|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
4-650 |
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: 997.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 4 LNLTFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAEALALLRHATSHLLAQ 83
Cdd:COG0441 2 IKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 84 ALKRMpkFANMHFGVGPFIDNGFYYDTDNGagNQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEMFAT--DPYKM 161
Cdd:COG0441 82 AVKRL--YPDAKLTIGPVIENGFYYDFDLE--RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 162 ALITDLPEDEILTIAIQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAEVTRREE 241
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 242 AKERDHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDM 321
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 322 FpPMDMgDGEFLELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEE 401
Cdd:COG0441 318 F-PTES-DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIED 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 402 EFKSILTMMMAVYRDFNITDYRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLDVQTK 481
Cdd:COG0441 396 EIKKVIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 482 TALGNEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQIIPVNlG 561
Cdd:COG0441 472 DAIGREWQCGTIQLDFNLPERFDLTYVGEDGEK-HRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPIS-D 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 562 AHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFIDFQMAIL 641
Cdd:COG0441 550 KHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLK 629
|
....*....
gi 498373677 642 ADVARYSRT 650
Cdd:COG0441 630 EEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
74-644 |
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: 695.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 74 RHATSHLLAQALKRmpKFANMHFGVGPFIDNGFYYDTDNGAgnQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEM 153
Cdd:TIGR00418 1 RHSIAHLLAEALKQ--LYPDVKLAIGPVVEDGFYYDFELDR--SFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 154 FAT-DPYKMALITDLPEDEILTIAIQGDH-IELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQAD 231
Cdd:TIGR00418 77 FKVlEPYKLELLDEIPNGVKRTPYGWGKAfVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 232 VDAEVTRREEAKERDHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTS 311
Cdd:TIGR00418 157 LAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 312 GHWDHYREDMFPPMDMGDGEFLeLRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGH 391
Cdd:TIGR00418 237 GHWDNYKERMFPFTELDNREFM-LKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 392 TFVDPEKIEEEFKSILTMMMAVYRDFNITDYRFRLSYRDPkntEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAF 471
Cdd:TIGR00418 316 IFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDP---EDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 472 YGPKLDVQTKTALGNEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPL 551
Cdd:TIGR00418 393 YGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEE-KRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 552 QVQIIPVNlGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTM 631
Cdd:TIGR00418 472 QVVVIPVN-ERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKM 550
|
570
....*....|...
gi 498373677 632 SFIDFQMAILADV 644
Cdd:TIGR00418 551 SLDEFLEKLRKEV 563
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-644 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 666.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 1 MSALNLTFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAEALALLRHATSHL 80
Cdd:PRK12444 3 EQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 81 LAQALKRMpkFANMHFGVGPFIDNGFYYDTDngAGNQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEMF--ATDP 158
Cdd:PRK12444 83 LAQAVKRL--YGDVNLGVGPVIENGFYYDMD--LPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFqeMNDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 159 YKMALITDLPEDEILTIAIQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAEVTR 238
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 239 REEAKERDHRTIGRDLDLFFTSQEvGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYR 318
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 319 EDM-FPPMDmgDGEFlELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPE 397
Cdd:PRK12444 318 DNMyFSEVD--NKSF-ALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 398 KIEEEFKSILTMMMAVYRDFNItDYRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLD 477
Cdd:PRK12444 395 QIEDEIKSVMAQIDYVYKTFGF-EYEVELSTR----PEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKID 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 478 VQTKTALGNEETMSTIQLDFLLPERFDLTYIGADGQdNHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQIIP 557
Cdd:PRK12444 470 FHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNE-KRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIP 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 558 VNLGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFIDFQ 637
Cdd:PRK12444 549 VSNAVHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFV 628
|
....*..
gi 498373677 638 MAILADV 644
Cdd:PRK12444 629 ESIKEEI 635
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
246-550 |
3.33e-157 |
|
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: 454.32 E-value: 3.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 246 DHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDMFPPM 325
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 326 dmGDGEFLELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEEEFKS 405
Cdd:cd00771 81 --EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 406 ILTMMMAVYRDFNITDYRFRLSYRDpkntEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLDVQTKTALG 485
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498373677 486 NEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSP 550
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEK-KRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 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 ... |
330-540 |
1.55e-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: 109.42 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 330 GEFLELRPMNCPSHIMVF-KHKPRSYReLPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEEEFKSILT 408
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 409 MMMAVYRDFNITDYRFRLSYRDpkntekyfdddemweksqaqlkramddlkldyyeaegEAAFYGPKLDVQTKT-ALGNE 487
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498373677 488 ETMSTIQLD-FLLPERFDLTYIGADGQdNHRPVMLHRGIVGtMERFTAYLIEMY 540
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNE-SKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
177-221 |
4.59e-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: 4.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 498373677 177 IQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRgkssnpmMQRI 221
Cdd:smart00863 6 IGDFSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
4-650 |
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: 997.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 4 LNLTFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAEALALLRHATSHLLAQ 83
Cdd:COG0441 2 IKITLPDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 84 ALKRMpkFANMHFGVGPFIDNGFYYDTDNGagNQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEMFAT--DPYKM 161
Cdd:COG0441 82 AVKRL--YPDAKLTIGPVIENGFYYDFDLE--RPFTPEDLEKIEKEMKEIIKEDLPIEREEVSREEAIELFKEkgEPYKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 162 ALITDLPEDEILTIAIQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAEVTRREE 241
Cdd:COG0441 158 ELIEDIPEDEEISLYRQGEFVDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 242 AKERDHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDM 321
Cdd:COG0441 238 AKKRDHRKLGKELDLFHFQEEVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 322 FpPMDMgDGEFLELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEE 401
Cdd:COG0441 318 F-PTES-DGEEYALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIED 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 402 EFKSILTMMMAVYRDFNITDYRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLDVQTK 481
Cdd:COG0441 396 EIKKVIDLVLEVYKDFGFEDYYVKLSTR----PEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 482 TALGNEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQIIPVNlG 561
Cdd:COG0441 472 DAIGREWQCGTIQLDFNLPERFDLTYVGEDGEK-HRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPIS-D 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 562 AHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFIDFQMAIL 641
Cdd:COG0441 550 KHADYAKEVAKKLRAAGIRVEVDLRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLK 629
|
....*....
gi 498373677 642 ADVARYSRT 650
Cdd:COG0441 630 EEIRSRSLE 638
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
74-644 |
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: 695.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 74 RHATSHLLAQALKRmpKFANMHFGVGPFIDNGFYYDTDNGAgnQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEM 153
Cdd:TIGR00418 1 RHSIAHLLAEALKQ--LYPDVKLAIGPVVEDGFYYDFELDR--SFTQEDLEKIEKDMKEIAKKNYPVAKLSVSLEEALEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 154 FAT-DPYKMALITDLPEDEILTIAIQGDH-IELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQAD 231
Cdd:TIGR00418 77 FKVlEPYKLELLDEIPNGVKRTPYGWGKAfVDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 232 VDAEVTRREEAKERDHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTS 311
Cdd:TIGR00418 157 LAAYLLRLEEAKKRDHRKLGKELELFSFEPEIGPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 312 GHWDHYREDMFPPMDMGDGEFLeLRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGH 391
Cdd:TIGR00418 237 GHWDNYKERMFPFTELDNREFM-LKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 392 TFVDPEKIEEEFKSILTMMMAVYRDFNITDYRFRLSYRDPkntEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAF 471
Cdd:TIGR00418 316 IFCTEDQIKEEFKNQFRLIQKVYSDFGFSFDKYELSTRDP---EDFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 472 YGPKLDVQTKTALGNEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPL 551
Cdd:TIGR00418 393 YGPKIDFAFKDALGREWQCATVQLDFELPERFDLTYVDEDNEE-KRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 552 QVQIIPVNlGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTM 631
Cdd:TIGR00418 472 QVVVIPVN-ERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKM 550
|
570
....*....|...
gi 498373677 632 SFIDFQMAILADV 644
Cdd:TIGR00418 551 SLDEFLEKLRKEV 563
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
1-644 |
0e+00 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 666.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 1 MSALNLTFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAEALALLRHATSHL 80
Cdd:PRK12444 3 EQMIEIKFPDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 81 LAQALKRMpkFANMHFGVGPFIDNGFYYDTDngAGNQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEMF--ATDP 158
Cdd:PRK12444 83 LAQAVKRL--YGDVNLGVGPVIENGFYYDMD--LPSSVNVEDLRKIEKEMKKIINENIKIERVEVSREEAAKLFqeMNDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 159 YKMALITDLPEDEILTIAIQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAEVTR 238
Cdd:PRK12444 159 LKLELLEAIPSGESITLYKQGEFVDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 239 REEAKERDHRTIGRDLDLFFTSQEvGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYR 318
Cdd:PRK12444 239 VEEAAKRNHRKLGKELELFMFSEE-APGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 319 EDM-FPPMDmgDGEFlELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPE 397
Cdd:PRK12444 318 DNMyFSEVD--NKSF-ALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 398 KIEEEFKSILTMMMAVYRDFNItDYRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLD 477
Cdd:PRK12444 395 QIEDEIKSVMAQIDYVYKTFGF-EYEVELSTR----PEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKID 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 478 VQTKTALGNEETMSTIQLDFLLPERFDLTYIGADGQdNHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQIIP 557
Cdd:PRK12444 470 FHIKDALNRSHQCGTIQLDFQMPEKFDLNYIDEKNE-KRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIP 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 558 VNLGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFIDFQ 637
Cdd:PRK12444 549 VSNAVHVQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFV 628
|
....*..
gi 498373677 638 MAILADV 644
Cdd:PRK12444 629 ESIKEEI 635
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
6-648 |
3.72e-178 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 522.41 E-value: 3.72e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 6 LTFPDGAVKvfpDGTK----PIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAEALALLRHATSHLL 81
Cdd:PLN02908 54 VTLPDGAVK---DGKKwvttPMDIAKEISKGLANSALIAQVDGVLWDMTRPLEGDCKLKLFKFDDDEGRDTFWHSSAHIL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 82 AQALKrmpkfanMHFG----VGPFIDN--GFYYDTDNGaGNQVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALEMFA 155
Cdd:PLN02908 131 GEALE-------LEYGcklcIGPCTTRgeGFYYDAFYG-DRTLNEEDFKPIEARAEKAVKEKQPFERIEVTREEALEMFS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 156 TDPYKMALITDLPEDEILTIAIQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAE 235
Cdd:PLN02908 203 ENKFKVEIINDLPEDATITVYRCGPLVDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 236 VTRREEAKERDHRTIGRDLDLFFtSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWD 315
Cdd:PLN02908 283 KHRIEEAKKRDHRLLGQKQELFF-FHELSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 316 HYREDMFPpMDMGDGEFlELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVD 395
Cdd:PLN02908 362 HYKENMFV-FEIEKQEF-GLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCR 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 396 PEKIEEEFKSILTMMMAVYRDFNITdYRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPK 475
Cdd:PLN02908 440 EDQIKDEVKGVLDFLDYVYEVFGFT-YELKLSTR----PEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPK 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 476 LDVQTKTALGNEETMSTIQLDFLLPERFDLTYIGADGQDNHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQI 555
Cdd:PLN02908 515 IDITVSDALKRKFQCATVQLDFQLPIRFKLSYSAEDEAKIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIV 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 556 IPVNLGAHgEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFID 635
Cdd:PLN02908 595 VPISEKSQ-DYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEE 673
|
650
....*....|...
gi 498373677 636 FQMAILADVARYS 648
Cdd:PLN02908 674 LLTEFKEERAEFK 686
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
26-636 |
1.11e-167 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 493.26 E-value: 1.11e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 26 AQSISKSLAKKSVSAKLNDAYVGMNDIIPESgnFQLITTNDAEALALLRHATSHLLAQALKRMpkFANMHFGVGPFIDNG 105
Cdd:PLN02837 1 VSAAAASAATEEASAAAASDEKGPGEAEPER--VVLPTNESSEKLLKIRHTCAHVMAMAVQKL--FPDAKVTIGPWIENG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 106 FYYDTDNGAgnqVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEALE--MFATDPYKMALITDLPEDEILTIAIQGDHIE 183
Cdd:PLN02837 77 FYYDFDMEP---LTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKriMAINEPYKLEILEGIKEEPITIYHIGEEWWD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 184 LDKGGLVPSTGWI--KHFKLTSVAGAYWRGKSSNPMMQRIYGISEWKQADVDAEVTRREEAKERDHRTIGRDLDLFFTSQ 261
Cdd:PLN02837 154 LCAGPHVERTGKInkKAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 262 EVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDMFPPMDMGDgEFLELRPMNCP 341
Cdd:PLN02837 234 DAGGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYDQMDIED-ELYQLRPMNCP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 342 SHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEEEFKSILTMMMAVYRDFNITD 421
Cdd:PLN02837 313 YHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILKQFGFSK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 422 YRFRLSYRdpknTEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLDVQTKTALGNEETMSTIQLDFLLPE 501
Cdd:PLN02837 393 YEINLSTR----PEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 502 RFDLTYIGADgQDNHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSPLQVQIIPVNlGAHGEYADGIQKKLQSAGLRA 581
Cdd:PLN02837 469 RFDITYVDSN-SEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVT-DNELEYCKEVVAKLKAKGIRA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 498373677 582 NVETKEaKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTMSFIDF 636
Cdd:PLN02837 547 EVCHGE-RLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDF 600
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
246-550 |
3.33e-157 |
|
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: 454.32 E-value: 3.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 246 DHRTIGRDLDLFFTSQEVGSGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDMFPPM 325
Cdd:cd00771 1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 326 dmGDGEFLELRPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEEEFKS 405
Cdd:cd00771 81 --EEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDAHIFCTPDQIKEEIKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 406 ILTMMMAVYRDFNITDYRFRLSYRDpkntEKYFDDDEMWEKSQAQLKRAMDDLKLDYYEAEGEAAFYGPKLDVQTKTALG 485
Cdd:cd00771 159 VLDLIKEVYSDFGFFDYKVELSTRP----EKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGPKIDFHVKDALG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498373677 486 NEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERFTAYLIEMYKGAFPTWLSP 550
Cdd:cd00771 235 REWQCSTIQLDFNLPERFDLTYIGEDGEK-KRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
232-647 |
7.50e-44 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 166.59 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 232 VDAEV-TRREEAKERDHRTIGRDLDlfFTSQEVGS--GLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLY 308
Cdd:PRK03991 183 VDYEVgKKELVGGEPPHVKLMREKE--LADYEPASdvGHMRYYPKGRLIRDLLEDYVYNLVVELGAMPVETPIMYDLSHP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 309 KTSGHWDHYREDMFPpMDMGDGEFLeLRPMNCPSHIMVFKHKPRSYRELPIRIAELGMM-HRYEKSGALTGLSRVREMTL 387
Cdd:PRK03991 261 AIREHADKFGERQYR-VKSDKKDLM-LRFAACFGQFLMLKDMTISYKNLPLKMYELSTYsFRLEQRGELVGLKRLRAFTM 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 388 NDGHTFV-DPEKIEEEFKSILTMMMAVYRDFNIT---DYRFrlsyrdpknTEKYFDDDEMWEKSQAqlKR-------AMD 456
Cdd:PRK03991 339 PDMHTLCkDMEQAMEEFEKQYEMILETGEDLGRDyevAIRF---------TEDFYEENKDWIVELV--KRegkpvllEIL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 457 DLKLDYYEAEGEAAFygpkLDvqtktALGNEETMSTIQLDFLLPERFDLTYIGADGQDnHRPVMLHRGIVGTMERF---- 532
Cdd:PRK03991 408 PERKHYWVLKVEFAF----ID-----SLGRPIENPTVQIDVENAERFGIKYVDENGEE-KYPIILHCSPTGSIERViyal 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 533 --TAYlIEMYKG---AFPTWLSPLQVQIIPVNlGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLV 607
Cdd:PRK03991 478 leKAA-KEEEEGkvpMLPTWLSPTQVRVIPVS-ERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVV 555
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 498373677 608 LGDSEVEAQTVTVRKYGEEKTQTMSFIDFQMAILADVARY 647
Cdd:PRK03991 556 IGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETKGY 595
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
330-540 |
1.55e-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: 109.42 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 330 GEFLELRPMNCPSHIMVF-KHKPRSYReLPIRIAELGMMHRYEKSGALTGLSRVREMTLNDGHTFVDPEKIEEEFKSILT 408
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFrEEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 409 MMMAVYRDFNITDYRFRLSYRDpkntekyfdddemweksqaqlkramddlkldyyeaegEAAFYGPKLDVQTKT-ALGNE 487
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSD-------------------------------------GSAFYGPKLDFEVVFpSLGKQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498373677 488 ETMSTIQLD-FLLPERFDLTYIGADGQdNHRPVMLHRGIVGtMERFTAYLIEMY 540
Cdd:pfam00587 130 RQTGTIQNDgFRLPRRLGIRYKDEDNE-SKFPYMIHRAGLG-VERFLAAILENN 181
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
550-636 |
4.81e-27 |
|
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: 104.89 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 550 PLQVQIIPVNlGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQ 629
Cdd:cd00860 1 PVQVVVIPVT-DEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
....*..
gi 498373677 630 TMSFIDF 636
Cdd:cd00860 80 SMSLDEF 86
|
|
| 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 ... |
274-537 |
3.53e-21 |
|
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: 92.84 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 274 GATIRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYREDMF---PPMDMGDGEFLELRPMNCPSHIMVFKHK 350
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYtfeDKGRELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 351 PRSYRELPIRIAELGMMHRYEKSGAlTGLSRVREMTLNDGHTFVDPEKIEEEFKSILTMMMAVYRDFNItDYRFRLSyrd 430
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGL-PVRVVVA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 431 pkntekyfDDDEMWEKSQaqlkramddlkldyyeaEGEAAFYGPKLDVQTKTALGNEE-TMSTIQLDFLLPERFDLTYIG 509
Cdd:cd00670 156 --------DDPFFGRGGK-----------------RGLDAGRETVVEFELLLPLPGRAkETAVGSANVHLDHFGASFKID 210
|
250 260
....*....|....*....|....*...
gi 498373677 510 ADGQDNHrPVMLHRGivGTMERFTAYLI 537
Cdd:cd00670 211 EDGGGRA-HTGCGGA--GGEERLVLALL 235
|
|
| TGS_ThrRS |
cd01667 |
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ... |
4-68 |
9.76e-20 |
|
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: 83.31 E-value: 9.76e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498373677 4 LNLTFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLITTNDAE 68
Cdd:cd01667 1 IKITLPDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDPE 65
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
552-636 |
4.56e-17 |
|
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: 76.47 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 552 QVQIIPVN--LGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQ 629
Cdd:pfam03129 1 QVVVIPLGekAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*..
gi 498373677 630 TMSFIDF 636
Cdd:pfam03129 81 TVSLDEL 87
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
277-432 |
1.50e-12 |
|
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: 67.14 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 277 IRRQVERYITDKELANGYQHVYTPVLSNLNLYKTSGHWDHYredMFPPMDmGDGEFLELRPMNCPSHIMVFKHKPRSyre 356
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKD---LLPVGA-ENEEDLYLRPTLEPGLVRLFVSHIRK--- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498373677 357 LPIRIAELGMMHRYEKSGAltGLSRVREMTLNDGHTFVDPEKIEEEFKSILTMMMAVYRDFNIT-DYRFRLSYRDPK 432
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKlDIVFVEKTPGEF 148
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
535-631 |
5.99e-11 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 64.87 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 535 YLIEMYKGAFPT---WLSPLQVQIIPVNlGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDS 611
Cdd:PRK14938 256 FLLESIRKQPPTlpdWLNPIQVRILPVK-KDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGER 334
|
90 100
....*....|....*....|..
gi 498373677 612 EVEAQTVTV--RKYGEEKTQTM 631
Cdd:PRK14938 335 EVKTSTLTVkiRANNEQKSMTV 356
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
263-403 |
5.40e-10 |
|
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: 60.28 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 263 VGSGLPVWLPNGATIRRQVERyITDKELAN-GYQHVYTPVLSNLNLYKTSGHWDHYREDMFPPMDMGDGEFLeLRPMNCP 341
Cdd:cd00779 19 TSSGLYSWLPLGLRVLKKIEN-IIREEMNKiGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGKEFL-LGPTHEE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498373677 342 SHIMVFKHKPRSYRELPIRIAELGMMHRYEKSGALtGLSRVREMTLNDGHTF-VDPEKIEEEF 403
Cdd:cd00779 97 VITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRF-GLMRGREFLMKDAYSFdIDEESLEETY 158
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
261-423 |
1.72e-09 |
|
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: 58.92 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 261 QEVGSGLPVWLPNGATIRRQVERyITDKELA-NGYQHVYTPVLSNLNLYKTSGHWDHY-REDMFPPMDMGDGEFLE---L 335
Cdd:cd00772 18 QGPGRGIINFLPLAKAILDKIEN-VLDKMFKeHGAQNALFPFFILASFLEKEAEHDEGfSKELAVFKDAGDEELEEdfaL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 336 RPMNCPSHIMVFKHKPRSYRELPIRIAELGMMHRYEKSgALTGLSRVREMTLNDGHTF-VDPEKIEEEFKSILTMMMAVY 414
Cdd:cd00772 97 RPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIR-PRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIA 175
|
....*....
gi 498373677 415 RDFNITDYR 423
Cdd:cd00772 176 RDLAAIDFI 184
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-417 |
3.61e-09 |
|
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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 57.99 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 265 SGLPVWLPNGATIRRQVERYITDKELANGYQHVYTPVLSNLNLY-KTSGHWDHYREDMFPPMDMGDGEFLE---LRPMN- 339
Cdd:cd00778 22 KGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELeKEKEHIEGFAPEVAWVTHGGLEELEEplaLRPTSe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 340 ---CPShimvFKHKPRSYRELPIRIAELGMMHRYEKSgALTGLSRVREMTLNDGHT-FVDPEKIEEEFKSILTMMMAVYR 415
Cdd:cd00778 102 taiYPM----FSKWIRSYRDLPLKINQWVNVFRWETK-TTRPFLRTREFLWQEGHTaHATEEEAEEEVLQILDLYKEFYE 176
|
..
gi 498373677 416 DF 417
Cdd:cd00778 177 DL 178
|
|
| tRNA_SAD |
smart00863 |
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ... |
177-221 |
4.59e-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: 4.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 498373677 177 IQGDHIELDKGGLVPSTGWIKHFKLTSVAGAYWRgkssnpmMQRI 221
Cdd:smart00863 6 IGDFSVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
550-621 |
9.58e-09 |
|
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: 53.17 E-value: 9.58e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498373677 550 PLQVQIIPVNLGAHG--EYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVR 621
Cdd:cd00738 1 PIDVAIVPLTDPRVEarEYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVK 74
|
|
| TGS |
pfam02824 |
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ... |
7-63 |
1.28e-08 |
|
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: 51.39 E-value: 1.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 498373677 7 TFPDGAVKVFPDGTKPIEVAQSISKSLAKKSVSAKLNDAYVGMNDIIPESGNFQLIT 63
Cdd:pfam02824 4 YTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
552-636 |
9.73e-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: 47.15 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 552 QVQIIPVNLGAHGEYADgIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVRKYGEEKTQTM 631
Cdd:cd00859 3 DVYVVPLGEGALSEALE-LAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETV 81
|
....*
gi 498373677 632 SFIDF 636
Cdd:cd00859 82 ALDEL 86
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
549-634 |
1.72e-05 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 47.80 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 549 SPLQVQIIPvnLGAHGEYADGIQKKLQSAGLRANVETKEAKLGYLIREAQTNKIPYTLVLGDSEVEAQTVTVR--KYGEE 626
Cdd:PRK12420 337 STADVFIIP--LGTELQCLQIAQQLRSTTGLKVELELAGRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRnmKEGSE 414
|
....*...
gi 498373677 627 KTQTMSFI 634
Cdd:PRK12420 415 VKVPLSSL 422
|
|
| AlaX |
COG2872 |
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ... |
74-204 |
2.64e-05 |
|
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442119 [Multi-domain] Cd Length: 238 Bit Score: 45.95 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 74 RHATSHLLAQALKRMPKFANMHFGVGP---FIDngfyYDTDNgagnqVSVEDFSEIEAMMHKIVKEDLPIISRQITRAEA 150
Cdd:COG2872 99 LHTALHLLSAVVYREYGAPVTGGQIGEdraRID----FDLPE-----FDEEDLEEIEAEANELIAADLPVRIYWITREEL 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498373677 151 LEMfatdPYKMALITDLP---EDEILTIAIQGdhieLDK---GGL-VPSTGWIKHFKLTSV 204
Cdd:COG2872 170 EAI----PGLVRTMSVLPppgVGRVRIVEIGG----VDLqpcGGThVANTGEIGRIKITKI 222
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
263-429 |
6.14e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 46.23 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 263 VGSGLPVWLPNGATIRRQVERyITDKELAN-GYQHVYTPVLSNLNLYKTSGHWDHYREDMFPPMDMGDGEFlelrpmnC- 340
Cdd:PRK09194 35 LASGIYTYLPLGLRVLRKIEN-IVREEMNKiGAQEVLMPALQPAELWQESGRWEEYGPELLRLKDRHGRDF-------Vl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498373677 341 -PSHIMVF----KHKPRSYRELP-------------IRiaelgmmHRYeksgaltGLSRVREMTLNDGHTF-VDPEKIEE 401
Cdd:PRK09194 107 gPTHEEVItdlvRNEIKSYKQLPlnlyqiqtkfrdeIR-------PRF-------GLMRGREFIMKDAYSFhADEESLDE 172
|
170 180
....*....|....*....|....*...
gi 498373677 402 EFKSiltmMMAVYRdfNITDyRFRLSYR 429
Cdd:PRK09194 173 TYDA----MYQAYS--RIFD-RLGLDFR 193
|
|
| |
