|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1-636 |
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: 1169.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 1 MMKISFPDGSSKEFEKGIKVYDVAKSISEGLARNALGAMVNDEVLGINDPINCDAEVKILTFEDKEGKKIFWHTSAHVLA 80
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 81 HAIMNLWPETKFAIGPAIDNGFYYDIDLEHKIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKAIEFFKERGQDYKVELI 160
Cdd:COG0441 81 QAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 161 EGI-EDKNVGIYKMGNFVDLCRGPHIGNVKIIKAFKLLSIAGAYWRGDSNNKMLQRIYGISFEKKKQLDEYIERMEEAEK 239
Cdd:COG0441 161 EDIpEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 240 RDHRRIGRELDLFTMRDE-GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMYFT 318
Cdd:COG0441 241 RDHRKLGKELDLFHFQEEvGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 319 KIDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCLPEQVKDEVFKM 398
Cdd:COG0441 321 ESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 399 IDLAELLYSTFGFK-YEIELSTRPDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDFHLEDAIGRTWQC 477
Cdd:COG0441 401 IDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQC 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 478 GTIQLDFQMPENFELTYINADGEKARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAPVQVEIIPVSEKFHDYAEEVKN 557
Cdd:COG0441 481 GTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAK 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519540504 558 KLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMKEEVKEKKITE 636
Cdd:COG0441 561 KLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEIRSRSLEP 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: 852.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 1 MMKISFPDGSSKEFEKGIKVYDVAKSISEGLARNALGAMVNDEVLGINDPINCDAEVKILTFEDKEGKKIFWHTSAHVLA 80
Cdd:PRK12444 5 MIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 81 HAIMNLWPETKFAIGPAIDNGFYYDIDLEHKIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKAIEFFKERGQDYKVELI 160
Cdd:PRK12444 85 QAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLKLELL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 161 EGI-EDKNVGIYKMGNFVDLCRGPHIGNVKIIKAFKLLSIAGAYWRGDSNNKMLQRIYGISFEKKKQLDEYIERMEEAEK 239
Cdd:PRK12444 165 EAIpSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 240 RDHRRIGRELDLFTMRDEGPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMYFTK 319
Cdd:PRK12444 245 RNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFSE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 320 IDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCLPEQVKDEVFKMI 399
Cdd:PRK12444 325 VDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSVM 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 400 DLAELLYSTFGFKYEIELSTRPDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDFHLEDAIGRTWQCGT 479
Cdd:PRK12444 405 AQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCGT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 480 IQLDFQMPENFELTYINADGEKARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAPVQVEIIPVSEKFH-DYAEEVKNK 558
Cdd:PRK12444 485 IQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVHvQYADEVADK 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519540504 559 LKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMKEEVKEKK 633
Cdd:PRK12444 565 LAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIKNRK 639
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
72-629 |
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: 726.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 72 WHTSAHVLAHAIMNLWPETKFAIGPAIDNGFYYDIDLEHKIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKAIEFFKeR 151
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 152 GQDYKVELIEGIEDKN-VGIYKMGN-FVDLCRGPHIGNVKIIKAFKLLSIAGAYWRGDSNNKMLQRIYGISFEKKKQLDE 229
Cdd:TIGR00418 80 LEPYKLELLDEIPNGVkRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 230 YIERMEEAEKRDHRRIGRELDLFTMRDE-GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHW 308
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEiGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 309 DHYKDNMY-FTKIDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCL 387
Cdd:TIGR00418 240 DNYKERMFpFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 388 PEQVKDEVFKMIDLAELLYSTFGFKYE-IELSTR-PDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDF 465
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDkYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 466 HLEDAIGRTWQCGTIQLDFQMPENFELTYINADGEKARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAPVQVEIIPVS 545
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 546 EKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQM 625
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEKL 559
|
....
gi 2519540504 626 KEEV 629
Cdd:TIGR00418 560 RKEV 563
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
2-633 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 720.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 2 MKISFPDGSSKEFEKGIKV-YDVAKSISEGLARNALGAMVNDEVLGINDPINCDAEVKILTFEDKEGKKIFWHTSAHVLA 80
Cdd:PLN02908 52 IKVTLPDGAVKDGKKWVTTpMDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 81 HAIMNLWpETKFAIGPAIDN--GFYYDIDLEHK-IVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKAIEFFKErgQDYKV 157
Cdd:PLN02908 132 EALELEY-GCKLCIGPCTTRgeGFYYDAFYGDRtLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSE--NKFKV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 158 ELIEGI-EDKNVGIYKMGNFVDLCRGPHIGNVKIIKAFKLLSIAGAYWRGDSNNKMLQRIYGISFEKKKQLDEYIERMEE 236
Cdd:PLN02908 209 EIINDLpEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 237 AEKRDHRRIGRELDLFTMRDEGPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMY 316
Cdd:PLN02908 289 AKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 317 FTKIDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCLPEQVKDEVF 396
Cdd:PLN02908 369 VFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 397 KMIDLAELLYSTFGFKYEIELSTRPDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDFHLEDAIGRTWQ 476
Cdd:PLN02908 449 GVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 477 CGTIQLDFQMPENFELTYINADGEK-ARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAPVQVEIIPVSEKFHDYAEEV 555
Cdd:PLN02908 529 CATVQLDFQLPIRFKLSYSAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEV 608
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519540504 556 KNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMKEEVKEKK 633
Cdd:PLN02908 609 RAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
73-632 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 615.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 73 HTSAHVLAHAIMNLWPETKFAIGPAIDNGFYYDIDLEhKIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKAIEFFKERG 152
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDME-PLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAIN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 153 QDYKVELIEGIEDKNVGIYKMGN-FVDLCRGPHIGNVKII--KAFKLLSIAGAYWRGDSNNKMLQRIYGISFEKKKQLDE 229
Cdd:PLN02837 127 EPYKLEILEGIKEEPITIYHIGEeWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 230 YIERMEEAEKRDHRRIGRELDLFTMRDE-GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHW 308
Cdd:PLN02837 207 YLHFKEEAKRRDHRRLGQDLDLFSIQDDaGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 309 DHYKDNMYFT-KIDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCL 387
Cdd:PLN02837 287 DFYKENMYDQmDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 388 PEQVKDEVFKMIDLAELLYSTFGF-KYEIELSTRPDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDFH 466
Cdd:PLN02837 367 EDQIKDEIRGVLDLTEEILKQFGFsKYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 467 LEDAIGRTWQCGTIQLDFQMPENFELTYINADGEKARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAPVQVEIIPVSE 546
Cdd:PLN02837 447 IEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTD 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 547 KFHDYAEEVKNKLKESGFRVEMdTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMK 626
Cdd:PLN02837 527 NELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQ 605
|
....*.
gi 2519540504 627 EEVKEK 632
Cdd:PLN02837 606 LAVENR 611
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
241-536 |
3.62e-172 |
|
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: 491.68 E-value: 3.62e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 241 DHRRIGRELDLFTMRDE-GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMYFTK 319
Cdd:cd00771 1 DHRRLGGELELFFFFDEaGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 320 IDGEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCLPEQVKDEVFKMI 399
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 400 DLAELLYSTFGFK-YEIELSTRPDDFMGTIEAWNIAEKNLKDALEERGLKYTINEGDGAFYGPKIDFHLEDAIGRTWQCG 478
Cdd:cd00771 161 DLIKEVYSDFGFFdYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519540504 479 TIQLDFQMPENFELTYINADGEKARPVMLHRALLGSIERFMGILIEHFAGKFPLWLAP 536
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
264-630 |
6.36e-61 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 213.58 E-value: 6.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 264 FLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNeaLWHRS--GHWDHYKDNMYFTKIDGEDYAVKPMNCPGSILVYEE 341
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYD--LSHPAirEHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 342 KAHSYRDLPIRLSEFGQV-HRHELSGALHGLFRVRTFTQDDAHVYCLP-EQVKDEVFKMIDLAELLYSTFGFKYEIELS- 418
Cdd:PRK03991 300 MTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDYEVAIRf 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 419 TRpdDFMGTIEAW--NIAEKNLKDALEErglkyTINEGDGAFYGpKIDFHLEDAIGRTWQCGTIQLDFQMPENFELTYIN 496
Cdd:PRK03991 380 TE--DFYEENKDWivELVKREGKPVLLE-----ILPERKHYWVL-KVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVD 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 497 ADGEKARPVMLHRALLGSIERFM-GIL----IEHFAGK---FPLWLAPVQVEIIPVSEKFHDYAEEVKNKLKESGFRVEM 568
Cdd:PRK03991 452 ENGEEKYPIILHCSPTGSIERVIyALLekaaKEEEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDV 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519540504 569 DTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMKEEVK 630
Cdd:PRK03991 532 DDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
322-526 |
4.87e-45 |
|
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: 158.34 E-value: 4.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 322 GEDYAVKPMNCPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSGALHGLFRVRTFTQDDAHVYCLPEQVKDEVFKMIDL 401
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 402 AELLYSTFGFK-YEIELSTRPddfmgtieawniaeknlkdaleerglkytinegDGAFYGPKIDFHLEDAI-GRTWQCGT 479
Cdd:pfam00587 88 IDRVYSRLGLEvRVVRLSNSD---------------------------------GSAFYGPKLDFEVVFPSlGKQRQTGT 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2519540504 480 IQLD-FQMPENFELTYINADGEKARPVMLHRALLGsIERFMGILIEHF 526
Cdd:pfam00587 135 IQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
536-626 |
6.96e-38 |
|
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: 135.32 E-value: 6.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 536 PVQVEIIPVSEKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKD 615
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 2519540504 616 VKIEDFISQMK 626
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| 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 ... |
271-523 |
3.97e-36 |
|
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: 135.60 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 271 LKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMYFTK-----IDGEDYAVKPMNCPGSILVYEEKAHS 345
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEdkgreLRDTDLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 346 YRDLPIRLSEFGQVHRHELSGAlHGLFRVRTFTQDDAHVYCLPEQVKDEVFKMIDLAELLYSTFGFKYEIELSTRPDDFM 425
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPFFGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 426 GTieawniaeknlkdaleerglkytiNEGDGAFYGPKIDFHLEDAI-GRTWQCGTIQLDFQMPENFELTYINADGEKARP 504
Cdd:cd00670 163 GG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGGRAH 218
|
250
....*....|....*....
gi 2519540504 505 VMLHRAllGSIERFMGILI 523
Cdd:cd00670 219 TGCGGA--GGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
538-628 |
6.29e-24 |
|
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: 96.12 E-value: 6.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 538 QVEIIPVSEK---FHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVK 614
Cdd:pfam03129 1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 2519540504 615 DVKIEDFISQMKEE 628
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
271-518 |
6.75e-24 |
|
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: 99.88 E-value: 6.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 271 LKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWdhYKDNMYFTKIDGEDYAVKPMNCPGsiLVYEEKAHSyRDLP 350
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPG--LVRLFVSHI-RKLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 351 IRLSEFGQVHRHELSGAlhGLFRVRTFTQDDAHVYCLPEQVKDEVFKMIDLAELLYSTFGFKyeielstrpDDFMgtiea 430
Cdd:cd00768 76 LRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIK---------LDIV----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 431 wniaeknlkdaleeRGLKYTINEGDGaFYGPKIDFHLEDAIGRTWQCGTIQLDFQMPEN-FELTYINADGEKARPVMLHR 509
Cdd:cd00768 140 --------------FVEKTPGEFSPG-GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGF 204
|
....*....
gi 2519540504 510 ALlgSIERF 518
Cdd:cd00768 205 GL--GLERL 211
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
2-66 |
7.28e-23 |
|
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: 92.17 E-value: 7.28e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519540504 2 MKISFPDGSSKEFEKGIKVYDVAKSISEGLARNALGAMVNDEVLGINDPINCDAEVKILTFEDKE 66
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
531-632 |
5.46e-17 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 83.36 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 531 PLWLAPVQVEIIPVSEKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSG 610
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRAN 348
|
90 100
....*....|....*....|....
gi 2519540504 611 EEVKDVKIEDFISQMK--EEVKEK 632
Cdd:PRK14938 349 NEQKSMTVEELVKEIKraDELKER 372
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
536-612 |
3.45e-14 |
|
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: 68.58 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 536 PVQVEIIPVSEKFH---DYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEE 612
Cdd:cd00738 1 PIDVAIVPLTDPRVearEYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
168-216 |
2.85e-13 |
|
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: 64.33 E-value: 2.85e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2519540504 168 VGIYKMGNF-VDLCRGPHIGNVKIIKAFKLLSIAGAYWRgdsnnkmLQRI 216
Cdd:smart00863 1 VRVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
260-631 |
1.44e-12 |
|
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: 69.77 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 260 GFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMY-FTKIDGEDYAVKPMNCPGSILV 338
Cdd:COG0124 9 GTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEKEMYtFEDRGGRSLTLRPEGTAPVARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 339 YEEKAHsYRDLPIRLSEFGQVHRHELSGAlhGlfRVRTFTQDDAhvyclpeqvkdEVF---------KMIDLAELLYSTF 409
Cdd:COG0124 89 VAEHGN-ELPFPFKLYYIGPVFRYERPQK--G--RYRQFHQFGV-----------EVIgsdspladaEVIALAADLLKAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 410 GFK-YEIELST------RPDDFMGTIEAWNI--AEKNLKDALEERGLKYTI-------NEGDGAFYG--PKI-DF----- 465
Cdd:COG0124 153 GLKdFTLEINSrglpeeRAEALLRYLDKLDKigHEDVLDEDSQRRLETNPLraildskGPDCQEVLAdaPKLlDYlgeeg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 466 --HLE------DAIGRTWQ------------CGTIqldfqmpenFELTyinADGEKArpvmlhralLGSI---------- 515
Cdd:COG0124 233 laHFEevlellDALGIPYVidprlvrgldyyTGTV---------FEIV---TDGLGA---------QGSVcgggrydglv 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 516 ERF-----------MGI-----LIEHfAGKFPLWLAPVQVEIIPVSEKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKI 579
Cdd:COG0124 292 EQLggpptpavgfaIGLerlllLLEE-LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQL 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2519540504 580 RQAQLRKVNYMLVIGEQEVESGLLSIRK-RSGEEVKdVKIEDFISQMKEEVKE 631
Cdd:COG0124 371 KYADKSGAPFVLILGEDELANGTVTLKDlATGEQET-VPLDELVEYLKELLAE 422
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
232-415 |
4.11e-12 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 67.20 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 232 ERMEEAEKRDHRRIGRELDLFTMRD----EGPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGH 307
Cdd:cd00770 11 PRVFDFKPKDHVELGEKLDILDFERgakvSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 308 WDHYKDNMYftKIDGEDYAVKPM-NCPGSILVYEEkAHSYRDLPIRLSEFGQVHRHELSGA---LHGLFRVRTFTQDDAH 383
Cdd:cd00770 91 LPKFDEQLY--KVEGEDLYLIATaEVPLAALHRDE-ILEEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRVHQFEKVEQF 167
|
170 180 190
....*....|....*....|....*....|..
gi 2519540504 384 VYCLPEQVKDEVFKMIDLAELLYSTFGFKYEI 415
Cdd:cd00770 168 VFTKPEESWEELEELISNAEEILQELGLPYRV 199
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
168-216 |
4.59e-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: 4.59e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2519540504 168 VGIYKMGN-FVDLCRGPHIGNVKIIKAFKLLsiagaywRGDSNNKMLQRI 216
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
2-61 |
1.38e-11 |
|
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: 59.87 E-value: 1.38e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 2 MKISFPDGSSKEFEKGIKVYDVAKSISEGLARNALGAMVNDEVLGINDPINCDAEVKILT 61
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
488-630 |
6.35e-11 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 65.11 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 488 ENFELTYINADGEKARPVMlhrallGS----IERFMGILIEHFAGK----FPLWLAPVQVEIIPVSEKFHD---YAEEVK 556
Cdd:PRK09194 418 EAMNATVLDENGKAQPLIM------GCygigVSRLVAAAIEQNHDEkgiiWPKAIAPFDVHIVPVNMKDEEvkeLAEKLY 491
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519540504 557 NKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEEVKDVKIEDFISQMKEEVK 630
Cdd:PRK09194 492 AELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
536-626 |
6.51e-11 |
|
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: 59.09 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 536 PVQVEIIPVSEKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRK-RSGEEVk 614
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDlETGEQE- 79
|
90
....*....|..
gi 2519540504 615 DVKIEDFISQMK 626
Cdd:cd00859 80 TVALDELVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
535-631 |
2.77e-10 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. 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, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 60.39 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 535 APVQVEIIPV------SEKFHDYAEEVKNKLKESGFRVEMDTRAEKV-GYKIRQAQLRKVNYMLVIGEQEVESGLLSIRK 607
Cdd:cd00862 9 APIQVVIVPIgikdekREEVLEAADELAERLKAAGIRVHVDDRDNYTpGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100
....*....|....*....|....
gi 2519540504 608 RSGEEVKDVKIEDFISQMKEEVKE 631
Cdd:cd00862 89 RDTGEKKTVPLAELVEKVPELLDE 112
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
240-431 |
3.38e-10 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 62.63 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 240 RDHRRIGRELDLFTMRD----EGPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGhWDHYKDNM 315
Cdd:PLN02320 200 KDHLQLGKELDLFDFDAaaevSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCG-FQPRGDNT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 316 YFTKIDGEDYA-VKPMNCP-GSILVYEEKAHSyrDLPIRLSEFGQVHRHELSGA---LHGLFRVRTFTQDDAHVYCLPEQ 390
Cdd:PLN02320 279 QVYSIDGSDQClIGTAEIPvGGIHMDSILLES--ALPLKYVAFSHCFRTEAGAAgaaTRGLYRVHQFSKVEMFVICRPEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2519540504 391 VKDEVFKMIDLAELLYSTFGFKYE-IELST----RPDDFMGTIEAW 431
Cdd:PLN02320 357 SESFHEELIQIEEDLFTSLGLHFKtLDMATadlgAPAYRKFDIEAW 402
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
536-626 |
6.04e-10 |
|
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: 56.44 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 536 PVQVEIIPV---SEKFHDYAEEVKNKLKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRKRSGEE 612
Cdd:cd00861 1 PFDVVIIPMnmkDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|....
gi 2519540504 613 VKDVKIEDFISQMK 626
Cdd:cd00861 81 KEEISIDELLEFLQ 94
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
73-195 |
2.41e-08 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 55.20 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 73 HTSAHVLAHAIMNL--WPETKFAIGPaiDNGfYYDIDLEHkIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDkaiEFFKE 150
Cdd:COG2872 100 HTALHLLSAVVYREygAPVTGGQIGE--DRA-RIDFDLPE-FDEEDLEEIEAEANELIAADLPVRIYWITRE---ELEAI 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2519540504 151 ------------RGQDyKVELIEgIEDknvgiykmgnfVDL--CRGPH------IGNVKIIKAFK 195
Cdd:COG2872 173 pglvrtmsvlppPGVG-RVRIVE-IGG-----------VDLqpCGGTHvantgeIGRIKITKIEK 224
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
529-630 |
3.77e-06 |
|
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: 46.40 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 529 KFPLWLAPVQVEIIPVS--EKFHDYAEEVKNKLKESGFRVEMDT---------RAEKVGykirqaqlrkVNYMLVIGEQE 597
Cdd:cd00858 19 RLPPALAPIKVAVLPLVkrDELVEIAKEISEELRELGFSVKYDDsgsigrryaRQDEIG----------TPFCVTVDFDT 88
|
90 100 110
....*....|....*....|....*....|...
gi 2519540504 598 VESGLLSIRKRSGEEVKDVKIEDFISQMKEEVK 630
Cdd:cd00858 89 LEDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
258-426 |
1.79e-05 |
|
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: 46.98 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 258 GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHY--KDNMYFTKIDGE----DYAVKPMN 331
Cdd:cd00772 21 GRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGfsKELAVFKDAGDEeleeDFALRPTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 332 CPGSILVYEEKAHSYRDLPIRLSEFGQVHRHELSgALHGLFRVRTFTQDDAH-VYCLPEQVKDEVFKMIDL-AELLYSTF 409
Cdd:cd00772 101 EENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHsAHADAEEADEEFLNMLSAyAEIARDLA 179
|
170
....*....|....*..
gi 2519540504 410 GFKYEIELSTRPDDFMG 426
Cdd:cd00772 180 AIDFIEGEADEGAKFAG 196
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
559-619 |
6.77e-05 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 45.88 E-value: 6.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519540504 559 LKESGFRVEMDTRAEKVGYKIRQAQLRKVNYMLVIGEQEVESGLLSIRK-RSGEEVKdVKIE 619
Cdd:PRK12420 360 RSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNmKEGSEVK-VPLS 420
|
|
| PLN02900 |
PLN02900 |
alanyl-tRNA synthetase |
73-201 |
1.93e-04 |
|
alanyl-tRNA synthetase
Pssm-ID: 215487 [Multi-domain] Cd Length: 936 Bit Score: 44.62 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 73 HTSAHVLAHAImnlwpetKFAIGPAID--------NGFYYDIDLEHKIVPEDLPKIEEEMQKIVKDAHEVTFETMPRDKA 144
Cdd:PLN02900 598 HTATHLLNSAL-------KEVLGDHVDqkgslvafEKLRFDFSHGKPMTPEELREVESLVNEWIGDALPVEAKEMPLADA 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2519540504 145 ------IEFFKERGQDyKVELIEgiedknVG-IYKMgnfvDLCRGPHIGNVKIIKAFKLLSIAG 201
Cdd:PLN02900 671 kringlRAVFGEKYPD-PVRVVS------VGgVYSM----ELCGGTHVSNTAEAEAFKLLSEEG 723
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
258-382 |
3.44e-04 |
|
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: 42.56 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 258 GPGFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNMY-FTKIDGEDYAVKPMNcpgsi 336
Cdd:cd00779 20 SSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLrLKDRHGKEFLLGPTH----- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2519540504 337 lvyEE--------KAHSYRDLPIRLSEFGQVHRHELSgALHGLFRVRTFTQDDA 382
Cdd:cd00779 95 ---EEvitdlvanEIKSYKQLPLNLYQIQTKFRDEIR-PRFGLMRGREFLMKDA 144
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
275-452 |
3.46e-04 |
|
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: 42.97 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 275 LLNWWRNVLLEN----GYGEIQTPIILNEALWHRSGHWDHYKdNMY-FTKIDGEDYAVKPMNCPGSILVYEEKaHSYRDL 349
Cdd:cd00773 4 LRRYIEDTLREVferyGYEEIDTPVFEYTELFLRKSGDEVSK-EMYrFKDKGGRDLALRPDLTAPVARAVAEN-LLSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 350 PIRLSEFGQVHRHELSGALhglfRVRTFTQDDAHVYCLPEQVKD-EVFKMIDlaELLYSTFGFKYEIELSTR-------- 420
Cdd:cd00773 82 PLKLYYIGPVFRYERPQKG----RYREFYQVGVEIIGSDSPLADaEVIALAV--EILEALGLKDFQIKINHRgildgiag 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2519540504 421 --PDDFMGTIEAWNIAEK-------NLKDALEERGL--KYTIN 452
Cdd:cd00773 156 llEDREEYIERLIDKLDKealahleKLLDYLEALGVdiKYSID 198
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
254-523 |
6.40e-04 |
|
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: 41.81 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 254 MRDEGP--GFPFFLPHGMILKNTLLNWWRNVLLENGYGEIQTPIILNEALWHR-SGHWDHYKDNMYF-TKIDGED----Y 325
Cdd:cd00778 15 LIDYGPvkGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKeKEHIEGFAPEVAWvTHGGLEEleepL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 326 AVKPMN----CPgsilVYEEKAHSYRDLPIRLSEFGQVHRHELSgALHGLFRVRTFTQDDAH-VYCLPEQVKDEVFKMID 400
Cdd:cd00778 95 ALRPTSetaiYP----MFSKWIRSYRDLPLKINQWVNVFRWETK-TTRPFLRTREFLWQEGHtAHATEEEAEEEVLQILD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519540504 401 LAELLYSTF-GFKYEIELSTRPDDFMgtieawniaeknlkdaleerglkytinegdGAFYGPKIDFHLEDaiGRTWQCGT 479
Cdd:cd00778 170 LYKEFYEDLlAIPVVKGRKTEWEKFA------------------------------GADYTYTIEAMMPD--GRALQSGT 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2519540504 480 I-QLDFQMPENFELTYINADGEKARPvmlHRALLGSIERFMGILI 523
Cdd:cd00778 218 ShNLGQNFSKAFDIKYQDKDGQKEYV---HQTSWGISTRLIGAII 259
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
266-315 |
1.04e-03 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 42.04 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2519540504 266 PHGMILKNTLLN-WWR-NVLLENGYGEIQTPIILNEALWHRSGHWDHYKDNM 315
Cdd:PRK04173 35 PLGVELKNNIKRaWWKsFVQEREDVVGIDSPIIMPPEVWEASGHVDNFSDPL 86
|
|
| |
