdd:PRK14900 671 ALASEDPEAR---RSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLraqvgaSAWADSVLAAEYPRKGE--ADEAAEAAF 745
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
3-306 |
2.78e-21 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 97.70 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPiEPLNFSTKELMSRPyQVISTLYHLHTFY 82
Cdd:PLN02943 566 PFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLALGTAG-QDLNLSTERLTSNK-AFTNKLWNAGKFV 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 83 RQN-------SEYD-----KFDINETTIEwakknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLS 150
Cdd:PLN02943 644 LQNlpsqsdtSAWEhilacKFDKEESLLS-------LPLPECWVVSKLHELIDSVTTSYDKYFFGDVGREIYDFFWSDFA 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 151 QIYIPITKSELWDEDDsqKNRRSTIYAILAKTLKTIDILIHPFSPFTTQYLYSTIFGEKENILLETWPKQDTSLIDEKIE 230
Cdd:PLN02943 717 DWYIEASKTRLYHSGD--NSALSRAQAVLLYVFENILKLLHPFMPFVTEELWQALPYRKEALIVSPWPQTSLPKDLKSIK 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 231 EsFDLLKDVV----------SVAAASRMKGKLKRRwplNEAIICLEKgQKNILESLSELVKSQMNIQNY------KIFEI 294
Cdd:PLN02943 795 R-FENLQSLTrairnaraeySVEPAKRISASIVAS---AEVIEYISK-EKEVLALLSRLDLQNVHFTDSppgdanQSVHL 869
|
330
....*....|..
gi 663503655 295 ESSEGIEQYLEL 306
Cdd:PLN02943 870 VASEGLEAYLPL 881
|
|
| Anticodon_Ia_Val |
cd07962 |
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA ... |
107-205 |
1.16e-20 |
|
Anticodon-binding domain of valyl tRNA synthetases; This domain is found in valyl tRNA synthetases (ValRS), 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. ValRS catalyzes the transfer of valine to the 3'-end of its tRNA.
Pssm-ID: 153416 [Multi-domain] Cd Length: 135 Bit Score: 87.61 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 107 LTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSELWDEDDSQKNrrsTIYAILAKTLKTI 186
Cdd:cd07962 40 LSLADRWILSRLNKTVEEVTEALENYRFSEAATALYEFFWNDFCDWYLELVKPRLYGEDEEEKK---AARATLYYVLETI 116
|
90
....*....|....*....
gi 663503655 187 DILIHPFSPFTTQYLYSTI 205
Cdd:cd07962 117 LRLLHPFMPFITEELWQRL 135
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
3-279 |
5.08e-16 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 81.21 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIE-----------------------------ASELLEK-YP-------VDLVRF 45
Cdd:PTZ00419 568 PFKTVFLHAMVRDSQGEKMSKSKGNVIDpleviegislqdlnqklyegnlpekeikrAIELQKKeFPngipecgTDALRF 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 46 YFMWKSSPIEPLNFSTKELMSrpYQ---------VISTLYHL-HTFYRQNSEYDKFDINETTiEWAkknnlltppDIWLL 115
Cdd:PTZ00419 648 GLLAYTQQGRNINLDINRVVG--YRhfcnklwnaVKFALMKLlKDFNLPNSTLFKPNNVESL-PWE---------DKWIL 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 116 SKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSELWDEDDSQKNRRS--TIYAILAKTLKtidiLIHPF 193
Cdd:PTZ00419 716 HRLNVAIKEVTEGFKEYDFSEATQATYNFWLYELCDVYLELIKPRLSKQSDGERKQHAqdVLHTVLDIGLR----LLHPM 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 194 SPFTTQYLYSTIFGEK---ENILLETWPKQDTSLIDEKIEESFDLLKDVV----SVAAASRMKGKLKRRWPL---NEAII 263
Cdd:PTZ00419 792 MPFITEELYQRLPNYLrksESISIAKYPQPNPGWNNEALDEEMKIIMSIVksirSLIATLGIPNKTKPDCYVtakDAELI 871
|
330
....*....|....*.
gi 663503655 264 CLEKGQKNILESLSEL 279
Cdd:PTZ00419 872 ELIESAENLISTLAKI 887
|
|
| Anticodon_Ia_Ile_BEm |
cd07960 |
Anticodon-binding domain of bacterial and eukaryotic mitochondrial isoleucyl tRNA synthetases; ... |
91-239 |
1.30e-15 |
|
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: 74.87 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 91 FDINETTIEWAKknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLSQIYIPITKSELW-DEDDSQK 169
Cdd:cd07960 30 FDPAKDAVPYEE----LLELDRYALHRLNELIKEVREAYENYEFHKVYQALNNFCTVDLSAFYLDIIKDRLYcDAKDSLE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663503655 170 nRRSTIYAiLAKTLKTIDILIHPFSPFTTQYLYSTIFGEK--ENILLETWPKQDTSLIDEKIEESFDLLKDV 239
Cdd:cd07960 106 -RRSAQTV-LYHILDALLKLLAPILPFTAEEVWEHLPGEKkeESVFLEDWPELPEEWKDEELEEKWEKLLAL 175
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
17-203 |
2.46e-15 |
|
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: 78.23 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSRpyqVistlyhlhtfyrqNSEY-DKFD--I 93
Cdd:COG0143 324 EGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVAR---V-------------NSDLaNDLGnlA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 94 NEtTIEWAKKN--------NLLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDF--LINSlsqiYipITKSELWD 163
Cdd:COG0143 388 SR-TLSMIHKYfdgkvpepGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALarAANK----Y--IDETAPWK 460
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 663503655 164 E-DDSQKNRRSTIYAILAKTLKTIDILIHPFSPFTTQYLYS 203
Cdd:COG0143 461 LaKDEDPERLATVLYTLLEALRILAILLKPFLPETAEKILE 501
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
2-59 |
4.13e-14 |
|
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: 73.42 E-value: 4.13e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNF 59
Cdd:cd00818 281 APYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAEDLRF 338
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
3-230 |
7.05e-14 |
|
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: 74.32 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLD--ENGN------KMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTK--ELMSRpyqvi 72
Cdd:COG0495 564 PFKRLLTQGMVLEvgKDGVviggieKMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPPERDLEWSDSgvEGAYR----- 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 73 stlyHLHTFYR---QNSEYDKFDINEttiewakknnlLTPPDIWLLSKLQRMVQKTTDanneckfhesgkAIEDFLIN-S 148
Cdd:COG0495 639 ----FLNRVWRlvvDEAEALKLDVAD-----------LSEADKELRRALHKTIKKVTE------------DIERLRFNtA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 149 LSQIYI---PITKSELWDEDDSqknrrstiyAILAKTLKTIDILIHPFSPFTTQYLYStIFGEKENILLETWPKQDTS-L 224
Cdd:COG0495 692 IAALMElvnALYKAKDSGEADR---------AVLREALETLVLLLAPFAPHIAEELWE-RLGHEGSVADAPWPEADEAaL 761
|
....*.
gi 663503655 225 IDEKIE 230
Cdd:COG0495 762 VEDEVT 767
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
2-426 |
3.19e-12 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 69.23 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMwKSSPI--EPLNFSTKELMSRPYQVISTLYHLH 79
Cdd:PTZ00427 702 APFKNLICNGLVLASDGKKMSKRLKNYPDPLYILDKYGADSLRLYLI-NSVAVraENLKFQEKGVNEVVKSFILPFYHSF 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 80 TFYRQN-SEYD-----KFDINEttiEWAKKNNLLTppDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFlINSLSQIY 153
Cdd:PTZ00427 781 RFFSQEvTRYEclnkkQFLFNT---DYIYKNDNIM--DQWIFSSVQSLTKSVHTEMKAYKLYNVLPKLLQF-IENLTNWY 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 154 IPITKSELWDEDDSQKNRRStiYAILAKTLKTIDILIHPFSPFTTQYLY------------------STIFGEK------ 209
Cdd:PTZ00427 855 IRLNRDRMRGSLGEENCLQS--LCTTYRTLHLFTVLMAPFTPFITEYIYqqlrrvkstnehnennetGNTKEGDlnrgvi 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 210 -ENILLETWPKQDTS-LIDEKIEESFDLLKDVVSVAAASRMKGKLKRRWPLnEAIICLEKGQKNI--LESLSELVKSQMN 285
Cdd:PTZ00427 933 hKSVHFIMLPQVDEKyIIDYEIIELIEKMKDVILLGRVLRERRKVASKKPL-KSITILHPNESYFknFDQISNYIKEELN 1011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 286 IQNykifeIESSEGIEQYlelkqnGLPVVPKIELERSAIGPKAKQDMGKLLKMFSETdpetiITELNSNGsftfQIDQNS 365
Cdd:PTZ00427 1012 VLN-----VECSNDTSCL------DFSAIPNYKTLGVKLGYNLKKVQNKIKNMDSES-----IKLYQQEG----KITLDN 1071
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663503655 366 IVLDKEDFIVDFD---VDEKYQFAKRQNLVVMISLERDNEMMAKGLIKDLARRLQTLRKERGYN 426
Cdd:PTZ00427 1072 VTLEGDDIIIQMKpnfQNDNTDIISNNYVTILMDFTTDQQLENMASARELCNHIQKMRKNLSLN 1135
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
2-54 |
3.29e-12 |
|
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: 67.44 E-value: 3.29e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPI 54
Cdd:cd00668 255 IPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYG 307
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
17-212 |
4.18e-12 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 67.98 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFYFMwKSSPIE-PLNFSTKELMSRPYQVISTLYHLH-----TFYRQNSEYDK 90
Cdd:PRK11893 296 DGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLL-REIPFGqDGDFSREAFINRINADLANDLGNLaqrtlSMIAKNFDGKV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 91 FDINEttiewakknnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDfLINSLSQiYIPITKseLWDEDDSQKN 170
Cdd:PRK11893 375 PEPGA-----------LTEADEALLEAAAALLERVRAAMDNLAFDKALEAILA-LVRAANK-YIDEQA--PWSLAKTDPE 439
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663503655 171 RRSTIYAILAKTLKTIDILIHPFSPFTTQYLYsTIFGEKENI 212
Cdd:PRK11893 440 RLATVLYTLLEVLRGIAVLLQPVMPELAAKIL-DQLGVEEDE 480
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
11-67 |
1.03e-09 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 60.38 E-value: 1.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 663503655 11 GHVLDENGnKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFSTKELMSR 67
Cdd:pfam09334 316 GYLTYEGG-KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVER 371
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
11-59 |
3.25e-09 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 58.31 E-value: 3.25e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 663503655 11 GHVLDENGnKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNF 59
Cdd:cd00814 272 GYLTVEGK-KMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
3-45 |
3.94e-09 |
|
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: 58.41 E-value: 3.94e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRF 45
Cdd:cd00817 326 PFKEVYLHGLVRDEDGRKMSKSLGNVIDPLDVIDGYGADALRF 368
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
2-252 |
4.25e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 59.01 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLE---------KYPVDLVRfyfMWKSSpiepLNFsTKELMSRPyQVI 72
Cdd:PLN02843 593 APYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVIEggknqkqepAYGADVLR---LWVAS----VDY-TGDVLIGP-QIL 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 73 stlyhlhtfyRQNSE-YDKFdinETTI--------EWAKKNNL----LTPPDIWLLSKLQRMVQKTTDANNECKFHESGK 139
Cdd:PLN02843 664 ----------KQMSDiYRKL---RGTLryllgnlhDWKPDNAVpyedLPSIDKYALFQLENVVNEIEESYDNYQFFKIFQ 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 140 AIEDFLINSLSQIYIPITKSELWDEDDSQKNRRS---TIYAILAKTLKTI-DILIHPFSPFTTQYLYSTIFGEKENILLE 215
Cdd:PLN02843 731 ILQRFTIVDLSNFYLDVAKDRLYVGGTTSFTRRScqtVLAAHLLSLLRAIaPILPHLAEDAWQNLPFQEDGSAAESVFEA 810
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 663503655 216 TWPKQDTSLIDEKIEES------FDLLKDVVSVAAASRMkGKL 252
Cdd:PLN02843 811 GWPTPNEEWLSFPAEDVdfwsllLEVRDEVNKVLESARN-GKL 852
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
2-60 |
4.84e-09 |
|
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: 58.58 E-value: 4.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 663503655 2 SPYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYfMWKSSPIEPLNFS 60
Cdd:pfam00133 545 VPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADALRLW-LANSDYGRDINLS 602
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
3-48 |
6.01e-09 |
|
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: 57.26 E-value: 6.01e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 663503655 3 PYKSFLFQGHVLdENGNKMSKSKGNVIEASELLEKYPVDLVRFYFM 48
Cdd:cd00812 259 PPKGLIVQGMVL-LEGEKMSKSKGNVVTPDEAIKKYGADAARLYIL 303
|
|
| DUF5915 |
pfam19302 |
Domain of unknown function (DUF5915); This presumed domain is found at the C-terminus of ... |
278-487 |
1.60e-08 |
|
Domain of unknown function (DUF5915); This presumed domain is found at the C-terminus of isoleucyl tRNA ligase enzymes.
Pssm-ID: 437134 [Multi-domain] Cd Length: 195 Bit Score: 54.40 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 278 ELVKSQMNIQnykifEIESSEGIEQYLEL--KQNgLPVvpkielersaIGPKAKQDMGKLLKMFSETDPETIITeLNSNG 355
Cdd:pfam19302 2 DIIKEELNVK-----EVEFGADESELVEYsaKPN-FPV----------LGKELGKLMKAAAKEIASLNQMEIQK-ILDGG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 356 SFTFQIDQNSIVLDKEDFIVDFDVDEKYQFAKRQNLVVMISLERDNEMMAKGLIKDLARRLQTLRKERGYNPTDilsKAS 435
Cdd:pfam19302 65 TLTIDVDGEEIELTSEDLLVTRQGKEGLAVANEGTLTVALDTTITEELREEGLVREIVSKIQNLRKESGFEVTD---RIN 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 663503655 436 ILELDSESL-DLIKGKTDEIAFLVRVKQVDFEEScKEYKDDDIDGMKIRISVE 487
Cdd:pfam19302 142 LYVSGNEMLeAAIEKFEDYIKKETLAVEIIFNEE-KEYTEVDINGEKLKIAVE 193
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
17-199 |
1.59e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 54.04 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRfYFMWKSSPI-EPLNFSTKELMSRpyqvIstlyhlhtfyrqNSE-------- 87
Cdd:PRK12267 296 KDGKMSKSKGNVVDPEELVDRYGLDALR-YYLLREVPFgSDGDFSPEALVER----I------------NSDlandlgnl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 88 ----------YDKFDINettiewAKKNnlLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLinSLSQIYipIT 157
Cdd:PRK12267 359 lnrtvaminkYFDGEIP------APGN--VTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLI--SRANKY--ID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663503655 158 KSELW--DEDDSQKNRRSTIYAILAKTLKTIDILIHPFSPFTTQ 199
Cdd:PRK12267 427 ETAPWvlAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSK 470
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
17-67 |
1.85e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 53.62 E-value: 1.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSP-IEPLNFSTKELMSR 67
Cdd:PRK00133 326 EGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPEtIDDLDFNWEDFQQR 377
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
3-298 |
2.65e-07 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 53.36 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 3 PYKSFLFQGHVLDENGNKMSKSKGNVIEASELLEKYPVDLVRfyfmwksSPIEPLNFSTKEL-MSRPYQV---------- 71
Cdd:PLN02381 638 PFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGISLEGLH-------KRLEEGNLDPKELvVAKEGQKkdfpngiaec 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 72 -ISTLYHLHTFYRQNSEYDKFDI--------------NETTIEWAKKNNLLTPPDI-----------WLLSKLQRMVQKT 125
Cdd:PLN02381 711 gTDALRFALVSYTAQSDKINLDIlrvvgyrqwcnklwNAVRFAMSKLGDDYTPPATlsvetmpfsckWILSVLNKAISKT 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 126 TDANNECKFHESGKAIEDFLINSLSQIYIPITKSELWDEDDSQKNRRSTIYAILAKTLKTIDILIHPFSPFTTQYLYSTI 205
Cdd:PLN02381 791 VSSLDAYEFSDAASTVYSWWQYQFCDVFIEAIKPYFAGDNPEFASERAAAQDTLWICLDTGLRLLHPFMPFVTEELWQRL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 206 -----FGEKENILLETWPKQDTSLIDEKIEESFDLLKDVVSVAAASRMKGKLKRRwplNEAI----ICLEKGQKNILESL 276
Cdd:PLN02381 871 pqpkdHTRKDSIMISEYPSAVEAWTNEKVEYEMDLVLSTVKCLRSLRAEVLEKQK---NERLpafaLCRNQEIAAIIKSH 947
|
330 340
....*....|....*....|..
gi 663503655 277 SELVKSQMNIQNYKIFEIESSE 298
Cdd:PLN02381 948 QLEILTLANLSSLKVLLSENDA 969
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
13-121 |
3.25e-07 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 52.51 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 13 VLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFMWKSSPIEPLNFStkelmsrpyqVISTLYhlhtfyrqnSEYDKFD 92
Cdd:PRK00750 273 FLDKKGEKISKSKGNVITIEDWLEYAPPESLRLFMFARPKPAKRLDFD----------VIPKLV---------DEYDRFE 333
|
90 100
....*....|....*....|....*....
gi 663503655 93 INETTIEWAKKNNLLTPPdIWLLSKLQRM 121
Cdd:PRK00750 334 RKYFGQEEKKEEEELANP-VYHIHNGNPL 361
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
17-60 |
4.35e-07 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 52.03 E-value: 4.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFYFM---WKSspiePLNFS 60
Cdd:COG0215 262 NGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahYRS----PLDFS 304
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
7-60 |
5.81e-07 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 50.27 E-value: 5.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 663503655 7 FLFQGHVLdENGNKMSKSKGNVIEASELLEKYPVDLVRFYFM---WKSspiePLNFS 60
Cdd:cd00672 162 WLHTGHLT-IDGEKMSKSLGNFITVRDALKKYDPEVLRLALLsshYRS----PLDFS 213
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
13-47 |
1.14e-05 |
|
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: 47.32 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*
gi 663503655 13 VLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYF 47
Cdd:cd00674 268 IGLKGGGKMSSSKGNVITPSDWLEVAPPEVLRYLY 302
|
|
| Anticodon_Ia_Leu_AEc |
cd07959 |
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ... |
71-205 |
1.42e-05 |
|
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: 44.12 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 71 VISTLYHLHTFYRQNSEYDKFDINETTIewakknnlltppDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFLINSLS 150
Cdd:cd07959 9 AILRLERFYELAEELIETEGELEELTFI------------DRWLLSRLNRLIKETTEAYENMQFREALKEGLYELQNDLD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 663503655 151 QiYIPITKSElwdeddsqKNRRstiyaILAKTLKTIDILIHPFSPFTTQYLYSTI 205
Cdd:cd07959 77 W-YRERGGAG--------MNKD-----LLRRFIEVWTRLLAPFAPHLAEEIWHEL 117
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
13-47 |
1.47e-05 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 47.50 E-value: 1.47e-05
10 20 30
....*....|....*....|....*....|....*
gi 663503655 13 VLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYF 47
Cdd:COG1384 280 FLDENGEKISKSKGNGLTVEEWLEYAEPESLRYFM 314
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
13-53 |
1.58e-05 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 46.87 E-value: 1.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 663503655 13 VLDENGNKMSKSKGNVIEASELLEKYPVDLVRfYFMWKSSP 53
Cdd:pfam01921 272 ILLKGGGKMSSSKGNVITPEDWLEYAPPESLR-FLMFRTKP 311
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
7-60 |
7.74e-04 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 41.94 E-value: 7.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 663503655 7 FLFQGHvLDENGNKMSKSKGNVIEASELLEKYPVDLVRFYFM---WKSspiePLNFS 60
Cdd:PTZ00399 303 FLHSGH-LHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLlhkWDK----PMNYS 354
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
78-193 |
1.37e-03 |
|
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: 38.64 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 78 LHTFYRQNSEYDKFdINETTIEWakKNNLLTPPDIWLLSKLQRMVQKTTDANNECKFHESGKAIEDFlINSLSQiYIPIT 157
Cdd:cd07375 11 LNRLYRLLSFFRKA-LGGTQPKW--DNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKF-TNELNW-YLDEL 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 663503655 158 KSELWDEDDSQKnRRSTIYAILAKTLKtidiLIHPF 193
Cdd:cd07375 86 KPALQTEELREA-VLAVLRAALVVLTK----LLAPF 116
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
17-128 |
3.97e-03 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 39.70 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663503655 17 NGNKMSKSKGNVIEASELLEKYPVDLVRFyFMWKSSPIEPLNFSTKELMSRPyqviSTLYHLHTFYRqNSEYDKFDINET 96
Cdd:PRK14535 505 DGEKMSKSLGNFFTIREVLKQYDPEVVRF-FILRAHYRSPLNYSDAHLDDAK----GALTRLYTTLK-NTPAAEFMLSEN 578
|
90 100 110
....*....|....*....|....*....|....*...
gi 663503655 97 TIEWAKK------NNLLTPPDIWLLSKLQRMVQKTTDA 128
Cdd:PRK14535 579 VNDYTRRfyaamnDDFGTVEAVAVLFELAGEVNKTNDA 616
|
|
| |
