|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
112-771 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1070.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 112 PSFIEDRLKLYETLKKEHDALLAyRAANEtkPIKITLTDGKIADGESWKTTPYQLAVGISQGLASNAVIAKVNGELWDLD 191
Cdd:PLN02908 23 SAVIKKRIELFEKIQARQLARLE-SAGGD--PIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVDGVLWDMT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 192 RPLEGDCTLELLTFDDQEAQAVYWHSSAHILGEAMEGYYGGCLCYGPPIEN--GFYYDMYIEDRGVSSTEFPALENRCKN 269
Cdd:PLN02908 100 RPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 270 IIKEKQPFERLEVKKEILLDMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGK 349
Cdd:PLN02908 180 AVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 350 ADMETLQRIYGISFPDNKMMKEWEKFQEEARNRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFLYNTLTDFIREEYHRRN 429
Cdd:PLN02908 260 VDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 430 FTEVVSPNIFNSKLWETSGHWQHYSENMFSFEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGT 509
Cdd:PLN02908 340 YDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 510 LSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCLDFLKSVYSIFGFTFQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGV 589
Cdd:PLN02908 420 LTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 590 QWTLNPGDGAFYGPKIDIKIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDGDDKKRPVIIHRAVLGSVERMIAILAENY 669
Cdd:PLN02908 500 PWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMFAILLEHY 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 670 GGKWPFWLSPRQVMVVPVGPTSEEYAQQVCSEFFEAGFMSDVDLDQScTLNKKIRNAQLAQYNFILVVGEKEKANHAVNV 749
Cdd:PLN02908 580 AGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEAATGTVNV 658
|
650 660
....*....|....*....|..
gi 2099396949 750 RTRDNKVHGEISVSSAIEKLKK 771
Cdd:PLN02908 659 RTRDNVVHGEKKIEELLTEFKE 680
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
144-771 |
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: 890.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 144 IKITLTDGKIADGESwKTTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELLTFDDQEAQAVYWHSSAHILG 223
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 224 EAMEGYYGGC-LCYGPPIENGFYYDMYIEdRGVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKY--NKFKCRI 300
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 301 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMMKEWEKFQEEAR 380
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 381 NRDHRKIGKEQELFFFHD-LSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFS 459
Cdd:COG0441 240 KRDHRKLGKELDLFHFQEeVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 460 FEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKG 539
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 540 CLDFLKSVYSIFGFT-FQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDIKIKDALGRYHQ 618
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 619 CATIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVPVGPTSEEYAQQV 698
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099396949 699 CSEFFEAGFMSDVDLdQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIEKLKK 771
Cdd:COG0441 559 AKKLRAAGIRVEVDL-RNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
215-771 |
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: 672.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 215 WHSSAHILGEA-MEGYYGGCLCYGPPIENGFYYDMYIeDRGVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKY 293
Cdd:TIGR00418 1 RHSIAHLLAEAlKQLYPDVKLAIGPVVEDGFYYDFEL-DRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 294 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMMKE 371
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 372 WEKFQEEARNRDHRKIGKEQELFFFHDLS-PGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHW 450
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 451 QHYSENMFSF-EIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCT 529
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 530 IEQIEEEIKGCLDFLKSVYSIFGFTF-QLHLSTR-PENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDI 607
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 608 KIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVPV 687
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 688 GPTSEEYAQQVCSEFFEAGFMSDVDlDQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIE 767
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 2099396949 768 KLKK 771
Cdd:TIGR00418 558 KLRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
382-679 |
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: 525.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 382 RDHRKIGKEQELFFFHDLSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFSFE 461
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 462 IEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCL 541
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 542 DFLKSVYSIFGFT-FQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDIKIKDALGRYHQCA 620
Cdd:cd00771 161 DLIKEVYSDFGFFdYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099396949 621 TIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSP 679
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
458-669 |
1.94e-37 |
|
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: 138.31 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 458 FSFEIE-KETFALKPMNCPGHCLMFA-HRPRSWReMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEE 535
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 536 EIKGCLDFLKSVYSIFGFTFQ-LHLSTRPENylgeleiwdhaekqlqnsldnfgvqwtlnpgdgAFYGPKIDIKIKD-AL 613
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEVVFpSL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099396949 614 GRYHQCATIQLD-FQLPIRFNLTYVGKDgDDKKRPVIIHRAVLGsVERMIAILAENY 669
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
311-358 |
1.47e-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: 62.40 E-value: 1.47e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2099396949 311 TVYRCGPL-IDLCRGPHVRHTGKIKALKIFKNSSTYWEgkadmetLQRI 358
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
112-771 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1070.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 112 PSFIEDRLKLYETLKKEHDALLAyRAANEtkPIKITLTDGKIADGESWKTTPYQLAVGISQGLASNAVIAKVNGELWDLD 191
Cdd:PLN02908 23 SAVIKKRIELFEKIQARQLARLE-SAGGD--PIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVDGVLWDMT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 192 RPLEGDCTLELLTFDDQEAQAVYWHSSAHILGEAMEGYYGGCLCYGPPIEN--GFYYDMYIEDRGVSSTEFPALENRCKN 269
Cdd:PLN02908 100 RPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKPIEARAEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 270 IIKEKQPFERLEVKKEILLDMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGK 349
Cdd:PLN02908 180 AVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 350 ADMETLQRIYGISFPDNKMMKEWEKFQEEARNRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFLYNTLTDFIREEYHRRN 429
Cdd:PLN02908 260 VDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIREQYWERG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 430 FTEVVSPNIFNSKLWETSGHWQHYSENMFSFEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGT 509
Cdd:PLN02908 340 YDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 510 LSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCLDFLKSVYSIFGFTFQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGV 589
Cdd:PLN02908 420 LTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 590 QWTLNPGDGAFYGPKIDIKIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDGDDKKRPVIIHRAVLGSVERMIAILAENY 669
Cdd:PLN02908 500 PWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMFAILLEHY 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 670 GGKWPFWLSPRQVMVVPVGPTSEEYAQQVCSEFFEAGFMSDVDLDQScTLNKKIRNAQLAQYNFILVVGEKEKANHAVNV 749
Cdd:PLN02908 580 AGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEAATGTVNV 658
|
650 660
....*....|....*....|..
gi 2099396949 750 RTRDNKVHGEISVSSAIEKLKK 771
Cdd:PLN02908 659 RTRDNVVHGEKKIEELLTEFKE 680
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
144-771 |
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: 890.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 144 IKITLTDGKIADGESwKTTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELLTFDDQEAQAVYWHSSAHILG 223
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 224 EAMEGYYGGC-LCYGPPIENGFYYDMYIEdRGVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKY--NKFKCRI 300
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 301 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMMKEWEKFQEEAR 380
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 381 NRDHRKIGKEQELFFFHD-LSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFS 459
Cdd:COG0441 240 KRDHRKLGKELDLFHFQEeVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 460 FEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKG 539
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 540 CLDFLKSVYSIFGFT-FQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDIKIKDALGRYHQ 618
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 619 CATIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVPVGPTSEEYAQQV 698
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099396949 699 CSEFFEAGFMSDVDLdQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIEKLKK 771
Cdd:COG0441 559 AKKLRAAGIRVEVDL-RNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
215-771 |
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: 672.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 215 WHSSAHILGEA-MEGYYGGCLCYGPPIENGFYYDMYIeDRGVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKY 293
Cdd:TIGR00418 1 RHSIAHLLAEAlKQLYPDVKLAIGPVVEDGFYYDFEL-DRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 294 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMMKE 371
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 372 WEKFQEEARNRDHRKIGKEQELFFFHDLS-PGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHW 450
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 451 QHYSENMFSF-EIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCT 529
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 530 IEQIEEEIKGCLDFLKSVYSIFGFTF-QLHLSTR-PENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDI 607
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 608 KIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVPV 687
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 688 GPTSEEYAQQVCSEFFEAGFMSDVDlDQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIE 767
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 2099396949 768 KLKK 771
Cdd:TIGR00418 558 KLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
144-771 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 651.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 144 IKITLTDGKIADGESwKTTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELLTFDDQEAQAVYWHSSAHILG 223
Cdd:PRK12444 6 IEIKFPDGSVKEFVK-GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 224 EAMEGYYGGC-LCYGPPIENGFYYDMYIEdRGVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKYN--KFKCRI 300
Cdd:PRK12444 85 QAVKRLYGDVnLGVGPVIENGFYYDMDLP-SSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndRLKLEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 301 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMMKEWEKFQEEAR 380
Cdd:PRK12444 164 LEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 381 NRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFSF 460
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 461 EIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKGC 540
Cdd:PRK12444 324 EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 541 LDFLKSVYSIFGFTFQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDIKIKDALGRYHQCA 620
Cdd:PRK12444 404 MAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 621 TIQLDFQLPIRFNLTYVGKDgDDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVPVG-PTSEEYAQQVC 699
Cdd:PRK12444 484 TIQLDFQMPEKFDLNYIDEK-NEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSnAVHVQYADEVA 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099396949 700 SEFFEAGFMSDVDLDQScTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIEKLKK 771
Cdd:PRK12444 563 DKLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
382-679 |
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: 525.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 382 RDHRKIGKEQELFFFHDLSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFSFE 461
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 462 IEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCL 541
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 542 DFLKSVYSIFGFT-FQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKIDIKIKDALGRYHQCA 620
Cdd:cd00771 161 DLIKEVYSDFGFFdYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099396949 621 TIQLDFQLPIRFNLTYVGKDGdDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSP 679
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
216-770 |
1.12e-148 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 448.96 E-value: 1.12e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 216 HSSAHILGEAMEGYYGGC-LCYGPPIENGFYYDMYIEDrgVSSTEFPALENRCKNIIKEKQPFERLEVKKEILLDMFKY- 293
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAkVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 294 -NKFKCRILnEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKI--KALKIFKNSSTYWEGKADMETLQRIYGISFPDNKMM 369
Cdd:PLN02837 126 nEPYKLEIL-EGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 370 KEWEKFQEEARNRDHRKIGKEQELFFFHDLSPGS-CFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSG 448
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 449 HWQHYSENMFS-FEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIF 527
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 528 CTIEQIEEEIKGCLDFLKSVYSIFGFT-FQLHLSTRPENYLGELEIWDHAEKQLQNSLDNFGVQWTLNPGDGAFYGPKID 606
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 607 IKIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDgDDKKRPVIIHRAVLGSVERMIAILAENYGGKWPFWLSPRQVMVVP 686
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 687 VGPTSEEYAQQVCSEFFEAGFMSDVDLDQSctLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSSAI 766
Cdd:PLN02837 524 VTDNELEYCKEVVAKLKAKGIRAEVCHGER--LPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFI 601
|
....
gi 2099396949 767 EKLK 770
Cdd:PLN02837 602 NRIQ 605
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
369-778 |
1.68e-42 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 163.89 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 369 MKEWEKFQEEARNRDHRKIGKEQELFFFHDLS-PGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETS 447
Cdd:PRK03991 184 DYEVGKKELVGGEPPHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLSHPAIR 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 448 GHWQHYSENMFSFEIEKETFALKPMNCPGHCLMFAHRPRSWREMPLR---LADFGvlHRNELSGTLSGLTRVRRFQQDDA 524
Cdd:PRK03991 264 EHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDM 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 525 HIFC-----TIEQIEEEIKGCLDFLKSV----YSIFGFT---FQLHlstrpENYLGEL----------EIWDhaekqlqn 582
Cdd:PRK03991 342 HTLCkdmeqAMEEFEKQYEMILETGEDLgrdyEVAIRFTedfYEEN-----KDWIVELvkregkpvllEILP-------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 583 sldnfgvqwtlnpgDGAFYGP-KIDIKIKDALGRYHQCATIQLDFQLPIRFNLTYVGKDGDdKKRPVIIHRAVLGSVERM 661
Cdd:PRK03991 409 --------------ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGE-EKYPIILHCSPTGSIERV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 662 IAILAEN-----YGGK---WPFWLSPRQVMVVPVGPTSEEYAQQVCSEFFEAGFMSDVDlDQSCTLNKKIRNAQLAQYNF 733
Cdd:PRK03991 474 IYALLEKaakeeEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIPY 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2099396949 734 ILVVGEKEKANHAVNVRTRDNKVHGEISVSSAIEKLKK------FKSLRLP 778
Cdd:PRK03991 553 VVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEetkgypYRPLPLP 603
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
458-669 |
1.94e-37 |
|
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: 138.31 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 458 FSFEIE-KETFALKPMNCPGHCLMFA-HRPRSWReMPLRLADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTIEQIEE 535
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 536 EIKGCLDFLKSVYSIFGFTFQ-LHLSTRPENylgeleiwdhaekqlqnsldnfgvqwtlnpgdgAFYGPKIDIKIKD-AL 613
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEVVFpSL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099396949 614 GRYHQCATIQLD-FQLPIRFNLTYVGKDgDDKKRPVIIHRAVLGsVERMIAILAENY 669
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
679-770 |
6.38e-34 |
|
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: 124.92 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 679 PRQVMVVPVGPTSEEYAQQVCSEFFEAGFMSDVDLDqSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHG 758
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 2099396949 759 EISVSSAIEKLK 770
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
144-209 |
3.13e-26 |
|
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: 101.80 E-value: 3.13e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099396949 144 IKITLTDGKIADGESwKTTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELLTFDDQE 209
Cdd:cd01667 1 IKITLPDGSVKEFPK-GTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| 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 ... |
410-665 |
7.10e-25 |
|
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: 104.01 E-value: 7.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 410 GAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFSFEIEKET-----FALKPMNCPGHCLMFAHR 484
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtdLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 485 PRSWREMPLRLADFGVLHRNELSGTlSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCLDFLKSVYSIFGFTFQLHLSTRPE 564
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 565 NYLGEleiwdhaekqlqnsldnfgvqwtlNPGDGAFYGPKIDIKIKDAL-GRYHQCATIQLDFQLPIRFNLTYVGKDGDD 643
Cdd:cd00670 160 FGRGG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|..
gi 2099396949 644 KKrPVIIHRAvlGSVERMIAIL 665
Cdd:cd00670 216 RA-HTGCGGA--GGEERLVLAL 234
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
681-771 |
3.98e-23 |
|
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: 94.19 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 681 QVMVVPVGPTSE---EYAQQVCSEFFEAGFMSDVDlDQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNKVH 757
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....
gi 2099396949 758 GEISVSSAIEKLKK 771
Cdd:pfam03129 80 ETVSLDELVEKLKE 93
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
144-204 |
2.94e-16 |
|
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: 73.35 E-value: 2.94e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099396949 144 IKITLTDGKIADGESWkTTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELLT 204
Cdd:pfam02824 1 IRVYTPDGKVPDLPRG-ATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
420-661 |
9.09e-15 |
|
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: 74.08 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 420 FIREEYHRRNFTEVVSPNIFNSKLWETSGHWqhYSENMFSFEIEKETFALKPMNCPGHCLMFAHRPRSwreMPLRLADFG 499
Cdd:cd00768 8 KLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRK---LPLRLAEIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 500 VLHRNElsGTLSGLTRVRRFQQDDAHIFCTIEQIEEEIKGCLDFLksvYSIFGFTFQLHLSTRPENYLGELEIwdhaekq 579
Cdd:cd00768 83 PAFRNE--GGRRGLRRVREFTQLEGEVFGEDGEEASEFEELIELT---EELLRALGIKLDIVFVEKTPGEFSP------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 580 lqnsldnfgvqwtlnpgdgAFYGPKIDIKIKDALGRYHQCATIQLDFQLPIR-FNLTYVGKDGDDKKrPVIIHRAvlGSV 658
Cdd:cd00768 151 -------------------GGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRY-PPTIGFG--LGL 208
|
...
gi 2099396949 659 ERM 661
Cdd:cd00768 209 ERL 211
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
311-358 |
1.47e-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: 62.40 E-value: 1.47e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2099396949 311 TVYRCGPL-IDLCRGPHVRHTGKIKALKIFKNSSTYWEgkadmetLQRI 358
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
311-358 |
3.05e-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: 55.91 E-value: 3.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2099396949 311 TVYRCGPL-IDLCRGPHVRHTGKIKALKIFKnsstyWEGKADMetLQRI 358
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-----GESKNKG--LRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
674-778 |
4.91e-07 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 52.92 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 674 PFWLSPRQVMVVPVGPTSEEYAQQVCSEFFEAGFMSDV-DLDQSctLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTR 752
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVdDLDDS--LGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
90 100
....*....|....*....|....*.
gi 2099396949 753 DNKVHGEISVSSAIEKLKKFKSLRLP 778
Cdd:PRK14938 347 ANNEQKSMTVEELVKEIKRADELKER 372
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
626-774 |
3.71e-06 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 50.47 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 626 FQLPIR----FNLTYVGKDGddKKRPVIihravLGS----VERMIAILAE-NY---GGKWPFWLSPRQVMVVPVGPTSE- 692
Cdd:PRK09194 410 FQLGTKyseaMNATVLDENG--KAQPLI-----MGCygigVSRLVAAAIEqNHdekGIIWPKAIAPFDVHIVPVNMKDEe 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 693 --EYAQQVCSEFFEAGFmsDVDLDqsctlNKKIR------NAQLAQYNFILVVGEKEKANHAVNVRTRDNKVHGEISVSS 764
Cdd:PRK09194 483 vkELAEKLYAELQAAGI--EVLLD-----DRKERpgvkfaDADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDE 555
|
170
....*....|
gi 2099396949 765 AIEKLKKFKS 774
Cdd:PRK09194 556 LVEFLKALKK 565
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
679-770 |
5.00e-06 |
|
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: 45.47 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 679 PRQVMVVP-VGPTSE--EYAQQVCSEFFEAGFMSDVDLDQScTLNKKIRNAQLAQYNFILVVGEKEKANHAVNVRTRDNK 755
Cdd:cd00738 1 PIDVAIVPlTDPRVEarEYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 2099396949 756 VHGEISVSSAIEKLK 770
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
399-527 |
1.76e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. 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: 47.19 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 399 LSPGSCFFLPRGAFLYNTLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGHWQHYSENMFSFEIEKE-TFALKPMNCPGH 477
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGkEFLLGPTHEEVI 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2099396949 478 CLMFAHRPRSWREMPLRLADFGVLHRNELSgTLSGLTRVRRFQQDDAHIF 527
Cdd:cd00779 99 TDLVANEIKSYKQLPLNLYQIQTKFRDEIR-PRFGLMRGREFLMKDAYSF 147
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
402-568 |
3.57e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 46.21 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 402 GSCFFLPRGAFLYntltDFIREEYHRRnFTEVVSPNIFNS-----KLWETSG-HWQHYSENMFSF-----EIEKETFALK 470
Cdd:cd00772 23 GIINFLPLAKAIL----DKIENVLDKM-FKEHGAQNALFPffilaSFLEKEAeHDEGFSKELAVFkdagdEELEEDFALR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 471 PMNCPGHCLMFAHRPRSWREMPLRLADFGVLHRNELSgTLSGLTRVRRFQQDDAHIF-CTIEQIEEEIKGCLDFLKSVYS 549
Cdd:cd00772 98 PTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIAR 176
|
170 180
....*....|....*....|
gi 2099396949 550 IFG-FTFQLHLSTRPENYLG 568
Cdd:cd00772 177 DLAaIDFIEGEADEGAKFAG 196
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
382-556 |
3.87e-04 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 43.76 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 382 RDHRKIGKEQELFFFH---DLSPGSCFFLPRGAFLYN-TLTDFIREEYHRRNFTEVVSPNIFNSKLWETSGhWQHYSENM 457
Cdd:PLN02320 200 KDHLQLGKELDLFDFDaaaEVSGSKFYYLKNEAVLLEmALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCG-FQPRGDNT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 458 FSFEIEKETFAL-KPMNCP-GHCLMFAHRPRSwrEMPLRLADFGVLHRNE--LSGTLS-GLTRVRRFQQDDAHIFCTIEQ 532
Cdd:PLN02320 279 QVYSIDGSDQCLiGTAEIPvGGIHMDSILLES--ALPLKYVAFSHCFRTEagAAGAATrGLYRVHQFSKVEMFVICRPEE 356
|
170 180
....*....|....*....|....
gi 2099396949 533 IEEEIKGCLDFLKSVYSIFGFTFQ 556
Cdd:PLN02320 357 SESFHEELIQIEEDLFTSLGLHFK 380
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
681-770 |
6.86e-04 |
|
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: 39.45 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 681 QVMVVPVGPTSEEYAQQVCSEFFEAGFMSDVDLdqsctLNKKIRnAQLAQYN-----FILVVGEKEKANHAVNVrtRDNK 755
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK-KQFKYADrsgarFAVILGEDELAAGVVTV--KDLE 74
|
90
....*....|....*..
gi 2099396949 756 VHGEISVSSA--IEKLK 770
Cdd:cd00859 75 TGEQETVALDelVEELK 91
|
|
| TGS |
cd01616 |
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ... |
152-203 |
1.70e-03 |
|
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role.
Pssm-ID: 340455 [Multi-domain] Cd Length: 61 Bit Score: 37.20 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099396949 152 KIADGESWK----TTPYQLAVGISQGLASNAVIAKVNGELWDLDRPLEGDCTLELL 203
Cdd:cd01616 6 GKTPGTVFVmnkgATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKFL 61
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
674-771 |
8.57e-03 |
|
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: 38.43 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396949 674 PFWLSPRQVMVVPVGPTSE------EYAQQVCSEFFEAGFMSDVDLDQSCTLNKKIRNAQLAQYNFILVVGEKEKANHAV 747
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
90 100
....*....|....*....|....
gi 2099396949 748 NVRTRDNKVHGEISVSSAIEKLKK 771
Cdd:cd00862 85 VIVRRDTGEKKTVPLAELVEKVPE 108
|
|
| |
