|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
3-645 |
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: 1165.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 3 QINIQFPDGNTKEFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIITPGSEEALEVLRHSTAHLMA 82
Cdd:COG0441 1 MIKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 83 QALKRLYGDVKFGVGPVIEGGFYYDFDMDDKVSSDDFDKIEKTMKQIVNENHKIVREVVSKEKAKDFFK--DDPYKLELI 160
Cdd:COG0441 81 QAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 161 DAIPEDESVTLYTQGEFTDLCRGVHVPSTSKIKEFKLLSTAGAYWRGNSDNKMLQRIYGTAFFDKKDLKAHLKMLEERRE 240
Cdd:COG0441 161 EDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 241 RDHRKIGKDLELFTNNQLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMFPa 320
Cdd:COG0441 241 RDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 321 MKLDeDEAMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFK 400
Cdd:COG0441 320 TESD-GEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 401 RVVNMIQDVYKDFGFEDYRFRLSYRdPEdkhKYFDDDEMWEKAESMLKEASDELGLTYEEAIGEAAFYGPKLDVQVKTAM 480
Cdd:COG0441 399 KVIDLVLEVYKDFGFEDYYVKLSTR-PE---KRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 481 GKEETLSTAQLDFLLPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPMQVEIIPVNiDLHYD 560
Cdd:COG0441 475 GREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPIS-DKHAD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 561 YARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEFIWNVIDEIR 640
Cdd:COG0441 554 YAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEIR 633
|
....*
gi 488370792 641 LKKHR 645
Cdd:COG0441 634 SRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
74-632 |
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: 822.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 74 RHSTAHLMAQALKRLYGDVKFGVGPVIEGGFYYDFDMDDKVSSDDFDKIEKTMKQIVNENHKIVREVVSKEKAKDFFK-D 152
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKvL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 153 DPYKLELIDAIPEDESVTLYTQGE-FTDLCRGVHVPSTSKIKEFKLLSTAGAYWRGNSDNKMLQRIYGTAFFDKKDLKAH 231
Cdd:TIGR00418 81 EPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 232 LKMLEERRERDHRKIGKDLELFTNNQLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWD 311
Cdd:TIGR00418 161 LLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 312 HYQEDMFPAMKLDEDEaMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVR 391
Cdd:TIGR00418 241 NYKERMFPFTELDNRE-FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 392 PDQIKEEFKRVVNMIQDVYKDFGFEDYRFRLSYRDPEDKhkyFDDDEMWEKAESMLKEASDELGLTYEEAIGEAAFYGPK 471
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDF---IGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 472 LDVQVKTAMGKEETLSTAQLDFLLPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPMQVEII 551
Cdd:TIGR00418 397 IDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 552 PVNiDLHYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEF 631
Cdd:TIGR00418 477 PVN-ERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEF 555
|
.
gi 488370792 632 I 632
Cdd:TIGR00418 556 L 556
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-643 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 807.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 1 MNQINIQFPDGNTKEFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIITPGSEEALEVLRHSTAHL 80
Cdd:PRK12444 3 EQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 81 MAQALKRLYGDVKFGVGPVIEGGFYYDFDMDDKVSSDDFDKIEKTMKQIVNENHKIVREVVSKEKAKDFFK--DDPYKLE 158
Cdd:PRK12444 83 LAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQemNDRLKLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 159 LIDAIPEDESVTLYTQGEFTDLCRGVHVPSTSKIKEFKLLSTAGAYWRGNSDNKMLQRIYGTAFFDKKDLKAHLKMLEER 238
Cdd:PRK12444 163 LLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 239 RERDHRKIGKDLELFTNNQlVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMF 318
Cdd:PRK12444 243 AKRNHRKLGKELELFMFSE-EAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 319 PAmKLDEDEaMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEE 398
Cdd:PRK12444 322 FS-EVDNKS-FALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 399 FKRVVNMIQDVYKDFGFEdYRFRLSYRdPEDKhkyFDDDEMWEKAESMLKEASDELGLTYEEAIGEAAFYGPKLDVQVKT 478
Cdd:PRK12444 400 IKSVMAQIDYVYKTFGFE-YEVELSTR-PEDS---MGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 479 AMGKEETLSTAQLDFLLPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPMQVEIIPVNIDLH 558
Cdd:PRK12444 475 ALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVH 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 559 YDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEFIWNVIDE 638
Cdd:PRK12444 555 VQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEE 634
|
....*
gi 488370792 639 IRLKK 643
Cdd:PRK12444 635 IKNRK 639
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
3-616 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 587.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 3 QINIQFPDGNTKEFDKGTTTE-DIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIITPGSEEALEVLRHSTAHLM 81
Cdd:PLN02908 51 PIKVTLPDGAVKDGKKWVTTPmDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHIL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 82 AQALKRLYGdVKFGVGPVIE--GGFYYD-FDMDDKVSSDDFDKIEKTMKQIVNENHKIVREVVSKEKAKDFFKDDPYKLE 158
Cdd:PLN02908 131 GEALELEYG-CKLCIGPCTTrgEGFYYDaFYGDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 159 LIDAIPEDESVTLYTQGEFTDLCRGVHVPSTSKIKEFKLLSTAGAYWRGNSDNKMLQRIYGTAFFDKKDLKAHLKMLEER 238
Cdd:PLN02908 210 IINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 239 RERDHRKIGKDLELFTNNQLvGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMF 318
Cdd:PLN02908 290 KKRDHRLLGQKQELFFFHEL-SPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 319 pamKLD-EDEAMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKE 397
Cdd:PLN02908 369 ---VFEiEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 398 EFKRVVNMIQDVYKDFGFeDYRFRLSYRdPEdkhKYFDDDEMWEKAESMLKEASDELGLTYEEAIGEAAFYGPKLDVQVK 477
Cdd:PLN02908 446 EVKGVLDFLDYVYEVFGF-TYELKLSTR-PE---KYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 478 TAMGKEETLSTAQLDFLLPERFDLTYIGQDGEQ-HRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAPMQVEIIPVNID 556
Cdd:PLN02908 521 DALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEK 600
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 557 lHYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVR 616
Cdd:PLN02908 601 -SQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVR 659
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
54-632 |
0e+00 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 537.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 54 EQDGAIEIITPGSEEALEVLRHSTAHLMAQALKRLYGDVKFGVGPVIEGGFYYDFDMDdKVSSDDFDKIEKTMKQIVNEN 133
Cdd:PLN02837 27 AEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDME-PLTDKDLKRIKKEMDRIISRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 134 HKIVREVVSKEKAKDFFK--DDPYKLELIDAIPEdESVTLYTQG-EFTDLCRGVHVPSTSKI--KEFKLLSTAGAYWRGN 208
Cdd:PLN02837 106 LPLVREEVSREEAQKRIMaiNEPYKLEILEGIKE-EPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 209 SDNKMLQRIYGTAFFDKKDLKAHLKMLEERRERDHRKIGKDLELFTNNQLVGAGLPLWLPNGATIRREIERYIVDKEVSM 288
Cdd:PLN02837 185 EKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 289 GYDHVYTPVLANVDLYKTSGHWDHYQEDMFPAMKLdEDEAMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEA 368
Cdd:PLN02837 265 GYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDI-EDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 369 SGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVVNMIQDVYKDFGFEDYRFRLSYRdPEdkhKYFDDDEMWEKAESMLK 448
Cdd:PLN02837 344 SGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTR-PE---KSVGSDDIWEKATTALR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 449 EASDELGLTYEEAIGEAAFYGPKLDVQVKTAMGKEETLSTAQLDFLLPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFV 528
Cdd:PLN02837 420 DALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFF 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 529 AFLTEETKGAFPTWLAPMQVEIIPVNiDLHYDYARLLQDELKSQGVRVEIdDRNEKMGYKIREAQMKKIPYQIVVGDQEV 608
Cdd:PLN02837 500 GVLIEHYAGDFPLWLAPVQARVLPVT-DNELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKEV 577
|
570 580
....*....|....*....|....
gi 488370792 609 ENQEVNVRKYGSEKQESVEKDEFI 632
Cdd:PLN02837 578 ETRTLTVRSRHGGELGTMPVDDFI 601
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
242-545 |
2.45e-167 |
|
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: 479.74 E-value: 2.45e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 242 DHRKIGKDLELFTNNQLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMFPAM 321
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 322 KldEDEAMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFKR 401
Cdd:cd00771 81 E--EDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 402 VVNMIQDVYKDFGFEDYRFRLSYRDpedkHKYFDDDEMWEKAESMLKEASDELGLTYEEAIGEAAFYGPKLDVQVKTAMG 481
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488370792 482 KEETLSTAQLDFLLPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFVAFLTEETKGAFPTWLAP 545
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
266-640 |
4.60e-57 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 203.56 E-value: 4.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 266 WLPNGATIRREIERYIVDKEVSMGYDHVYTPV---LANVDLYKtsgHWDHYQEDMFpAMKLDEDEaMVLRPMNCPHHMMI 342
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPImydLSHPAIRE---HADKFGERQY-RVKSDKKD-LMLRFAACFGQFLM 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 343 YKNKPHSYRELPIRIAELGTM-HRYEASGAVSGLQRVRGMTLNDSHIFVRP-DQIKEEFKRVVNMIQDVYKDFGFeDYR- 419
Cdd:PRK03991 297 LKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGR-DYEv 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 420 -FRLSyRDPEDKHKYFdddemwekaesmLKEASDELG---LTyeEAIGEAAFYGP-KLDVQVKTAMGKEETLSTAQLDFL 494
Cdd:PRK03991 376 aIRFT-EDFYEENKDW------------IVELVKREGkpvLL--EILPERKHYWVlKVEFAFIDSLGRPIENPTVQIDVE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 495 LPERFDLTYIGQDGEQHRPVVIHRGVVSTMERFVAFLTEET--------KGAFPTWLAPMQVEIIPVNiDLHYDYARLLQ 566
Cdd:PRK03991 441 NAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAakeeeegkVPMLPTWLSPTQVRVIPVS-ERHLDYAEEVA 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488370792 567 DELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEFIWNVIDEIR 640
Cdd:PRK03991 520 DKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
545-632 |
6.71e-36 |
|
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: 129.93 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 545 PMQVEIIPVNiDLHYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQE 624
Cdd:cd00860 1 PVQVVVIPVT-DEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
....*...
gi 488370792 625 SVEKDEFI 632
Cdd:cd00860 80 SMSLDEFI 87
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
324-534 |
3.54e-32 |
|
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: 122.52 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 324 DEDEAMVLRPMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVV 403
Cdd:pfam00587 6 ENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 404 NMIQDVYKDFGFEDYRFRLSYRDpedkhkyfdddemwekaesmlkeasdelgltyeeaigEAAFYGPKLDVQVKT-AMGK 482
Cdd:pfam00587 86 KLIDRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGK 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488370792 483 EETLSTAQLD-FLLPERFDLTYIGQDGEQHRPVVIHRGVVStMERFVAFLTEE 534
Cdd:pfam00587 129 QRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILEN 180
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
4-68 |
2.13e-27 |
|
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: 104.88 E-value: 2.13e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488370792 4 INIQFPDGNTKEFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIITPGSEE 68
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
547-632 |
3.11e-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: 96.89 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 547 QVEIIPVNI--DLHYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQE 624
Cdd:pfam03129 1 QVVVIPLGEkaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*...
gi 488370792 625 SVEKDEFI 632
Cdd:pfam03129 81 TVSLDELV 88
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
270-532 |
2.02e-23 |
|
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: 99.39 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 270 GATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMF---PAMKLDEDEAMVLRPMNCPHHMMIYKNK 346
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYtfeDKGRELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 347 PHSYRELPIRIAELGTMHRYEASGAvSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVVNMIQDVYKDFGfEDYRFRLSyrd 426
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG-LPVRVVVA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 427 pedkhkyfDDDEMWEKAEsmlkeasdelgltyeeaIGEAAFYGPKLDVQVKTAMGKEE-TLSTAQLDFLLPERFDLTYIG 505
Cdd:cd00670 156 --------DDPFFGRGGK-----------------RGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFKID 210
|
250 260
....*....|....*....|....*..
gi 488370792 506 QDGEQHRPVVIHRGVVstMERFVAFLT 532
Cdd:cd00670 211 EDGGGRAHTGCGGAGG--EERLVLALL 235
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
4-63 |
5.27e-17 |
|
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: 75.28 E-value: 5.27e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 4 INIQFPDGNTKEFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIIT 63
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
273-527 |
4.43e-16 |
|
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: 77.54 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 273 IRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWdhYQEDMFPAMKLDEDeaMVLRPMNCPHHMMIYKNkphSYRE 352
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEED--LYLRPTLEPGLVRLFVS---HIRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 353 LPIRIAELGTMHRYEASGAvsGLQRVRGMTLNDSHIFVRPDQIKEEFKRVVNMIQDVYKDFG-FEDYRFRLSYRDPEDkh 431
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGiKLDIVFVEKTPGEFS-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 432 kyfdddemwekaesmlkeasdelgltyeeaigeAAFYGPKLDVQVKTAMGKEETLSTAQLDFLLPER-FDLTYIGQDGEQ 510
Cdd:cd00768 150 ---------------------------------PGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEY 196
|
250
....*....|....*..
gi 488370792 511 HRPVVIHRGVvsTMERF 527
Cdd:cd00768 197 RYPPTIGFGL--GLERL 211
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
169-217 |
4.99e-15 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 69.33 E-value: 4.99e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488370792 169 VTLYTQGEF-TDLCRGVHVPSTSKIKEFKLLSTAGAYWRgnsdnkmLQRI 217
Cdd:smart00863 1 VRVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
169-217 |
6.46e-14 |
|
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: 65.93 E-value: 6.46e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488370792 169 VTLYTQGE-FTDLCRGVHVPSTSKIKEFKLLstagaywRGNSDNKMLQRI 217
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
530-642 |
6.70e-14 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 73.73 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 530 FLTEETKGAFPT---WLAPMQVEIIPVNIDLhYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQ 606
Cdd:PRK14938 256 FLLESIRKQPPTlpdWLNPIQVRILPVKKDF-LDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGER 334
|
90 100 110
....*....|....*....|....*....|....*...
gi 488370792 607 EVE--NQEVNVRKYGSEKQESVEKDEFIWNVIDEIRLK 642
Cdd:PRK14938 335 EVKtsTLTVKIRANNEQKSMTVEELVKEIKRADELKER 372
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
545-632 |
8.23e-14 |
|
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: 67.23 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 545 PMQVEIIPVNIDL--HYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEK 622
Cdd:cd00861 1 PFDVVIIPMNMKDevQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|
gi 488370792 623 QESVEKDEFI 632
Cdd:cd00861 81 KEEISIDELL 90
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
545-632 |
2.04e-13 |
|
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: 66.27 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 545 PMQVEIIPVNIDLH--YDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEK 622
Cdd:cd00738 1 PIDVAIVPLTDPRVeaREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|
gi 488370792 623 QESVEKDEFI 632
Cdd:cd00738 81 SETLHVDELP 90
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
544-643 |
3.90e-11 |
|
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: 62.70 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 544 APMQVEIIPVNIDLH-----YDYARLLQDELKSQGVRVEIDDR-NEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNV-- 615
Cdd:cd00862 9 APIQVVIVPIGIKDEkreevLEAADELAERLKAAGIRVHVDDRdNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIvr 88
|
90 100 110
....*....|....*....|....*....|..
gi 488370792 616 ----RKYGSEKQESVEKDEFIWNVIDEIRLKK 643
Cdd:cd00862 89 rdtgEKKTVPLAELVEKVPELLDEIQEDLYER 120
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
497-632 |
1.21e-10 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 64.33 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 497 ERFDLTYIGQDGEQHRPVV----IhrGVvstmERFVAFLTEET---KG-AFPTWLAPMQVEIIPVNI--DLHYDYARLLQ 566
Cdd:PRK09194 418 EAMNATVLDENGKAQPLIMgcygI--GV----SRLVAAAIEQNhdeKGiIWPKAIAPFDVHIVPVNMkdEEVKELAEKLY 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488370792 567 DELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEFI 632
Cdd:PRK09194 492 AELQAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELV 557
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
547-632 |
2.11e-10 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 57.55 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 547 QVEIIPVNIDLHYDYARLLQdELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESV 626
Cdd:cd00859 3 DVYVVPLGEGALSEALELAE-QLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETV 81
|
....*.
gi 488370792 627 EKDEFI 632
Cdd:cd00859 82 ALDELV 87
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
259-368 |
2.61e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 49.11 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 259 VGAGLPLWLPNGATIRREIERyIVDKEV-SMGYDHVYTPVLANVDLYKTSGHWDHYQEDMFpAMKLDEDEAMVLRPMncp 337
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIEN-IIREEMnKIGAQEILMPILQPAELWKESGRWDAYGPELL-RLKDRHGKEFLLGPT--- 93
|
90 100 110
....*....|....*....|....*....|....
gi 488370792 338 HHMMI---YKNKPHSYRELPIRIAELGTMHRYEA 368
Cdd:cd00779 94 HEEVItdlVANEIKSYKQLPLNLYQIQTKFRDEI 127
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
74-200 |
2.38e-05 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 46.34 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 74 RHSTAHLMAQALKRLYGdvkfgvGPVIEGGFYY-----DFDMDDkVSSDDFDKIEKTMKQIVNENHKIVREVVSKEkakD 148
Cdd:COG2872 99 LHTALHLLSAVVYREYG------APVTGGQIGEdrariDFDLPE-FDEEDLEEIEAEANELIAADLPVRIYWITRE---E 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488370792 149 FFKDDPY-KLELIDAIPEDESVTLYTQGEFtDL--CRGVHVPSTSKIKEFKLLST 200
Cdd:COG2872 169 LEAIPGLvRTMSVLPPPGVGRVRIVEIGGV-DLqpCGGTHVANTGEIGRIKITKI 222
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
544-632 |
4.49e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 46.39 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 544 APMQVEIIPVNI--DLHYDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSE 621
Cdd:PRK12325 344 APFKVGIINLKQgdEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTG 423
|
90
....*....|.
gi 488370792 622 KQESVEKDEFI 632
Cdd:PRK12325 424 EREELSVEAAI 434
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
257-419 |
9.28e-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: 44.67 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 257 QLVGAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMFPAMKLDEDEAM----VLR 332
Cdd:cd00772 18 QGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVFKDAGDEELeedfALR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 333 PMNCPHHMMIYKNKPHSYRELPIRIAELGTMHRYEASgAVSGLQRVRGMTLNDSHIF-VRPDQIKEEFKRVVNMIQDVYK 411
Cdd:cd00772 98 PTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIAR 176
|
....*...
gi 488370792 412 DFGFEDYR 419
Cdd:cd00772 177 DLAAIDFI 184
|
|
| TGS_RSH |
cd01668 |
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ... |
9-63 |
1.74e-04 |
|
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT homolog (RSH) family consists of long RSH proteins and short RSH proteins. Long RSH proteins have been characterized as containing an N-terminal region and a C-terminal region. The N-terminal region contains a pseudo-hydrolase (inactive-hydrolase) domain and a (p)ppGpp synthetase domain. The C-terminal region contains a ubiquitin-like TGS (ThrRS, GTPase and SpoT) domain, a conserved cysteine domain (CC), helical and ACT (aspartate kinase, chorismate mutase, TyrA domain) domains connected by a linker region. Short RSH proteins have a truncated C-terminal region without ACT domain. The RSH family includes two classes of enzyme: i) monofunctional (p)ppGpp synthetase I, RelA, and ii) bifunctional (p)ppGpp synthetase II/hydrolase, SpoT (also called Rel). Both classes are capable of synthesizing (p)ppGpp but only bifunctional enzymes are capable of (p)ppGpp hydrolysis. SpoT is a ribosome-associated protein that is activated during amino acid starvation and thought to mediate the stringent response. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in respond to environmental stress. RelA is an ATP:GTP(GDP) pyrophosphate transferase that is recruited to stalled ribosomes and activated to synthesize (p)ppGpp, which acts as a pleiotropic secondary messenger.
Pssm-ID: 340459 [Multi-domain] Cd Length: 59 Bit Score: 39.82 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488370792 9 PDGNTKEFDKGTTTEDIAQSISPGLRKKAVAGKFNGQLVDLTRPLEQDGAIEIIT 63
Cdd:cd01668 5 PKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT 59
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
262-413 |
5.30e-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: 42.20 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 262 GLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLY-KTSGHWDHYQEDMFPAMKL---DEDEAMVLRPMN-- 335
Cdd:cd00778 23 GCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELeKEKEHIEGFAPEVAWVTHGgleELEEPLALRPTSet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 336 --CPhhmmIYKNKPHSYRELPIRIAELGTMHRYEASGAVSGLqRVRGMTLNDSH-IFVRPDQIKEEFKRVVNMIQDVYKD 412
Cdd:cd00778 103 aiYP----MFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFL-RTREFLWQEGHtAHATEEEAEEEVLQILDLYKEFYED 177
|
.
gi 488370792 413 F 413
Cdd:cd00778 178 L 178
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
539-630 |
1.04e-03 |
|
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: 39.46 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 539 FPTWLAPMQVEIIP-VNIDLHYDYARLLQDELKSQGVRVEIDD---------RNEKMGykireaqmkkIPYQIVVGDQEV 608
Cdd:cd00858 20 LPPALAPIKVAVLPlVKRDELVEIAKEISEELRELGFSVKYDDsgsigrryaRQDEIG----------TPFCVTVDFDTL 89
|
90 100
....*....|....*....|..
gi 488370792 609 ENQEVNVRKYGSEKQESVEKDE 630
Cdd:cd00858 90 EDGTVTIRERDSMRQVRVKIEE 111
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
210-425 |
1.31e-03 |
|
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: 41.39 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 210 DNKmLQRIYGTAFFDKKDLKAHLKMLEERRERDHRKIGKdlelftnnqLVGAGLPLWLPNGATIRREIERYIVDKEVSMG 289
Cdd:cd00770 1 DNV-EIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAK---------VSGSRFYYLKGDGALLERALINFALDFLTKRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 290 YDHVYTPVLANVDLYKTSGHWDHYQEDMFpamKLDEDE------AMVlrPMNCphhmmIYKNKPHSYRELPIRIAELGTM 363
Cdd:cd00770 71 FTPVIPPFLVRKEVMEGTGQLPKFDEQLY---KVEGEDlyliatAEV--PLAA-----LHRDEILEEEELPLKYAGYSPC 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488370792 364 HRYEASGA---VSGLQRVRGMTLNDSHIFVRPDQIKEEFKRVVNMIQDVYKDFGfedyrfrLSYR 425
Cdd:cd00770 141 FRKEAGSAgrdTRGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELG-------LPYR 198
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
548-621 |
1.31e-03 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 41.64 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488370792 548 VEIIPVNIDLhyDYARLLQDELKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVR--KYGSE 621
Cdd:PRK12420 341 VFIIPLGTEL--QCLQIAQQLRSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRnmKEGSE 414
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
260-355 |
1.45e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 41.38 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 260 GAGLPLWLPNGATIRREIERYIVDKEVSMGYDHVYTPVLANVDLYKTSGHWDHYQEDMFpAMKLDEDEAMVLRPMNcpHH 339
Cdd:PRK12325 36 AAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEML-RIKDRHDREMLYGPTN--EE 112
|
90
....*....|....*...
gi 488370792 340 MM--IYKNKPHSYRELPI 355
Cdd:PRK12325 113 MItdIFRSYVKSYKDLPL 130
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
75-197 |
1.88e-03 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 41.30 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488370792 75 HSTAHLMAQALKRLYGDVKFGVGPVI-EGGFYYDFDMDDKVSSDDFDKIEktmkQIVNENHK----IVREVVSKEKAKD- 148
Cdd:PRK01584 457 HTATHLLHKALRLVLGDHVRQKGSNItAERLRFDFSHPEKMTDDEIKKVE----DIVNLQIKndlsVKKEVMSLEEAREk 532
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488370792 149 ----FFkDDPYklelidaipeDESVTLYTQGEF-TDLCRGVHVPSTSKIKEFKL 197
Cdd:PRK01584 533 gamaLF-GEKY----------EDIVKVYEIDGFsKEVCGGPHVENTGELGTFKI 575
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
569-631 |
6.36e-03 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 39.50 E-value: 6.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488370792 569 LKSQGVRVEIDDRNEKMGYKIREAQMKKIPYQIVVGDQEVENQEVNVRKYGSEKQESVEKDEF 631
Cdd:CHL00201 348 LEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNF 410
|
|
| |
