|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
79-740 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1101.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 79 LPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRV 158
Cdd:PLN02908 22 LSAVIKKRIELFEKIQARQLARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVDGVLWDMTRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 159 LEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIEN--GFYYDMHLEGEGISTNDYGAMEGLVKQIV 236
Cdd:PLN02908 102 LEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEKAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 237 KEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKAD 316
Cdd:PLN02908 182 KEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 317 AETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQ 396
Cdd:PLN02908 262 RESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 397 EVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALT 476
Cdd:PLN02908 342 EVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 477 GLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPW 556
Cdd:PLN02908 422 GLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPW 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 557 KENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKK-RPVIIHRAILGSVERMIAILTENFAG 635
Cdd:PLN02908 502 QLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMFAILLEHYAG 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 636 KWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFmsEADCDAGD-TMNKKIRNAQLAQFNFILVVGDKERSSNTVNVR 714
Cdd:PLN02908 582 KWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGF--YVDVDVTDrKIQKKVREAQLAQYNYILVVGEAEAATGTVNVR 659
|
650 660
....*....|....*....|....*.
gi 24583839 715 TRDNKVHGEVSVAELITKLQKIRDEF 740
Cdd:PLN02908 660 TRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
109-735 |
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: 907.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 109 IKVTLPDG--KQVDAtswETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHI 186
Cdd:COG0441 2 IKITLPDGsvREFEA---GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 187 MGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY--NEFKV 263
Cdd:COG0441 79 LAQAVKRLYPDaKLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 264 RILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEE 343
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 344 AAKRDHRKIGREQELFFFH-ELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENM 422
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 423 FSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEM 502
Cdd:COG0441 318 FPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 503 KGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRA 581
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 582 HQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQS 661
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583839 662 VRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 735
Cdd:COG0441 558 VAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
180-735 |
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: 691.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 180 WHSSAHIMGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY 258
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELD-RSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 259 NE-FKVRILNEKVTTDRTTVYKCG-SLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKE 336
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 337 WEKLQEEAAKRDHRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHW 415
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 416 QHYAENMFSFEAEKEK-FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 494
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 495 PEQIKSEMKGCLEFLKYVYTIFGFSFQLV-LSTR-PDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDI 572
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 573 TIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVG 652
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 653 PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITK 732
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEK 558
|
...
gi 24583839 733 LQK 735
Cdd:TIGR00418 559 LRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
347-643 |
0e+00 |
|
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: 541.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 347 RDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFE 426
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 427 AEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCL 506
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 507 EFLKYVYTIFGF-SFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 585
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24583839 586 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSP 643
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
423-633 |
1.68e-41 |
|
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: 149.48 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 423 FSFEAE-KEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSE 501
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 502 MKGCLEFLKYVYTIFGFSFQ-LVLSTRPDNylgeleqwndaekalaeslnefgmpwkenpgdgAFYGPKIDIT-IMDALK 579
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEvVFPSLG 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24583839 580 RAHQCATIQLD-FQLPIRFNLSYIADDGEKKRPVIIHRAILGsVERMIAILTENF 633
Cdd:pfam00587 128 KQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
276-323 |
1.74e-12 |
|
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: 62.01 E-value: 1.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24583839 276 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKNSSTYWEgkadaetLQRV 323
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
79-740 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1101.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 79 LPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRV 158
Cdd:PLN02908 22 LSAVIKKRIELFEKIQARQLARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVDGVLWDMTRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 159 LEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIEN--GFYYDMHLEGEGISTNDYGAMEGLVKQIV 236
Cdd:PLN02908 102 LEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEKAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 237 KEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKAD 316
Cdd:PLN02908 182 KEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 317 AETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQ 396
Cdd:PLN02908 262 RESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 397 EVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALT 476
Cdd:PLN02908 342 EVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 477 GLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPW 556
Cdd:PLN02908 422 GLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPW 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 557 KENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKK-RPVIIHRAILGSVERMIAILTENFAG 635
Cdd:PLN02908 502 QLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMIHRAILGSVERMFAILLEHYAG 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 636 KWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFmsEADCDAGD-TMNKKIRNAQLAQFNFILVVGDKERSSNTVNVR 714
Cdd:PLN02908 582 KWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGF--YVDVDVTDrKIQKKVREAQLAQYNYILVVGEAEAATGTVNVR 659
|
650 660
....*....|....*....|....*.
gi 24583839 715 TRDNKVHGEVSVAELITKLQKIRDEF 740
Cdd:PLN02908 660 TRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
109-735 |
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: 907.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 109 IKVTLPDG--KQVDAtswETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHI 186
Cdd:COG0441 2 IKITLPDGsvREFEA---GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 187 MGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY--NEFKV 263
Cdd:COG0441 79 LAQAVKRLYPDaKLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 264 RILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEE 343
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 344 AAKRDHRKIGREQELFFFH-ELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENM 422
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 423 FSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEM 502
Cdd:COG0441 318 FPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 503 KGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRA 581
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 582 HQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQS 661
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583839 662 VRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 735
Cdd:COG0441 558 VAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
180-735 |
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: 691.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 180 WHSSAHIMGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY 258
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELD-RSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 259 NE-FKVRILNEKVTTDRTTVYKCG-SLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKE 336
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 337 WEKLQEEAAKRDHRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHW 415
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 416 QHYAENMFSFEAEKEK-FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 494
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 495 PEQIKSEMKGCLEFLKYVYTIFGFSFQLV-LSTR-PDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDI 572
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 573 TIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVG 652
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 653 PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITK 732
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEK 558
|
...
gi 24583839 733 LQK 735
Cdd:TIGR00418 559 LRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
109-735 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 659.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 109 IKVTLPDGkQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMG 188
Cdd:PRK12444 6 IEIKFPDG-SVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 189 EAMERIYGG-HLCYGPPIENGFYYDMHLeGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNE--FKVRI 265
Cdd:PRK12444 85 QAVKRLYGDvNLGVGPVIENGFYYDMDL-PSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNdrLKLEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 266 LNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAA 345
Cdd:PRK12444 164 LEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 346 KRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSF 425
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 426 EAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGC 505
Cdd:PRK12444 324 EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 506 LEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 585
Cdd:PRK12444 404 MAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 586 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPA-YDQYAQSVRD 664
Cdd:PRK12444 484 TIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVAD 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24583839 665 QLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 735
Cdd:PRK12444 564 KLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
347-643 |
0e+00 |
|
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: 541.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 347 RDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFE 426
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 427 AEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCL 506
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 507 EFLKYVYTIFGF-SFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 585
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24583839 586 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSP 643
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
181-734 |
4.61e-150 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 451.27 E-value: 4.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 181 HSSAHIMGEAMERIY-GGHLCYGPPIENGFYYDMHLEGegISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFK-Y 258
Cdd:PLN02837 48 HTCAHVMAMAVQKLFpDAKVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMaI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 259 NE-FKVRILnEKVTTDRTTVYKCGS-LIDLCRGPHVRHTGKV--KALKITKNSSTYWEGKADAETLQRVYGISFPDPKQL 334
Cdd:PLN02837 126 NEpYKLEIL-EGIKEEPITIYHIGEeWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 335 KEWEKLQEEAAKRDHRKIGREQELFFFHELSPGS-CFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSG 413
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 414 HWQHYAENMFS-FEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 492
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 493 CAPEQIKSEMKGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKID 571
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 572 ITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPV 651
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPV 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 652 GPAYDQYAQSVRDQLHDAGFMSEAdCDaGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELIT 731
Cdd:PLN02837 525 TDNELEYCKEVVAKLKAKGIRAEV-CH-GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFIN 602
|
...
gi 24583839 732 KLQ 734
Cdd:PLN02837 603 RIQ 605
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
327-735 |
2.56e-50 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 186.23 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 327 SFPDPKQLKEWEKLQEEAAKRD--HRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNI 403
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 404 YNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRM---ADFGvlHRNELSGALTGLTR 480
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKMyelSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 481 VRRFQQDDAHIFC-----APEQIKSEMKGCLEFLK-----YVyTIFGFsfqlvlsTRpDNYlgelEQWNDAEKALAEsln 550
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEdlgrdYE-VAIRF-------TE-DFY----EENKDWIVELVK--- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 551 EFGMP-----WKEnpgdGAFYGP-KIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVER 624
Cdd:PRK03991 397 REGKPvlleiLPE----RKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 625 MIAILTENFA-----GK---WPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFN 696
Cdd:PRK03991 473 VIYALLEKAAkeeeeGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 24583839 697 FILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 735
Cdd:PRK03991 552 YVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKE 590
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
423-633 |
1.68e-41 |
|
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: 149.48 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 423 FSFEAE-KEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSE 501
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 502 MKGCLEFLKYVYTIFGFSFQ-LVLSTRPDNylgeleqwndaekalaeslnefgmpwkenpgdgAFYGPKIDIT-IMDALK 579
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEvVFPSLG 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24583839 580 RAHQCATIQLD-FQLPIRFNLSYIADDGEKKRPVIIHRAILGsVERMIAILTENF 633
Cdd:pfam00587 128 KQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
643-734 |
8.51e-37 |
|
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: 133.01 E-value: 8.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 643 PRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHG 722
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 24583839 723 EVSVAELITKLQ 734
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
375-630 |
1.45e-28 |
|
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: 114.41 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 375 GAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEK-----FALKPMNCPGHCLIFDNR 449
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtdLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 450 NRSWRELPLRMADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPD 529
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 530 nylgeleqwndaekalaeslneFGMPWKEnpGDGAFYGPKIDITIMDAL-KRAHQCATIQLDFQLPIRFNLSYIADDGEK 608
Cdd:cd00670 160 ----------------------FGRGGKR--GLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|..
gi 24583839 609 KRPVIIHRAilGSVERMIAILT 630
Cdd:cd00670 216 RAHTGCGGA--GGEERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
109-174 |
2.77e-25 |
|
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: 99.10 E-value: 2.77e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24583839 109 IKVTLPDGKQVDAtSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPE 174
Cdd:cd01667 1 IKITLPDGSVKEF-PKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
645-736 |
1.11e-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: 98.43 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 645 QVMVVPVGP---AYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVH 721
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 24583839 722 GEVSVAELITKLQKI 736
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
378-625 |
2.09e-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: 90.25 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 378 IYNTLMGFIKAeyrkRGFQEVISPNIYNAKLWMTSGHWqhYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSwreLP 457
Cdd:cd00768 5 IEQKLRRFMAE----LGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRK---LP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 458 LRMADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLstrpdnylgeLEQ 537
Cdd:cd00768 76 LRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIVF----------VEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 538 WNDAEKAlaeslnefgmpwkenpgdgAFYGPKIDITIMDALKRAHQCATIQLDFQLPIR-FNLSYIADDGEKKRPVIIHR 616
Cdd:cd00768 144 TPGEFSP-------------------GGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGF 204
|
....*....
gi 24583839 617 AIlgSVERM 625
Cdd:cd00768 205 GL--GLERL 211
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|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
109-169 |
1.43e-18 |
|
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: 79.90 E-value: 1.43e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24583839 109 IKVTLPDGKQVDATSWETtPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLK 169
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGAT-PEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
276-323 |
1.74e-12 |
|
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: 62.01 E-value: 1.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24583839 276 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKNSSTYWEgkadaetLQRV 323
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
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|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
276-323 |
1.23e-10 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 429764 [Multi-domain] Cd Length: 43 Bit Score: 57.07 E-value: 1.23e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24583839 276 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKnsstyweGKADAETLQRV 323
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-------GESKNKGLRRI 43
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|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
643-734 |
1.96e-08 |
|
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: 52.40 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 643 PRQVMVVPVG---PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNK 719
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 24583839 720 VHGEVSVAELITKLQ 734
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
638-735 |
5.93e-07 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 52.54 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 638 PFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRD 717
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRA 347
|
90
....*....|....*...
gi 24583839 718 NKVHGEVSVAELITKLQK 735
Cdd:PRK14938 348 NNEQKSMTVEELVKEIKR 365
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
645-734 |
7.35e-07 |
|
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: 47.53 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 645 QVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADCdagdtMNKKIRnaqlAQFN--------FILVVGDKERSSNTVNVR-- 714
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK----KQFKyadrsgarFAVILGEDELAAGVVTVKdl 73
|
90 100
....*....|....*....|
gi 24583839 715 TRDNKVhgEVSVAELITKLQ 734
Cdd:cd00859 74 ETGEQE--TVALDELVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
638-740 |
6.07e-05 |
|
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: 44.60 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 638 PFWLSPRQVMVVPVGPAYD------QYAQSVRDQLHDAGFMSEADCDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTV 711
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
90 100
....*....|....*....|....*....
gi 24583839 712 NVRTRDNKVHGEVSVAELITKLQKIRDEF 740
Cdd:cd00862 85 VIVRRDTGEKKTVPLAELVEKVPELLDEI 113
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
367-533 |
4.88e-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: 42.74 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 367 GSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSG-HWQHYAENMFSF-----EAEKEKFALKPMNCP 440
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 441 GHCLIFDNRNRSWRELPLRMADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCAP-EQIKSEMKGCLEFLKYVYTIFG-F 518
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHADaEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 24583839 519 SFQLVLSTRPDNYLG 533
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
362-492 |
5.84e-04 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 42.18 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583839 362 HELSPGSCFFQPRGAHIYNTL-MGF---------IKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEK 431
Cdd:cd00779 7 HKLLLRAGFIRQTSSGLYSWLpLGLrvlkkieniIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24583839 432 -FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALtGLTRVRRFQQDDAHIF 492
Cdd:cd00779 87 eFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSF 147
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