|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
44-716 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1080.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 44 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIAKVN 123
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 124 NVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSS 201
Cdd:PLN02908 93 GVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 202 LEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNS 281
Cdd:PLN02908 173 IEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 282 STYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIR 361
Cdd:PLN02908 253 SAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 362 SEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLH 441
Cdd:PLN02908 333 EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLH 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 442 RNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLEN 521
Cdd:PLN02908 413 RNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 522 SLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMI 601
Cdd:PLN02908 493 ALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMF 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 602 AILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEK 681
Cdd:PLN02908 573 AILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEA 651
|
650 660 670
....*....|....*....|....*....|....*
gi 38202255 682 ISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 716
Cdd:PLN02908 652 ATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
83-717 |
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: 891.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 83 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMG 162
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 163 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY--NKFKCRI 239
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 240 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAK 319
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 320 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 398
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 399 FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 478
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 479 CLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQ 557
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 558 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 637
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 638 RQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQlkEFRSK 717
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
154-710 |
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: 671.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 154 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 232
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 233 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 310
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 311 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 389
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 390 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 468
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 469 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 546
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 547 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 626
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 627 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIE 706
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 38202255 707 RLQQ 710
Cdd:TIGR00418 558 KLRK 561
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
321-618 |
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: 542.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 321 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 400
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 401 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 480
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 481 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 559
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 38202255 560 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 618
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 ... |
397-608 |
1.88e-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: 140.62 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 397 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 474
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 475 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 552
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 38202255 553 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 608
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
250-297 |
2.13e-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: 2.13e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 38202255 250 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 297
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
44-716 |
0e+00 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 1080.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 44 RAELNPWpeyIYTRLEMYNILKAEHdsiLAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIAKVN 123
Cdd:PLN02908 19 EEYLSAV---IKKRIELFEKIQARQ---LARLESAGGDPIKVTLPDGAVKDGKKWVTTPMDIAKEISKGLANSALIAQVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 124 NVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIEN--GFYYDMYLEEGGVSSNDFSS 201
Cdd:PLN02908 93 GVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHILGEALELEYGCKLCIGPCTTRgeGFYYDAFYGDRTLNEEDFKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 202 LEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNS 281
Cdd:PLN02908 173 IEARAEKAVKEKQPFERIEVTREEALEMFSENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 282 STYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIR 361
Cdd:PLN02908 253 SAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELSPGSCFFLPHGARIYNKLMDFIR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 362 SEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLH 441
Cdd:PLN02908 333 EQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLH 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 442 RNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLEN 521
Cdd:PLN02908 413 RNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 522 SLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMI 601
Cdd:PLN02908 493 ALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMF 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 602 AILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEK 681
Cdd:PLN02908 573 AILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDR-KIQKKVREAQLAQYNYILVVGEAEA 651
|
650 660 670
....*....|....*....|....*....|....*
gi 38202255 682 ISGTVNIRTRDNKVHGERTISETIERLQQLKEFRS 716
Cdd:PLN02908 652 ATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEFK 686
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
83-717 |
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: 891.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 83 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMG 162
Cdd:COG0441 2 IKITLPDGSVREFEA-GVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 163 EAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY--NKFKCRI 239
Cdd:COG0441 81 QAVKRLYPDAkLTIGPVIENGFYYDFDLERP-FTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKVEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 240 LNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAK 319
Cdd:COG0441 160 IEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 320 NRDHRKIGRDQELYFFH-ELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFS 398
Cdd:COG0441 240 KRDHRKLGKELDLFHFQeEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 399 FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKG 478
Cdd:COG0441 320 TESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 479 CLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQ 557
Cdd:COG0441 400 VIDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 558 CATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKV 637
Cdd:COG0441 480 CGTIQLDFNLPERFDLTYVGEDG-EKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 638 RQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQlkEFRSK 717
Cdd:COG0441 559 AKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE--EIRSR 635
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
154-710 |
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: 671.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 154 WHSSAHIMGEAMERVYGG-CLCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY 232
Cdd:TIGR00418 1 RHSIAHLLAEALKQLYPDvKLAIGPVVEDGFYYDFELDRS-FTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEAFKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 233 NK-FKCRILNEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKE 310
Cdd:TIGR00418 80 LEpYKLELLDEIPNGVKRTPYGWGkAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 311 WEKFQEEAKNRDHRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHW 389
Cdd:TIGR00418 160 YLLRLEEAKKRDHRKLGKELELFSFEPEIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 390 QHYSENMFSF-EVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCA 468
Cdd:TIGR00418 240 DNYKERMFPFtELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 469 MEQIEDEIKGCLDFLRTVYSVFGFSF-KLNLSTR-PEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDI 546
Cdd:TIGR00418 320 EDQIKEEFKNQFRLIQKVYSDFGFSFdKYELSTRdPEDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 547 QIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPV 626
Cdd:TIGR00418 400 AFKDALGREWQCATVQLDFELPERFDLTYVDEDN-EEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 627 GPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIE 706
Cdd:TIGR00418 479 NERHLDYAKKVAQKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLE 557
|
....
gi 38202255 707 RLQQ 710
Cdd:TIGR00418 558 KLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
80-710 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 651.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 80 SKPIKVTLPDG--KQVDAeswKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSS 157
Cdd:PRK12444 3 EQMIEIKFPDGsvKEFVK---GITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 158 AHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEGgVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYN--K 234
Cdd:PRK12444 80 AHILAQAVKRLYGDVnLGVGPVIENGFYYDMDLPSS-VNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFQEMndR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 235 FKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKF 314
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 315 QEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSE 394
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEEAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 395 NMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 474
Cdd:PRK12444 319 NMYFSEVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIED 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 475 EIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGR 554
Cdd:PRK12444 399 EIKSVMAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 555 YHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTC-DEY 633
Cdd:PRK12444 479 SHQCGTIQLDFQMPEKFDLNYIDEK-NEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAVhVQY 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38202255 634 AQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 710
Cdd:PRK12444 558 ADEVADKLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKE 633
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
321-618 |
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: 542.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 321 RDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFE 400
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 401 VEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL 480
Cdd:cd00771 81 EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 481 DFLRTVYSVFGF-SFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCA 559
Cdd:cd00771 161 DLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGREWQCS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 38202255 560 TIQLDFQLPIRFNLTYVSHDGdDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSP 618
Cdd:cd00771 241 TIQLDFNLPERFDLTYIGEDG-EKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
155-716 |
6.35e-155 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 462.83 E-value: 6.35e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 155 HSSAHIMGEAMERVYGGC-LCYGPPIENGFYYDMYLEEggVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKY- 232
Cdd:PLN02837 48 HTCAHVMAMAVQKLFPDAkVTIGPWIENGFYYDFDMEP--LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 233 -NKFKCRILnEKVNTPTTTVYRCG-PLIDLCRGPHVRHTGKI--KALKIHKNSSTYWEGKADMETLQRIYGISFPDPKML 308
Cdd:PLN02837 126 nEPYKLEIL-EGIKEEPITIYHIGeEWWDLCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 309 KEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGS-CFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG 387
Cdd:PLN02837 205 KAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 388 HWQHYSENMFS-FEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIF 466
Cdd:PLN02837 285 HLDFYKENMYDqMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 467 CAMEQIEDEIKGCLDFLRTVYSVFGFS-FKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKID 545
Cdd:PLN02837 365 CLEDQIKDEIRGVLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKID 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 546 IQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDgDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVP 625
Cdd:PLN02837 445 LKIEDALGRKWQCSTIQVDFNLPERFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 626 VGPTCDEYAQKVRQQFHDAKFMADIDLdpGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETI 705
Cdd:PLN02837 524 VTDNELEYCKEVVAKLKAKGIRAEVCH--GERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFI 601
|
570
....*....|.
gi 38202255 706 ERLQQLKEFRS 716
Cdd:PLN02837 602 NRIQLAVENRT 612
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
301-710 |
7.29e-44 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 167.36 E-value: 7.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 301 SFPDPKMLKEWEKFQEEAKNRD--HRKIGRDQELYFFHELS-PGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNI 377
Cdd:PRK03991 175 GYEDLKALVDYEVGKKELVGGEppHVKLMREKELADYEPASdVGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 378 FNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLR---LADFGvlHRNELSGALTGLTR 454
Cdd:PRK03991 255 YDLSHPAIREHADKFGERQYRVKSDKKDLMLRFAACFGQFLMLKDMTISYKNLPLKmyeLSTYS--FRLEQRGELVGLKR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 455 VRRFQQDDAHIFC-----AMEQIEDEIKGCL----DFLRTVYSVFGFSfklnlstrpEKFlgdievWDQAEKQLENSLNE 525
Cdd:PRK03991 333 LRAFTMPDMHTLCkdmeqAMEEFEKQYEMILetgeDLGRDYEVAIRFT---------EDF------YEENKDWIVELVKR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 526 FG-----EKWElnsgDGAFYGP-KIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVsHDGDDKKRPVIVHRAILGSVER 599
Cdd:PRK03991 398 EGkpvllEILP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENAERFGIKYV-DENGEEKYPIILHCSPTGSIER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 600 MIAILTEN-----YGGK---WPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYN 671
Cdd:PRK03991 473 VIYALLEKaakeeEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKLEAAGIRVDVD-DRDESLGKKIRDAGKEWIP 551
|
410 420 430
....*....|....*....|....*....|....*....
gi 38202255 672 FILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQ 710
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 ... |
397-608 |
1.88e-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: 140.62 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 397 FSFEVE-KELFALKPMNCPGHCLMF-DHRPRSWReLPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIED 474
Cdd:pfam00587 1 YKVEDEnGDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 475 EIKGCLDFLRTVYSVFGFSF-KLNLSTRPEkflgdievwdqaekqlenslnefgekwelnsgdGAFYGPKIDIQIKDAI- 552
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVrVVRLSNSDG---------------------------------SAFYGPKLDFEVVFPSl 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 38202255 553 GRYHQCATIQLD-FQLPIRFNLTYVSHDgDDKKRPVIVHRAILGsVERMIAILTENY 608
Cdd:pfam00587 127 GKQRQTGTIQNDgFRLPRRLGIRYKDED-NESKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
618-709 |
1.09e-35 |
|
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: 129.55 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 618 PRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDpGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHG 697
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLR-NEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
90
....*....|..
gi 38202255 698 ERTISETIERLQ 709
Cdd:cd00860 80 SMSLDEFIEKLK 91
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
83-148 |
6.49e-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: 103.72 E-value: 6.49e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38202255 83 IKVTLPDGKQVDAESwKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEE 148
Cdd:cd01667 1 IKITLPDGSVKEFPK-GTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| 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 ... |
349-605 |
9.89e-27 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 109.02 E-value: 9.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 349 GAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKE-----LFALKPMNCPGHCLMFDHR 423
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 424 PRSWRELPLRLADFGVLHRNELSGAlTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPE 503
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 504 KFLGDievwdqaekqlenslnefgekwelNSGDGAFYGPKIDIQIKDAI-GRYHQCATIQLDFQLPIRFNLTYVSHDGDD 582
Cdd:cd00670 160 FGRGG------------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHFGASFKIDEDGGG 215
|
250 260
....*....|....*....|...
gi 38202255 583 KKrPVIVHRAilGSVERMIAILT 605
Cdd:cd00670 216 RA-HTGCGGA--GGEERLVLALL 235
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
620-711 |
2.73e-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: 94.58 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 620 QVMVVPVGPTCD---EYAQKVRQQFHDAKFMADIDLDPGcTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVH 696
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNE-SIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 38202255 697 GERTISETIERLQQL 711
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
83-143 |
3.61e-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: 3.61e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38202255 83 IKVTLPDGKQVDAESWkTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLK 143
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 ... |
352-520 |
2.39e-15 |
|
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: 75.62 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 352 IYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWqhYSENMFSFEVEKELFALKPMNCPGHCLMF-DHRprswREL 430
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE--PKDLLPVGAENEEDLYLRPTLEPGLVRLFvSHI----RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 431 PLRLADFGVLHRNELSGAltGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFS--FKLNLSTRPEKFLG- 507
Cdd:cd00768 75 PLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKldIVFVEKTPGEFSPGg 152
|
170
....*....|....*...
gi 38202255 508 -----DIEVWDQAEKQLE 520
Cdd:cd00768 153 agpgfEIEVDHPEGRGLE 170
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
250-297 |
2.13e-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: 2.13e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 38202255 250 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKNSSTYWEgkadmetLQRI 297
Cdd:smart00863 2 RVVSIGDFsVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
250-297 |
9.93e-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: 9.93e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 38202255 250 TVYRCGPL-IDLCRGPHVRHTGKIKALKIHKnsstyWEGKADMetLQRI 297
Cdd:pfam07973 2 RVVSIGDFdVDLCGGTHVPNTGEIGAFKILK-----GESKNKG--LRRI 43
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
613-718 |
2.41e-06 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 50.61 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 613 PFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADID-LDPGctLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTR 691
Cdd:PRK14938 269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDdLDDS--LGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIR 346
|
90 100
....*....|....*....|....*..
gi 38202255 692 DNKVHGERTISETIERLQQLKEFRSKQ 718
Cdd:PRK14938 347 ANNEQKSMTVEELVKEIKRADELKERS 373
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
341-507 |
9.07e-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: 47.75 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 341 GSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSG-HWQHYSENMFSF-----EVEKELFALKPMNCP 414
Cdd:cd00772 23 GIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAeHDEGFSKELAVFkdagdEELEEDFALRPTLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 415 GHCLMFDHRPRSWRELPLRLADFGVLHRNELSgALTGLTRVRRFQQDDAHIFCA-MEQIEDEIKGCLDFLRTVYSVFG-F 492
Cdd:cd00772 103 NIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAHAdAEEADEEFLNMLSAYAEIARDLAaI 181
|
170
....*....|....*
gi 38202255 493 SFKLNLSTRPEKFLG 507
Cdd:cd00772 182 DFIEGEADEGAKFAG 196
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
338-474 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 338 LSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSF-EVEKELFALKPMNCPGH 416
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkDRHGKEFLLGPTHEEVI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38202255 417 CLMFDHRPRSWRELPLRLADFGVLHRNELSGALtGLTRVRRFQQDDAHIF-----CAMEQIED 474
Cdd:cd00779 99 TDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdideeSLEETYEK 160
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
618-709 |
2.28e-05 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 43.54 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 618 PRQVMVVPVG---PTCDEYAQKVRQQFHDAKFMADIDlDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNK 694
Cdd:cd00738 1 PIDVAIVPLTdprVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 38202255 695 VHGERTISETIERLQ 709
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
620-709 |
1.79e-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: 37.90 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38202255 620 QVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLdpgctLNKKIRnAQLAQYN-----FILVVGEKEKISGTVNIrtRDNK 694
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDY-----GGRKLK-KQFKYADrsgarFAVILGEDELAAGVVTV--KDLE 74
|
90
....*....|....*..
gi 38202255 695 VHGERTISET--IERLQ 709
Cdd:cd00859 75 TGEQETVALDelVEELK 91
|
|
| |
