|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
7-573 |
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: 782.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 7 LNHSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYE-MRKV-----GIEQYSF 80
Cdd:COG0441 71 LRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPiEREEvsreeAIELFKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 81 ENQPYKKELYEEfKKEGKEITFFQYWNpktkeilFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCW 160
Cdd:COG0441 151 KGEPYKVELIED-IPEDEEISLYRQGE-------FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAF 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 161 ETKDELAKYLDILRERKERDHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKK 240
Cdd:COG0441 223 PKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 241 LYEISGHWAHYQDTMFaPIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDL 320
Cdd:COG0441 303 LWETSGHWDHYRENMF-PTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 321 TEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHISLSLRdpqdTQKFFQNDEMWNKAENDLREVLGELNIKYKEFIG 400
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPG 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 401 EAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWL 480
Cdd:COG0441 458 EGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 481 SPRQITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSK 560
Cdd:COG0441 538 APVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLG 617
|
570
....*....|...
gi 518846816 561 TYSKEEFVNYLKQ 573
Cdd:COG0441 618 TMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
9-573 |
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: 636.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 9 HSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYEMRKVGIEQYS----FE-NQ 83
Cdd:TIGR00418 2 HSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEaleaFKvLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 84 PYKKELYEEFKKEGKEITFFQYwnpktkeILFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCWETK 163
Cdd:TIGR00418 82 PYKLELLDEIPNGVKRTPYGWG-------KAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 164 DELAKYLDILRERKERDHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYE 243
Cdd:TIGR00418 155 KQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 244 ISGHWAHYQDTMFAPIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEG 323
Cdd:TIGR00418 235 ISGHWDNYKERMFPFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 324 HIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHISLSLRDPQDtqkFFQNDEMWNKAENDLREVLGELNIKYKEFIGEAA 403
Cdd:TIGR00418 315 HIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPED---FIGEDELWEKAEAALEEALKELGVPYEIDPGRGA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 404 FYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWLSPR 483
Cdd:TIGR00418 392 FYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 484 QITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSKTYS 563
Cdd:TIGR00418 472 QVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMS 551
|
570
....*....|
gi 518846816 564 KEEFVNYLKQ 573
Cdd:TIGR00418 552 LDEFLEKLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
7-579 |
6.53e-164 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 481.56 E-value: 6.53e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 7 LNHSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYEMRKVGI------EQYSF 80
Cdd:PRK12444 75 ARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVsreeaaKLFQE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 81 ENQPYKKELYEEFKkEGKEITFFQYWNpktkeilFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCW 160
Cdd:PRK12444 155 MNDRLKLELLEAIP-SGESITLYKQGE-------FVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 161 ETKDELAKYLDILRERKERDHRKIGRDLNLFTFNQlGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKK 240
Cdd:PRK12444 227 SSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSE-EAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 241 LYEISGHWAHYQDTMFAPiKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDL 320
Cdd:PRK12444 306 LWERSGHWDHYKDNMYFS-EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 321 TEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDhISLSLRdPQDTqkfFQNDEMWNKAENDLREVLGELNIKYKEFIG 400
Cdd:PRK12444 385 DDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYE-VELSTR-PEDS---MGDDELWEQAEASLENVLQSLNYKYRLNEG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 401 EAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWL 480
Cdd:PRK12444 460 DGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 481 SPRQITIIPINDELNEK-AQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDS 559
Cdd:PRK12444 540 APVQVKVIPVSNAVHVQyADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS 619
|
570 580
....*....|....*....|
gi 518846816 560 KTYSKEEFVNYLKQLKKNLK 579
Cdd:PRK12444 620 EVIELDMFVESIKEEIKNRK 639
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
180-482 |
1.21e-135 |
|
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: 396.54 E-value: 1.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 180 DHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYEISGHWAHYQDTMFaPI 259
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMF-PF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 260 KMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEGHIFVRPDQIKSEFKHL 339
Cdd:cd00771 80 EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 340 YKMILQALKDFNIEIDHISLSLRDpqdtQKFFQNDEMWNKAENDLREVLGELNIKYKEFIGEAAFYGPKVDFQVKTALNR 419
Cdd:cd00771 160 LDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGR 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518846816 420 IITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWLSP 482
Cdd:cd00771 236 EWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
264-471 |
1.89e-27 |
|
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: 109.04 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 264 ETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEGHIFVRPDQIKSEFKHLYKMI 343
Cdd:pfam00587 9 DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 344 LQALKDFNIEIDHISLSLRDpqdtqkffqndemwnkaendlrevlgelnikykefigEAAFYGPKVDFQVKT-ALNRIIT 422
Cdd:pfam00587 89 DRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQRQ 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518846816 423 MSTLQLD-FLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTyERFIATLLEQ 471
Cdd:pfam00587 132 TGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLGV-ERFLAAILEN 180
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
114-155 |
3.30e-09 |
|
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: 52.38 E-value: 3.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518846816 114 LFTDLCAGGHIENSREIKYFKLLGIAGAYWRgdsknkmLTRI 155
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
7-573 |
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: 782.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 7 LNHSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYE-MRKV-----GIEQYSF 80
Cdd:COG0441 71 LRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEKEMKEIIKEDLPiEREEvsreeAIELFKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 81 ENQPYKKELYEEfKKEGKEITFFQYWNpktkeilFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCW 160
Cdd:COG0441 151 KGEPYKVELIED-IPEDEEISLYRQGE-------FVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAF 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 161 ETKDELAKYLDILRERKERDHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKK 240
Cdd:COG0441 223 PKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 241 LYEISGHWAHYQDTMFaPIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDL 320
Cdd:COG0441 303 LWETSGHWDHYRENMF-PTESDGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 321 TEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHISLSLRdpqdTQKFFQNDEMWNKAENDLREVLGELNIKYKEFIG 400
Cdd:COG0441 382 DDAHIFCTPDQIEDEIKKVIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPG 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 401 EAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWL 480
Cdd:COG0441 458 EGAFYGPKIDFQLKDAIGREWQCGTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWL 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 481 SPRQITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSK 560
Cdd:COG0441 538 APVQVVVLPISDKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLG 617
|
570
....*....|...
gi 518846816 561 TYSKEEFVNYLKQ 573
Cdd:COG0441 618 TMSLDEFIARLKE 630
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
9-573 |
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: 636.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 9 HSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYEMRKVGIEQYS----FE-NQ 83
Cdd:TIGR00418 2 HSIAHLLAEALKQLYPDVKLAIGPVVEDGFYYDFELDRSFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEaleaFKvLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 84 PYKKELYEEFKKEGKEITFFQYwnpktkeILFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCWETK 163
Cdd:TIGR00418 82 PYKLELLDEIPNGVKRTPYGWG-------KAFVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 164 DELAKYLDILRERKERDHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYE 243
Cdd:TIGR00418 155 KQLAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 244 ISGHWAHYQDTMFAPIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEG 323
Cdd:TIGR00418 235 ISGHWDNYKERMFPFTELDNREFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 324 HIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHISLSLRDPQDtqkFFQNDEMWNKAENDLREVLGELNIKYKEFIGEAA 403
Cdd:TIGR00418 315 HIFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDPED---FIGEDELWEKAEAALEEALKELGVPYEIDPGRGA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 404 FYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWLSPR 483
Cdd:TIGR00418 392 FYGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 484 QITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSKTYS 563
Cdd:TIGR00418 472 QVVVIPVNERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMS 551
|
570
....*....|
gi 518846816 564 KEEFVNYLKQ 573
Cdd:TIGR00418 552 LDEFLEKLRK 561
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
7-579 |
6.53e-164 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 481.56 E-value: 6.53e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 7 LNHSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFENPILESDLPNIEKVMKELAKEGYEMRKVGI------EQYSF 80
Cdd:PRK12444 75 ARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLRKIEKEMKKIINENIKIERVEVsreeaaKLFQE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 81 ENQPYKKELYEEFKkEGKEITFFQYWNpktkeilFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCW 160
Cdd:PRK12444 155 MNDRLKLELLEAIP-SGESITLYKQGE-------FVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 161 ETKDELAKYLDILRERKERDHRKIGRDLNLFTFNQlGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKK 240
Cdd:PRK12444 227 SSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSE-EAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 241 LYEISGHWAHYQDTMFAPiKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDL 320
Cdd:PRK12444 306 LWERSGHWDHYKDNMYFS-EVDNKSFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 321 TEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDhISLSLRdPQDTqkfFQNDEMWNKAENDLREVLGELNIKYKEFIG 400
Cdd:PRK12444 385 DDAHLFVTPDQIEDEIKSVMAQIDYVYKTFGFEYE-VELSTR-PEDS---MGDDELWEQAEASLENVLQSLNYKYRLNEG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 401 EAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWL 480
Cdd:PRK12444 460 DGAFYGPKIDFHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 481 SPRQITIIPINDELNEK-AQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDS 559
Cdd:PRK12444 540 APVQVKVIPVSNAVHVQyADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKS 619
|
570 580
....*....|....*....|
gi 518846816 560 KTYSKEEFVNYLKQLKKNLK 579
Cdd:PRK12444 620 EVIELDMFVESIKEEIKNRK 639
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
6-572 |
5.60e-145 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 432.01 E-value: 5.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 6 KLNHSASHLLAAAILKLYPNAKLAIGPAIEEGFYYDFEFEnPILESDLPNIEKVM------------KELAKEGYEMRKV 73
Cdd:PLN02837 45 KIRHTCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDME-PLTDKDLKRIKKEMdriisrnlplvrEEVSREEAQKRIM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 74 GIeqysfeNQPYKKELYEEFKKEgkEITFF----QYWnpktkeilftDLCAGGHIENSREI--KYFKLLGIAGAYWRGDS 147
Cdd:PLN02837 124 AI------NEPYKLEILEGIKEE--PITIYhigeEWW----------DLCAGPHVERTGKInkKAVELESVAGAYWRGDE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 148 KNKMLTRIYGTCWETKDELAKYLDILRERKERDHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFG 227
Cdd:PLN02837 186 KNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQDDAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 228 FREVLTPHFGEKKLYEISGHWAHYQDTMFAPIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASG 307
Cdd:PLN02837 266 YDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 308 ALSGLERVRGMDLTEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHISLSLRdpqdTQKFFQNDEMWNKAENDLREV 387
Cdd:PLN02837 346 SLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTR----PEKSVGSDDIWEKATTALRDA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 388 LGELNIKYKEFIGEAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIAT 467
Cdd:PLN02837 422 LDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 468 LLEQTKGVLPFWLSPRQITIIPINDELNEKAQDLYNEFLDEDFNVNIdIRPERINKKIRDAQILKTKFIVVIGKKEIETN 547
Cdd:PLN02837 502 LIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVVAKLKAKGIRAEV-CHGERLPKLIRNAETQKIPLMAVVGPKEVETR 580
|
570 580
....*....|....*....|....*
gi 518846816 548 TLSVREYGKDDSKTYSKEEFVNYLK 572
Cdd:PLN02837 581 TLTVRSRHGGELGTMPVDDFINRIQ 605
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
180-482 |
1.21e-135 |
|
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: 396.54 E-value: 1.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 180 DHRKIGRDLNLFTFNQLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYEISGHWAHYQDTMFaPI 259
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMF-PF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 260 KMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEGHIFVRPDQIKSEFKHL 339
Cdd:cd00771 80 EEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 340 YKMILQALKDFNIEIDHISLSLRDpqdtQKFFQNDEMWNKAENDLREVLGELNIKYKEFIGEAAFYGPKVDFQVKTALNR 419
Cdd:cd00771 160 LDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALGR 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518846816 420 IITMSTLQLDFLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWLSP 482
Cdd:cd00771 236 EWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
9-579 |
1.61e-134 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 407.62 E-value: 1.61e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 9 HSASHLLAAAILKLYpNAKLAIGPAIE--EGFYYDFEFENPIL-ESDLPNIEKVMKELAKEGYEMRKVGIEQYS----FE 81
Cdd:PLN02908 124 HSSAHILGEALELEY-GCKLCIGPCTTrgEGFYYDAFYGDRTLnEEDFKPIEARAEKAVKEKQPFERIEVTREEalemFS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 82 NQPYKKELYEEFKkEGKEITFFQYwNPktkeilFTDLCAGGHIENSREIKYFKLLGIAGAYWRGDSKNKMLTRIYGTCWE 161
Cdd:PLN02908 203 ENKFKVEIINDLP-EDATITVYRC-GP------LVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 162 TKDELAKYLDILRERKERDHRKIGRDLNLFTFNQLGgQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKL 241
Cdd:PLN02908 275 DKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHELS-PGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 242 YEISGHWAHYQDTMFApIKMDNETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLT 321
Cdd:PLN02908 354 WETSGHAAHYKENMFV-FEIEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 322 EGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDhISLSLRdpqdTQKFFQNDEMWNKAENDLREVLGELNIKYKEFIGE 401
Cdd:PLN02908 433 DAHIFCREDQIKDEVKGVLDFLDYVYEVFGFTYE-LKLSTR----PEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGD 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 402 AAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSRFEMKFVDSNE-QFVTPVLIHRGLIGTYERFIATLLEQTKGVLPFWL 480
Cdd:PLN02908 508 GAFYGPKIDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEaKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWL 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 481 SPRQITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSK 560
Cdd:PLN02908 588 SPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHG 667
|
570
....*....|....*....
gi 518846816 561 TYSKEEFVNYLKQLKKNLK 579
Cdd:PLN02908 668 EKKIEELLTEFKEERAEFK 686
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
204-573 |
6.38e-50 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 182.38 E-value: 6.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 204 WLEDGMKIHNAIRDYVLKLDKKFGFREVLTP---HFGEKKLYEisgHWAHYQDTMFApIKMDNETLVARPMTCPHHIILF 280
Cdd:PRK03991 222 YYPKGRLIRDLLEDYVYNLVVELGAMPVETPimyDLSHPAIRE---HADKFGERQYR-VKSDKKDLMLRFAACFGQFLML 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 281 NSTRRSYKDLPIRYSEQSRL-YRYEASGALSGLERVRGMDLTEGHIFVRP-DQIKSEFKHLYKMILQALKDFNIEIDHIS 358
Cdd:PRK03991 298 KDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTMPDMHTLCKDmEQAMEEFEKQYEMILETGEDLGRDYEVAI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 359 lslrdpQDTQKFFQNDEMWnkaendLREVLGELNikyK----EFIGEAAFYGP-KVDFQVKTALNRIITMSTLQLDFLLP 433
Cdd:PRK03991 378 ------RFTEDFYEENKDW------IVELVKREG---KpvllEILPERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENA 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 434 SRFEMKFVDSNEQFVTPVLIHRGLIGTYERFIATLLEQT--------KGVLPFWLSPRQITIIPINDELNEKAQDLYNEF 505
Cdd:PRK03991 443 ERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEKAakeeeegkVPMLPTWLSPTQVRVIPVSERHLDYAEEVADKL 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518846816 506 LDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSKTYSKEEFVNYLKQ 573
Cdd:PRK03991 523 EAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKE 590
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
482-572 |
6.84e-30 |
|
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: 112.60 E-value: 6.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 482 PRQITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSKT 561
Cdd:cd00860 1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGS 80
|
90
....*....|.
gi 518846816 562 YSKEEFVNYLK 572
Cdd:cd00860 81 MSLDEFIEKLK 91
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
264-471 |
1.89e-27 |
|
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: 109.04 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 264 ETLVARPMTCPHHIILFNSTRRSYKDLPIRYSEQSRLYRYEASGALSGLERVRGMDLTEGHIFVRPDQIKSEFKHLYKMI 343
Cdd:pfam00587 9 DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 344 LQALKDFNIEIDHISLSLRDpqdtqkffqndemwnkaendlrevlgelnikykefigEAAFYGPKVDFQVKT-ALNRIIT 422
Cdd:pfam00587 89 DRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQRQ 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518846816 423 MSTLQLD-FLLPSRFEMKFVDSNEQFVTPVLIHRGLIGTyERFIATLLEQ 471
Cdd:pfam00587 132 TGTIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLGV-ERFLAAILEN 180
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
484-574 |
9.36e-20 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 84.17 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 484 QITIIPIN---DELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSK 560
Cdd:pfam03129 1 QVVVIPLGekaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 518846816 561 TYSKEEFVNYLKQL 574
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| 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 ... |
208-469 |
2.87e-16 |
|
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: 78.20 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 208 GMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYEISGHWAHYQDTMF----APIKMDNETLVARPMTCPHHIILFNST 283
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYtfedKGRELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 284 RRSYKDLPIRYSEQSRLYRYEASGAlSGLERVRGMDLTEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIdhislslrd 363
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPV--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 364 pqdtqkffqndemwnkaendlreVLGELNIKYKEF---IGEAAFYGPKVDFQVKTALN-RIITMSTLQLDFLLPSRFEMK 439
Cdd:cd00670 151 -----------------------RVVVADDPFFGRggkRGLDAGRETVVEFELLLPLPgRAKETAVGSANVHLDHFGASF 207
|
250 260 270
....*....|....*....|....*....|
gi 518846816 440 FVDSNEQFVTPVLIHRGLIgtYERFIATLL 469
Cdd:cd00670 208 KIDEDGGGRAHTGCGGAGG--EERLVLALL 235
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
381-573 |
3.31e-12 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 68.33 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 381 ENDLREVLGELNIKYKEFIGEAAfygPKVDFQvktalNRIITMSTLQLDFLLPSRFE-----MKFVDSNEQFVTpvlIHR 455
Cdd:PRK14938 181 ENNENVSNGEMSILYRNVEGRIL---PCINEN-----PRIIAVYGGVKELDFPKEFIdsknrIKIWWVNESRTY---VDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 456 GLIGTYerFIATLLEQTKGVLPFWLSPRQITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKF 535
Cdd:PRK14938 250 GLLVYY--FLLESIRKQPPTLPDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPF 327
|
170 180 190
....*....|....*....|....*....|....*...
gi 518846816 536 IVVIGKKEIETNTLSVREYGKDDSKTYSKEEFVNYLKQ 573
Cdd:PRK14938 328 VIIIGEREVKTSTLTVKIRANNEQKSMTVEELVKEIKR 365
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
482-572 |
3.90e-11 |
|
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: 59.72 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 482 PRQITIIPIND---ELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDD 558
Cdd:cd00738 1 PIDVAIVPLTDprvEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 518846816 559 SKTYSKEEFVNYLK 572
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
179-348 |
1.21e-09 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 59.50 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 179 RDHRKIGRDLNLFTFN---QLGGQGFPFWLEDGMKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYEISGHWAHYQDTM 255
Cdd:cd00770 19 KDHVELGEKLDILDFErgaKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKEVMEGTGQLPKFDEQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 256 FApIKMDNETLVArpmTCPHHII-LFNSTRRSYKDLPIRYSEQSRLYRYEASGA---LSGLERVRGMDLTEGHIFVRPDQ 331
Cdd:cd00770 99 YK-VEGEDLYLIA---TAEVPLAaLHRDEILEEEELPLKYAGYSPCFRKEAGSAgrdTRGLFRVHQFEKVEQFVFTKPEE 174
|
170 180
....*....|....*....|
gi 518846816 332 IKSEFKHLYKM---ILQALK 348
Cdd:cd00770 175 SWEELEELISNaeeILQELG 194
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
114-155 |
3.30e-09 |
|
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: 52.38 E-value: 3.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 518846816 114 LFTDLCAGGHIENSREIKYFKLLGIAGAYWRgdsknkmLTRI 155
Cdd:smart00863 9 FSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| tRNA_SAD |
pfam07973 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ... |
115-155 |
4.68e-09 |
|
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: 52.06 E-value: 4.68e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518846816 115 FTDLCAGGHIENSREIKYFKLLgiagaywRGDSKNKMLTRI 155
Cdd:pfam07973 10 DVDLCGGTHVPNTGEIGAFKIL-------KGESKNKGLRRI 43
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
227-457 |
2.04e-08 |
|
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: 54.82 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 227 GFREVLTPHFGEKKLYEISGHWAHYQDTmfaPIKMDNETLVARPMTCPHHIILFNSTRRsykDLPIRYSEQSRLYRYEAS 306
Cdd:cd00768 17 GFQEVETPIVEREPLLEKAGHEPKDLLP---VGAENEEDLYLRPTLEPGLVRLFVSHIR---KLPLRLAEIGPAFRNEGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 307 GAlsGLERVRGMDLTEGHIFVRPDQIKSEFKHLYKMILQALKDFNIEIDHIslslrdpqdtqkFFQNDEMwnkaendlre 386
Cdd:cd00768 91 RR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIV------------FVEKTPG---------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518846816 387 vlgelnikykEFigEAAFYGPKVDFQVKTALNRIITMSTLQLDFLLPSR-FEMKFVDSNEQFVTPVLIHRGL 457
Cdd:cd00768 147 ----------EF--SPGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYFLDEALEYRYPPTIGFGL 206
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
482-572 |
3.19e-08 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. 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.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 51.44 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 482 PRQITIIPINDeLNEKAQD----LYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKD 557
Cdd:cd00861 1 PFDVVIIPMNM-KDEVQQElaekLYAELQAAGVDVLLDDRNERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTG 79
|
90
....*....|....*
gi 518846816 558 DSKTYSKEEFVNYLK 572
Cdd:cd00861 80 EKEEISIDELLEFLQ 94
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
484-572 |
1.26e-07 |
|
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: 49.46 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 484 QITIIPINDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKFIVVIGKKEIETNTLSVREYGKDDSKTYS 563
Cdd:cd00859 3 DVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVA 82
|
....*....
gi 518846816 564 KEEFVNYLK 572
Cdd:cd00859 83 LDELVEELK 91
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
463-576 |
1.92e-07 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 53.93 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 463 RFIATLLEQT---KGVLpfW---LSPRQITIIPIN---DELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKT 533
Cdd:PRK09194 445 RLVAAAIEQNhdeKGII--WpkaIAPFDVHIVPVNmkdEEVKELAEKLYAELQAAGIEVLLDDRKERPGVKFADADLIGI 522
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 518846816 534 KFIVVIGKKEIETNTLSVREYGKDDSKTYSKEEFVNYLKQLKK 576
Cdd:PRK09194 523 PHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
476-553 |
6.48e-07 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 48.32 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 476 LPFWLSPRQITIIPI--NDELNEKAQDLYNEFLDEDFNVNIDIRPErINKKIRDAQILKTKFIVVIGKKEIETNTLSVRE 553
Cdd:cd00858 20 LPPALAPIKVAVLPLvkRDELVEIAKEISEELRELGFSVKYDDSGS-IGRRYARQDEIGTPFCVTVDFDTLEDGTVTIRE 98
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
9-159 |
1.83e-05 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 46.34 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 9 HSASHLLAAAILKLY--PNAKLAIGPaieEGFYYDFEFENPiLESDLPNIEKVMKELAKEGYEMRKVGIEQYSFENQP-Y 85
Cdd:COG2872 100 HTALHLLSAVVYREYgaPVTGGQIGE---DRARIDFDLPEF-DEEDLEEIEAEANELIAADLPVRIYWITREELEAIPgL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518846816 86 KKELYEEFKKEGKEItffqywnpKTKEILFTDLCA-GG-HIENSREIKYFKLLGIagaywrgDSKNKMLTRIYGTC 159
Cdd:COG2872 176 VRTMSVLPPPGVGRV--------RIVEIGGVDLQPcGGtHVANTGEIGRIKITKI-------EKKGKGNRRVYFTL 236
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
209-304 |
4.90e-04 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine 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. 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. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 42.20 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 209 MKIHNAIRDYVLKLDKKFGFREVLTPHFGEKKLYeISGHWAHYQDTMFAPIKMDNETLVARP-MTCPhhIILFNSTRRSY 287
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELF-LRKSGDEVSKEMYRFKDKGGRDLALRPdLTAP--VARAVAENLLS 78
|
90
....*....|....*..
gi 518846816 288 KDLPIRYSEQSRLYRYE 304
Cdd:cd00773 79 LPLPLKLYYIGPVFRYE 95
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
463-572 |
2.12e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 40.61 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518846816 463 RFIATLLEQT---KGVL-PFWLSPRQITIIPI---NDELNEKAQDLYNEFLDEDFNVNIDIRPERINKKIRDAQILKTKF 535
Cdd:PRK12325 322 RLVAAIIEAShddKGIIwPESVAPFKVGIINLkqgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPW 401
|
90 100 110
....*....|....*....|....*....|....*..
gi 518846816 536 IVVIGKKEIETNTLSVREYGKDDSKTYSKEEFVNYLK 572
Cdd:PRK12325 402 QIIVGPKGLAEGKVELKDRKTGEREELSVEAAINRLT 438
|
|
| |
