|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
27-689 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 801.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 27 EASAPTP----PHWLAERFGLFEELWTAHVKKLASmtqKKARAIKISLPEGQKVDAVAWNTTPYQLAHQISVTLADTAVA 102
Cdd:PLN02908 12 APSHPSDeeylSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 103 AEVNGELYDLDRPLETDCHLRFLTFDSPEGKAVFWHSSAHVLGAAAEQQLGAVLCRGPSTES--GFYHDFFLGkERTVRS 180
Cdd:PLN02908 89 AQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLNE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 181 AELPILERICQELIAAAQPFRRLEASRDQLRQLFKDNHFKLHLIEEKVTGPTATVYGCGMSVDLCRGPHLRHTGQIGALK 260
Cdd:PLN02908 168 EDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 261 LLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNAL 340
Cdd:PLN02908 248 CLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 341 VAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdgvdnsqsghparCPKDTLALKPMNCPAHCLM 420
Cdd:PLN02908 328 MDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFE-----------------IEKQEFGLKPMNCPGHCLM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 421 FAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHLALS 500
Cdd:PLN02908 391 FAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 501 TRPPGFLGEPRLWDQAEQ--------------------------IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPA 554
Cdd:PLN02908 471 TRPEKYLGDLETWDKAEAaltealnafgkpwqlnegdgafygpkIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAED 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 555 GT-PECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDAdSGLTLS 633
Cdd:PLN02908 551 EAkIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKIQ 629
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 254692867 634 RRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 689
Cdd:PLN02908 630 KKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
66-684 |
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: 727.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 66 IKISLPEGQKVDaVAWNTTPYQLAHQISVTLADTAVAAEVNGELYDLDRPLETDCHLRFLTFDSPEGKAVFWHSSAHVLg 145
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 146 AAAEQQL--GAVLCRGPSTESGFYHDFFLgkERTVRSAELPILERICQELIAAAQPFRRLEASRDQLRQLFK--DNHFKL 221
Cdd:COG0441 80 AQAVKRLypDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 222 HLIEEKVTGPTATVYGCGMSVDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREA 301
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 302 AELRDHRRIGKEQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADM 380
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 381 FSLKppgTDGVDnsqsghparcpkdtLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQ 460
Cdd:COG0441 318 FPTE---SDGEE--------------YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 461 QDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAEQ--------------------- 518
Cdd:COG0441 381 QDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAalrealeelgleyvinpgega 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 519 -----IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPL 593
Cdd:COG0441 461 fygpkIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPV 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 594 QVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGER 673
Cdd:COG0441 541 QVVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTM 619
|
650
....*....|.
gi 254692867 674 DLAESVQRLLE 684
Cdd:COG0441 620 SLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
137-682 |
0e+00 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 545.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 137 WHSSAHVLGAAAEQ-QLGAVLCRGPSTESGFYHDFFLGKERTVrsAELPILERICQELIAAAQPFRRLEASRDQLRQLFK 215
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 216 -DNHFKLHLIEEKVTGPTATVYGCGMS-VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLR 293
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKAfVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 294 NWEARREAAELRDHRRIGKEQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGH 372
Cdd:TIGR00418 159 AYLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 373 WEHYRADMFSLKppgtdGVDNSqsghparcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGG 452
Cdd:TIGR00418 239 WDNYKERMFPFT-----ELDNR-----------EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 453 LTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHLA-LSTRPPG-FLGEPRLWDQAE------------- 517
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRDPEdFIGEDELWEKAEaaleealkelgvp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 518 -------------QIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGG 584
Cdd:TIGR00418 383 yeidpgrgafygpKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 585 KWPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRT 664
Cdd:TIGR00418 463 NFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*...
gi 254692867 665 RDNRQLGERDLAESVQRL 682
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKL 559
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
305-592 |
1.31e-143 |
|
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: 420.80 E-value: 1.31e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 305 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 385 PPgtdgvdnsqsghparcpKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDA 464
Cdd:cd00771 81 EE-----------------DEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 465 HIFCAPHQLEAEIQGCLDFLRCVYSVLGF-SFHLALSTRPPGFLGEPRLWDQAEQ------------------------- 518
Cdd:cd00771 144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAalrealeeiglpyeinegegafygp 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254692867 519 -IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSP 592
Cdd:cd00771 224 kIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
404-581 |
4.09e-35 |
|
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: 131.38 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 404 KDTLALKPMNCPAHCLMFA-HRPRSWReLPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLD 482
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 483 FLRCVYSVLGFSFH-LALSTRPPGFLGEPRLwdqaeQIDVHLHdALGRPHQCGTIQLD-FQLPLRFDLQYKGPAGTPECP 560
Cdd:pfam00587 87 LIDRVYSRLGLEVRvVRLSNSDGSAFYGPKL-----DFEVVFP-SLGKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFP 160
|
170 180
....*....|....*....|.
gi 254692867 561 VLIHRAVLGsVERLLGVLAES 581
Cdd:pfam00587 161 YMIHRAGLG-VERFLAAILEN 180
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
234-281 |
2.76e-11 |
|
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: 58.55 E-value: 2.76e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 254692867 234 TVYGCG-MSVDLCRGPHLRHTGQIGALKLLTNSSALWRslgapetLQRV 281
Cdd:smart00863 2 RVVSIGdFSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
27-689 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 801.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 27 EASAPTP----PHWLAERFGLFEELWTAHVKKLASmtqKKARAIKISLPEGQKVDAVAWNTTPYQLAHQISVTLADTAVA 102
Cdd:PLN02908 12 APSHPSDeeylSAVIKKRIELFEKIQARQLARLES---AGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 103 AEVNGELYDLDRPLETDCHLRFLTFDSPEGKAVFWHSSAHVLGAAAEQQLGAVLCRGPSTES--GFYHDFFLGkERTVRS 180
Cdd:PLN02908 89 AQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYG-DRTLNE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 181 AELPILERICQELIAAAQPFRRLEASRDQLRQLFKDNHFKLHLIEEKVTGPTATVYGCGMSVDLCRGPHLRHTGQIGALK 260
Cdd:PLN02908 168 EDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 261 LLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNAL 340
Cdd:PLN02908 248 CLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 341 VAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdgvdnsqsghparCPKDTLALKPMNCPAHCLM 420
Cdd:PLN02908 328 MDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFE-----------------IEKQEFGLKPMNCPGHCLM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 421 FAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHLALS 500
Cdd:PLN02908 391 FAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 501 TRPPGFLGEPRLWDQAEQ--------------------------IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPA 554
Cdd:PLN02908 471 TRPEKYLGDLETWDKAEAaltealnafgkpwqlnegdgafygpkIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAED 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 555 GT-PECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDAdSGLTLS 633
Cdd:PLN02908 551 EAkIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDV-TDRKIQ 629
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 254692867 634 RRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 689
Cdd:PLN02908 630 KKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
66-684 |
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: 727.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 66 IKISLPEGQKVDaVAWNTTPYQLAHQISVTLADTAVAAEVNGELYDLDRPLETDCHLRFLTFDSPEGKAVFWHSSAHVLg 145
Cdd:COG0441 2 IKITLPDGSVRE-FEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 146 AAAEQQL--GAVLCRGPSTESGFYHDFFLgkERTVRSAELPILERICQELIAAAQPFRRLEASRDQLRQLFK--DNHFKL 221
Cdd:COG0441 80 AQAVKRLypDAKLTIGPVIENGFYYDFDL--ERPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKekGEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 222 HLIEEKVTGPTATVYGCGMSVDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREA 301
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 302 AELRDHRRIGKEQELFFFH-ELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADM 380
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 381 FSLKppgTDGVDnsqsghparcpkdtLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQ 460
Cdd:COG0441 318 FPTE---SDGEE--------------YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 461 QDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAEQ--------------------- 518
Cdd:COG0441 381 QDDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAalrealeelgleyvinpgega 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 519 -----IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPL 593
Cdd:COG0441 461 fygpkIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPV 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 594 QVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGER 673
Cdd:COG0441 541 QVVVLPISDKHADYAKEVAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTM 619
|
650
....*....|.
gi 254692867 674 DLAESVQRLLE 684
Cdd:COG0441 620 SLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
137-682 |
0e+00 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 545.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 137 WHSSAHVLGAAAEQ-QLGAVLCRGPSTESGFYHDFFLGKERTVrsAELPILERICQELIAAAQPFRRLEASRDQLRQLFK 215
Cdd:TIGR00418 1 RHSIAHLLAEALKQlYPDVKLAIGPVVEDGFYYDFELDRSFTQ--EDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 216 -DNHFKLHLIEEKVTGPTATVYGCGMS-VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLR 293
Cdd:TIGR00418 79 vLEPYKLELLDEIPNGVKRTPYGWGKAfVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 294 NWEARREAAELRDHRRIGKEQELFFFHELS-PGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGH 372
Cdd:TIGR00418 159 AYLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 373 WEHYRADMFSLKppgtdGVDNSqsghparcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGG 452
Cdd:TIGR00418 239 WDNYKERMFPFT-----ELDNR-----------EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 453 LTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHLA-LSTRPPG-FLGEPRLWDQAE------------- 517
Cdd:TIGR00418 303 LMRVRGFTQDDAHIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRDPEdFIGEDELWEKAEaaleealkelgvp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 518 -------------QIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGG 584
Cdd:TIGR00418 383 yeidpgrgafygpKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 585 KWPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRT 664
Cdd:TIGR00418 463 NFPLWLAPVQVVVIPVNERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRT 541
|
570
....*....|....*...
gi 254692867 665 RDNRQLGERDLAESVQRL 682
Cdd:TIGR00418 542 RKGQKLEKMSLDEFLEKL 559
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
62-689 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 529.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 62 KARAIKISLPEGQKVDAVAwNTTPYQLAHQISVTLADTAVAAEVNGELYDLDRPLETDCHLRFLTFDSPEGKAVFWHSSA 141
Cdd:PRK12444 2 KEQMIEIKFPDGSVKEFVK-GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 142 HVLGAAAEQQLGAV-LCRGPSTESGFYHDFFLGKerTVRSAELPILERICQELIAAAQPFRRLEASRDQLRQLFKDN--H 218
Cdd:PRK12444 81 HILAQAVKRLYGDVnLGVGPVIENGFYYDMDLPS--SVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 219 FKLHLIEEKVTGPTATVYGCGMSVDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEAR 298
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 299 REAAELRDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRA 378
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 379 DM-FSlkppgtdGVDNSqsghparcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLW 457
Cdd:PRK12444 319 NMyFS-------EVDNK-----------SFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 458 RFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHLALSTRPPGFLGEPRLWDQAE-------------------- 517
Cdd:PRK12444 381 TFCQDDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEaslenvlqslnykyrlnegd 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 518 ------QIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLS 591
Cdd:PRK12444 461 gafygpKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 592 PLQVVVIPVRTE-QEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQL 670
Cdd:PRK12444 541 PVQVKVIPVSNAvHVQYADEVADKLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS 619
|
650
....*....|....*....
gi 254692867 671 GERDLAESVQRLLELQNAR 689
Cdd:PRK12444 620 EVIELDMFVESIKEEIKNR 638
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
305-592 |
1.31e-143 |
|
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: 420.80 E-value: 1.31e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 305 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 385 PPgtdgvdnsqsghparcpKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDA 464
Cdd:cd00771 81 EE-----------------DEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 465 HIFCAPHQLEAEIQGCLDFLRCVYSVLGF-SFHLALSTRPPGFLGEPRLWDQAEQ------------------------- 518
Cdd:cd00771 144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAalrealeeiglpyeinegegafygp 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254692867 519 -IDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSP 592
Cdd:cd00771 224 kIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
138-682 |
2.52e-106 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 336.10 E-value: 2.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 138 HSSAHVLgAAAEQQL--GAVLCRGPSTESGFYHDF----FLGKErtvrsaelpiLERICQEL---IAAAQPFRRLEASRD 208
Cdd:PLN02837 48 HTCAHVM-AMAVQKLfpDAKVTIGPWIENGFYYDFdmepLTDKD----------LKRIKKEMdriISRNLPLVREEVSRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 209 QLRQLFK--DNHFKLHLIEEKVTGPTaTVYGCGMSV-DLCRGPHLRHTGQIG--ALKLLTNSSALWRSLGAPETLQRVSG 283
Cdd:PLN02837 117 EAQKRIMaiNEPYKLEILEGIKEEPI-TIYHIGEEWwDLCAGPHVERTGKINkkAVELESVAGAYWRGDEKNQMLQRIYG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 284 ISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHELSPGS-CFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLF 362
Cdd:PLN02837 196 TAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 363 STKLWEQSGHWEHYRADMFSlkppgtdgvdnsqsghPARCPKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALH 442
Cdd:PLN02837 276 KADLWKTSGHLDFYKENMYD----------------QMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 443 RAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAE---- 517
Cdd:PLN02837 340 RYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATtalr 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 518 ----------------------QIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLL 575
Cdd:PLN02837 420 dalddkgweykvdegggafygpKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFF 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 576 GVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLdaDSGLTLSRRVRRAQLAHYNFQFVVGQREQ 655
Cdd:PLN02837 500 GVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV--CHGERLPKLIRNAETQKIPLMAVVGPKEV 577
|
570 580
....*....|....*....|....*..
gi 254692867 656 SQRTVNVRTRDNRQLGERDLAESVQRL 682
Cdd:PLN02837 578 ETRTLTVRSRHGGELGTMPVDDFINRI 604
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
404-581 |
4.09e-35 |
|
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: 131.38 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 404 KDTLALKPMNCPAHCLMFA-HRPRSWReLPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLD 482
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 483 FLRCVYSVLGFSFH-LALSTRPPGFLGEPRLwdqaeQIDVHLHdALGRPHQCGTIQLD-FQLPLRFDLQYKGPAGTPECP 560
Cdd:pfam00587 87 LIDRVYSRLGLEVRvVRLSNSDGSAFYGPKL-----DFEVVFP-SLGKQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFP 160
|
170 180
....*....|....*....|.
gi 254692867 561 VLIHRAVLGsVERLLGVLAES 581
Cdd:pfam00587 161 YMIHRAGLG-VERFLAAILEN 180
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
427-684 |
7.46e-29 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 122.29 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 427 SWRELPVR---LADFGalHRAEASGSLGGLTRLWRFQQDDAHIFC-----APHQLEAEIQGCLDFLRCV---YSVL---- 491
Cdd:PRK03991 303 SYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdYEVAirft 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 492 --------GFSFHLALSTRPPGFLgepRLWDQAE-----QIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPE 558
Cdd:PRK03991 381 edfyeenkDWIVELVKREGKPVLL---EILPERKhywvlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 559 CPVLIHRAVLGSVERLLGVLAE-----SCGGK---WPLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGL 630
Cdd:PRK03991 458 YPIILHCSPTGSIERVIYALLEkaakeEEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDE 536
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 254692867 631 TLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTR-DNRQLgERDLAESVQRLLE 684
Cdd:PRK03991 537 SLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIReESEKV-EMTLEELIERIKE 590
|
|
| 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 ... |
333-578 |
8.43e-27 |
|
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: 109.40 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 333 GTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKPPGTDGVDNSqsghparcpkdtLALKPM 412
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRDTD------------LVLRPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 413 NCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSlGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLG 492
Cdd:cd00670 69 ACEPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 493 FSFHLALSTRPPGFLGEPRLWD-QAEQ-IDVHLHDAL-GRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAvlG 569
Cdd:cd00670 148 LPVRVVVADDPFFGRGGKRGLDaGRETvVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGGRAHTGCGGA--G 225
|
....*....
gi 254692867 570 SVERLLGVL 578
Cdd:cd00670 226 GEERLVLAL 234
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
592-683 |
2.45e-26 |
|
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: 102.97 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 592 PLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLG 671
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 254692867 672 ERDLAESVQRLL 683
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
66-131 |
6.51e-22 |
|
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: 89.47 E-value: 6.51e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254692867 66 IKISLPEGqKVDAVAWNTTPYQLAHQISVTLADTAVAAEVNGELYDLDRPLETDCHLRFLTFDSPE 131
Cdd:cd01667 1 IKITLPDG-SVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
594-685 |
1.26e-18 |
|
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: 81.09 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 594 QVVVIPV---RTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQL 670
Cdd:pfam03129 1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 254692867 671 GERDLAESVQRLLEL 685
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
338-574 |
9.22e-14 |
|
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: 70.99 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 338 NALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRAdmfslkpPGTDGVDNSqsghparcpkdtLALKPMNCPAH 417
Cdd:cd00768 3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLL-------PVGAENEED------------LYLRPTLEPGL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 418 CLMFAHRPRSwreLPVRLADFGALHRAEASGSlgGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGFSFHL 497
Cdd:cd00768 64 VRLFVSHIRK---LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDI 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254692867 498 ALSTRPPGFLGEPRLWDqaeQIDVHLHDALGRPHQCGTIQLDFQLPLR-FDLQYKGPAGTPECPVLIHRAvlGSVERL 574
Cdd:cd00768 139 VFVEKTPGEFSPGGAGP---GFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGFG--LGLERL 211
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
66-126 |
3.24e-13 |
|
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: 64.49 E-value: 3.24e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254692867 66 IKISLPEGQKVDAVAWnTTPYQLAHQISVTLADTAVAAEVNGELYDLDRPLETDCHLRFLT 126
Cdd:pfam02824 1 IRVYTPDGKVPDLPRG-ATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
234-281 |
2.76e-11 |
|
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: 58.55 E-value: 2.76e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 254692867 234 TVYGCG-MSVDLCRGPHLRHTGQIGALKLLTNSSALWRslgapetLQRV 281
Cdd:smart00863 2 RVVSIGdFSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
234-266 |
2.80e-08 |
|
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: 50.14 E-value: 2.80e-08
10 20 30
....*....|....*....|....*....|....
gi 254692867 234 TVYGCG-MSVDLCRGPHLRHTGQIGALKLLTNSS 266
Cdd:pfam07973 2 RVVSIGdFDVDLCGGTHVPNTGEIGAFKILKGES 35
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
322-384 |
3.68e-08 |
|
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: 54.89 E-value: 3.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254692867 322 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLK 81
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
587-687 |
2.93e-07 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 53.31 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 587 PLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRD 666
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRA 347
|
90 100
....*....|....*....|....*..
gi 254692867 667 N---RQLGERDLAESVQR---LLELQN 687
Cdd:PRK14938 348 NneqKSMTVEELVKEIKRadeLKERSN 374
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
592-683 |
1.08e-05 |
|
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: 44.31 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 592 PLQVVVIPV---RTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNR 668
Cdd:cd00738 1 PIDVAIVPLtdpRVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 254692867 669 QLGERDLAESVQRLL 683
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProS |
COG0442 |
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
329-384 |
2.38e-05 |
|
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: 47.46 E-value: 2.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254692867 329 FLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:COG0442 42 YLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVT 97
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
322-384 |
1.02e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 45.46 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254692867 322 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:PRK09194 35 LASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELWQESGRWEEYGPELLRLK 97
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
329-384 |
3.44e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.69 E-value: 3.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254692867 329 FLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 384
Cdd:PRK12325 42 WLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLRIK 97
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
591-697 |
1.24e-03 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 40.74 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 591 SPLQVVVIPV------RTEQEEYARQVQQCLQAAGLVSDLDADSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRT 664
Cdd:cd00862 9 APIQVVIVPIgikdekREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 254692867 665 RDNR---QLGERDLAESVQRLLEL-QNARVPNAEEVF 697
Cdd:cd00862 89 RDTGekkTVPLAELVEKVPELLDEiQEDLYERALEFR 125
|
|
| PRK01584 |
PRK01584 |
alanyl-tRNA synthetase; Provisional |
138-261 |
7.92e-03 |
|
alanyl-tRNA synthetase; Provisional
Pssm-ID: 234962 [Multi-domain] Cd Length: 594 Bit Score: 39.37 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254692867 138 HSSAHVLGAAAEQQLGA-VLCRGPS-TESGFYHDFflGKERTVRSAELPILERICQELIAAAQPFRRLEASRDQLRQLFK 215
Cdd:PRK01584 457 HTATHLLHKALRLVLGDhVRQKGSNiTAERLRFDF--SHPEKMTDDEIKKVEDIVNLQIKNDLSVKKEVMSLEEAREKGA 534
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 254692867 216 dnhfkLHLIEEKVtGPTATVYGC-GMSVDLCRGPHLRHTGQIGALKL 261
Cdd:PRK01584 535 -----MALFGEKY-EDIVKVYEIdGFSKEVCGGPHVENTGELGTFKI 575
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
587-639 |
8.48e-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: 36.77 E-value: 8.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 254692867 587 PLWLSPLQVVVIPV--RTEQEEYARQVQQCLQAAGLVSDLDaDSGlTLSRRVRRA 639
Cdd:cd00858 21 PPALAPIKVAVLPLvkRDELVEIAKEISEELRELGFSVKYD-DSG-SIGRRYARQ 73
|
|
| |
