|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
110-519 |
2.73e-172 |
|
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: 502.64 E-value: 2.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTS-IYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMY--E 186
Cdd:COG0441 242 DHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFptE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 187 VrgrgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIF 266
Cdd:COG0441 322 S--------------DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 267 CRPQQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKI 346
Cdd:COG0441 388 CTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPEK-RIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKI 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 347 DIQLQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEedynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWL 426
Cdd:COG0441 467 DFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGE---------KHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 427 SPRQGIILTVNqdEAVLKQAQEAAAKI--SGFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLI 504
Cdd:COG0441 538 APVQVVVLPIS--DKHADYAKEVAKKLraAGIR----------------------VEVDLRNEKIGYKIREAQLQKVPYM 593
|
410
....*....|....*
gi 1475578741 505 FILGPKDIADSSVTV 519
Cdd:COG0441 594 LVVGDKEVENGTVSV 608
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
110-428 |
1.95e-159 |
|
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: 457.01 E-value: 1.95e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVRG 189
Cdd:cd00771 2 HRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 190 rgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCRP 269
Cdd:cd00771 82 ------------EDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 270 QQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKIDIQ 349
Cdd:cd00771 150 DQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTRPEK-FIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFH 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1475578741 350 LQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEEDYnpatpgratPVLVHRANFGSLERFLALLIEQYAGRWPFWLSP 428
Cdd:cd00771 229 VKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKR---------PVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
110-519 |
1.82e-155 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 461.16 E-value: 1.82e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMY--EV 187
Cdd:PLN02908 293 DHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFvfEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 188 rgrgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFC 267
Cdd:PLN02908 373 --------------EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFC 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 268 RPQQIKGEIASALGFVDMVMTTFGLgPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKID 347
Cdd:PLN02908 439 REDQIKDEVKGVLDFLDYVYEVFGF-TYELKLSTRPEK-YLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKID 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 348 IQLQDQAGKYHQLSTIQLDMNLPQRFGLEYqVAEGEEDynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLS 427
Cdd:PLN02908 517 ITVSDALKRKFQCATVQLDFQLPIRFKLSY-SAEDEAK-------IERPVMIHRAILGSVERMFAILLEHYAGKWPFWLS 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 428 PRQGIILTVNqdEAVLKQAQEAAAKISGfrplvAGkdkaspkplssvdstFLIDVDTSSQTLGKKIQRAKQMKYNLIFIL 507
Cdd:PLN02908 589 PRQAIVVPIS--EKSQDYAEEVRAQLHA-----AG---------------FYVDVDVTDRKIQKKVREAQLAQYNYILVV 646
|
410
....*....|..
gi 1475578741 508 GPKDIADSSVTV 519
Cdd:PLN02908 647 GEAEAATGTVNV 658
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
110-541 |
3.14e-145 |
|
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: 430.59 E-value: 3.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYS-PGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVR 188
Cdd:TIGR00418 171 DHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWDNYKERMFPFT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 189 GrgatgeadgeaGEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCR 268
Cdd:TIGR00418 251 E-----------LDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 269 PQQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKDFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKIDI 348
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 349 QLQDQAGKYHQLSTIQLDMNLPQRFGLEYqVAEGEEdynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLSP 428
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTY-VDEDNE--------EKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAP 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 429 RQGIILTVNqdEAVLKQAQEAAAKIS--GFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLIFI 506
Cdd:TIGR00418 471 VQVVVIPVN--ERHLDYAKKVAQKLKkaGIR----------------------VDVDDRNERLGKKIREAQKQKIPYMLV 526
|
410 420 430
....*....|....*....|....*....|....*.
gi 1475578741 507 LGPKDIADSSVTV-DVTGQMQTKTDADgqklkEVLE 541
Cdd:TIGR00418 527 VGDKEMESLAVNVrTRKGQKLEKMSLD-----EFLE 557
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
202-418 |
1.45e-40 |
|
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: 145.25 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 202 EDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCRPQQIKGEIASALG 281
Cdd:pfam00587 7 NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 282 FVDMVMTTFGLGPYRLVLSTRPEkdfigslelwdsaeaqlrealdnsgrewamnegdGAFYGPKIDIQLQDQA-GKYHQL 360
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSDG----------------------------------SAFYGPKLDFEVVFPSlGKQRQT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475578741 361 STIQLDM-NLPQRFGLEYQVAEGEEDynpatpgraTPVLVHRANFGsLERFLALLIEQY 418
Cdd:pfam00587 133 GTIQNDGfRLPRRLGIRYKDEDNESK---------FPYMIHRAGLG-VERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
110-519 |
2.73e-172 |
|
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: 502.64 E-value: 2.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTS-IYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMY--E 186
Cdd:COG0441 242 DHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFptE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 187 VrgrgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIF 266
Cdd:COG0441 322 S--------------DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 267 CRPQQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKI 346
Cdd:COG0441 388 CTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTRPEK-RIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKI 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 347 DIQLQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEedynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWL 426
Cdd:COG0441 467 DFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGE---------KHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 427 SPRQGIILTVNqdEAVLKQAQEAAAKI--SGFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLI 504
Cdd:COG0441 538 APVQVVVLPIS--DKHADYAKEVAKKLraAGIR----------------------VEVDLRNEKIGYKIREAQLQKVPYM 593
|
410
....*....|....*
gi 1475578741 505 FILGPKDIADSSVTV 519
Cdd:COG0441 594 LVVGDKEVENGTVSV 608
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
110-428 |
1.95e-159 |
|
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: 457.01 E-value: 1.95e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVRG 189
Cdd:cd00771 2 HRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 190 rgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCRP 269
Cdd:cd00771 82 ------------EDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 270 QQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKIDIQ 349
Cdd:cd00771 150 DQIKEEIKGVLDLIKEVYSDFGFFDYKVELSTRPEK-FIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFH 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1475578741 350 LQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEEDYnpatpgratPVLVHRANFGSLERFLALLIEQYAGRWPFWLSP 428
Cdd:cd00771 229 VKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKR---------PVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
110-519 |
1.82e-155 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 461.16 E-value: 1.82e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMY--EV 187
Cdd:PLN02908 293 DHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFvfEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 188 rgrgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFC 267
Cdd:PLN02908 373 --------------EKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFC 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 268 RPQQIKGEIASALGFVDMVMTTFGLgPYRLVLSTRPEKdFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKID 347
Cdd:PLN02908 439 REDQIKDEVKGVLDFLDYVYEVFGF-TYELKLSTRPEK-YLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKID 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 348 IQLQDQAGKYHQLSTIQLDMNLPQRFGLEYqVAEGEEDynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLS 427
Cdd:PLN02908 517 ITVSDALKRKFQCATVQLDFQLPIRFKLSY-SAEDEAK-------IERPVMIHRAILGSVERMFAILLEHYAGKWPFWLS 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 428 PRQGIILTVNqdEAVLKQAQEAAAKISGfrplvAGkdkaspkplssvdstFLIDVDTSSQTLGKKIQRAKQMKYNLIFIL 507
Cdd:PLN02908 589 PRQAIVVPIS--EKSQDYAEEVRAQLHA-----AG---------------FYVDVDVTDRKIQKKVREAQLAQYNYILVV 646
|
410
....*....|..
gi 1475578741 508 GPKDIADSSVTV 519
Cdd:PLN02908 647 GEAEAATGTVNV 658
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
110-541 |
3.14e-145 |
|
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: 430.59 E-value: 3.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYS-PGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVR 188
Cdd:TIGR00418 171 DHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWDNYKERMFPFT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 189 GrgatgeadgeaGEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCR 268
Cdd:TIGR00418 251 E-----------LDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 269 PQQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKDFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKIDI 348
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 349 QLQDQAGKYHQLSTIQLDMNLPQRFGLEYqVAEGEEdynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLSP 428
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTY-VDEDNE--------EKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAP 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 429 RQGIILTVNqdEAVLKQAQEAAAKIS--GFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLIFI 506
Cdd:TIGR00418 471 VQVVVIPVN--ERHLDYAKKVAQKLKkaGIR----------------------VDVDDRNERLGKKIREAQKQKIPYMLV 526
|
410 420 430
....*....|....*....|....*....|....*.
gi 1475578741 507 LGPKDIADSSVTV-DVTGQMQTKTDADgqklkEVLE 541
Cdd:TIGR00418 527 VGDKEMESLAVNVrTRKGQKLEKMSLD-----EFLE 557
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
110-543 |
5.21e-114 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 352.90 E-value: 5.21e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMY--EV 187
Cdd:PRK12444 246 NHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYfsEV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 188 rgrgatgeadgeagEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFC 267
Cdd:PRK12444 326 --------------DNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 268 RPQQIKGEIASALGFVDMVMTTFGLgPYRLVLSTRPEkDFIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKID 347
Cdd:PRK12444 392 TPDQIEDEIKSVMAQIDYVYKTFGF-EYEVELSTRPE-DSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKID 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 348 IQLQDQAGKYHQLSTIQLDMNLPQRFGLEYqVAEGEEdynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLS 427
Cdd:PRK12444 470 FHIKDALNRSHQCGTIQLDFQMPEKFDLNY-IDEKNE--------KRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 428 PRQGIILTVNqDEAVLKQAQEAAAKI--SGFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLIF 505
Cdd:PRK12444 541 PVQVKVIPVS-NAVHVQYADEVADKLaqAGIR----------------------VERDERDEKLGYKIREAQMQKIPYVL 597
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1475578741 506 ILGPKDIADSSVTVDVTGQMQTKT---DADGQKLKEVLETR 543
Cdd:PRK12444 598 VIGDKEMENGAVNVRKYGEEKSEVielDMFVESIKEEIKNR 638
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
110-519 |
1.84e-99 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 314.53 E-value: 1.84e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 110 DYRALGTAQDLFTTSIYSPGSPLFL-PNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYevr 188
Cdd:PLN02837 218 DHRRLGQDLDLFSIQDDAGGGLVFWhPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMY--- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 189 grgatgeaDGEAGEDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCR 268
Cdd:PLN02837 295 --------DQMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 269 PQQIKGEIASALGFVDMVMTTFGLGPYRLVLSTRPEKDfIGSLELWDSAEAQLREALDNSGREWAMNEGDGAFYGPKIDI 348
Cdd:PLN02837 367 EDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKS-VGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 349 QLQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEedynpatpgRATPVLVHRANFGSLERFLALLIEQYAGRWPFWLSP 428
Cdd:PLN02837 446 KIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSE---------KKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAP 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 429 RQGIILTVNQDEavLKQAQEAAAKI--SGFRPLVAGKDKaspkplssvdstflidvdtssqtLGKKIQRAKQMKYNLIFI 506
Cdd:PLN02837 517 VQARVLPVTDNE--LEYCKEVVAKLkaKGIRAEVCHGER-----------------------LPKLIRNAETQKIPLMAV 571
|
410
....*....|...
gi 1475578741 507 LGPKDIADSSVTV 519
Cdd:PLN02837 572 VGPKEVETRTLTV 584
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
202-418 |
1.45e-40 |
|
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: 145.25 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 202 EDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSGLTRVRRFHQDDGHIFCRPQQIKGEIASALG 281
Cdd:pfam00587 7 NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 282 FVDMVMTTFGLGPYRLVLSTRPEkdfigslelwdsaeaqlrealdnsgrewamnegdGAFYGPKIDIQLQDQA-GKYHQL 360
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSDG----------------------------------SAFYGPKLDFEVVFPSlGKQRQT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475578741 361 STIQLDM-NLPQRFGLEYQVAEGEEDynpatpgraTPVLVHRANFGsLERFLALLIEQY 418
Cdd:pfam00587 133 GTIQNDGfRLPRRLGIRYKDEDNESK---------FPYMIHRAGLG-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 ... |
142-415 |
1.38e-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: 108.25 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 142 NRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVrgrgatgEADGEAGEDESYGLKPMNCPGHCLLFK 221
Cdd:cd00670 6 RALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTF-------EDKGRELRDTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 222 SQNHSYRELPIRYADFSPLHRNEVSGSlSGLTRVRRFHQDDGHIFCRPQQIKGEIASALGFVDMVMTTFGLgPYRLVLST 301
Cdd:cd00670 79 GEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 302 RPEKdFIGSlelwdsaeaqlrealdnsgrewamNEGDGAFYGPKIDIQLQDQAGKYH-QLSTIQLDMNLPQRFGLEYQVA 380
Cdd:cd00670 157 DPFF-GRGG------------------------KRGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFKIDE 211
|
250 260 270
....*....|....*....|....*....|....*
gi 1475578741 381 EGEedynpatpGRATPVLVhraNFGSLERFLALLI 415
Cdd:cd00670 212 DGG--------GRAHTGCG---GAGGEERLVLALL 235
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
126-521 |
1.08e-20 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 96.09 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 126 YSPGSPL----FLPNGahvinRLISFLRTQY-----LQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVrgrgatgea 196
Cdd:PRK03991 211 YEPASDVghmrYYPKG-----RLIRDLLEDYvynlvVELGAMPVETPIMYDLSHPAIREHADKFGERQYRV--------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 197 dgEAGEDEsYGLKPMNCPGHCLLFKSQNHSYRELPIR-Y--ADFSplHRNEVSGSLSGLTRVRRFHQDDGHIFCRpqQIK 273
Cdd:PRK03991 277 --KSDKKD-LMLRFAACFGQFLMLKDMTISYKNLPLKmYelSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCK--DME 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 274 GEIASALGFVDMVMTT---FGLgPYRLVLstRPEKDFigslelWDSAEAQLREALDNSGRE-----WamnegDGAFY--G 343
Cdd:PRK03991 350 QAMEEFEKQYEMILETgedLGR-DYEVAI--RFTEDF------YEENKDWIVELVKREGKPvlleiL-----PERKHywV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 344 PKIDIQLQDQAGKYHQLSTIQLDMNLPQRFGLEYQVAEGEEDYnpatpgratPVLVHRANFGSLERFL-ALL----IEQY 418
Cdd:PRK03991 416 LKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKY---------PIILHCSPTGSIERVIyALLekaaKEEE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 419 AG---RWPFWLSPRQGIILTVNqdEAVLKQAQEAAAKI--SGFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKI 493
Cdd:PRK03991 487 EGkvpMLPTWLSPTQVRVIPVS--ERHLDYAEEVADKLeaAGIR----------------------VDVDDRDESLGKKI 542
|
410 420
....*....|....*....|....*...
gi 1475578741 494 QRAKQMKYNLIFILGPKDIADSSVTVDV 521
Cdd:PRK03991 543 RDAGKEWIPYVVVIGDKEMESGKLTVTI 570
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
140-390 |
6.51e-20 |
|
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: 88.33 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 140 VINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWqnyKDDMYEVRGRgatgeadgeagEDESYGLKPMNCPGHCLL 219
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE---PKDLLPVGAE-----------NEEDLYLRPTLEPGLVRL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 220 FKSQNhsyRELPIRYADFSPLHRNEVSGSlsGLTRVRRFHQDDGHIFCRPQQIKGEIASALGFV-DMVMTTFGLGPYRLV 298
Cdd:cd00768 67 FVSHI---RKLPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTeELLRALGIKLDIVFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 299 LSTRPEKdfigslelwdsaeaqlrealdnsgrewamnegDGAFYGPKIDIQLQDQAGKYHQLSTIQLDMNLP-QRFGLEY 377
Cdd:cd00768 142 EKTPGEF--------------------------------SPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQaRAADLYF 189
|
250
....*....|...
gi 1475578741 378 QVAEGEEDYNPAT 390
Cdd:cd00768 190 LDEALEYRYPPTI 202
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
428-519 |
7.47e-10 |
|
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: 55.97 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 428 PRQGIILTVNqdEAVLKQAQEAAAKIS--GFRplvagkdkaspkplssvdstflIDVDTSSQTLGKKIQRAKQMKYNLIF 505
Cdd:cd00860 1 PVQVVVIPVT--DEHLDYAKEVAKKLSdaGIR----------------------VEVDLRNEKLGKKIREAQLQKIPYIL 56
|
90
....*....|....
gi 1475578741 506 ILGPKDIADSSVTV 519
Cdd:cd00860 57 VVGDKEVETGTVSV 70
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
125-266 |
5.81e-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 prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 51.04 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 125 IYSPGSPLF--LPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVRGRGatgeadgeage 202
Cdd:cd00779 16 IRQTSSGLYswLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRH----------- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475578741 203 DESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLsGLTRVRRFHQDDGHIF 266
Cdd:cd00779 85 GKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSF 147
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
478-519 |
2.53e-05 |
|
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: 42.96 E-value: 2.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1475578741 478 FLIDVDTSSQTLGKKIQRAKQMKYNLIFILGPKDIADSSVTV 519
Cdd:pfam03129 30 IRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTV 71
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
126-415 |
1.34e-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: 43.74 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 126 YSP--GSPLFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEV-SGHWQNYKDDMYEV-RGrgatgeadGEAG 201
Cdd:cd00778 18 YGPvkGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKeKEHIEGFAPEVAWVtHG--------GLEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 202 EDESYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSGSLSgLTRVRRFHQDDGH-IFCRPQQIKGEIASAL 280
Cdd:cd00778 90 LEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRP-FLRTREFLWQEGHtAHATEEEAEEEVLQIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 281 GFVDMVMTTFGLGPYrlVLSTRPEKD-FIGSLELWDSaeaqlrEALDNSGRewAMnegdgafygpkidiqlqdQAGKYHQ 359
Cdd:cd00778 169 DLYKEFYEDLLAIPV--VKGRKTEWEkFAGADYTYTI------EAMMPDGR--AL------------------QSGTSHN 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1475578741 360 LSTiqldmNLPQRFGLEYQVAEGEEDYnpatpgratpvlVHRANFGSLERFLALLI 415
Cdd:cd00778 221 LGQ-----NFSKAFDIKYQDKDGQKEY------------VHQTSWGISTRLIGAII 259
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
126-310 |
1.18e-03 |
|
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: 41.20 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 126 YSPGSPL--FLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSG-HWQNYKDDMYEVRGRGatgeaDGEAGE 202
Cdd:cd00772 18 QGPGRGIinFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFKDAG-----DEELEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 203 DesYGLKPMNCPGHCLLFKSQNHSYRELPIRYADFSPLHRNEVSgSLSGLTRVRRFHQDDGHIF-CRPQQIKGEIASALG 281
Cdd:cd00772 93 D--FALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLS 169
|
170 180
....*....|....*....|....*....
gi 1475578741 282 FVDMVMTTFGLGPYRLVLSTRPEKdFIGS 310
Cdd:cd00772 170 AYAEIARDLAAIDFIEGEADEGAK-FAGA 197
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
139-331 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 139 HVINRLISFLRtqylQYGFREVLTPTIYKRSLWEVSGHWQNYKdDMYEVRGRGatgeadgeageDESYGLKPMNCPGHCL 218
Cdd:cd00773 7 YIEDTLREVFE----RYGYEEIDTPVFEYTELFLRKSGDEVSK-EMYRFKDKG-----------GRDLALRPDLTAPVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 219 LFkSQNHSYRELPIRYADFSPLHRNEVSGSLsgltRVRRFHQDDGHIFCRPQQIKgeIASALGFVDMVMTTFGLGPYRLV 298
Cdd:cd00773 71 AV-AENLLSLPLPLKLYYIGPVFRYERPQKG----RYREFYQVGVEIIGSDSPLA--DAEVIALAVEILEALGLKDFQIK 143
|
170 180 190
....*....|....*....|....*....|....
gi 1475578741 299 LSTR-PEKDFIGSLELWDSAEAQLREALDNSGRE 331
Cdd:cd00773 144 INHRgILDGIAGLLEDREEYIERLIDKLDKEALA 177
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
156-259 |
2.04e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 40.77 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 156 GFREVLTPTIYKRSLWEVSGH--------------------WQNYKDDMY---EVrgrgaTGEADGEAGEDESYGLKPMN 212
Cdd:PRK00960 242 GFDECLFPKLIPLEVMYKMRYleglpegmyyvcppkrdpeyFEEFVDEMMvkkEV-----PIEKLKEKLRDPGYVLAPAQ 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1475578741 213 CPGHCLLFKSQNHSYRELPIRYADFS-PLHRNEvSGSLSGLTRVRRFH 259
Cdd:PRK00960 317 CEPFYQFFQGETVDVDELPIKFFDRSgWTYRWE-GGGAHGLERVNEFH 363
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
125-234 |
3.68e-03 |
|
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: 40.14 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 125 IYSpgsplFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVRGRGatgeadgeageDE 204
Cdd:COG0442 39 IYT-----YLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVTDRL-----------ER 102
|
90 100 110
....*....|....*....|....*....|....
gi 1475578741 205 SYGLkpmnCPGH----CLLFKSQNHSYRELPIRY 234
Cdd:COG0442 103 EFCL----GPTHeeviTDLVRNEIKSYRDLPLLL 132
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
423-521 |
3.87e-03 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 39.83 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 423 PFWLSPRQGIILTVNQDeaVLKQAQEAAAKISGFRPLVagkdkaspkplssvdstfliDVDTSSQTLGKKIQRAKQMKYN 502
Cdd:PRK14938 269 PDWLNPIQVRILPVKKD--FLDFSIQVAERLRKEGIRV--------------------NVDDLDDSLGNKIRRAGTEWIP 326
|
90
....*....|....*....
gi 1475578741 503 LIFILGPKDIADSSVTVDV 521
Cdd:PRK14938 327 FVIIIGEREVKTSTLTVKI 345
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
125-232 |
8.61e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 38.69 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475578741 125 IYSpgsplFLPNGAHVINRLISFLRTQYLQYGFREVLTPTIYKRSLWEVSGHWQNYKDDMYEVRGR-------GATGEad 197
Cdd:PRK12325 39 IYS-----WLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLRIKDRhdremlyGPTNE-- 111
|
90 100 110
....*....|....*....|....*....|....*
gi 1475578741 198 gEAGEDesyglkpmncpghclLFKSQNHSYRELPI 232
Cdd:PRK12325 112 -EMITD---------------IFRSYVKSYKDLPL 130
|
|
| |
