|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
4-643 |
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: 975.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 4 SVTLPDGSKKDFDKAVSVKELASSIATSLGKAAVGAKINGVMKPLDYIVDEDVEAAIITDKDEEGLDILRATAAFLL-EA 82
Cdd:COG0441 3 KITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLaQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 83 VaKRKYPELRLGMHEADEGGFFVDTDKEDQIKVTELPELEKAMQKAIKNGEKIEYTSMKKSELEEIFK--DDQFKLDLLK 160
Cdd:COG0441 83 V-KRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVELIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 161 D--EEDEVAVYKLGDFVDFGFDALLPNTGKIKNFKLLSVAGAYWLGKSSNPMLQRIFGTAFFKKAALDEDLKRRAEIKER 238
Cdd:COG0441 162 DipEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKKR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 239 DHRTIGRDLDLFFVDPKVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFPpM 318
Cdd:COG0441 242 DHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP-T 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 319 DMgDGEMLELRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEFAK 398
Cdd:COG0441 321 ES-DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 399 VLKLIMDVYKDFDITDYYFRLSYRdpknTDKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPKLDIQTKTALG 478
Cdd:COG0441 400 VIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 479 NDETMSTIQLDFMLPERFGLTYVGQDGEEHRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAPVQAEIIPVNEEaHGEY 558
Cdd:COG0441 476 REWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDK-HADY 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 559 ADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDFIAEIDADVKS 638
Cdd:COG0441 555 AKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKEEIRS 634
|
....*
gi 560183246 639 YSREK 643
Cdd:COG0441 635 RSLEP 639
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
73-636 |
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: 677.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 73 RATAAFLLEAVAKRKYPELRLGMHEADEGGFFVDTDKEDQIKVTELPELEKAMQKAIKNGEKIEYTSMKKSELEEIFK-D 151
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKvL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 152 DQFKLDLLK--DEEDEVAVYKLGD-FVDFGFDALLPNTGKIKNFKLLSVAGAYWLGKSSNPMLQRIFGTAFFKKAALDED 228
Cdd:TIGR00418 81 EPYKLELLDeiPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 229 LKRRAEIKERDHRTIGRDLDLFFVDPKVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWA 308
Cdd:TIGR00418 161 LLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 309 HYRDDMFPPMDMgDGEMLELRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVA 388
Cdd:TIGR00418 241 NYKERMFPFTEL-DNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 389 LDQIREEFAKVLKLIMDVYKDFDITDYYFRLSYRDPKntdKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPK 468
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPE---DFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 469 LDIQTKTALGNDETMSTIQLDFMLPERFGLTYVGQDGEEHRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAPVQAEII 548
Cdd:TIGR00418 397 IDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 549 PVNEEaHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDF 628
Cdd:TIGR00418 477 PVNER-HLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEF 555
|
....*...
gi 560183246 629 IAEIDADV 636
Cdd:TIGR00418 556 LEKLRKEV 563
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-638 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 623.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 1 MSFSVTLPDGSKKDFDKAVSVKELASSIATSLGKAAVGAKINGVMKPLDYIVDEDVEAAIITDKDEEGLDILRATAAFLL 80
Cdd:PRK12444 4 QMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 81 EAVAKRKYPELRLGMHEADEGGFFVDTDKEDQIKVTELPELEKAMQKAIKNGEKIEYTSMKKSELEEIFK--DDQFKLDL 158
Cdd:PRK12444 84 AQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQemNDRLKLEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 159 LKD--EEDEVAVYKLGDFVDFGFDALLPNTGKIKNFKLLSVAGAYWLGKSSNPMLQRIFGTAFFKKAALDEDLKRRAEIK 236
Cdd:PRK12444 164 LEAipSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 237 ERDHRTIGRDLDLFFVDPKvGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFp 316
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMY- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 317 pMDMGDGEMLELRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEF 396
Cdd:PRK12444 322 -FSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 397 AKVLKLIMDVYKDFDItDYYFRLSYRdpknTDKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPKLDIQTKTA 476
Cdd:PRK12444 401 KSVMAQIDYVYKTFGF-EYEVELSTR----PEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 477 LGNDETMSTIQLDFMLPERFGLTYVGQDGEEHRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAPVQAEIIPVNEEAHG 556
Cdd:PRK12444 476 LNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVHV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 557 EYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDFIAEIDADV 636
Cdd:PRK12444 556 QYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEI 635
|
..
gi 560183246 637 KS 638
Cdd:PRK12444 636 KN 637
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
5-640 |
1.76e-159 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 474.26 E-value: 1.76e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 5 VTLPDGSKKDFDKAVSVK-ELASSIATSLGKAAVGAKINGVMKPLDYIVDEDVEAAIITDKDEEGLDILRATAAFLLEAV 83
Cdd:PLN02908 54 VTLPDGAVKDGKKWVTTPmDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 84 AKRKY-PELRLGMHEADEGGFFVDTDKEDQ-IKVTELPELEKAMQKAIKNGEKIEYTSMKKSELEEIFKDDQFKLDLLKD 161
Cdd:PLN02908 134 LELEYgCKLCIGPCTTRGEGFYYDAFYGDRtLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIIND 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 162 --EEDEVAVYKLGDFVDFGFDALLPNTGKIKNFKLLSVAGAYWLGKSSNPMLQRIFGTAFFKKAALDEDLKRRAEIKERD 239
Cdd:PLN02908 214 lpEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRD 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 240 HRTIGRDLDLFFVDPkVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFPpMD 319
Cdd:PLN02908 294 HRLLGQKQELFFFHE-LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFV-FE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 320 MgDGEMLELRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEFAKV 399
Cdd:PLN02908 372 I-EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGV 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 400 LKLIMDVYKDFDITdYYFRLSYRdpknTDKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPKLDIQTKTALGN 479
Cdd:PLN02908 451 LDFLDYVYEVFGFT-YELKLSTR----PEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 480 DETMSTIQLDFMLPERFGLTYVGQDGEE-HRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAPVQAEIIPVNEEAHgEY 558
Cdd:PLN02908 526 KFQCATVQLDFQLPIRFKLSYSAEDEAKiERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQ-DY 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 559 ADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDFIAEIDADVKS 638
Cdd:PLN02908 605 AEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAE 684
|
..
gi 560183246 639 YS 640
Cdd:PLN02908 685 FK 686
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
239-542 |
3.26e-154 |
|
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: 446.23 E-value: 3.26e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 239 DHRTIGRDLDLFFVDPKVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFPPM 318
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 319 dmGDGEMLELRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEFAK 398
Cdd:cd00771 81 --EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 399 VLKLIMDVYKDFDITDYYFRLSYRDpkntDKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPKLDIQTKTALG 478
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560183246 479 NDETMSTIQLDFMLPERFGLTYVGQDGEEHRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAP 542
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
26-640 |
5.71e-152 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 452.43 E-value: 5.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 26 SSIATSLGKAAVGAKINGVMKPLDyivDEDVEAAIITDKDEEGLDILRATAAFLLEAVAKRKYPELRLGMHEADEGGFFV 105
Cdd:PLN02837 3 AAAASAATEEASAAAASDEKGPGE---AEPERVVLPTNESSEKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 106 DTDKEdQIKVTELPELEKAMQKAIKNGEKIEYTSMKKSELEEIFK--DDQFKLDLLKD-EEDEVAVYKLG-DFVDFGFDA 181
Cdd:PLN02837 80 DFDME-PLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMaiNEPYKLEILEGiKEEPITIYHIGeEWWDLCAGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 182 LLPNTGKI--KNFKLLSVAGAYWLGKSSNPMLQRIFGTAFFKKAALDEDLKRRAEIKERDHRTIGRDLDLFFVDPKVGAG 259
Cdd:PLN02837 159 HVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 260 LPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFPPMDMGDgEMLELRPMNCPSHIQI 339
Cdd:PLN02837 239 LVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIED-ELYQLRPMNCPYHILV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 340 YKHHIRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEFAKVLKLIMDVYKDFDITDYYFRL 419
Cdd:PLN02837 318 YKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 420 SYRdpknTDKYYANDEMWERSQSMLKAAMDDLGLDYVEAEGEAAFYGPKLDIQTKTALGNDETMSTIQLDFMLPERFGLT 499
Cdd:PLN02837 398 STR----PEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDIT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 500 YVGQDGEEHRPVMIHRGIVGTMERFIAYLTEIYKGAFPTWLAPVQAEIIPVNEEaHGEYADKVRAELAKRGFRAEVDHrN 579
Cdd:PLN02837 474 YVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDN-ELEYCKEVVAKLKAKGIRAEVCH-G 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 560183246 580 EKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDFIAEIDADVKSYS 640
Cdd:PLN02837 552 ERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVENRT 612
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
220-639 |
2.23e-58 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 207.03 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 220 FKKAALDEDLKRRAEIKERDHRTIGRDLDLFFVDPKVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVD 299
Cdd:PRK03991 179 LKALVDYEVGKKELVGGEPPHVKLMREKELADYEPASDVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 300 AYKTSGHWahyrdDMFPP----MDMGDGEMLeLRPMNCPSHIQIYKHHIRSYRELPIRIAELGMM-HRYEKSGALSGLQR 374
Cdd:PRK03991 259 HPAIREHA-----DKFGErqyrVKSDKKDLM-LRFAACFGQFLMLKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 375 VREMTLNDGHTFVA-LDQIREEFAKVLKLIMDVYKDFDItDYY--FRLsyrdpknTDKYYANDEMWersqsmLKAAMDDL 451
Cdd:PRK03991 333 LRAFTMPDMHTLCKdMEQAMEEFEKQYEMILETGEDLGR-DYEvaIRF-------TEDFYEENKDW------IVELVKRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 452 GLD-YVEAEGEAAFYGP-KLDIQTKTALGNDETMSTIQLDFMLPERFGLTYVGQDGEEHRPVMIHRGIVGTMERFIAYLT 529
Cdd:PRK03991 399 GKPvLLEILPERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 530 E-----IYKG---AFPTWLAPVQAEIIPVNEEaHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLG 601
Cdd:PRK03991 479 EkaakeEEEGkvpMLPTWLSPTQVRVIPVSER-HLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIG 557
|
410 420 430
....*....|....*....|....*....|....*...
gi 560183246 602 DEEMNANGVNVRRYGTEEQISKSLDDFIAEIDADVKSY 639
Cdd:PRK03991 558 DKEMESGKLTVTIREESEKVEMTLEELIERIKEETKGY 595
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
323-532 |
7.99e-36 |
|
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: 132.92 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 323 GEMLELRPMNCPSHIQIY-KHHIRSYReLPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHTFVALDQIREEFAKVLK 401
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 402 LIMDVYKDFDITDYYFRLSYRDpkntdkyyandemwersqsmlkaamddlgldyveaegEAAFYGPKLDIQTKT-ALGND 480
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 560183246 481 ETMSTIQLD-FMLPERFGLTYVGQDGEEHRPVMIHRGIVGtMERFIAYLTEIY 532
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
542-632 |
1.19e-33 |
|
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: 123.38 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 542 PVQAEIIPVNEEaHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQI 621
Cdd:cd00860 1 PVQVVVIPVTDE-HLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|.
gi 560183246 622 SKSLDDFIAEI 632
Cdd:cd00860 80 SMSLDEFIEKL 90
|
|
| 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 ... |
267-529 |
4.12e-26 |
|
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: 107.09 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 267 GATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMF---PPMDMGDGEMLELRPMNCPSHIQIYKHH 343
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYtfeDKGRELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 344 IRSYRELPIRIAELGMMHRYEKSGAlSGLQRVREMTLNDGHTFVALDQIREEFAKVLKLIMDVYKDfditdyyFRLSYRD 423
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARE-------LGLPVRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 424 PKNTDKYYAndemwERSQsmlkaamddlgldyveaEGEAAFYGPKLDIQTKTALGNDE-TMSTIQLDFMLPERFGLTYVG 502
Cdd:cd00670 153 VVADDPFFG-----RGGK-----------------RGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFKID 210
|
250 260
....*....|....*....|....*..
gi 560183246 503 QDGEEHRPVMIHRGivGTMERFIAYLT 529
Cdd:cd00670 211 EDGGGRAHTGCGGA--GGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
544-632 |
1.12e-21 |
|
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: 89.95 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 544 QAEIIPVNE--EAHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQI 621
Cdd:pfam03129 1 QVVVIPLGEkaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|.
gi 560183246 622 SKSLDDFIAEI 632
Cdd:pfam03129 81 TVSLDELVEKL 91
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
4-67 |
1.83e-17 |
|
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: 76.76 E-value: 1.83e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 560183246 4 SVTLPDGSKKDFDKAVSVKELASSIATSLGKAAVGAKINGVMKPLDYIVDEDVEAAIITDKDEE 67
Cdd:cd01667 2 KITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
270-524 |
8.16e-17 |
|
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: 79.47 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 270 IRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRDdmfPPMDmGDGEMLELRPMNCPSHIQIYKHHIRSyre 349
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLL---PVGA-ENEEDLYLRPTLEPGLVRLFVSHIRK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 350 LPIRIAELGMMHRYEKSGAlsGLQRVREMTLNDGHTFVALDQIREEFAKVLKLIMDVYKDFDIT-DYYFRLSYRDPKntd 428
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKlDIVFVEKTPGEF--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 429 kyyandemwersqsmlkaamddlgldyveaegEAAFYGPKLDIQTKTALGNDETMSTIQLDFMLPER-FGLTYVGQDGEE 507
Cdd:cd00768 149 --------------------------------SPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEY 196
|
250
....*....|....*..
gi 560183246 508 HRPVMIHRGIvgTMERF 524
Cdd:cd00768 197 RYPPTIGFGL--GLERL 211
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
542-630 |
6.74e-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: 64.73 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 542 PVQAEIIPVNEEAHG--EYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEE 619
Cdd:cd00738 1 PIDVAIVPLTDPRVEarEYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|.
gi 560183246 620 QISKSLDDFIA 630
Cdd:cd00738 81 SETLHVDELPE 91
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
537-632 |
7.52e-12 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 67.56 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 537 PTWLAPVQAEIIPVNEEaHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYG 616
Cdd:PRK14938 269 PDWLNPIQVRILPVKKD-FLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRA 347
|
90
....*....|....*.
gi 560183246 617 TEEQISKSLDDFIAEI 632
Cdd:PRK14938 348 NNEQKSMTVEELVKEI 363
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
5-56 |
2.69e-11 |
|
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.
Pssm-ID: 427005 [Multi-domain] Cd Length: 60 Bit Score: 59.10 E-value: 2.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 560183246 5 VTLPDGSKKDFDKAVSVKELASSIATSLGKAAVGAKINGVMKPLDYIV-DEDV 56
Cdd:pfam02824 3 VYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLeDGDV 55
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
166-214 |
7.71e-09 |
|
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: 51.61 E-value: 7.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 560183246 166 VAVYKLGDF-VDFGFDALLPNTGKIKNFKLLSVAGAYWLgkssnpmLQRI 214
Cdd:smart00863 1 VRVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
547-632 |
1.45e-08 |
|
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: 52.16 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 547 IIPVNEEAHGEYADKVRaELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLD 626
Cdd:cd00859 6 VVPLGEGALSEALELAE-QLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALD 84
|
....*.
gi 560183246 627 DFIAEI 632
Cdd:cd00859 85 ELVEEL 90
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
166-214 |
4.14e-08 |
|
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: 49.36 E-value: 4.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 560183246 166 VAVYKLGD-FVDFGFDALLPNTGKIKNFKLLSvagaywlGKSSNPMLQRI 214
Cdd:pfam07973 1 VRVVSIGDfDVDLCGGTHVPNTGEIGAFKILK-------GESKNKGLRRI 43
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
255-386 |
6.30e-08 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. 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: 54.12 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 255 KVGAGLPYWMPKGATIRRVVERyIVDKEV-ADGYEHVYTPVLMNVDAYKTSGHWAHYRDDMFPPMDMGDGEMLeLRPMNC 333
Cdd:cd00779 18 QTSSGLYSWLPLGLRVLKKIEN-IIREEMnKIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGKEFL-LGPTHE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 560183246 334 PSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSGALsGLQRVREMTLNDGHTF 386
Cdd:cd00779 96 EVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSF 147
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
541-632 |
1.21e-07 |
|
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: 52.69 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 541 APVQAEIIPV-----NEEAHGEYADKVRAELAKRGFRAEVDHR-NEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRR 614
Cdd:cd00862 9 APIQVVIVPIgikdeKREEVLEAADELAERLKAAGIRVHVDDRdNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90
....*....|....*...
gi 560183246 615 YGTEEQISKSLDDFIAEI 632
Cdd:cd00862 89 RDTGEKKTVPLAELVEKV 106
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
263-410 |
1.83e-07 |
|
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: 52.98 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 263 WMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAY-KTSGHWAHYRDDMFPPMDMGDGEMLE---LRPMncpSHIQ 338
Cdd:cd00778 27 FRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELeKEKEHIEGFAPEVAWVTHGGLEELEEplaLRPT---SETA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 560183246 339 IY---KHHIRSYRELPIRIAELGMMHRYEKSGALSGLqRVREMTLNDGHTFVAldqIREEFAKVLKLIMDVYKDF 410
Cdd:cd00778 104 IYpmfSKWIRSYRDLPLKINQWVNVFRWETKTTRPFL-RTREFLWQEGHTAHA---TEEEAEEEVLQILDLYKEF 174
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
542-632 |
1.85e-07 |
|
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: 49.13 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 542 PVQAEIIPVN--EEAHGEYADKVRAELAKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEE 619
Cdd:cd00861 1 PFDVVIIPMNmkDEVQQELAEKLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|...
gi 560183246 620 QISKSLDDFIAEI 632
Cdd:cd00861 81 KEEISIDELLEFL 93
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
494-632 |
8.32e-06 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 48.93 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 494 ERFGLTYVGQDGEEHRPVMIHRGI-VGtmeRFIAYLTEIY---KG-AFPTWLAPVQAEIIPVN--EEAHGEYADKVRAEL 566
Cdd:PRK09194 418 EAMNATVLDENGKAQPLIMGCYGIgVS---RLVAAAIEQNhdeKGiIWPKAIAPFDVHIVPVNmkDEEVKELAEKLYAEL 494
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 560183246 567 AKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRYGTEEQISKSLDDFIAEI 632
Cdd:PRK09194 495 QAAGIEVLLDDRKERPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
251-415 |
1.01e-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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 44.67 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 251 FVDPKVGAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSG-HWAHYRDDMFPPMDMGDGEMLE-- 327
Cdd:cd00772 15 LADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFKDAGDEELEEdf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 328 -LRPMNCPSHIQIYKHHIRSYRELPIRIAELGMMHRYEKSgALSGLQRVREMTLNDGHTFVA-LDQIREEFAKVLKLIMD 405
Cdd:cd00772 95 aLRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYAE 173
|
170
....*....|
gi 560183246 406 VYKDFDITDY 415
Cdd:cd00772 174 IARDLAAIDF 183
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
547-625 |
7.55e-04 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 42.41 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 547 IIPVNEEAHgeyADKVRAEL-AKRGFRAEVDHRNEKLGYKIRESQTQKVPYTLVLGDEEMNANGVNVRRY--GTEEQISK 623
Cdd:PRK12420 343 IIPLGTELQ---CLQIAQQLrSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMkeGSEVKVPL 419
|
..
gi 560183246 624 SL 625
Cdd:PRK12420 420 SS 421
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
238-315 |
8.14e-04 |
|
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: 41.78 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 238 RDHRTIGRDLDLFfvDP----KV-GAGLPYWMPKGATIRRVVERYIVDKEVADGYEHVYTPVLMNVDAYKTSGHWAHYRD 312
Cdd:cd00770 19 KDHVELGEKLDIL--DFergaKVsGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKFDE 96
|
...
gi 560183246 313 DMF 315
Cdd:cd00770 97 QLY 99
|
|
| TGS_RSH |
cd01668 |
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ... |
5-62 |
9.99e-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: 37.51 E-value: 9.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 560183246 5 VTLPDGSKK-DFdkavsvkelASSIATSLGKAAVGAKINGVMKPLDYIVD--EDVEaaIIT 62
Cdd:cd01668 10 VSLPKGATPiDF---------AYAIHTDVGNKCVGAKVNGKIVPLDYVLKngDVVE--IIT 59
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
268-423 |
1.60e-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: 40.66 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 268 ATIRRVVERYivdkevadGYEHVYTPVLMNVDAYkTSGHWAHYRDDMFPPMDMGdGEMLELRPMNCPSHIQIYKHHiRSY 347
Cdd:cd00773 10 DTLREVFERY--------GYEEIDTPVFEYTELF-LRKSGDEVSKEMYRFKDKG-GRDLALRPDLTAPVARAVAEN-LLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560183246 348 RELPIRIAELGMMHRYEKSGALsglqRVREmtlndgHTFVALDQIREE----FAKVLKLIMDVYKDFDITDYYFRLSYRD 423
Cdd:cd00773 79 LPLPLKLYYIGPVFRYERPQKG----RYRE------FYQVGVEIIGSDsplaDAEVIALAVEILEALGLKDFQIKINHRG 148
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
536-576 |
2.85e-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: 37.92 E-value: 2.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 560183246 536 FPTWLAPVQAEIIP-VNEEAHGEYADKVRAELAKRGFRAEVD 576
Cdd:cd00858 20 LPPALAPIKVAVLPlVKRDELVEIAKEISEELRELGFSVKYD 61
|
|
| |
