|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1-641 |
0e+00 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 1197.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 1 MPVITLPDGSQRQFDGAVTGTQLAEAIGPGLKRAALVMEVNGQPMDMSREITEDSAVKFVTRKDEAALELIRHDAAHVMA 80
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 81 EAVQALFPGTQVTIGPAIENGFYYDFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEAIAYFEAKGERYKAELI 160
Cdd:COG0441 81 QAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 161 RDLPQDQTITVYRQGDWLDLCRGPHLRSTGDVGtAFKLMKVAGAYWRGNAKNQMLSRIYGTAWRDQKELEAYLHQIEEAE 240
Cdd:COG0441 161 EDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIK-AFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 241 RRDHRKIGREMDLFHIQEE-AVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFI 319
Cdd:COG0441 240 KRDHRKLGKELDLFHFQEEvGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 320 AEVVEEEstLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIFCTEDQIADET 399
Cdd:COG0441 320 TESDGEE--YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 400 VRFVGLLESVYQDFGFESFSVKFSDRPEVRAGSDEVWDRAESALKEACEKAGVAYTLNPGEGAFYGPKLEFVLRDAIGRD 479
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 480 WQCGTIQVDFVLPERLDAEYVTSESGRARPVMLHRAIIGSFERFLGILIEQYAGRFPLWLAPTQAVVATIVSDADEYAAE 559
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 560 VAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLKGEATPPDL 639
Cdd:COG0441 558 VAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEIRSRSL 637
|
..
gi 2541258028 640 KR 641
Cdd:COG0441 638 EP 639
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-633 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 725.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 1 MPVITLPDGSQRQFDGAVTGTQLAEAIGPGLKRAALVMEVNGQPMDMSREITEDSAVKFVTRKDEAALELIRHDAAHVMA 80
Cdd:PRK12444 5 MIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 81 EAVQALFPGTQVTIGPAIENGFYYDFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEAIAYFEAKGERYKAELI 160
Cdd:PRK12444 85 QAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLKLELL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 161 RDLPQDQTITVYRQGDWLDLCRGPHLRSTGDVgTAFKLMKVAGAYWRGNAKNQMLSRIYGTAWRDQKELEAYLHQIEEAE 240
Cdd:PRK12444 165 EAIPSGESITLYKQGEFVDLCRGPHLPSTGYL-KAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 241 RRDHRKIGREMDLFHIQEEAVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFIA 320
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 321 EVveEESTLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIFCTEDQIADETV 400
Cdd:PRK12444 324 EV--DNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 401 RFVGLLESVYQDFGFEsFSVKFSDRPEVRAGSDEVWDRAESALKEACEKAGVAYTLNPGEGAFYGPKLEFVLRDAIGRDW 480
Cdd:PRK12444 402 SVMAQIDYVYKTFGFE-YEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 481 QCGTIQVDFVLPERLDAEYVTSESGRARPVMLHRAIIGSFERFLGILIEQYAGRFPLWLAPTQAVVATiVSDA--DEYAA 558
Cdd:PRK12444 481 QCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIP-VSNAvhVQYAD 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541258028 559 EVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLKGE 633
Cdd:PRK12444 560 EVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEE 634
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
72-633 |
0e+00 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 708.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 72 RHDAAHVMAEAVQALFPGTQVTIGPAIENGFYYDFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEAIAYFEaK 151
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 152 GERYKAELIRDLPQDQTITVYRQGD-WLDLCRGPHLRSTGDVgTAFKLMKVAGAYWRGNAKNQMLSRIYGTAWRDQKELE 230
Cdd:TIGR00418 80 LEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFI-KAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 231 AYLHQIEEAERRDHRKIGREMDLFHIQEE-AVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGH 309
Cdd:TIGR00418 159 AYLLRLEEAKKRDHRKLGKELELFSFEPEiGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 310 WDKYRKNMFIAEVVEEEsTLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIF 389
Cdd:TIGR00418 239 WDNYKERMFPFTELDNR-EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 390 CTEDQIADETVRFVGLLESVYQDFGFESFSVKFSDR-PEVRAGSDEVWDRAESALKEACEKAGVAYTLNPGEGAFYGPKL 468
Cdd:TIGR00418 318 CTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 469 EFVLRDAIGRDWQCGTIQVDFVLPERLDAEYVTSESGRARPVMLHRAIIGSFERFLGILIEQYAGRFPLWLAPTQAVVAT 548
Cdd:TIGR00418 398 DFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 549 IVSDADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVT 628
Cdd:TIGR00418 478 VNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....*
gi 2541258028 629 LLKGE 633
Cdd:TIGR00418 558 KLRKE 562
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
4-633 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 637.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 4 ITLPDGSQR-QFDGAVTGTQLAEAIGPGLKRAALVMEVNGQPMDMSREITEDSAVKFVTRKDEAALELIRHDAAHVMAEA 82
Cdd:PLN02908 54 VTLPDGAVKdGKKWVTTPMDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 83 VQALFpGTQVTIGPAIEN--GFYYD-FARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEAIAYFEakGERYKAEL 159
Cdd:PLN02908 134 LELEY-GCKLCIGPCTTRgeGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFS--ENKFKVEI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 160 IRDLPQDQTITVYRQGDWLDLCRGPHLRSTGDVgTAFKLMKVAGAYWRGNAKNQMLSRIYGTAWRDQKELEAYLHQIEEA 239
Cdd:PLN02908 211 INDLPEDATITVYRCGPLVDLCRGPHIPNTSFV-KAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 240 ERRDHRKIGREMDLFHIQEEAVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFI 319
Cdd:PLN02908 290 KKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 320 AEVVEEEstLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIFCTEDQIADET 399
Cdd:PLN02908 370 FEIEKQE--FGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 400 VRFVGLLESVYQDFGFeSFSVKFSDRPEVRAGSDEVWDRAESALKEACEKAGVAYTLNPGEGAFYGPKLEFVLRDAIGRD 479
Cdd:PLN02908 448 KGVLDFLDYVYEVFGF-TYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 480 WQCGTIQVDFVLPERLDAEYVT-SESGRARPVMLHRAIIGSFERFLGILIEQYAGRFPLWLAPTQAVVATIVSDADEYAA 558
Cdd:PLN02908 527 FQCATVQLDFQLPIRFKLSYSAeDEAKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAE 606
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541258028 559 EVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLKGE 633
Cdd:PLN02908 607 EVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEE 681
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
50-631 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 601.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 50 EITEDSAVKFVTRKDEAALELIRHDAAHVMAEAVQALFPGTQVTIGPAIENGFYYDFARnEPFTPEDLPAIEAKMREIIA 129
Cdd:PLN02837 25 GEAEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDM-EPLTDKDLKRIKKEMDRIIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 130 ANATFDRDVWSREEAIAYFEAKGERYKAELIRDLpQDQTITVYRQG-DWLDLCRGPHLRSTGDVGT-AFKLMKVAGAYWR 207
Cdd:PLN02837 104 RNLPLVREEVSREEAQKRIMAINEPYKLEILEGI-KEEPITIYHIGeEWWDLCAGPHVERTGKINKkAVELESVAGAYWR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 208 GNAKNQMLSRIYGTAWRDQKELEAYLHQIEEAERRDHRKIGREMDLFHIQEEAVGS-IFWHAKGWKLYRTVEAYIRRRLD 286
Cdd:PLN02837 183 GDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 287 ANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFIAEVVEEEsTLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRY 366
Cdd:PLN02837 263 EHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDE-LYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 367 EPSGALHGIMRVRAFTQDDAHIFCTEDQIADETVRFVGLLESVYQDFGFESFSVKFSDRPEVRAGSDEVWDRAESALKEA 446
Cdd:PLN02837 342 ELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKSVGSDDIWEKATTALRDA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 447 CEKAGVAYTLNPGEGAFYGPKLEFVLRDAIGRDWQCGTIQVDFVLPERLDAEYVTSESGRARPVMLHRAIIGSFERFLGI 526
Cdd:PLN02837 422 LDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 527 LIEQYAGRFPLWLAPTQAVVATIVSDADEYAAEVAAALTKAGLSVELdTTNQKIQAKIREHSLHHVPNILVVGRKEAEER 606
Cdd:PLN02837 502 LIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKEVETR 580
|
570 580
....*....|....*....|....*
gi 2541258028 607 KVALRRLGGAAQEVLTLDEAVTLLK 631
Cdd:PLN02837 581 TLTVRSRHGGELGTMPVDDFINRIQ 605
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
242-541 |
1.43e-173 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 495.53 E-value: 1.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 242 RDHRKIGREMDLFHIQEEAVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFIAE 321
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 322 VVEEEstLALKPMNCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIFCTEDQIADETVR 401
Cdd:cd00771 81 EEDEE--YGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 402 FVGLLESVYQDFGFESFSVKFSDRPEVRAGSDEVWDRAESALKEACEKAGVAYTLNPGEGAFYGPKLEFVLRDAIGRDWQ 481
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 482 CGTIQVDFVLPERLDAEYVTSESGRARPVMLHRAIIGSFERFLGILIEQYAGRFPLWLAP 541
Cdd:cd00771 239 CSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
324-531 |
4.67e-47 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 163.74 E-value: 4.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 324 EEESTLALKPMNCPCHVQIF-KQGLRSYRqLPIRMAEFGSCHRYEPSGALHGIMRVRAFTQDDAHIFCTEDQIADETVRF 402
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 403 VGLLESVYQDFGFESFSVKfsdrpevragsdEVWDRaesalkeacekagvaytlnpgEGAFYGPKLEFVLRDAI-GRDWQ 481
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVVR------------LSNSD---------------------GSAFYGPKLDFEVVFPSlGKQRQ 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 482 CGTIQVD-FVLPERLDAEYVTSESGRARPVMLHRAIIGsFERFLGILIEQY 531
Cdd:pfam00587 132 TGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
270-528 |
2.08e-40 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 147.54 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 270 GWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFiaeVVEEEST------LALKPMNCPCHVQIF 343
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMY---TFEDKGRelrdtdLVLRPAACEPIYQIF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 344 KQGLRSYRQLPIRMAEFGSCHRYEPSGAlHGIMRVRAFTQDDAHIFCTEDQIADETVRFVGLLESVYQDFGfESFSVKFS 423
Cdd:cd00670 78 SGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG-LPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 424 DRPEVRAGSDEvwdraesalkeacekagvaytlnpGEGAFYGPKLEFVLRDAI-GRDWQCGTIQVDFVLPERLDAEYVTS 502
Cdd:cd00670 156 DDPFFGRGGKR------------------------GLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDE 211
|
250 260
....*....|....*....|....*.
gi 2541258028 503 ESGRARPVMLHRAiiGSFERFLGILI 528
Cdd:cd00670 212 DGGGRAHTGCGGA--GGEERLVLALL 235
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
338-633 |
5.83e-32 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 131.15 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 338 CHVQ--IFKQGLRSYRQLPIRMAEFGSC-HRYEPSGALHGIMRVRAFTQDDAHIFCTE-DQIADETVRFVGLLESVYQDF 413
Cdd:PRK03991 290 CFGQflMLKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 414 GFEsFSVKFsdrpevRAGSDeVWDRAESALKEACEKAG--VAYTLNPgEGAFYGP-KLEFVLRDAIGRDWQCGTIQVDFV 490
Cdd:PRK03991 370 GRD-YEVAI------RFTED-FYEENKDWIVELVKREGkpVLLEILP-ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 491 LPERLDAEYVTSESGRARPVMLHRAIIGSFERFL-GIL----IEQYAG---RFPLWLAPTQAVVATIVSDADEYAAEVAA 562
Cdd:PRK03991 441 NAERFGIKYVDENGEEKYPIILHCSPTGSIERVIyALLekaaKEEEEGkvpMLPTWLSPTQVRVIPVSERHLDYAEEVAD 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 563 ALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLKGE 633
Cdd:PRK03991 521 KLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEE 591
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
541-631 |
4.27e-27 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 104.89 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 541 PTQAVVATIVSDADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEV 620
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 2541258028 621 LTLDEAVTLLK 631
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
277-523 |
4.55e-27 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 109.13 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 277 VEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRknMFIAEVVEEEstLALKPMNCPCHVQIFKQGLrsyRQLPIR 356
Cdd:cd00768 5 IEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDL--LPVGAENEED--LYLRPTLEPGLVRLFVSHI---RKLPLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 357 MAEFGSCHRYEPSGAlhGIMRVRAFTQDDAHIFCTEDQIADETVRFVGLLESVYQDFG-FESFSVKFSDRPEVRAGsdev 435
Cdd:cd00768 78 LAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGiKLDIVFVEKTPGEFSPG---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 436 wdraesalkeacekagvaytlnpgegaFYGPKLEFVLRDAIGRDWQCGTIQVDFVLPERLDAEYVTSESGRAR-PVMLHR 514
Cdd:cd00768 152 ---------------------------GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALEYRyPPTIGF 204
|
....*....
gi 2541258028 515 AIigSFERF 523
Cdd:cd00768 205 GL--GLERL 211
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
2-65 |
4.54e-22 |
|
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340458 [Multi-domain] Cd Length: 65 Bit Score: 89.85 E-value: 4.54e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541258028 2 PVITLPDGSQRQFDGAVTGTQLAEAIGPGLKRAALVMEVNGQPMDMSREITEDSAVKFVTRKDE 65
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDP 64
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
543-631 |
8.65e-17 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 75.70 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 543 QAVVATIVSDAD---EYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQE 619
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|..
gi 2541258028 620 VLTLDEAVTLLK 631
Cdd:pfam03129 81 TVSLDELVEKLK 92
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
169-218 |
9.62e-15 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 68.18 E-value: 9.62e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 169 ITVYRQGD-WLDLCRGPHLRSTGDVGtAFKLMKVAGAYWRgnaknqmLSRI 218
Cdd:smart00863 1 VRVVSIGDfSVELCGGTHVPNTGEIG-AFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
169-218 |
3.80e-12 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 429764 [Multi-domain] Cd Length: 43 Bit Score: 60.92 E-value: 3.80e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 169 ITVYRQGDW-LDLCRGPHLRSTGDVGtAFKLMKvagaywrGNAKNQMLSRI 218
Cdd:pfam07973 1 VRVVSIGDFdVDLCGGTHVPNTGEIG-AFKILK-------GESKNKGLRRI 43
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
273-631 |
1.10e-11 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 67.07 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 273 LYRTVEAYIRRRLDANGYEEVRTP-----QLVDRKLWEmsghwdkyrknmfiaEVVEEE---------STLALKP-MNCP 337
Cdd:COG0124 20 KWQYVEDTIREVFERYGFQEIRTPifeytELFARKIGE---------------DIVEKEmytfedrggRSLTLRPeGTAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 338 ChvqifkqgLRSY------RQLPIRMAEFGSCHRYEPSGAlhGimRVRAFTQDDAHIFCTEDQIADetVRFVGLLESVYQ 411
Cdd:COG0124 85 V--------ARAVaehgneLPFPFKLYYIGPVFRYERPQK--G--RYRQFHQFGVEVIGSDSPLAD--AEVIALAADLLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 412 DFGFESFSVKFSDR--PEVRAG------------------SDEVWDRAES------------------------------ 441
Cdd:COG0124 151 ALGLKDFTLEINSRglPEERAEallryldkldkighedvlDEDSQRRLETnplraildskgpdcqevladapklldylge 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 442 -------ALKEACEKAGVAYTLNPGE--G-AFY-GPKLEFVLRD-----AI---GR-DwqcGtiqvdfvLPERLdaeyvt 501
Cdd:COG0124 231 eglahfeEVLELLDALGIPYVIDPRLvrGlDYYtGTVFEIVTDGlgaqgSVcggGRyD---G-------LVEQL------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 502 seSGRARPvmlhrAI---IGsFERFLGILIEQyaGRFPLWLAPTQAVVATIVSDADEYAAEVAAALTKAGLSVELDTTNQ 578
Cdd:COG0124 295 --GGPPTP-----AVgfaIG-LERLLLLLEEL--GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2541258028 579 KIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLK 631
Cdd:COG0124 365 KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLK 417
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
256-399 |
2.18e-11 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 64.52 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 256 IQEEAVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFIA-EVVEEESTLAlkpm 334
Cdd:cd00779 16 IRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkDRHGKEFLLG---- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 335 ncPCH----VQIFKQGLRSYRQLPIRMAEFGSCHRYE--PSGalhGIMRVRAFTQDDAHIFCTEDQIADET 399
Cdd:cd00779 92 --PTHeeviTDLVANEIKSYKQLPLNLYQIQTKFRDEirPRF---GLMRGREFLMKDAYSFDIDEESLEET 157
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
270-631 |
3.21e-11 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 66.33 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 270 GWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMFiaeVV----EEESTLAlkpmncPCH----VQ 341
Cdd:COG0442 46 GYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELA---RVtdrlEREFCLG------PTHeeviTD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 342 IFKQGLRSYRQLPIRMAEFGSCHRYE--PSgalHGIMRVRAFTQDDAHIFCTEDQIADETVRfvgLLESVYQDFgFESFS 419
Cdd:COG0442 117 LVRNEIKSYRDLPLLLYQIQTKFRDEirPR---FGLLRTREFLMKDAYSFHATEEELDEEYQ---KMLDAYERI-FERLG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 420 VKFsdRPeVRA-------------------GSDEV-----------WDRAESALKEACEKAG-----------------V 452
Cdd:COG0442 190 LPV--RA-VEAdsgaiggseshefmvladsGEDTIvycdacdyaanIEKAEALAPPAERAEPtkeleavatpgaktieeV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 453 AYTLN-----------------------PG---------EGAFYGPKLEFVLRDAI------------------------ 476
Cdd:COG0442 267 AEFLGvpaektvktlvykadgelvavlvRGdhelneiklENLLGASELELATEEEIeaalgavpgflgpvglgvpyiadr 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 477 ----GRDWQCG-----------TIQVDFVLPERLD-----------------------------------AE----YVTS 502
Cdd:COG0442 347 svagMSNFVCGaneddyhytnvNWGRDFPVDEVADlrnvvegdpcpdcggllqdgrgievghifklgtkySKamdaTFLD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 503 ESGRARPVmlhraIIGSF----ERFLGILIEQYA---G-RFPLWLAPTQAVVATI-VSDAD--EYAAEVAAALTKAGLSV 571
Cdd:COG0442 427 ENGKEQPV-----WMGCYgigvTRLIAAAIEQHHddkGiIWPPAIAPFQVVIVPInMKDEAvlEAAEELYAELKAAGIDV 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541258028 572 ELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVAL-RRLGGAAQEVlTLDEAVTLLK 631
Cdd:COG0442 502 LLDDRDERPGVKFADAELIGIPLRIVIGPRDLEEGQVEVkRRDTGEKEEV-PLDELVETVK 561
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
541-631 |
8.19e-11 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 58.95 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 541 PTQAVVATIVSD---ADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAA 617
Cdd:cd00738 1 PIDVAIVPLTDPrveAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 2541258028 618 QEVLTLDEAVTLLK 631
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
541-631 |
1.38e-10 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 57.93 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 541 PTQAVVATIVSDADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEV 620
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQET 80
|
90
....*....|.
gi 2541258028 621 LTLDEAVTLLK 631
Cdd:cd00859 81 VALDELVEELK 91
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
262-474 |
1.75e-08 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 55.84 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 262 GSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKY-RKNMFI---AEVVEEESTLALKPMNCP 337
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGfSKELAVfkdAGDEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 338 CHVQIFKQGLRSYRQLPIRMAEFGSCHRYEPSgALHGIMRVRAFTQDDAHIFCTEDQIADETV-RFVGLLESVYQDFGFE 416
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHADAEEADEEFlNMLSAYAEIARDLAAI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 417 SFSVKFSDRPEVRAGSdeVWDRAESALKE--ACEKAGVAYTLNPGEGAFYGPKLEFVLRD 474
Cdd:cd00772 182 DFIEGEADEGAKFAGA--SKSREFEALMEdgKAKQAETGHIFGEGFARAFDLKAKFLDKD 239
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
4-61 |
7.36e-08 |
|
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.
Pssm-ID: 427005 [Multi-domain] Cd Length: 60 Bit Score: 49.47 E-value: 7.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541258028 4 ITLPDGSQRQFDGAVTGTQLAEAIGPGLKRAALVMEVNGQPMDMSREITEDSAVKFVT 61
Cdd:pfam02824 3 VYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
270-399 |
1.76e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 54.32 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 270 GWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMF-IAEVVEEESTLAlkpmncPCH----VQIFK 344
Cdd:PRK09194 46 GLRVLRKIENIVREEMNKIGAQEVLMPALQPAELWQESGRWEEYGPELLrLKDRHGRDFVLG------PTHeeviTDLVR 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541258028 345 QGLRSYRQLP-------------IRmaefgscHRYepsgalhGIMRVRAFTQDDAHIFCTEDQIADET 399
Cdd:PRK09194 120 NEIKSYKQLPlnlyqiqtkfrdeIR-------PRF-------GLMRGREFIMKDAYSFHADEESLDET 173
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
256-632 |
2.28e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 53.71 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 256 IQEEAVGSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEMSGHWDKYRKNMF-IAEVVEEEstLALKPM 334
Cdd:PRK12325 32 IRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLrIKDRHDRE--MLYGPT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 335 NCPCHVQIFKQGLRSYRQLPIRMAEFGSCHRYE--PSgalHGIMRVRAFTQDDAHIFCTEDQ------------------ 394
Cdd:PRK12325 110 NEEMITDIFRSYVKSYKDLPLNLYHIQWKFRDEirPR---FGVMRGREFLMKDAYSFDLDEEgarhsynrmfvaylrtfa 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 395 --------------------------IADE---TV----RFVGLL-ESVYQDFGFESFSVKFSDRPEVRAGSDEVWDRAE 440
Cdd:PRK12325 187 rlglkaipmradtgpiggdlshefiiLAETgesTVfydkDFLDLLvPGEDIDFDVADLQPIVDEWTSLYAATEEMHDEAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 441 SAL---KEACEKAGVaytlnpgegafygpklefvlrdAIGRDWQCGTiqvdfVLPERLDAeYVTSESGRARPV-Mlhrai 516
Cdd:PRK12325 267 FAAvpeERRLSARGI----------------------EVGHIFYFGT-----KYSEPMNA-KVQGPDGKEVPVhM----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 517 iGSF----ERFLGILIEQY---AG-RFPLWLAPTQAVVATI-VSDA--DEYAAEVAAALTKAGLSVELDTTNQKIQAKIR 585
Cdd:PRK12325 314 -GSYgigvSRLVAAIIEAShddKGiIWPESVAPFKVGIINLkQGDEacDAACEKLYAALSAAGIDVLYDDTDERPGAKFA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2541258028 586 EHSLHHVPNILVVGRKEAEERKVALRRLGGAAQEVLTLDEAVTLLKG 632
Cdd:PRK12325 393 TMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEAAINRLTA 439
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
541-631 |
1.61e-06 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 46.81 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 541 PTQAVVATIVSD---ADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALR-RLGGA 616
Cdd:cd00861 1 PFDVVIIPMNMKdevQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKvRKTGE 80
|
90
....*....|....*
gi 2541258028 617 AQEVlTLDEAVTLLK 631
Cdd:cd00861 81 KEEI-SIDELLEFLQ 94
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
262-413 |
2.17e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 49.52 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 262 GSIFWHAKGWKLYRTVEAYIRRRLDANGYEEVRTPQLVDRKLWEM-SGHWDKYRKNMFIAEVV---EEESTLALKPMN-- 335
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKeKEHIEGFAPEVAWVTHGgleELEEPLALRPTSet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 336 --CPchvqIFKQGLRSYRQLPIRMAEFGSCHRYEPSGALHGImRVRAFTQDDAH-IFCTEDQIADETVRFVGLLESVYQD 412
Cdd:cd00778 103 aiYP----MFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFL-RTREFLWQEGHtAHATEEEAEEEVLQILDLYKEFYED 177
|
.
gi 2541258028 413 F 413
Cdd:cd00778 178 L 178
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
536-633 |
5.60e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 49.07 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 536 PLWLAPTQAVVATIVSDADEYAAEVAAALTKAGLSVELDTTNQKIQAKIREHSLHHVPNILVVGRKEAEERKVALRRLGG 615
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRAN 348
|
90
....*....|....*...
gi 2541258028 616 AAQEVLTLDEAVTLLKGE 633
Cdd:PRK14938 349 NEQKSMTVEELVKEIKRA 366
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
271-479 |
1.22e-05 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 47.21 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 271 WKLYRTVEAYIRRRLDANGYEEVRTP-----QLVDRKLWEMsghwdkYRKNMFiaeVVEEES--TLALKPMNCPCHVQIF 343
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPvfeytELFLRKSGDE------VSKEMY---RFKDKGgrDLALRPDLTAPVARAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 344 KQGLrSYRQLPIRMAEFGSCHRYEPSGALhgimRVRAFTQDDAHIFCTEDQIAD-ETVRfvgLLESVYQDFGFESFSVKF 422
Cdd:cd00773 73 AENL-LSLPLPLKLYYIGPVFRYERPQKG----RYREFYQVGVEIIGSDSPLADaEVIA---LAVEILEALGLKDFQIKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 423 SDR---------PEVRAGSDE-VWDRAE-------SALKEACEKAGVA--YTLNPGE--GAFY--GPKLEFVLRDAIGRD 479
Cdd:cd00773 145 NHRgildgiaglLEDREEYIErLIDKLDkealahlEKLLDYLEALGVDikYSIDLSLvrGLDYytGIVFEAVADGLGAQG 224
|
|
| AlaS |
COG0013 |
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ... |
105-198 |
6.53e-05 |
|
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439784 [Multi-domain] Cd Length: 880 Bit Score: 46.20 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 105 DFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEA-----IAYFeakGERYKAElIRdlpqdqTITVyrqGDW-L 178
Cdd:COG0013 601 DFSHFEALTPEELAEIEDLVNEKIRENLPVETREMPLDEAkalgaMALF---GEKYGDE-VR------VVSI---GDFsR 667
|
90 100
....*....|....*....|
gi 2541258028 179 DLCRGPHLRSTGDVGtAFKL 198
Cdd:COG0013 668 ELCGGTHVSRTGDIG-LFKI 686
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
73-200 |
8.51e-05 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 45.54 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 73 HDAAHVMAEAVQALFpGTQV-TIGPAI-ENGFYYDFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEA-----I 145
Cdd:PRK01584 457 HTATHLLHKALRLVL-GDHVrQKGSNItAERLRFDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEArekgaM 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541258028 146 AYFeakGERYkaelirdlpqDQTITVYRQGDW-LDLCRGPHLRSTGDVGTaFKLMK 200
Cdd:PRK01584 536 ALF---GEKY----------EDIVKVYEIDGFsKEVCGGPHVENTGELGT-FKIQK 577
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
534-576 |
3.15e-04 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 41.00 E-value: 3.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2541258028 534 RFPLWLAPTQAVVATIVSDAD--EYAAEVAAALTKAGLSVELDTT 576
Cdd:cd00858 19 RLPPALAPIKVAVLPLVKRDElvEIAKEISEELRELGFSVKYDDS 63
|
|
| PLN02900 |
PLN02900 |
alanyl-tRNA synthetase |
104-203 |
1.49e-03 |
|
alanyl-tRNA synthetase
Pssm-ID: 215487 [Multi-domain] Cd Length: 936 Bit Score: 41.92 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 104 YDFARNEPFTPEDLPAIEAKMREIIAANATFDRDVWSREEA------IAYFeakGERYkAELIR--DLPQDQTItvyrqg 175
Cdd:PLN02900 630 FDFSHGKPMTPEELREVESLVNEWIGDALPVEAKEMPLADAkringlRAVF---GEKY-PDPVRvvSVGGVYSM------ 699
|
90 100
....*....|....*....|....*...
gi 2541258028 176 dwlDLCRGPHLRSTGDVGtAFKLMKVAG 203
Cdd:PLN02900 700 ---ELCGGTHVSNTAEAE-AFKLLSEEG 723
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
72-201 |
2.44e-03 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 40.18 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541258028 72 RHDAAHVMAEAVQALFPGtqVTIGPAI-ENGFYYDFARNEpFTPEDLPAIEAKMREIIAANATFDRDVWSREEAiayfEA 150
Cdd:COG2872 99 LHTALHLLSAVVYREYGA--PVTGGQIgEDRARIDFDLPE-FDEEDLEEIEAEANELIAADLPVRIYWITREEL----EA 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2541258028 151 KGERYKAELIRDLPQDQTITVYRQGDWlDL--CRGPHLRSTGDVGtAFKLMKV 201
Cdd:COG2872 172 IPGLVRTMSVLPPPGVGRVRIVEIGGV-DLqpCGGTHVANTGEIG-RIKITKI 222
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
534-580 |
9.70e-03 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 38.96 E-value: 9.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2541258028 534 RFPLWLAPTQAVVATIVSDA--DEYAAEVAAALTKAGLSVELDTTNQKI 580
Cdd:PLN02734 563 RFPPLVAPIKCTVFPLVQNQqlNAVAKVISKELTAAGISHKIDITGTSI 611
|
|
| |
