|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-594 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 647.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 255 KLLSA--------------------------------------------------------------------------- 259
Cdd:PLN02908 247 ACLKAssaywrgdvdreslqrvygisfpdkkllkeykhrieeakkrdhrllgqkqelfffhelspgscfflphgariynk 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 260 -------EYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 332
Cdd:PLN02908 327 lmdfireQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 333 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 412
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 413 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 489
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 490 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 537
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513864 538 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 594
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-589 |
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: 606.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS-----------------------------AEYAHR---- 264
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSvagaywrgdeknkmlqriygtafpkkkelDAYLHRleea 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 265 --------------------------------------------------GFSEVKTPTLFSTKLWEQSGHWEHYQEDMF 294
Cdd:COG0441 239 kkrdhrklgkeldlfhfqeevgpglpfwhpkgaiirreledyirekhrkaGYQEVKTPHILDRELWETSGHWDHYRENMF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 295 AVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQ 374
Cdd:COG0441 319 PTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 375 DDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAF 453
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 454 YGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQ 499
Cdd:COG0441 462 YGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafPLWLAPVQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 500 VVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWD 579
Cdd:COG0441 542 VVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMS 620
|
650
....*....|
gi 2462513864 580 LPEAVQRLVE 589
Cdd:COG0441 621 LDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-588 |
5.96e-145 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 430.98 E-value: 5.96e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLSAEYA-------------------------- 262
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAywrgdsknkmlqriygtawadkkqla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 263 -------------HR--------------------------------------------GFSEVKTPTLFSTKLWEQSGH 285
Cdd:TIGR00418 159 ayllrleeakkrdHRklgkelelfsfepeigpglpfwlpkgatirnlledfvrqkqikyGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 286 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 365
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 366 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 443
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 444 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 491
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 492 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 569
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 2462513864 570 RDNRRLGEWDLPEAVQRLV 588
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-492 |
3.28e-122 |
|
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: 363.02 E-value: 3.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 255 KLLSAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGsdrppssqsddstrhitDTLALKPMNCPAHCLMF 334
Cdd:cd00771 38 DFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEEED-----------------EEYGLKPMNCPGHCLIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 335 AHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALS 413
Cdd:cd00771 101 KSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513864 414 TRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 492
Cdd:cd00771 181 TRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 259
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
318-491 |
7.48e-27 |
|
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: 107.50 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 318 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 396
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 397 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 475
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 2462513864 476 QLD-FQLPLRFDLQYKG 491
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-262 |
5.71e-07 |
|
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: 46.22 E-value: 5.71e-07
10 20 30
....*....|....*....|....*....|....*
gi 2462513864 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSAEYA 262
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGA 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-594 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 647.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 255 KLLSA--------------------------------------------------------------------------- 259
Cdd:PLN02908 247 ACLKAssaywrgdvdreslqrvygisfpdkkllkeykhrieeakkrdhrllgqkqelfffhelspgscfflphgariynk 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 260 -------EYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 332
Cdd:PLN02908 327 lmdfireQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 333 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 412
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 413 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 489
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 490 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 537
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513864 538 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 594
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-589 |
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: 606.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS-----------------------------AEYAHR---- 264
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSvagaywrgdeknkmlqriygtafpkkkelDAYLHRleea 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 265 --------------------------------------------------GFSEVKTPTLFSTKLWEQSGHWEHYQEDMF 294
Cdd:COG0441 239 kkrdhrklgkeldlfhfqeevgpglpfwhpkgaiirreledyirekhrkaGYQEVKTPHILDRELWETSGHWDHYRENMF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 295 AVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQ 374
Cdd:COG0441 319 PTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 375 DDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAF 453
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 454 YGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQ 499
Cdd:COG0441 462 YGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafPLWLAPVQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 500 VVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWD 579
Cdd:COG0441 542 VVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMS 620
|
650
....*....|
gi 2462513864 580 LPEAVQRLVE 589
Cdd:COG0441 621 LDEFIARLKE 630
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
61-594 |
3.01e-146 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 436.87 E-value: 3.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 61 IKISLPGGQKIDAVAwNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:PRK12444 6 IEIKFPDGSVKEFVK-GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 141 AAAEQFLGAV-LCRGPSTEYGFYHDFFLGKerTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDN--PFKLH 217
Cdd:PRK12444 85 QAVKRLYGDVnLGVGPVIENGFYYDMDLPS--SVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndRLKLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS-----------------------------AEYAH----- 263
Cdd:PRK12444 163 LLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHvsgaywrgdsnnqvlqriygvafssqkelEEYLHfveea 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 264 ------------------------------------------------RGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFA 295
Cdd:PRK12444 243 akrnhrklgkelelfmfseeapgmpfylpkgqiirneleaflreiqkeYNYQEVRTPFMMNQELWERSGHWDHYKDNMYF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 296 vqppgsdrppsSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQD 375
Cdd:PRK12444 323 -----------SEVDNKS------FALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 376 DAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYG 455
Cdd:PRK12444 386 DAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 456 PKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQVV 501
Cdd:PRK12444 466 PKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDeknekrrpvvihravlgsldrflailiehfggafPAWLAPVQVK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 502 VIPVGSE-QEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDL 580
Cdd:PRK12444 546 VIPVSNAvHVQYADEVADKLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIEL 624
|
650
....*....|....
gi 2462513864 581 PEAVQRLVELQNTR 594
Cdd:PRK12444 625 DMFVESIKEEIKNR 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-588 |
5.96e-145 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 430.98 E-value: 5.96e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLSAEYA-------------------------- 262
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAywrgdsknkmlqriygtawadkkqla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 263 -------------HR--------------------------------------------GFSEVKTPTLFSTKLWEQSGH 285
Cdd:TIGR00418 159 ayllrleeakkrdHRklgkelelfsfepeigpglpfwlpkgatirnlledfvrqkqikyGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 286 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 365
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 366 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 443
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 444 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 491
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 492 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 569
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 2462513864 570 RDNRRLGEWDLPEAVQRLV 588
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-492 |
3.28e-122 |
|
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: 363.02 E-value: 3.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 255 KLLSAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGsdrppssqsddstrhitDTLALKPMNCPAHCLMF 334
Cdd:cd00771 38 DFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEEED-----------------EEYGLKPMNCPGHCLIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 335 AHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALS 413
Cdd:cd00771 101 KSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513864 414 TRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 492
Cdd:cd00771 181 TRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 259
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
87-587 |
6.95e-80 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 264.07 E-value: 6.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 87 ISSTLADTAVAAQVNGEPYDLERPLETDSDLRFL-TFDSPEGKAVFWHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHD 164
Cdd:PLN02837 1 VSAAAASAATEEASAAAASDEKGPGEAEPERVVLpTNESSEKLLKIRHTCAHVMAMAVQKlFPDAKVTIGPWIENGFYYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 165 F----FLGKErtirgselpvLERICQELTAAAR---PFRRLEASRDQLRQLFK--DNPFKLHLIEEKVTGPTaTVYGCGT 235
Cdd:PLN02837 81 FdmepLTDKD----------LKRIKKEMDRIISrnlPLVREEVSREEAQKRIMaiNEPYKLEILEGIKEEPI-TIYHIGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 236 -LVDLCQGPHLRHTGQI--------------------------------------------------------------- 251
Cdd:PLN02837 150 eWWDLCAGPHVERTGKInkkavelesvagaywrgdeknqmlqriygtaweseeqlkaylhfkeeakrrdhrrlgqdldlf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 252 -------GGLKLLSAEYA---------------HRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFavqppgsdrppsSQS 309
Cdd:PLN02837 230 siqddagGGLVFWHPKGAivrhiiedswkkmhfEHGYDLLYTPHVAKADLWKTSGHLDFYKENMY------------DQM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 310 DdstrhITDTL-ALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEA 388
Cdd:PLN02837 298 D-----IEDELyQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 389 EIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALG 467
Cdd:PLN02837 373 EIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 468 RPHQCGTIQLDFQLPLRFDL--------------------------------QYKG--PLWLSPFQVVVIPVGSEQEEYA 513
Cdd:PLN02837 453 RKWQCSTIQVDFNLPERFDItyvdsnsekkrpimihrailgslerffgvlieHYAGdfPLWLAPVQARVLPVTDNELEYC 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462513864 514 KEAQQSLRAAGLVSDLdaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRL 587
Cdd:PLN02837 533 KEVVAKLKAKGIRAEV--CHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRI 604
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
497-588 |
3.47e-27 |
|
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: 105.28 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 497 PFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLG 576
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 2462513864 577 EWDLPEAVQRLV 588
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
318-491 |
7.48e-27 |
|
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: 107.50 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 318 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 396
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 397 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 475
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 2462513864 476 QLD-FQLPLRFDLQYKG 491
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
340-570 |
1.68e-24 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 108.03 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 340 SWRELPLR---LADFGalHRAEASGGLGGLTRLRCFQQDDAHIFC-----TTDQLEAEIQSCLDFLRSV---YAVLgfsF 408
Cdd:PRK03991 303 SYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdYEVA---I 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 409 RLalsTRpsGFlgdpclWDQAEQVLKQALKEFGEP-----WDlnsgDGAFYGP-KIDVHLHDALGRPHQCGTIQLDFQLP 482
Cdd:PRK03991 378 RF---TE--DF------YEENKDWIVELVKREGKPvlleiLP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 483 LRFDLQY-------------------------------------KG-----PLWLSPFQVVVIPVGSEQEEYAKEAQQSL 520
Cdd:PRK03991 443 ERFGIKYvdengeekypiilhcsptgsierviyallekaakeeeEGkvpmlPTWLSPTQVRVIPVSERHLDYAEEVADKL 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462513864 521 RAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTR 570
Cdd:PRK03991 523 EAAGIRVDVD-DRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIR 571
|
|
| 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 ... |
262-434 |
2.86e-22 |
|
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: 95.92 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 262 AHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGsdrppssqsddstRHITDT-LALKPMNCPAHCLMFAHRPRS 340
Cdd:cd00670 17 AEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKG-------------RELRDTdLVLRPAACEPIYQIFSGEILS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 341 WRELPLRLADFGALHRAEASGGlGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFL 420
Cdd:cd00670 84 YRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPFFGR 162
|
170
....*....|....*
gi 2462513864 421 GDPCLWD-QAEQVLK 434
Cdd:cd00670 163 GGKRGLDaGRETVVE 177
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
61-126 |
2.14e-21 |
|
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: 87.93 E-value: 2.14e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462513864 61 IKISLPGGqKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPE 126
Cdd:cd01667 1 IKITLPDG-SVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
499-590 |
1.06e-19 |
|
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: 84.17 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 499 QVVVIPVGS---EQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRL 575
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 2462513864 576 GEWDLPEAVQRLVEL 590
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
61-121 |
1.70e-11 |
|
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.
Pssm-ID: 427005 [Multi-domain] Cd Length: 60 Bit Score: 59.48 E-value: 1.70e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462513864 61 IKISLPGGQKIDAVAWnTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLT 121
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 ... |
264-467 |
4.24e-11 |
|
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: 62.91 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 264 RGFSEVKTPTLFSTKLWEQSGHWehyqedmFAVQPPGSDRPPssqsddstrhitDTLALKPMNCPAHCLMFAHRPRSwre 343
Cdd:cd00768 16 LGFQEVETPIVEREPLLEKAGHE-------PKDLLPVGAENE------------EDLYLRPTLEPGLVRLFVSHIRK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 344 LPLRLADFGALHRAEASGglGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDP 423
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSPG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462513864 424 CLWDQAEQVLKQALKEFGE--------PWDLNSGDGAFYGP----KIDVHLHDALG 467
Cdd:cd00768 152 GAGPGFEIEVDHPEGRGLEigsggyrqDEQARAADLYFLDEaleyRYPPTIGFGLG 207
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-262 |
5.71e-07 |
|
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: 46.22 E-value: 5.71e-07
10 20 30
....*....|....*....|....*....|....*
gi 2462513864 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSAEYA 262
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGA 36
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
492-574 |
1.03e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 51.38 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 492 PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKE--QSKRTVNIRT 569
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREvkTSTLTVKIRA 347
|
....*
gi 2462513864 570 RDNRR 574
Cdd:PRK14938 348 NNEQK 352
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
497-588 |
1.19e-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: 47.01 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 497 PFQVVVIPVG---SEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNR 573
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 2462513864 574 RLGEWDLPEAVQRLV 588
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
229-258 |
6.60e-06 |
|
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: 43.20 E-value: 6.60e-06
10 20 30
....*....|....*....|....*....|.
gi 2462513864 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLS 258
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK 32
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
496-590 |
5.24e-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: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 496 SPFQVVVIPVGSEQE------EYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 569
Cdd:cd00862 9 APIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100
....*....|....*....|.
gi 2462513864 570 RDNRRLGEWDLPEAVQRLVEL 590
Cdd:cd00862 89 RDTGEKKTVPLAELVEKVPEL 109
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
483-589 |
1.60e-03 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 38.69 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 483 LRFdlqykgPLWLSPFQVVVIPVGSEQE--EYAKEAQQSLRAAGLVSDLDaDSGlTLSRRIRRAQLAHYNFQFVVGQKEQ 560
Cdd:cd00858 18 LRL------PPALAPIKVAVLPLVKRDElvEIAKEISEELRELGFSVKYD-DSG-SIGRRYARQDEIGTPFCVTVDFDTL 89
|
90 100 110
....*....|....*....|....*....|..
gi 2462513864 561 SKRTVNIRTRDNR---RLGEWDLPEAVQRLVE 589
Cdd:cd00858 90 EDGTVTIRERDSMrqvRVKIEELPSYLRELIR 121
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-391 |
1.83e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. 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: 40.25 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 265 GFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsDrppssqsddstRHiTDTLALKPMNCPAHCLMFAHRPRSWREL 344
Cdd:cd00779 49 GAQEILMPILQPAELWKESGRWDAYGPELLRLK----D-----------RH-GKEFLLGPTHEEVITDLVANEIKSYKQL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462513864 345 PLRLADFGALHRAEASgGLGGLTRLRCFQQDDAHIFcTTDQLEAEIQ 391
Cdd:cd00779 113 PLNLYQIQTKFRDEIR-PRFGLMRGREFLMKDAYSF-DIDEESLEET 157
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
499-568 |
6.84e-03 |
|
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: 35.98 E-value: 6.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513864 499 QVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIR 568
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-GGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVK 71
|
|
| |
