|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-627 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 731.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 255 ------------------------------KLLSE-------------------QELFFFHELSPGSCFFLPRGTRVYNA 285
Cdd:PLN02908 247 aclkassaywrgdvdreslqrvygisfpdkKLLKEykhrieeakkrdhrllgqkQELFFFHELSPGSCFFLPHGARIYNK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 286 LVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 365
Cdd:PLN02908 327 LMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 366 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 445
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 446 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 522
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 523 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 570
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034562054 571 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 627
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-622 |
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: 659.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS--------------------------------------- 258
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSvagaywrgdeknkmlqriygtafpkkkeldaylhrleea 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 259 ----------EQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMF 327
Cdd:COG0441 239 kkrdhrklgkELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 328 AVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQ 407
Cdd:COG0441 319 PTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 408 DDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAF 486
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 487 YGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQ 532
Cdd:COG0441 462 YGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafPLWLAPVQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 533 VVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWD 612
Cdd:COG0441 542 VVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMS 620
|
650
....*....|
gi 1034562054 613 LPEAVQRLVE 622
Cdd:COG0441 621 LDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-621 |
1.54e-163 |
|
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: 479.90 E-value: 1.54e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLS------------------------------ 258
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKvagaywrgdsknkmlqriygtawadkkqla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 259 -------------------EQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGH 318
Cdd:TIGR00418 159 ayllrleeakkrdhrklgkELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 319 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 398
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 399 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 476
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 477 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 524
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 525 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 602
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 1034562054 603 RDNRRLGEWDLPEAVQRLV 621
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-525 |
3.31e-141 |
|
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: 412.71 E-value: 3.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 255 KLLSEQELFFF-HELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPG 333
Cdd:cd00771 4 RLGGELELFFFfDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEEED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 334 sdrppssqsddstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIF 413
Cdd:cd00771 84 -----------------EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 414 CTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKID 492
Cdd:cd00771 147 CTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270
....*....|....*....|....*....|...
gi 1034562054 493 VHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 525
Cdd:cd00771 227 FHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 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 ... |
351-524 |
1.39e-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: 106.73 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 351 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 429
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 430 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 508
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 1034562054 509 QLD-FQLPLRFDLQYKG 524
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-259 |
4.03e-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: 46.61 E-value: 4.03e-07
10 20 30
....*....|....*....|....*....|..
gi 1034562054 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSE 259
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSV 33
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
17-627 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 731.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 17 ACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASmaqKEPRTIKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAV 96
Cdd:PLN02908 11 AAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 97 AAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEY--GFYHDFFLGkERTIR 174
Cdd:PLN02908 88 IAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 175 GSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGL 254
Cdd:PLN02908 167 EEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 255 ------------------------------KLLSE-------------------QELFFFHELSPGSCFFLPRGTRVYNA 285
Cdd:PLN02908 247 aclkassaywrgdvdreslqrvygisfpdkKLLKEykhrieeakkrdhrllgqkQELFFFHELSPGSCFFLPHGARIYNK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 286 LVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGSDrppssqsddstrhitdtLALKPMNCPAHCL 365
Cdd:PLN02908 327 LMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQE-----------------FGLKPMNCPGHCL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 366 MFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLAL 445
Cdd:PLN02908 390 MFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 446 STRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQY--- 522
Cdd:PLN02908 470 STRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYsae 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 523 --------------------------------KGPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTL 570
Cdd:PLN02908 550 deakierpvmihrailgsvermfaillehyagKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKI 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034562054 571 SRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTR 627
Cdd:PLN02908 629 QKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
61-622 |
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: 659.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 61 IKISLPGGQKIDaVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 141 AAAEQ-FLGAVLCRGPSTEYGFYHDFFLgkERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK--DNPFKLH 217
Cdd:COG0441 81 QAVKRlYPDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS--------------------------------------- 258
Cdd:COG0441 159 LIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSvagaywrgdeknkmlqriygtafpkkkeldaylhrleea 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 259 ----------EQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMF 327
Cdd:COG0441 239 kkrdhrklgkELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 328 AVQppgsdrppssqSDDstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQ 407
Cdd:COG0441 319 PTE-----------SDG------EEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 408 DDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAF 486
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 487 YGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQ 532
Cdd:COG0441 462 YGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGedgekhrpvmihrailgsierfigiliehyagafPLWLAPVQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 533 VVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWD 612
Cdd:COG0441 542 VVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMS 620
|
650
....*....|
gi 1034562054 613 LPEAVQRLVE 622
Cdd:COG0441 621 LDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
132-621 |
1.54e-163 |
|
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: 479.90 E-value: 1.54e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 132 WHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHDFFLGKERTIrgSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 211 -DNPFKLHLIEEKVTGPTATVYGCGT-LVDLCQGPHLRHTGQIGGLKLLS------------------------------ 258
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKaFVDLCKGPHLPNTSFIKAFKLEKvagaywrgdsknkmlqriygtawadkkqla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 259 -------------------EQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGH 318
Cdd:TIGR00418 159 ayllrleeakkrdhrklgkELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 319 WEHYQEDMFavqppgsdrpPSSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGG 398
Cdd:TIGR00418 239 WDNYKERMF----------PFTELDNRE------FMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 399 LTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSF-RLALSTR-PSGFLGDPCLWDQAEQVLKQALKEFGEP 476
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 477 WDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG-------------------------------- 524
Cdd:TIGR00418 383 YEIDPGRGAFYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDedneekrpvmihrailgsierfiaillekyag 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 525 --PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 602
Cdd:TIGR00418 463 nfPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*....
gi 1034562054 603 RDNRRLGEWDLPEAVQRLV 621
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKLR 560
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
61-627 |
1.05e-161 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 478.09 E-value: 1.05e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 61 IKISLPGGQKIDAVAwNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFLTFDSPEGKAVFWHSSTHVLG 140
Cdd:PRK12444 6 IEIKFPDGSVKEFVK-GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 141 AAAEQFLGAV-LCRGPSTEYGFYHDFFLGKerTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFKDN--PFKLH 217
Cdd:PRK12444 85 QAVKRLYGDVnLGVGPVIENGFYYDMDLPS--SVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndRLKLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 218 LIEEKVTGPTATVYGCGTLVDLCQGPHLRHTGQIGGLKLLS--------------------------------------- 258
Cdd:PRK12444 163 LLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHvsgaywrgdsnnqvlqriygvafssqkeleeylhfveea 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 259 ----------EQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFA 328
Cdd:PRK12444 243 akrnhrklgkELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 329 vqppgsdrppsSQSDDSTrhitdtLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQD 408
Cdd:PRK12444 323 -----------SEVDNKS------FALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 409 DAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYG 488
Cdd:PRK12444 386 DAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 489 PKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKG----------------------------------PLWLSPFQVV 534
Cdd:PRK12444 466 PKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDeknekrrpvvihravlgsldrflailiehfggafPAWLAPVQVK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 535 VIPVGSE-QEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDL 613
Cdd:PRK12444 546 VIPVSNAvHVQYADEVADKLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIEL 624
|
650
....*....|....
gi 1034562054 614 PEAVQRLVELQNTR 627
Cdd:PRK12444 625 DMFVESIKEEIKNR 638
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
255-525 |
3.31e-141 |
|
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: 412.71 E-value: 3.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 255 KLLSEQELFFF-HELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPG 333
Cdd:cd00771 4 RLGGELELFFFfDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFEEED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 334 sdrppssqsddstrhitDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIF 413
Cdd:cd00771 84 -----------------EEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 414 CTTDQLEAEIQSCLDFLRSVYAVLGF-SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKID 492
Cdd:cd00771 147 CTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKID 226
|
250 260 270
....*....|....*....|....*....|...
gi 1034562054 493 VHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGP 525
Cdd:cd00771 227 FHVKDALGREWQCSTIQLDFNLPERFDLTYIGE 259
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
87-620 |
4.41e-86 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 281.40 E-value: 4.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 87 ISSTLADTAVAAQVNGEPYDLERPLETDSDLRFL-TFDSPEGKAVFWHSSTHVLGAAAEQ-FLGAVLCRGPSTEYGFYHD 164
Cdd:PLN02837 1 VSAAAASAATEEASAAAASDEKGPGEAEPERVVLpTNESSEKLLKIRHTCAHVMAMAVQKlFPDAKVTIGPWIENGFYYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 165 F----FLGKErtirgselpvLERICQELTAAAR---PFRRLEASRDQLRQLFK--DNPFKLHLIEEKVTGPTaTVYGCGT 235
Cdd:PLN02837 81 FdmepLTDKD----------LKRIKKEMDRIISrnlPLVREEVSREEAQKRIMaiNEPYKLEILEGIKEEPI-TIYHIGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 236 -LVDLCQGPHLRHTGQIG---------------------------GLKLLSE----------------------QELFFF 265
Cdd:PLN02837 150 eWWDLCAGPHVERTGKINkkavelesvagaywrgdeknqmlqriyGTAWESEeqlkaylhfkeeakrrdhrrlgQDLDLF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 266 ---HELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFavqppgsdrppsSQS 342
Cdd:PLN02837 230 siqDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMY------------DQM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 343 DdstrhITDTL-ALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEA 421
Cdd:PLN02837 298 D-----IEDELyQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 422 EIQSCLDFLRSVYAVLGFS-FRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALG 500
Cdd:PLN02837 373 EIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 501 RPHQCGTIQLDFQLPLRFDL--------------------------------QYKG--PLWLSPFQVVVIPVGSEQEEYA 546
Cdd:PLN02837 453 RKWQCSTIQVDFNLPERFDItyvdsnsekkrpimihrailgslerffgvlieHYAGdfPLWLAPVQARVLPVTDNELEYC 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034562054 547 KEAQQSLRAAGLVSDLdaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRL 620
Cdd:PLN02837 533 KEVVAKLKAKGIRAEV--CHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRI 604
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
530-621 |
3.81e-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: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 530 PFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLG 609
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 1034562054 610 EWDLPEAVQRLV 621
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 ... |
351-524 |
1.39e-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: 106.73 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 351 DTLALKPMNCPAHCLMFA-HRPRSWReLPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDF 429
Cdd:pfam00587 9 DELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 430 LRSVYAVLGFSFRLALstrpsgflgdpclwdqaeqvlkqalkefgepwDLNSGDGAFYGPKIDVHLHD-ALGRPHQCGTI 508
Cdd:pfam00587 88 IDRVYSRLGLEVRVVR--------------------------------LSNSDGSAFYGPKLDFEVVFpSLGKQRQTGTI 135
|
170
....*....|....*..
gi 1034562054 509 QLD-FQLPLRFDLQYKG 524
Cdd:pfam00587 136 QNDgFRLPRRLGIRYKD 152
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
373-603 |
1.99e-24 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 108.03 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 373 SWRELPLR---LADFGalHRAEASGGLGGLTRLRCFQQDDAHIFC-----TTDQLEAEIQSCLDFLRSV---YAVLgfsF 441
Cdd:PRK03991 303 SYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdYEVA---I 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 442 RLalsTRpsGFlgdpclWDQAEQVLKQALKEFGEP-----WDlnsgDGAFYGP-KIDVHLHDALGRPHQCGTIQLDFQLP 515
Cdd:PRK03991 378 RF---TE--DF------YEENKDWIVELVKREGKPvlleiLP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 516 LRFDLQY-------------------------------------KG-----PLWLSPFQVVVIPVGSEQEEYAKEAQQSL 553
Cdd:PRK03991 443 ERFGIKYvdengeekypiilhcsptgsierviyallekaakeeeEGkvpmlPTWLSPTQVRVIPVSERHLDYAEEVADKL 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034562054 554 RAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTR 603
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 ... |
279-467 |
1.37e-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: 99.77 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 279 GTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQPPGsdrppssqsddstRHITDT-LALKP 357
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKG-------------RELRDTdLVLRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 358 MNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGlGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVL 437
Cdd:cd00670 68 AACEPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIAREL 146
|
170 180 190
....*....|....*....|....*....|.
gi 1034562054 438 GFSFRLALSTRPSGFLGDPCLWD-QAEQVLK 467
Cdd:cd00670 147 GLPVRVVVADDPFFGRGGKRGLDaGRETVVE 177
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
61-126 |
2.26e-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: 2.26e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034562054 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 ... |
532-623 |
1.12e-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: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 532 QVVVIPVGS---EQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRL 608
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 1034562054 609 GEWDLPEAVQRLVEL 623
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
61-121 |
1.80e-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: 1.80e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034562054 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 ... |
280-500 |
4.17e-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: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 280 TRVYNALVAFIRAeyahRGFSEVKTPTLFSTKLWEQSGHWehyqedmFAVQPPGSDRPPssqsddstrhitDTLALKPMN 359
Cdd:cd00768 3 SKIEQKLRRFMAE----LGFQEVETPIVEREPLLEKAGHE-------PKDLLPVGAENE------------EDLYLRPTL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 360 CPAHCLMFAHRPRSwreLPLRLADFGALHRAEASGglGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGF 439
Cdd:cd00768 60 EPGLVRLFVSHIRK---LPLRLAEIGPAFRNEGGR--RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGI 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034562054 440 SFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGE--------PWDLNSGDGAFYGP----KIDVHLHDALG 500
Cdd:cd00768 135 KLDIVFVEKTPGEFSPGGAGPGFEIEVDHPEGRGLEigsggyrqDEQARAADLYFLDEaleyRYPPTIGFGLG 207
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
229-259 |
4.03e-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: 46.61 E-value: 4.03e-07
10 20 30
....*....|....*....|....*....|..
gi 1034562054 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSE 259
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSV 33
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
268-424 |
4.52e-07 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 51.42 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 268 LSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsDrppssqsddstR 347
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLK----D-----------R 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034562054 348 HiTDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASgGLGGLTRLRCFQQDDAHIFcTTDQLEAEIQ 424
Cdd:cd00779 84 H-GKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIR-PRFGLMRGREFLMKDAYSF-DIDEESLEET 157
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
525-607 |
1.11e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 51.38 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 525 PLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKE--QSKRTVNIRT 602
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREvkTSTLTVKIRA 347
|
....*
gi 1034562054 603 RDNRR 607
Cdd:PRK14938 348 NNEQK 352
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
530-621 |
1.14e-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: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 530 PFQVVVIPVG---SEQEEYAKEAQQSLRAAGLVSDLDaDSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNR 606
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 1034562054 607 RLGEWDLPEAVQRLV 621
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
229-261 |
1.21e-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: 45.51 E-value: 1.21e-06
10 20 30
....*....|....*....|....*....|....
gi 1034562054 229 TVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSEQE 261
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILKGES 35
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
529-623 |
5.59e-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: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 529 SPFQVVVIPVGSEQE------EYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRT 602
Cdd:cd00862 9 APIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100
....*....|....*....|.
gi 1034562054 603 RDNRRLGEWDLPEAVQRLVEL 623
Cdd:cd00862 89 RDTGEKKTVPLAELVEKVPEL 109
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
275-381 |
4.27e-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: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 275 FLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsDRppssqsddSTRHitdtLA 354
Cdd:COG0442 42 YLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVT----DR--------LERE----FC 105
|
90 100 110
....*....|....*....|....*....|.
gi 1034562054 355 LkpmnCPAH----CLMFAHRPRSWRELPLRL 381
Cdd:COG0442 106 L----GPTHeeviTDLVRNEIKSYRDLPLLL 132
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
271-454 |
1.19e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 41.20 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 271 GSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsdrppssqSDDSTRHIT 350
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVF-----------KDAGDEELE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 351 DTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLgGLTRLRCFQQDDAHIF-CTTDQLEAEIQSCLDF 429
Cdd:cd00772 92 EDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRF-GFLRAREFIMKDGHSAhADAEEADEEFLNMLSA 170
|
170 180
....*....|....*....|....*.
gi 1034562054 430 LRSVYAVLG-FSFRLALSTRPSGFLG 454
Cdd:cd00772 171 YAEIARDLAaIDFIEGEADEGAKFAG 196
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
275-381 |
1.20e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 41.77 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 275 FLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTKLWEQSGHWEHYQEDMFAVQppgsDrppssqsddstRHITDTLa 354
Cdd:PRK12325 42 WLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLRIK----D-----------RHDREML- 105
|
90 100
....*....|....*....|....*..
gi 1034562054 355 LKPMNCPAHCLMFAHRPRSWRELPLRL 381
Cdd:PRK12325 106 YGPTNEEMITDIFRSYVKSYKDLPLNL 132
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
516-622 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 516 LRFdlqykgPLWLSPFQVVVIPVGSEQE--EYAKEAQQSLRAAGLVSDLDaDSGlTLSRRIRRAQLAHYNFQFVVGQKEQ 593
Cdd:cd00858 18 LRL------PPALAPIKVAVLPLVKRDElvEIAKEISEELRELGFSVKYD-DSG-SIGRRYARQDEIGTPFCVTVDFDTL 89
|
90 100 110
....*....|....*....|....*....|..
gi 1034562054 594 SKRTVNIRTRDNR---RLGEWDLPEAVQRLVE 622
Cdd:cd00858 90 EDGTVTIRERDSMrqvRVKIEELPSYLRELIR 121
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
133-260 |
4.91e-03 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 39.76 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 133 HSSTHVLGAAAEQFLGA-VLCRGPS-TEYGFYHDFflGKERTIRGSELPVLERICQELTAAARPFRRLEASRDQLRQLFK 210
Cdd:PRK01584 457 HTATHLLHKALRLVLGDhVRQKGSNiTAERLRFDF--SHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREKGA 534
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034562054 211 dnpfkLHLIEEKVtGPTATVYGCGTL-VDLCQGPHLRHTGQIGGLKLLSEQ 260
Cdd:PRK01584 535 -----MALFGEKY-EDIVKVYEIDGFsKEVCGGPHVENTGELGTFKIQKEQ 579
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
532-601 |
7.24e-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: 7.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562054 532 QVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDAdSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIR 601
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-GGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVK 71
|
|
| |
