|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
1-683 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1100.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 1 MKKEKKEKPSGGGDTRKELSPLPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQ 80
Cdd:PLN02908 1 MAMPAATASAAAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 81 GLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIEN--GFYYDMHL 158
Cdd:PLN02908 81 GLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 159 EGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHT 238
Cdd:PLN02908 161 GDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 239 GKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRG 318
Cdd:PLN02908 241 SFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 319 AHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRE 398
Cdd:PLN02908 321 ARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 399 LPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGEL 478
Cdd:PLN02908 401 LPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 479 EQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKK-RPVII 557
Cdd:PLN02908 481 ETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 558 HRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFmsEADCDAGD-TMNKKIRNAQLA 636
Cdd:PLN02908 561 HRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGF--YVDVDVTDrKIQKKVREAQLA 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 22946308 637 QFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQKIRDEF 683
Cdd:PLN02908 639 QYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
52-678 |
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: 904.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 52 IKVTLPDG--KQVDAtswETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHI 129
Cdd:COG0441 2 IKITLPDGsvREFEA---GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 130 MGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY--NEFKV 206
Cdd:COG0441 79 LAQAVKRLYPDaKLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 207 RILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEE 286
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 287 AAKRDHRKIGREQELFFFH-ELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENM 365
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 366 FSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEM 445
Cdd:COG0441 318 FPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 446 KGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRA 524
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 525 HQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQS 604
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22946308 605 VRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 678
Cdd:COG0441 558 VAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
123-678 |
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: 686.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 123 WHSSAHIMGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY 201
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELD-RSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 202 NE-FKVRILNEKVTTDRTTVYKCG-SLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKE 279
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 280 WEKLQEEAAKRDHRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHW 358
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 359 QHYAENMFSFEAEKEK-FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 437
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 438 PEQIKSEMKGCLEFLKYVYTIFGFSFQLV-LSTR-PDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDI 515
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 516 TIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVG 595
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 596 PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITK 675
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEK 558
|
...
gi 22946308 676 LQK 678
Cdd:TIGR00418 559 LRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
290-586 |
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: 539.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 290 RDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFE 369
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 370 AEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCL 449
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 450 EFLKYVYTIFGF-SFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 528
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 22946308 529 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSP 586
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
366-576 |
1.53e-41 |
|
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: 149.10 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 366 FSFEAE-KEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSE 444
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 445 MKGCLEFLKYVYTIFGFSFQ-LVLSTRPDNylgeleqwndaekalaeslnefgmpwkenpgdgAFYGPKIDIT-IMDALK 522
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEvVFPSLG 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22946308 523 RAHQCATIQLD-FQLPIRFNLSYIADDGEKKRPVIIHRAILGsVERMIAILTENF 576
Cdd:pfam00587 128 KQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
219-266 |
1.61e-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: 1.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 22946308 219 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKNSSTYWEgkadaetLQRV 266
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
1-683 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1100.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 1 MKKEKKEKPSGGGDTRKELSPLPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQ 80
Cdd:PLN02908 1 MAMPAATASAAAPSHPSDEEYLSAVIKKRIELFEKIQARQLARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 81 GLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIEN--GFYYDMHL 158
Cdd:PLN02908 81 GLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 159 EGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHT 238
Cdd:PLN02908 161 GDRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 239 GKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRG 318
Cdd:PLN02908 241 SFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 319 AHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRE 398
Cdd:PLN02908 321 ARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 399 LPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGEL 478
Cdd:PLN02908 401 LPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 479 EQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKK-RPVII 557
Cdd:PLN02908 481 ETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIeRPVMI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 558 HRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFmsEADCDAGD-TMNKKIRNAQLA 636
Cdd:PLN02908 561 HRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGF--YVDVDVTDrKIQKKVREAQLA 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 22946308 637 QFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQKIRDEF 683
Cdd:PLN02908 639 QYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
52-678 |
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: 904.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 52 IKVTLPDG--KQVDAtswETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHI 129
Cdd:COG0441 2 IKITLPDGsvREFEA---GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 130 MGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY--NEFKV 206
Cdd:COG0441 79 LAQAVKRLYPDaKLTIGPVIENGFYYDFDLE-RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 207 RILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEE 286
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 287 AAKRDHRKIGREQELFFFH-ELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENM 365
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 366 FSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEM 445
Cdd:COG0441 318 FPTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 446 KGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRA 524
Cdd:COG0441 398 KKVIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGRE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 525 HQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQS 604
Cdd:COG0441 478 WQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22946308 605 VRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 678
Cdd:COG0441 558 VAKKLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
123-678 |
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: 686.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 123 WHSSAHIMGEAMERIYGG-HLCYGPPIENGFYYDMHLEgEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKY 201
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELD-RSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 202 NE-FKVRILNEKVTTDRTTVYKCG-SLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKE 279
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 280 WEKLQEEAAKRDHRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHW 358
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 359 QHYAENMFSFEAEKEK-FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 437
Cdd:TIGR00418 240 DNYKERMFPFTELDNReFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 438 PEQIKSEMKGCLEFLKYVYTIFGFSFQLV-LSTR-PDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDI 515
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFDKYeLSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 516 TIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVG 595
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 596 PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITK 675
Cdd:TIGR00418 480 ERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEK 558
|
...
gi 22946308 676 LQK 678
Cdd:TIGR00418 559 LRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
52-678 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 655.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 52 IKVTLPDGkQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMG 131
Cdd:PRK12444 6 IEIKFPDG-SVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 132 EAMERIYGG-HLCYGPPIENGFYYDMHLeGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNE--FKVRI 208
Cdd:PRK12444 85 QAVKRLYGDvNLGVGPVIENGFYYDMDL-PSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMNdrLKLEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 209 LNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAA 288
Cdd:PRK12444 164 LEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 289 KRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSF 368
Cdd:PRK12444 244 KRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMYFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 369 EAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGC 448
Cdd:PRK12444 324 EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 449 LEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 528
Cdd:PRK12444 404 MAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 529 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPA-YDQYAQSVRD 607
Cdd:PRK12444 484 TIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVAD 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22946308 608 QLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 678
Cdd:PRK12444 564 KLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
290-586 |
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: 539.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 290 RDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFE 369
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 370 AEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCL 449
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 450 EFLKYVYTIFGF-SFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCA 528
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 22946308 529 TIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSP 586
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
124-677 |
4.73e-150 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 448.96 E-value: 4.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 124 HSSAHIMGEAMERIY-GGHLCYGPPIENGFYYDMHLEGegISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFK-Y 201
Cdd:PLN02837 48 HTCAHVMAMAVQKLFpDAKVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMaI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 202 NE-FKVRILnEKVTTDRTTVYKCGS-LIDLCRGPHVRHTGKV--KALKITKNSSTYWEGKADAETLQRVYGISFPDPKQL 277
Cdd:PLN02837 126 NEpYKLEIL-EGIKEEPITIYHIGEeWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 278 KEWEKLQEEAAKRDHRKIGREQELFFFHELSPGS-CFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSG 356
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 357 HWQHYAENMFS-FEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 435
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 436 CAPEQIKSEMKGCLEFLKYVYTIFGFS-FQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKID 514
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 515 ITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPV 594
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPV 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 595 GPAYDQYAQSVRDQLHDAGFMSEAdCDaGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELIT 674
Cdd:PLN02837 525 TDNELEYCKEVVAKLKAKGIRAEV-CH-GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFIN 602
|
...
gi 22946308 675 KLQ 677
Cdd:PLN02837 603 RIQ 605
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
270-678 |
6.66e-50 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 184.30 E-value: 6.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 270 SFPDPKQLKEWEKLQEEAAKRD--HRKIGREQELFFFHELS-PGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNI 346
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 347 YNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRM---ADFGvlHRNELSGALTGLTR 423
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKMyelSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 424 VRRFQQDDAHIFC-----APEQIKSEMKGCLEFLK-----YVyTIFGFsfqlvlsTRpDNYlgelEQWNDAEKALAEsln 493
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEdlgrdYE-VAIRF-------TE-DFY----EENKDWIVELVK--- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 494 EFGMP-----WKEnpgdGAFYGP-KIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVER 567
Cdd:PRK03991 397 REGKPvlleiLPE----RKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYVDENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 568 MIAILTENFA-----GK---WPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFN 639
Cdd:PRK03991 473 VIYALLEKAAkeeeeGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 22946308 640 FILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQK 678
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 ... |
366-576 |
1.53e-41 |
|
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: 149.10 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 366 FSFEAE-KEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSE 444
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 445 MKGCLEFLKYVYTIFGFSFQ-LVLSTRPDNylgeleqwndaekalaeslnefgmpwkenpgdgAFYGPKIDIT-IMDALK 522
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRvVRLSNSDGS---------------------------------AFYGPKLDFEvVFPSLG 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22946308 523 RAHQCATIQLD-FQLPIRFNLSYIADDGEKKRPVIIHRAILGsVERMIAILTENF 576
Cdd:pfam00587 128 KQRQTGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
586-677 |
1.64e-36 |
|
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: 131.86 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 586 PRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHG 665
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 22946308 666 EVSVAELITKLQ 677
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 ... |
318-573 |
2.01e-28 |
|
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: 114.03 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 318 GAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEK-----FALKPMNCPGHCLIFDNR 392
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtdLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 393 NRSWRELPLRMADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPD 472
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 473 nylgeleqwndaekalaeslneFGMPWKEnpGDGAFYGPKIDITIMDAL-KRAHQCATIQLDFQLPIRFNLSYIADDGEK 551
Cdd:cd00670 160 ----------------------FGRGGKR--GLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|..
gi 22946308 552 KRPVIIHRAilGSVERMIAILT 573
Cdd:cd00670 216 RAHTGCGGA--GGEERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
52-117 |
4.18e-25 |
|
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: 98.71 E-value: 4.18e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22946308 52 IKVTLPDGKQVDAtSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPE 117
Cdd:cd01667 1 IKITLPDGSVKEF-PKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
588-679 |
2.49e-24 |
|
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: 97.27 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 588 QVMVVPVGP---AYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVH 664
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 22946308 665 GEVSVAELITKLQKI 679
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 ... |
321-568 |
2.67e-20 |
|
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: 89.87 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 321 IYNTLMGFIKAeyrkRGFQEVISPNIYNAKLWMTSGHWqhYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSwreLP 400
Cdd:cd00768 5 IEQKLRRFMAE----LGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRK---LP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 401 LRMADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLstrpdnylgeLEQ 480
Cdd:cd00768 76 LRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIVF----------VEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 481 WNDAEKAlaeslnefgmpwkenpgdgAFYGPKIDITIMDALKRAHQCATIQLDFQLPIR-FNLSYIADDGEKKRPVIIHR 559
Cdd:cd00768 144 TPGEFSP-------------------GGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGF 204
|
....*....
gi 22946308 560 AIlgSVERM 568
Cdd:cd00768 205 GL--GLERL 211
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|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
52-112 |
1.32e-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: 79.90 E-value: 1.32e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22946308 52 IKVTLPDGKQVDATSWETtPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLK 112
Cdd:pfam02824 1 IRVYTPDGKVPDLPRGAT-PEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
219-266 |
1.61e-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: 1.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 22946308 219 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKNSSTYWEgkadaetLQRV 266
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
219-266 |
1.14e-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: 57.07 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 22946308 219 TVYKCGSL-IDLCRGPHVRHTGKVKALKITKnsstyweGKADAETLQRV 266
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-------GESKNKGLRRI 43
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|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
586-677 |
2.66e-08 |
|
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: 51.63 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 586 PRQVMVVPVG---PAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNK 662
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 22946308 663 VHGEVSVAELITKLQ 677
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
581-678 |
6.75e-07 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 52.15 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 581 PFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADcDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRD 660
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRA 347
|
90
....*....|....*...
gi 22946308 661 NKVHGEVSVAELITKLQK 678
Cdd:PRK14938 348 NNEQKSMTVEELVKEIKR 365
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
588-677 |
1.02e-06 |
|
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: 47.15 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 588 QVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADCdagdtMNKKIRnaqlAQFN--------FILVVGDKERSSNTVNVR-- 657
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK----KQFKyadrsgarFAVILGEDELAAGVVTVKdl 73
|
90 100
....*....|....*....|
gi 22946308 658 TRDNKVhgEVSVAELITKLQ 677
Cdd:cd00859 74 ETGEQE--TVALDELVEELK 91
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
581-683 |
7.58e-05 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 44.21 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 581 PFWLSPRQVMVVPVGPAYD------QYAQSVRDQLHDAGFMSEADCDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTV 654
Cdd:cd00862 5 PPRVAPIQVVIVPIGIKDEkreevlEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTV 84
|
90 100
....*....|....*....|....*....
gi 22946308 655 NVRTRDNKVHGEVSVAELITKLQKIRDEF 683
Cdd:cd00862 85 VIVRRDTGEKKTVPLAELVEKVPELLDEI 113
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
310-476 |
4.94e-04 |
|
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: 42.36 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 310 GSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSG-HWQHYAENMFSF-----EAEKEKFALKPMNCP 383
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 384 GHCLIFDNRNRSWRELPLRMADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCAP-EQIKSEMKGCLEFLKYVYTIFG-F 461
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHADaEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 22946308 462 SFQLVLSTRPDNYLG 476
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
305-435 |
5.70e-04 |
|
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: 42.18 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946308 305 HELSPGSCFFQPRGAHIYNTL-MGF---------IKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEK 374
Cdd:cd00779 7 HKLLLRAGFIRQTSSGLYSWLpLGLrvlkkieniIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22946308 375 -FALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALtGLTRVRRFQQDDAHIF 435
Cdd:cd00779 87 eFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSF 147
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