|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-676 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 790.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 255 KLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNA 334
Cdd:PLN02908 247 ACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 335 LVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 414
Cdd:PLN02908 327 LMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 415 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 494
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 495 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 571
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 572 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 619
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 578801529 620 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 676
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-671 |
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: 701.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGlkllsnssslwrssGA-------PETLQRVSGISFPTTELLRVW 290
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAfkll-------svaGAywrgdekNKMLQRIYGTAFPKKKELDAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 291 EAWREEAELRDHRRIGKEQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWE 369
Cdd:COG0441 232 LHRLEEAKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 370 HYQEDMFAVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLT 449
Cdd:COG0441 312 HYRENMFPTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 450 RLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDL 528
Cdd:COG0441 375 RVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 529 NSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------P 574
Cdd:COG0441 455 NPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafP 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 575 LWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDN 654
Cdd:COG0441 535 LWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGG 613
|
650
....*....|....*..
gi 578801529 655 RRLGEWDLPEAVQRLVE 671
Cdd:COG0441 614 GDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-670 |
1.41e-180 |
|
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: 525.35 E-value: 1.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLR 288
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 289 VWEAWREEAELRDHRRIGKEQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGH 367
Cdd:TIGR00418 159 AYLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 368 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 447
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 448 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 525
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 526 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 573
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 574 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 651
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 578801529 652 RDNRRLGEWDLPEAVQRLV 670
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
300-574 |
1.67e-144 |
|
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: 422.73 E-value: 1.67e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 300 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQ 379
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 380 PPGsdrppssqsddstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDA 459
Cdd:cd00771 81 EED-----------------EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 460 HIFCTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGP 538
Cdd:cd00771 144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGP 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 578801529 539 KIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 574
Cdd:cd00771 224 KIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 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 ... |
400-573 |
2.37e-26 |
|
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: 106.34 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 400 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 478
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 479 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 557
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 578801529 558 QLD-FQLPLRFDLQYKG 573
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-252 |
5.36e-04 |
|
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: 38.13 E-value: 5.36e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-676 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 790.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 255 KLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNA 334
Cdd:PLN02908 247 ACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 335 LVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 414
Cdd:PLN02908 327 LMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 415 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 494
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 495 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 571
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 572 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 619
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 578801529 620 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 676
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-671 |
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: 701.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGlkllsnssslwrssGA-------PETLQRVSGISFPTTELLRVW 290
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAfkll-------svaGAywrgdekNKMLQRIYGTAFPKKKELDAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 291 EAWREEAELRDHRRIGKEQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWE 369
Cdd:COG0441 232 LHRLEEAKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 370 HYQEDMFAVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLT 449
Cdd:COG0441 312 HYRENMFPTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 450 RLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDL 528
Cdd:COG0441 375 RVRGFTQDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 529 NSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------P 574
Cdd:COG0441 455 NPGEGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafP 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 575 LWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDN 654
Cdd:COG0441 535 LWLAPVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGG 613
|
650
....*....|....*..
gi 578801529 655 RRLGEWDLPEAVQRLVE 671
Cdd:COG0441 614 GDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-670 |
1.41e-180 |
|
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: 525.35 E-value: 1.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLR 288
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 289 VWEAWREEAELRDHRRIGKEQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGH 367
Cdd:TIGR00418 159 AYLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 368 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 447
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 448 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 525
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 526 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 573
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 574 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 651
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 578801529 652 RDNRRLGEWDLPEAVQRLV 670
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
61-676 |
2.09e-176 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 517.38 E-value: 2.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 61 IKISLPGGQKIDAVAwNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:PRK12444 6 IEIKFPDGSVKEFVK-GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 141 AAAEQFLGAV-LCRGPSTEYGFYHDFFLGKerTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDN--PFKLH 217
Cdd:PRK12444 85 QAVKRLYGDVnLGVGPVIENGFYYDMDLPS--SVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndRLKLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEA 297
Cdd:PRK12444 163 LLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 298 ELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFA 377
Cdd:PRK12444 243 AKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 378 vqppgsdrppsSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQD 457
Cdd:PRK12444 323 -----------SEVDNKS------FALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 458 DAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYG 537
Cdd:PRK12444 386 DAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 538 PKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQVV 583
Cdd:PRK12444 466 PKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDeknekrrpvvihravlgsldrflailiehfggafPAWLAPVQVK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 584 VIPVGSE-QEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDL 662
Cdd:PRK12444 546 VIPVSNAvHVQYADEVADKLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIEL 624
|
650
....*....|....
gi 578801529 663 PEAVQRLVELQNTR 676
Cdd:PRK12444 625 DMFVESIKEEIKNR 638
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
300-574 |
1.67e-144 |
|
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: 422.73 E-value: 1.67e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 300 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQ 379
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 380 PPGsdrppssqsddstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDA 459
Cdd:cd00771 81 EED-----------------EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 460 HIFCTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGP 538
Cdd:cd00771 144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGP 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 578801529 539 KIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 574
Cdd:cd00771 224 KIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 259
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
87-669 |
1.69e-103 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 328.40 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 87 ISSTLADTAVAAQVNGEPYDLERPLETDSDLRFL-TFDSPEGKAVFWHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHD 164
Cdd:PLN02837 1 VSAAAASAATEEASAAAASDEKGPGEAEPERVVLpTNESSEKLLKIRHTCAHVMAMAVQKlFPDAKVTIGPWIENGFYYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 165 F----FLGKErtirgselpvLERICQELTAAAR---PFRRLEASRDQLRQLFK--DNPFKLHLIEEKVTGPTaTVYGCGT 235
Cdd:PLN02837 81 FdmepLTDKD----------LKRIKKEMDRIISrnlPLVREEVSREEAQKRIMaiNEPYKLEILEGIKEEPI-TIYHIGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 236 -LVDLCQGPHLRHTGQIGGLKLLSNSSSLWRSSG--APETLQRVSGISFPTTELLRVWEAWREEAELRDHRRIGKEQELF 312
Cdd:PLN02837 150 eWWDLCAGPHVERTGKINKKAVELESVAGAYWRGdeKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 313 FFHELSPGS-CFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFavqppgsdrppsSQS 391
Cdd:PLN02837 230 SIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMY------------DQM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 392 DdstrhITDTL-ALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEA 470
Cdd:PLN02837 298 D-----IEDELyQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 471 EIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALG 549
Cdd:PLN02837 373 EIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 550 RPHQCGTIQLDFQLPLRFDL--------------------------------QYKG--PLWLSPFQVVVIPVGSEQEEYA 595
Cdd:PLN02837 453 RKWQCSTIQVDFNLPERFDItyvdsnsekkrpimihrailgslerffgvlieHYAGdfPLWLAPVQARVLPVTDNELEYC 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578801529 596 KEAQQSLRAAGLVSDLdaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRL 669
Cdd:PLN02837 533 KEVVAKLKAKGIRAEV--CHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRI 604
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
579-670 |
4.23e-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: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 579 PFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLG 658
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 578801529 659 EWDLPEAVQRLV 670
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 ... |
400-573 |
2.37e-26 |
|
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: 106.34 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 400 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 478
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 479 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 557
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 578801529 558 QLD-FQLPLRFDLQYKG 573
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
422-652 |
2.45e-24 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 108.03 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 422 SWRELPLR---LADFGalHRAEASGGLGGLTRLRCFQQDDAHIFC-----TTDQLEAEIQSCLDFLRSV---YAVLgfsF 490
Cdd:PRK03991 303 SYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdYEVA---I 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 491 RLalsTRpsGFlgdpclWDQAEQVLKQALKEFGEP-----WDlnsgDGAFYGP-KIDVHLHDALGRPHQCGTIQLDFQLP 564
Cdd:PRK03991 378 RF---TE--DF------YEENKDWIVELVKREGKPvlleiLP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 565 LRFDLQY-------------------------------------KG-----PLWLSPFQVVVIPVGSEQEEYAKEAQQSL 602
Cdd:PRK03991 443 ERFGIKYvdengeekypiilhcsptgsierviyallekaakeeeEGkvpmlPTWLSPTQVRVIPVSERHLDYAEEVADKL 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578801529 603 RAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTR 652
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 ... |
328-516 |
2.90e-23 |
|
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: 99.00 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 328 GTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGsdrppssqsddstRHITDT-LALKP 406
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKG-------------RELRDTdLVLRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 407 MNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGlGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVL 486
Cdd:cd00670 68 AACEPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIAREL 146
|
170 180 190
....*....|....*....|....*....|.
gi 578801529 487 GFSFRLALSTRPSGFLGDPCLWD-QAEQVLK 516
Cdd:cd00670 147 GLPVRVVVADDPFFGRGGKRGLDaGRETVVE 177
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
61-126 |
2.45e-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: 2.45e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578801529 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 ... |
581-672 |
1.22e-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: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 581 QVVVIPVGS---EQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRL 657
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 578801529 658 GEWDLPEAVQRLVEL 672
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
61-121 |
1.94e-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: 1.94e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578801529 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 ... |
329-549 |
9.29e-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: 62.14 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 329 TRVYNALVAFIRAeyahRGFSEVKTPTLFSTKLWEQSGHWehyqedmFAVQPPGSDRPPssqsddstrhitDTLALKPMN 408
Cdd:cd00768 3 SKIEQKLRRFMAE----LGFQEVETPIVEREPLLEKAGHE-------PKDLLPVGAENE------------EDLYLRPTL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 409 CPAHCLMFAHRPRSwreLPLRLADFGALHRAEASGglGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGF 488
Cdd:cd00768 60 EPGLVRLFVSHIRK---LPLRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGI 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578801529 489 SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGE--------PWDLNSGDGAFYGP----KIDVHLHDALG 549
Cdd:cd00768 135 KLDIVFVEKTPGEFSPGGAGPGFEIEVDHPEGRGLEigsggyrqDEQARAADLYFLDEaleyRYPPTIGFGLG 207
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
296-473 |
2.55e-07 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 52.58 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 296 EAELRDHR---RIGkeqelfFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQ 372
Cdd:cd00779 1 DAEIISHKlllRAG------FIRQTSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 373 EDMFAVQppgsDrppssqsddstRHiTDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASgGLGGLTRLR 452
Cdd:cd00779 75 PELLRLK----D-----------RH-GKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIR-PRFGLMRGR 137
|
170 180
....*....|....*....|.
gi 578801529 453 CFQQDDAHIFcTTDQLEAEIQ 473
Cdd:cd00779 138 EFLMKDAYSF-DIDEESLEET 157
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
574-656 |
1.23e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 51.38 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 574 PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKE--QSKRTVNIRT 651
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREvkTSTLTVKIRA 347
|
....*
gi 578801529 652 RDNRR 656
Cdd:PRK14938 348 NNEQK 352
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
579-670 |
1.54e-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: 46.62 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 579 PFQVVVIPVG---SEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNR 655
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 578801529 656 RLGEWDLPEAVQRLV 670
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
578-672 |
6.11e-05 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 44.60 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 578 SPFQVVVIPVGSEQE------EYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 651
Cdd:cd00862 9 APIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100
....*....|....*....|.
gi 578801529 652 RDNRRLGEWDLPEAVQRLVEL 672
Cdd:cd00862 89 RDTGEKKTVPLAELVEKVPEL 109
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
296-430 |
3.99e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.31 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 296 EAELRDHR---RIGkeqelfFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQ 372
Cdd:PRK12325 17 EAEIVSHRlmlRAG------MIRQQAAGIYSWLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578801529 373 EDMFAVQppgsDrppssqsddstRHITDTLaLKPMNCPAHCLMFAHRPRSWRELPLRL 430
Cdd:PRK12325 91 KEMLRIK----D-----------RHDREML-YGPTNEEMITDIFRSYVKSYKDLPLNL 132
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
324-430 |
4.71e-04 |
|
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 43.22 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 324 FLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsDRppssqsddSTRHitdtLA 403
Cdd:COG0442 42 YLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVT----DR--------LERE----FC 105
|
90 100 110
....*....|....*....|....*....|.
gi 578801529 404 LkpmnCPAH----CLMFAHRPRSWRELPLRL 430
Cdd:COG0442 106 L----GPTHeeviTDLVRNEIKSYRDLPLLL 132
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-252 |
5.36e-04 |
|
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: 38.13 E-value: 5.36e-04
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
229-252 |
5.96e-04 |
|
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: 37.81 E-value: 5.96e-04
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
320-503 |
1.82e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 40.81 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 320 GSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsdrppssqSDDSTRHIT 399
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVF-----------KDAGDEELE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 400 DTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLgGLTRLRCFQQDDAHIF-CTTDQLEAEIQSCLDF 478
Cdd:cd00772 92 EDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRF-GFLRAREFIMKDGHSAhADAEEADEEFLNMLSA 170
|
170 180
....*....|....*....|....*.
gi 578801529 479 LRSVYAVLG-FSFRLALSTRPSGFLG 503
Cdd:cd00772 171 YAEIARDLAaIDFIEGEADEGAKFAG 196
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
565-671 |
2.49e-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: 38.31 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 565 LRFdlqykgPLWLSPFQVVVIPVGSEQE--EYAKEAQQSLRAAGLVSDLDaDSGlTLSRRIRRAQLAHYNFQFVVGQKEQ 642
Cdd:cd00858 18 LRL------PPALAPIKVAVLPLVKRDElvEIAKEISEELRELGFSVKYD-DSG-SIGRRYARQDEIGTPFCVTVDFDTL 89
|
90 100 110
....*....|....*....|....*....|..
gi 578801529 643 SKRTVNIRTRDNR---RLGEWDLPEAVQRLVE 671
Cdd:cd00858 90 EDGTVTIRERDSMrqvRVKIEELPSYLRELIR 121
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
581-650 |
7.83e-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: 7.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578801529 581 QVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIR 650
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-GGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVK 71
|
|
| |
