|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
1-643 |
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: 1244.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 1 MIHITLPDGSQREYPGPVTVAEVAASIGTGLAKAALAGKVgtgdDAKVVDTSFVINKDMPLSIVTAKDADGLDVIRHSTA 80
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKV----NGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 81 HLLAYAVKDLFPDAQVTIGPVIENGFYYDFSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYFKGIGENYK 160
Cdd:COG0441 77 HLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEKGEPYK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 161 AEIIASIPSNEDVSLYREGSFEDLCRGPHVPSTGKLKFFKLMKVAGAYWRGDHRNEMLQRVYGTAWASKDDLQQYLHMLE 240
Cdd:COG0441 157 VELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 241 EAEKRDHRKLGRELDLFHI-DEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYREN 319
Cdd:COG0441 237 EAKKRDHRKLGKELDLFHFqEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYREN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 320 MFTTESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQPE 399
Cdd:COG0441 317 MFPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 400 VLAFTTLLQKVYADFGFSDIIYKVATRPEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEYTLKDAIGR 479
Cdd:COG0441 397 IKKVIDLVLEVYKDFGFEDYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 480 QWQCGTIQVDFSMPERLDAEYVGEDGDRHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAPVQAAVLNITDAQADYVR 559
Cdd:COG0441 477 EWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 560 EVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDAFIELVAKDI 639
Cdd:COG0441 557 EVAKKLRAA----GIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEI 632
|
....
gi 238687213 640 AAKA 643
Cdd:COG0441 633 RSRS 636
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-639 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 773.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 1 MIHITLPDGSQREYPGPVTVAEVAASIGTGLAKAALAGKVgtgdDAKVVDTSFVINKDMPLSIVTAKDADGLDVIRHSTA 80
Cdd:PRK12444 5 MIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKV----NDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 81 HLLAYAVKDLFPDAQVTIGPVIENGFYYDFSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYFKGIGENYK 160
Cdd:PRK12444 81 HILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 161 AEIIASIPSNEDVSLYREGSFEDLCRGPHVPSTGKLKFFKLMKVAGAYWRGDHRNEMLQRVYGTAWASKDDLQQYLHMLE 240
Cdd:PRK12444 161 LELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 241 EAEKRDHRKLGRELDLFHIDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENM 320
Cdd:PRK12444 241 EAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 321 FTTESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQPEV 400
Cdd:PRK12444 321 YFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 401 LAFTTLLQKVYADFGFSdiiYKVA--TRPEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEYTLKDAIG 478
Cdd:PRK12444 401 KSVMAQIDYVYKTFGFE---YEVElsTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 479 RQWQCGTIQVDFSMPERLDAEYVGEDGDRHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAPVQAAVLNITDA-QADY 557
Cdd:PRK12444 478 RSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQY 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 558 VREVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDAFIELVAK 637
Cdd:PRK12444 558 ADEVADKLAQA----GIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
..
gi 238687213 638 DI 639
Cdd:PRK12444 634 EI 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
76-639 |
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: 760.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 76 RHSTAHLLAYAVKDLFPDAQVTIGPVIENGFYYDFSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYFKgI 155
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 156 GENYKAEIIASIPSNEDVSLYREG-SFEDLCRGPHVPSTGKLKFFKLMKVAGAYWRGDHRNEMLQRVYGTAWASKDDLQQ 234
Cdd:TIGR00418 80 LEPYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 235 YLHMLEEAEKRDHRKLGRELDLFHIDEHS-PGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHW 313
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 314 DKYRENMF-TTESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCT 392
Cdd:TIGR00418 240 DNYKERMFpFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 393 EDQIQPEVLAFTTLLQKVYADFGFSDIIYKVATR-PEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEY 471
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 472 TLKDAIGRQWQCGTIQVDFSMPERLDAEYVGEDGDRHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAPVQAAVLNIT 551
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 552 DAQADYVREVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDAF 631
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKA----GIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEF 555
|
....*...
gi 238687213 632 IELVAKDI 639
Cdd:TIGR00418 556 LEKLRKEV 563
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
2-642 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 612.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 2 IHITLPDGSQREYPGPVTVA-EVAASIGTGLAKAALAGKVgtgdDAKVVDTSFVINKDMPLSIVTAKDADGLDVIRHSTA 80
Cdd:PLN02908 52 IKVTLPDGAVKDGKKWVTTPmDIAKEISKGLANSALIAQV----DGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 81 HLLAYAVKDLFpDAQVTIGPVIEN--GFYYD-FSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYFKGigE 157
Cdd:PLN02908 128 HILGEALELEY-GCKLCIGPCTTRgeGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSE--N 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 158 NYKAEIIASIPSNEDVSLYREGSFEDLCRGPHVPSTGKLKFFKLMKVAGAYWRGDHRNEMLQRVYGTAWASKDDLQQYLH 237
Cdd:PLN02908 205 KFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 238 MLEEAEKRDHRKLGRELDLFHIDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYR 317
Cdd:PLN02908 285 RIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 318 ENMFTTESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQ 397
Cdd:PLN02908 365 ENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 398 PEVLAFTTLLQKVYADFGFsDIIYKVATRPEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEYTLKDAI 477
Cdd:PLN02908 445 DEVKGVLDFLDYVYEVFGF-TYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDAL 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 478 GRQWQCGTIQVDFSMPERLDAEYVGEDG-DRHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAPVQAAVLNITDAQAD 556
Cdd:PLN02908 524 KRKFQCATVQLDFQLPIRFKLSYSAEDEaKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQD 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 557 YVREVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDAFIELVA 636
Cdd:PLN02908 604 YAEEVRAQLHAA----GFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFK 679
|
....*.
gi 238687213 637 KDIAAK 642
Cdd:PLN02908 680 EERAEF 685
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
32-643 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 594.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 32 AKAALAGKVGTGDDAKVVDTSFVINKDMPLSIVTAKDADGLDVIRHSTAHLLAYAVKDLFPDAQVTIGPVIENGFYYDFS 111
Cdd:PLN02837 3 AAAASAATEEASAAAASDEKGPGEAEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 112 yKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYFKGIGENYKAEIIASIPSnEDVSLYREGS-FEDLCRGPHV 190
Cdd:PLN02837 83 -MEPLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAINEPYKLEILEGIKE-EPITIYHIGEeWWDLCAGPHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 191 PSTGKL--KFFKLMKVAGAYWRGDHRNEMLQRVYGTAWASKDDLQQYLHMLEEAEKRDHRKLGRELDLFHI-DEHSPGTV 267
Cdd:PLN02837 161 ERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIqDDAGGGLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 268 FWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENMFTT-ESEKRDYALKPMNCPGHILIFKQ 346
Cdd:PLN02837 241 FWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQmDIEDELYQLRPMNCPYHILVYKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 347 GIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQPEVLAFTTLLQKVYADFGFSDIIYKVATR 426
Cdd:PLN02837 321 KLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 427 PEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEYTLKDAIGRQWQCGTIQVDFSMPERLDAEYVGEDGD 506
Cdd:PLN02837 401 PEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 507 RHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAPVQAAVLNITDAQADYVREVAQKLQKafpnQGLRVATdLRNEKIT 586
Cdd:PLN02837 481 KKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKA----KGIRAEV-CHGERLP 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 238687213 587 YKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDAFIELVAKDIAAKA 643
Cdd:PLN02837 556 KLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVENRT 612
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
245-542 |
1.70e-178 |
|
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: 507.86 E-value: 1.70e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 245 RDHRKLGRELDLFHIDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENMFTTE 324
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 325 SEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQPEVLAFT 404
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 405 TLLQKVYADFGFSDIIYKVATRPEARIGSDESWDKAEAALINSLEASGCEYVISPGDGAFYGPKIEYTLKDAIGRQWQCG 484
Cdd:cd00771 161 DLIKEVYSDFGFFDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 238687213 485 TIQVDFSMPERLDAEYVGEDGDRHRPVMLHRAIVGSLERFIGILIEQHAGAMPTWLAP 542
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
321-532 |
7.20e-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: 163.35 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 321 FTTESE-KRDYALKPMNCPGHILIF-KQGIKSYrDLPLRYGEFGQCHRNEPTGGLHGIMRVRGFTQDDGHVFCTEDQIQP 398
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSK-DLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 399 EVLAFTTLLQKVYADFGFSDIIYKVATRPEarigsdeswdkaeaalinsleasgceyvispgdGAFYGPKIEYTLKDAI- 477
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVRVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 238687213 478 GRQWQCGTIQVD-FSMPERLDAEYVGEDGDRHRPVMLHRAIVGsLERFIGILIEQH 532
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-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 ... |
273-529 |
9.19e-46 |
|
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: 162.18 E-value: 9.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 273 GWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENMFTTESEKR-----DYALKPMNCPGHILIFKQG 347
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 348 IKSYRDLPLRYGEFGQCHRNEPtGGLHGIMRVRGFTQDDGHVFCTEDQIQPEVLAFTTLLQKVYADFGFsDIIYKVATRP 427
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEP-SGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PVRVVVADDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 428 EARIGSDEswdkaeaalinsleasgceyvispGDGAFYGPKIEYTLKDAI-GRQWQCGTIQVDFSMPERLDAEYVGEDGD 506
Cdd:cd00670 159 FFGRGGKR------------------------GLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGG 214
|
250 260
....*....|....*....|...
gi 238687213 507 RHRPVMLHRAivGSLERFIGILI 529
Cdd:cd00670 215 GRAHTGCGGA--GGEERLVLALL 235
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
247-642 |
1.19e-43 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 165.81 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 247 HRKLGRELDLFHIDEHS-PGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILD---KTLWEktgHWDKYRENMFT 322
Cdd:PRK03991 199 HVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDlshPAIRE---HADKFGERQYR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 323 TESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQC-HRNEPTGGLHGIMRVRGFTQDDGHVFCTE-DQIQPEV 400
Cdd:PRK03991 276 VKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEF 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 401 LAFTTLLQKVYADFGfsdIIYKVATRpeariGSDESWDKAEAALINSLEASGCEYVISPGDGAFY--GPKIEYTLKDAIG 478
Cdd:PRK03991 356 EKQYEMILETGEDLG---RDYEVAIR-----FTEDFYEENKDWIVELVKREGKPVLLEILPERKHywVLKVEFAFIDSLG 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 479 RQWQCGTIQVDFSMPERLDAEYVGEDGDRHRPVMLHRAIVGSLERFIGILIEQHAGAM--------PTWLAPVQAAVLNI 550
Cdd:PRK03991 428 RPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAAKEEeegkvpmlPTWLSPTQVRVIPV 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 551 TDAQADYVREVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDLGVMSVDA 630
Cdd:PRK03991 508 SERHLDYAEEVADKLEAA----GIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEE 583
|
410
....*....|..
gi 238687213 631 FIELVAKDIAAK 642
Cdd:PRK03991 584 LIERIKEETKGY 595
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
276-524 |
1.85e-33 |
|
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: 127.23 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 276 LWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRenMFTTESEKRDYALKPMNCPGHILIFKQGIksyRDLP 355
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDL--LPVGAENEEDLYLRPTLEPGLVRLFVSHI---RKLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 356 LRYGEFGQCHRNEPTGglHGIMRVRGFTQDDGHVFCTEDQIQPEVLAFTTLLQKVYADFGFS-DIIYKVATRPEARIGsd 434
Cdd:cd00768 76 LRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKlDIVFVEKTPGEFSPG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 435 eswdkaeaalinsleasgceyvispgdgaFYGPKIEYTLKDAIGRQWQCGTIQVDFSMPERL-DAEYVGEDGDRHRPVML 513
Cdd:cd00768 152 -----------------------------GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARAaDLYFLDEALEYRYPPTI 202
|
250
....*....|.
gi 238687213 514 HRAIvgSLERF 524
Cdd:cd00768 203 GFGL--GLERL 211
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
542-635 |
4.02e-28 |
|
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: 107.97 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 542 PVQAAVLNITDAQADYVREVAQKLQKAfpnqGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNK 621
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDA----GIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGG 76
|
90
....*....|....
gi 238687213 622 DLGVMSVDAFIELV 635
Cdd:cd00860 77 DLGSMSLDEFIEKL 90
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
2-70 |
4.73e-19 |
|
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: 81.38 E-value: 4.73e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238687213 2 IHITLPDGSQREYPGPVTVAEVAASIGTGLAKAALAGKVgtgdDAKVVDTSFVINKDMPLSIVTAKDAD 70
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKV----NGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
173-221 |
1.54e-14 |
|
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: 67.79 E-value: 1.54e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 238687213 173 VSLYR-EGSFEDLCRGPHVPSTGKLKFFKLMKVAGAYWRgdhrnemLQRV 221
Cdd:smart00863 1 VRVVSiGDFSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-436 |
3.05e-13 |
|
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: 70.09 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 265 GTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKY--RENMFTT----ESEKRDYALKPMNCP 338
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGfsKELAVFKdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 339 GHILIFKQGIKSYRDLPLRYGEFGQCHRNEpTGGLHGIMRVRGFTQDDGHVF-CTEDQIQPEVLAFTTLLQKVYADFGFS 417
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDE-IRPRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLAAI 181
|
170
....*....|....*....
gi 238687213 418 DIIYKVATRPEARIGSDES 436
Cdd:cd00772 182 DFIEGEADEGAKFAGASKS 200
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
241-390 |
1.85e-12 |
|
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: 67.60 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 241 EAEKRDHRKLGReldLFHIDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENM 320
Cdd:cd00779 1 DAEIISHKLLLR---AGFIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPEL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238687213 321 F-TTESEKRDYALKPMNCPGHILIFKQGIKSYRDLPLRYGEFGQCHRNE--PTGGLhgiMRVRGFTQDDGHVF 390
Cdd:cd00779 78 LrLKDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEirPRFGL---MRGREFLMKDAYSF 147
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
544-637 |
3.86e-12 |
|
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: 62.60 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 544 QAAVLNITDAQADYVrEVAQKLQKAFPNQGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNKDL 623
Cdd:pfam03129 1 QVVVIPLGEKAEELE-EYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....
gi 238687213 624 GVMSVDAFIELVAK 637
Cdd:pfam03129 80 ETVSLDELVEKLKE 93
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
542-633 |
6.21e-12 |
|
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: 62.03 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 542 PVQAAVLNITDAQaDYVREVAQKLQKAFPNQGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKEKAAGAVAVRARGNK 621
Cdd:cd00738 1 PIDVAIVPLTDPR-VEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|..
gi 238687213 622 DLGVMSVDAFIE 633
Cdd:cd00738 80 ESETLHVDELPE 91
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
259-390 |
7.12e-12 |
|
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: 68.26 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 259 IDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENMFT-TESEKRDYALkpmnC 337
Cdd:COG0442 32 IRKLASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARvTDRLEREFCL----G 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 238687213 338 PGH---I-LIFKQGIKSYRDLPLRYGEFGQCHRNE--PTGGLhgiMRVRGFTQDDGHVF 390
Cdd:COG0442 108 PTHeevItDLVRNEIKSYRDLPLLLYQIQTKFRDEirPRFGL---LRTREFLMKDAYSF 163
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
173-221 |
1.24e-10 |
|
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: 56.68 E-value: 1.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 238687213 173 VSLYREGSFE-DLCRGPHVPSTGKLKFFKLMKvagaywrGDHRNEMLQRV 221
Cdd:pfam07973 1 VRVVSIGDFDvDLCGGTHVPNTGEIGAFKILK-------GESKNKGLRRI 43
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
261-529 |
1.70e-09 |
|
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: 59.15 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 261 EHSP--GTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTG-HWDKYRENMFT-----TESEKRDYAL 332
Cdd:cd00778 17 DYGPvkGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKeHIEGFAPEVAWvthggLEELEEPLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 333 KPMN----CPghilIFKQGIKSYRDLPLRYGEFGQCHRNEpTGGLHGIMRVRGFTQDDGH-VFCTEDQIQPEVLAFTtll 407
Cdd:cd00778 97 RPTSetaiYP----MFSKWIRSYRDLPLKINQWVNVFRWE-TKTTRPFLRTREFLWQEGHtAHATEEEAEEEVLQIL--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 408 qKVYADFgFSD---IIYKVATRPEarigsdesWDKaeaalinsleasgceyvispgdgaFYGPKIEYTLkDAI---GRQW 481
Cdd:cd00778 169 -DLYKEF-YEDllaIPVVKGRKTE--------WEK------------------------FAGADYTYTI-EAMmpdGRAL 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 238687213 482 QCGTIQ---VDFSmpERLDAEYVGEDGDRHRPvmlHRAIVGSLERFIGILI 529
Cdd:cd00778 214 QSGTSHnlgQNFS--KAFDIKYQDKDGQKEYV---HQTSWGISTRLIGAII 259
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
2-65 |
4.85e-09 |
|
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: 52.55 E-value: 4.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238687213 2 IHITLPDGSQREYPGPVTVAEVAASIGTGLAKAALAGKVgtgdDAKVVDTSFVINKDMPLSIVT 65
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKV----NGQLVGLDHPLEDGDVVEIVT 60
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
243-395 |
2.65e-08 |
|
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: 55.64 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 243 EKRDHRKLGRELDLFHIDE--HSPGTVFWHPKGWSLWQE--VEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRE 318
Cdd:cd00770 17 KPKDHVELGEKLDILDFERgaKVSGSRFYYLKGDGALLEraLINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKFDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 319 NMFTTESEkrDYALKP----------MNcpgHILifkqgikSYRDLPLRYGEFGQCHRNEptGGLH-----GIMRVRGFT 383
Cdd:cd00770 97 QLYKVEGE--DLYLIAtaevplaalhRD---EIL-------EEEELPLKYAGYSPCFRKE--AGSAgrdtrGLFRVHQFE 162
|
170
....*....|..
gi 238687213 384 QDDGHVFCTEDQ 395
Cdd:cd00770 163 KVEQFVFTKPEE 174
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
76-194 |
6.51e-08 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 54.04 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 76 RHSTAHLLAYAVKDLFpDAQVTIGPVIENGFYYDFSYKRpFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEAVAYfKGI 155
Cdd:COG2872 99 LHTALHLLSAVVYREY-GAPVTGGQIGEDRARIDFDLPE-FDEEDLEEIEAEANELIAADLPVRIYWITREELEAI-PGL 175
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 238687213 156 GenyKAEIIASIPSNEDVSLYREGSFeDL--CRGPHVPSTG 194
Cdd:COG2872 176 V---RTMSVLPPPGVGRVRIVEIGGV-DLqpCGGTHVANTG 212
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
77-203 |
1.02e-07 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 55.17 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 77 HSTAHLLAYAVKDLFPDAQVTIGPVI-ENGFYYDFSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDE-----AVA 150
Cdd:PRK01584 457 HTATHLLHKALRLVLGDHVRQKGSNItAERLRFDFSHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEarekgAMA 536
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 238687213 151 YFkgiGENYKaeiiasipsnEDVSLYREGSFE-DLCRGPHVPSTGKLKFFKLMK 203
Cdd:PRK01584 537 LF---GEKYE----------DIVKVYEIDGFSkEVCGGPHVENTGELGTFKIQK 577
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
259-606 |
1.43e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 54.09 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 259 IDEHSPGTVFWHPKGWSLWQEVEQYMRRVYRDNGYQEVKGPQILDKTLWEKTGHWDKYRENMF-TTESEKRDYALKPMNC 337
Cdd:PRK12325 32 IRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLrIKDRHDREMLYGPTNE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 338 PGHILIFKQGIKSYRDLPLR-YgefgqcH-----RNE--PTgglHGIMRVRGFTQDDGHVF--CTEDQIQPEVLAFTTLL 407
Cdd:PRK12325 112 EMITDIFRSYVKSYKDLPLNlY------HiqwkfRDEirPR---FGVMRGREFLMKDAYSFdlDEEGARHSYNRMFVAYL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 408 qKVYADFGFSDIIYKVATRPearIGSDESW------DKAEAALI---NSLEASGCEYVISPGDGAFYGPKIEYT------ 472
Cdd:PRK12325 183 -RTFARLGLKAIPMRADTGP---IGGDLSHefiilaETGESTVFydkDFLDLLVPGEDIDFDVADLQPIVDEWTslyaat 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 473 --LKDA------------------IGRQWQCGTiqvDFSMPerLDAEYVGEDGDRHRPVMlhraivGS----LERFIGIL 528
Cdd:PRK12325 259 eeMHDEaafaavpeerrlsargieVGHIFYFGT---KYSEP--MNAKVQGPDGKEVPVHM------GSygigVSRLVAAI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 529 IEQ-HAGAMPTW---LAPVQAAVLNI--TDAQADyvrEVAQKLQKAFPNQGLRVATDLRNEKITYKIREHSLQKLPYILV 602
Cdd:PRK12325 328 IEAsHDDKGIIWpesVAPFKVGIINLkqGDEACD---AACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQII 404
|
....
gi 238687213 603 AGDK 606
Cdd:PRK12325 405 VGPK 408
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
292-390 |
1.62e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 54.32 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 292 GYQEVKGPQILDKTLWEKTGHWDKYRENMFT-TESEKRDYALKPMncpgH----ILIFKQGIKSYRDLPLRygeFGQCH- 365
Cdd:PRK09194 65 GAQEVLMPALQPAELWQESGRWEEYGPELLRlKDRHGRDFVLGPT----HeeviTDLVRNEIKSYKQLPLN---LYQIQt 137
|
90 100
....*....|....*....|....*....
gi 238687213 366 --RNE--PTGGLhgiMRVRGFTQDDGHVF 390
Cdd:PRK09194 138 kfRDEirPRFGL---MRGREFIMKDAYSF 163
|
|
| AlaS |
COG0013 |
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ... |
109-201 |
4.14e-07 |
|
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: 53.14 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 109 DFSYKRPFTPEDLVAIEKRMAELAAKDEPVVRRVLPRDEA-----VAYFkgiGENYKAEI-IASIPsneDVSlyREgsfe 182
Cdd:COG0013 601 DFSHFEALTPEELAEIEDLVNEKIRENLPVETREMPLDEAkalgaMALF---GEKYGDEVrVVSIG---DFS--RE---- 668
|
90
....*....|....*....
gi 238687213 183 dLCRGPHVPSTGKLKFFKL 201
Cdd:COG0013 669 -LCGGTHVSRTGDIGLFKI 686
|
|
| PLN02900 |
PLN02900 |
alanyl-tRNA synthetase |
64-206 |
5.60e-07 |
|
alanyl-tRNA synthetase
Pssm-ID: 215487 [Multi-domain] Cd Length: 936 Bit Score: 53.09 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 64 VTAK-DADGLDVIR--HSTAHLLAYAVKDlfpdaqvTIGP--------VIENGFYYDFSYKRPFTPEDLVAIEKRMAELA 132
Cdd:PLN02900 582 VTCKvDYDRRRRIApnHTATHLLNSALKE-------VLGDhvdqkgslVAFEKLRFDFSHGKPMTPEELREVESLVNEWI 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 133 AKDEPVVRRVLPRDEA------VAYFkgiGENYKAEI-IASIPsnedvslyREGSFEdLCRGPHVPSTGKLKFFKLMKVA 205
Cdd:PLN02900 655 GDALPVEAKEMPLADAkringlRAVF---GEKYPDPVrVVSVG--------GVYSME-LCGGTHVSNTAEAEAFKLLSEE 722
|
.
gi 238687213 206 G 206
Cdd:PLN02900 723 G 723
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
529-607 |
2.14e-05 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 47.15 E-value: 2.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238687213 529 IEQHAGAMPTWLAPVQAAVLNITDAQADYVREVAQKLQKafpnQGLRVATDLRNEKITYKIREHSLQKLPYILVAGDKE 607
Cdd:PRK14938 261 IRKQPPTLPDWLNPIQVRILPVKKDFLDFSIQVAERLRK----EGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGERE 335
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
494-606 |
2.57e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 43.92 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 494 ERLDAEYVGEDGDRHRPVMlhraivGS----LERFIGILIEQHA---GAM-PTWLAPVQAAVL--NITDAQadyVREVAQ 563
Cdd:PRK09194 418 EAMNATVLDENGKAQPLIM------GCygigVSRLVAAAIEQNHdekGIIwPKAIAPFDVHIVpvNMKDEE---VKELAE 488
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 238687213 564 KLQKAFPNQGLRVATDLRNEKITYKIREHSLQKLPYILVAGDK 606
Cdd:PRK09194 489 KLYAELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDR 531
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
547-606 |
4.55e-04 |
|
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: 39.50 E-value: 4.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 547 VLNITDAQADyvrEVAQKLQKAFPNQGLRVATDLRNEKITYKIREHSLQKLPYILVAGDK 606
Cdd:cd00861 8 PMNMKDEVQQ---ELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKK 64
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
274-479 |
3.17e-03 |
|
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: 39.89 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 274 WSLWQEVEQYMRRVYRDNGYQEVKGPQI-LDKTLWEKTGhwDKYRENMFTTESEK-RDYALKPMNCPGHILIFKQgIKSY 351
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFeYTELFLRKSG--DEVSKEMYRFKDKGgRDLALRPDLTAPVARAVAE-NLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687213 352 RDLPLRYGEFGQCHRNEPTGGLhgimRVRGFTQDDGHVFcTEDQIQP--EVLAfttLLQKVYADFGFSDIIYKVATR--P 427
Cdd:cd00773 79 LPLPLKLYYIGPVFRYERPQKG----RYREFYQVGVEII-GSDSPLAdaEVIA---LAVEILEALGLKDFQIKINHRgiL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 238687213 428 EARIGSDESWDKAEAALINSLEASG-------CEYVispgdgAFYGPKIEYTLKDAIGR 479
Cdd:cd00773 151 DGIAGLLEDREEYIERLIDKLDKEAlahleklLDYL------EALGVDIKYSIDLSLVR 203
|
|
| |
