|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
32-704 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1077.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 32 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIAKVN 111
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 112 NVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSS 189
Cdd:PLN02908 93 GVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 190 LEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNS 269
Cdd:PLN02908 173 IEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 270 STYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIR 349
Cdd:PLN02908 253 SAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 350 SEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLH 429
Cdd:PLN02908 333 EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLH 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 430 RNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRAVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLEN 509
Cdd:PLN02908 413 RNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 510 SLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMI 589
Cdd:PLN02908 493 ALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMF 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 590 AILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEK 669
Cdd:PLN02908 573 AILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEA 651
|
650 660 670
....*....|....*....|....*....|....*
gi 189055088 670 ISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 704
Cdd:PLN02908 652 ATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
71-705 |
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: 889.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 71 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMG 150
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 151 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY--NKFKCRI 227
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 228 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAK 307
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 308 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 386
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 387 FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 466
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 467 CLDFLRAVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQ 545
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 546 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 625
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 626 RQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQlkEFRSK 705
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
142-698 |
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: 667.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 142 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 220
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 221 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 298
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 299 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 377
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 378 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 456
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 457 MEQIEDEIKGCLDFLRAVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 534
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 535 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 614
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 615 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETIE 694
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 189055088 695 RLQQ 698
Cdd:TIGR00418 558 KLRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
309-606 |
0e+00 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 541.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 309 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 388
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 389 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 468
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 469 DFLRAVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 547
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 189055088 548 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 606
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
385-596 |
6.78e-38 |
|
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: 139.08 E-value: 6.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 385 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 462
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 463 EIKGCLDFLRAVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 540
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 189055088 541 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 596
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
238-285 |
2.10e-12 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 62.01 E-value: 2.10e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 189055088 238 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 285
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
32-704 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1077.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 32 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIAKVN 111
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 112 NVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSS 189
Cdd:PLN02908 93 GVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 190 LEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNS 269
Cdd:PLN02908 173 IEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 270 STYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIR 349
Cdd:PLN02908 253 SAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 350 SEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLH 429
Cdd:PLN02908 333 EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLH 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 430 RNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRAVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLEN 509
Cdd:PLN02908 413 RNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 510 SLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMI 589
Cdd:PLN02908 493 ALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMF 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 590 AILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEK 669
Cdd:PLN02908 573 AILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEA 651
|
650 660 670
....*....|....*....|....*....|....*
gi 189055088 670 ISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 704
Cdd:PLN02908 652 ATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
71-705 |
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: 889.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 71 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMG 150
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 151 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY--NKFKCRI 227
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 228 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAK 307
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 308 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 386
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 387 FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 466
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 467 CLDFLRAVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQ 545
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 546 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 625
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 626 RQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQlkEFRSK 705
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
142-698 |
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: 667.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 142 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 220
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 221 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 298
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 299 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 377
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 378 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 456
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 457 MEQIEDEIKGCLDFLRAVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 534
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 535 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 614
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 615 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETIE 694
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 189055088 695 RLQQ 698
Cdd:TIGR00418 558 KLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
68-698 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 651.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 68 SKPIKVTLPDG--KQVDAeswKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSS 145
Cdd:PRK12444 3 EQMIEIKFPDGsvKEFVK---GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 146 AHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYN--K 222
Cdd:PRK12444 80 AHILAQAVKRLYGDVnLGVGPVIENGFYYDMDLPSS-VNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 223 FKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKF 302
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 303 QEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSE 382
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 383 NMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 462
Cdd:PRK12444 319 NMYFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIED 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 463 EIKGCLDFLRAVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGR 542
Cdd:PRK12444 399 EIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 543 YHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTC-DEY 621
Cdd:PRK12444 479 SHQCGTIQLDFQMPEKFDLNYIDEK-NEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVhVQY 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189055088 622 AQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 698
Cdd:PRK12444 558 ADEVADKLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
309-606 |
0e+00 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 541.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 309 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 388
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 389 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 468
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 469 DFLRAVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 547
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 189055088 548 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 606
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
143-704 |
8.62e-155 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 462.06 E-value: 8.62e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 143 HSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEggVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY- 220
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAkVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 221 -NKFKCRILnEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKI--KALKIHKNSSTYWEGKADMETLQRIYGISFPDPKML 296
Cdd:PLN02837 126 nEPYKLEIL-EGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 297 KEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGS-CFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG 375
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 376 HWQHYSENMFS-FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 454
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 455 CAMEQIEDEIKGCLDFLRAVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKID 533
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 534 IQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVP 613
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 614 VGPTCDEYAQKVRQQFHDAKFMADIDLdpGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHGERTISETI 693
Cdd:PLN02837 524 VTDNELEYCKEVVAKLKAKGIRAEVCH--GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFI 601
|
570
....*....|.
gi 189055088 694 ERLQQLKEFRS 704
Cdd:PLN02837 602 NRIQLAVENRT 612
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
289-698 |
1.31e-42 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 163.50 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 289 SFPDPKMLKEWEKFQEEAKNRD--HRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNI 365
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 366 FNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLR---LADFGvlHRNELSGALTGLTR 442
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKmyeLSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 443 VRRFQQDDAHIFC-----AMEQIEDEIKGCLDFLRAV----YSVFGFSfklnlstrpEKFlgdievWDQAEKQLENSLNE 513
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdyEVAIRFT---------EDF------YEENKDWIVELVKR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 514 FG-----EKWElnsgDGAFYGP-KIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVsHDGDDKKRPVIVHRAILGSVER 587
Cdd:PRK03991 398 EGkpvllEILP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYV-DENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 588 MIAILTEN-----YGGK---WPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYN 659
Cdd:PRK03991 473 VIYALLEKaakeeEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 189055088 660 FTLVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 698
Cdd:PRK03991 552 YVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKE 590
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
385-596 |
6.78e-38 |
|
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: 139.08 E-value: 6.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 385 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 462
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 463 EIKGCLDFLRAVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 540
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 189055088 541 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 596
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
606-697 |
1.81e-34 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238437 [Multi-domain] Cd Length: 91 Bit Score: 126.08 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 606 PRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDpGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVHG 685
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 189055088 686 ERTISETIERLQ 697
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| 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 ... |
337-593 |
4.61e-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: 110.17 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 337 GAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKE-----LFALKPMNCPGHCLMFDHR 411
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 412 PRSWRELPLRLADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRAVYSVFGFSFKLNLSTRPE 491
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 492 KFLGDievwdqaekqlenslnefgekwelNSGDGAFYGPKIDIQIKDAI-GRYHQCATIQLDFQLPIRFNLTYVSHDGDD 570
Cdd:cd00670 160 FGRGG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|...
gi 189055088 571 KKrPVIVHRAilGSVERMIAILT 593
Cdd:cd00670 216 RA-HTGCGGA--GGEERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
71-136 |
5.84e-27 |
|
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: 104.11 E-value: 5.84e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189055088 71 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEE 136
Cdd:cd01667 1 IKITLPDGSVKEFPK-GTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
608-699 |
6.75e-23 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 93.42 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 608 QVMVVPVGPTCD---EYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNKVH 684
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNE-SIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 189055088 685 GERTISETIERLQQL 699
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
71-131 |
3.55e-18 |
|
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: 78.74 E-value: 3.55e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189055088 71 IKVTLPDGKQVDAESWkTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLK 131
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 ... |
340-508 |
5.01e-16 |
|
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: 77.54 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 340 IYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWqhYSENMFSFEVEKELFALKPMNCPGHCLMF-DHRprswREL 418
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFvSHI----RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 419 PLRLADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRAVYSVFGFS--FKLNLSTRPEKFLG- 495
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKldIVFVEKTPGEFSPGg 152
|
170
....*....|....*...
gi 189055088 496 -----DIEVWDQAEKQLE 508
Cdd:cd00768 153 agpgfEIEVDHPEGRGLE 170
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
238-285 |
2.10e-12 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 197931 [Multi-domain] Cd Length: 43 Bit Score: 62.01 E-value: 2.10e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 189055088 238 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 285
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
238-285 |
9.77e-10 |
|
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.
Pssm-ID: 429764 [Multi-domain] Cd Length: 43 Bit Score: 54.37 E-value: 9.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 189055088 238 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKnsstyWEGKADMetLQRI 285
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-----GESKNKG--LRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
601-706 |
5.04e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 49.46 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 601 PFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADID-LDPGctLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTR 679
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDdLDDS--LGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
90 100
....*....|....*....|....*..
gi 189055088 680 DNKVHGERTISETIERLQQLKEFRSKQ 706
Cdd:PRK14938 347 ANNEQKSMTVEELVKEIKRADELKERS 373
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
606-697 |
5.65e-06 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 45.08 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 606 PRQVMVVPVG---PTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTVNIRTRDNK 682
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 189055088 683 VHGERTISETIERLQ 697
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
329-495 |
8.65e-06 |
|
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: 48.13 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 329 GSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG-HWQHYSENMFSF-----EVEKELFALKPMNCP 402
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 403 GHCLMFDHRPRSWRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCA-MEQIEDEIKGCLDFLRAVYSVFG-F 480
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 189055088 481 SFKLNLSTRPEKFLG 495
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
326-462 |
1.66e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 46.80 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 326 LSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSF-EVEKELFALKPMNCPGH 404
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkDRHGKEFLLGPTHEEVI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189055088 405 CLMFDHRPRSWRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF-----CAMEQIED 462
Cdd:cd00779 99 TDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdideeSLEETYEK 160
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
608-697 |
3.35e-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: 37.13 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 608 QVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLdpgctLNKKIRnAQLAQYN-----FTLVVGEKEKISGTVNIrtRDNK 682
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK-KQFKYADrsgarFAVILGEDELAAGVVTV--KDLE 74
|
90
....*....|....*..
gi 189055088 683 VHGERTISET--IERLQ 697
Cdd:cd00859 75 TGEQETVALDelVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
601-711 |
5.50e-03 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 38.82 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189055088 601 PFWLSPRQVMVVPVGPTCD------EYAQKVRQQFHDAKFMADIDLDPGCTLNKKIRNAQLAQYNFTLVVGEKEKISGTV 674
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 189055088 675 NIRTRDNK----VHGERTISETIERLQQLKEFRSKQAEEEF 711
Cdd:cd00862 85 VIVRRDTGekktVPLAELVEKVPELLDEIQEDLYERALEFR 125
|
|
| |
