|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
1-473 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 531.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 1 MKKGKFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFR 80
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 81 KLQSTLNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSDLED-GKCPDH---PNLeieiI 156
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVDgGKCPDCgreVEL----V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 157 EEENYFFRLSKYQDKLLDFYEKNPSFVLPEKRFNEA-KKFVESGLSDFSISRlkEKMPWGVQVPDDQDHVMYVWFDALVN 235
Cdd:PRK12267 157 KEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMiNNFIKPGLEDLSISR--TSFDWGIPVPFDPKHVVYVWIDALLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 236 YISTLGWP-EDDKKFQAFWPG-VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVIHGFITSGGKKMSKTVGNVINPFETV 313
Cdd:PRK12267 235 YITALGYGsDDDELFKKFWPAdVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 314 DGYGTDALRYYLAREVsPF-EDSDFTEDKFKEAYNANLANGLGNLVSRIMKMFVAY---EVAEDKKKfifNDFKSFEVMV 389
Cdd:PRK12267 315 DRYGLDALRYYLLREV-PFgSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYfdgEIPAPGNV---TEFDEELIAL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 390 RGESYKEYREMMNNFEFGKVMDFAWGKIGEIDKQIQETQPFKLIK--TDKEKAIDEVARLVGELWSIANLLTPFMPETSH 467
Cdd:PRK12267 391 AEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKdeGKKERLATVMYHLAESLRKVAVLLSPFMPETSK 470
|
....*.
gi 1277159303 468 KIKEAI 473
Cdd:PRK12267 471 KIFEQL 476
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
5-469 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 522.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQS 84
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 85 TLNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSDL-EDGKCPDHPNLEIEIIEEENYFF 163
Cdd:PRK11893 82 ALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELiEDGYRCPPTGAPVEWVEEESYFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 164 RLSKYQDKLLDFYEKNPSFVLPEKRFNEAKKFVESGLSDFSISRLKEKmpWGVQVPDDQDHVMYVWFDALVNYISTLGWP 243
Cdd:PRK11893 162 RLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISRTNFD--WGIPVPGDPKHVIYVWFDALTNYLTALGYP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 244 EDD----KKFQAFWP-GVQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVIHGFITSGGKKMSKTVGNVINPFETVDGYGT 318
Cdd:PRK11893 240 DDEellaELFNKYWPaDVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 319 DALRYYLAREVSPFEDSDFTEDKFKEAYNANLANGLGNLVSRIMKMFVAYEVAEDKKKFIFNDFKSFEVMVRGESYKEYR 398
Cdd:PRK11893 320 DAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERVR 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277159303 399 EMMNNFEFGKVMDFAWGKIGEIDKQIQETQPFKLIKTDKEKAIDEVARLVGELWSIANLLTPFMPETSHKI 469
Cdd:PRK11893 400 AAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKI 470
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
5-473 |
1.76e-171 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 493.86 E-value: 1.76e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQS 84
Cdd:COG0143 2 KFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 85 TLNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSdLEDGKCPDHPNLEIEIIEEE----- 159
Cdd:COG0143 82 KLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDR-YVEGTCPKCGAEDAYGDQCEncgat 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 160 ------------------------NYFFRLSKYQDKLLDFYEKNPSfvLPEKRFNEAKKFVESGLSDFSISRlkeKMPWG 215
Cdd:COG0143 161 leptelinprsaisgappelreeeHYFFRLSKYQDRLLEWIEENPD--IQPEVRNEVLSWLKEGLQDLSISR---DFDWG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 216 VQVPDDQDHVMYVWFDALVNYIS-TLGWPED---DKKFQAFWPG-----VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQV 286
Cdd:COG0143 236 IPVPGDPGKVFYVWFDALIGYISaTKGYADDrglPEDFEKYWPApdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 287 VIHGFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFKEAYNANLANGLGNLVSRIMKMFV 366
Cdd:COG0143 316 FAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 367 --------AYEVAEDKKKFIFNDFKsfevmvrgESYKEYREMMNNFEFGKVMDFAWGKIGEIDKQIQETQPFKLIKTDKE 438
Cdd:COG0143 396 kyfdgkvpEPGELTEADEELLAEAE--------AALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDP 467
|
490 500 510
....*....|....*....|....*....|....*.
gi 1277159303 439 KAIDEV-ARLVGELWSIANLLTPFMPETSHKIKEAI 473
Cdd:COG0143 468 ERLATVlYTLLEALRILAILLKPFLPETAEKILEQL 503
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
6-473 |
4.25e-134 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 397.90 E-value: 4.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 6 FYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQST 85
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 86 LNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSDLEdGKCPDHPNLEIE----------- 154
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVE-GTCPKCGSEDARgdhcevcgrhl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 155 ------------------IIEEENYFFRLSKYQDKLLDFYEKNPSFV-LPEKRFNEAKKFVESGLSDFSISRLKEKmpWG 215
Cdd:TIGR00398 160 eptelinprckicgakpeLRDSEHYFFRLSAFEKELEEWIRKNPESGsPASNVKNKAQNWLKGGLKDLAITRDLVY--WG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 216 VQVPDDQDHVMYVWFDALVNYISTLGW-PEDDKKFQAFWPG------VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVI 288
Cdd:TIGR00398 238 IPVPNDPNKVVYVWFDALIGYISSLGIlSGDTEDWKKWWNNdedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 289 HGFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFKEAYNANLANGLGNLVSRIMKMFVAY 368
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 369 EVAEDKKKFIFNDFKSFEVMVRGESYKEYREMMNNFEFGKVMDFAWGKIGEIDKQIQETQPFKLIKTD-KEKAIDEVARL 447
Cdd:TIGR00398 398 FNGVLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSpRLKELLAVCSM 477
|
490 500
....*....|....*....|....*.
gi 1277159303 448 VGELWSIanLLTPFMPETSHKIKEAI 473
Cdd:TIGR00398 478 LIRVLSI--LLYPIMPKLSEKILKFL 501
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
5-337 |
2.56e-133 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 388.04 E-value: 2.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQS 84
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 85 TLNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCEL---EKTDSDledgkcpdhpnleieiieeeNY 161
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERflpEWREEE--------------------HY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 162 FFRLSKYQDKLLDFYEKNPSFVLPEKRFNEAKKFVESGLSDFSISRlkEKMPWGVQVPDDQDHVMYVWFDALVNYISTLG 241
Cdd:cd00814 141 FFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITR--DLFDWGIPVPLDPGKVIYVWFDALIGYISATG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 242 WPEDDKKFQAFW-----PGVQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVIHGFITSGGKKMSKTVGNVINPFETVDGY 316
Cdd:cd00814 219 YYNEEWGNSWWWkdgwpELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY 298
|
330 340
....*....|....*....|.
gi 1277159303 317 GTDALRYYLAREVSPFEDSDF 337
Cdd:cd00814 299 GADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
6-360 |
1.12e-121 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 360.84 E-value: 1.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 6 FYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQST 85
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 86 LNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSDLEdGKCP---------DH-------- 148
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVE-GTCPhcgsedargDQcencgrhl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 149 -PNLEIEII-----------EEENYFFRLSKYQDKLLDFYEKNpSFVLPEKRFNEAKKFVESGLSDFSISRlkeKMPWGV 216
Cdd:pfam09334 160 ePTELINPKcvicgttpevkETEHYFFDLSKFQDKLREWIEEN-NPEWPENVKNMVLEWLKEGLKDRAISR---DLDWGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 217 QVPDDQDHVMYVWFDALVNYISTLG-WPEDDKKFQAFWPG------VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVIH 289
Cdd:pfam09334 236 PVPGAEGKVFYVWLDAPIGYISATKeLSGNEEKWKEWWPNdpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAH 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277159303 290 GFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFKEAYNANLANGLGNLVSR 360
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNR 386
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
6-365 |
2.06e-102 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 319.35 E-value: 2.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 6 FYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQST 85
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 86 LNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSD-LEDGKCPDHpNLEIEIIEEENYFFR 164
Cdd:PLN02224 151 LDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKElLENNCCPVH-QMPCVARKEDNYFFA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 165 LSKYQDKLLDFYEKNPSFVLPEKRFNEAKKFVESGLSDFSISRlkEKMPWGVQVPDDQDHVMYVWFDALVNYISTLgwPE 244
Cdd:PLN02224 230 LSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSGLRDFSISR--ALVDWGIPVPDDDKQTIYVWFDALLGYISAL--TE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 245 DDKKFQ-----AF-WPG-VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQVVIHGFITSGGKKMSKTVGNVINPFETVDGYG 317
Cdd:PLN02224 306 DNKQQNletavSFgWPAsLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFG 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1277159303 318 TDALRYYLAREVSPFEDSDFTEDKFKEAYNANLANGLGNLVSRIMKMF 365
Cdd:PLN02224 386 PDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLL 433
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
8-487 |
2.62e-78 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 257.39 E-value: 2.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 8 ITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKG----EIIQNYCDSCADNFRKLq 83
Cdd:PRK00133 6 VTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGitpeELIARYHAEHKRDFAGF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 84 stlNLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYC------------VG--------------CE----- 132
Cdd:PRK00133 85 ---GISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDpekgmflpdrfvKGtcpkcgaedqygdnCEvcgat 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 133 LEKTDsdLEDGKC------P-----DHpnleieiieeenYFFRLSKYQDKLLDFYEKNPSfvLPEKRFNEAKKFVESGLS 201
Cdd:PRK00133 162 YSPTE--LINPKSaisgatPvlkesEH------------FFFKLPRFEEFLKEWITRSGE--LQPNVANKMKEWLEEGLQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 202 DFSISRlkeKMPW-GVQVPDDQDHVMYVWFDALVNYI-STLGWPE--DDKKFQAFWPG------VQLAGKDNLRQQAVMW 271
Cdd:PRK00133 226 DWDISR---DAPYfGFEIPGAPGKVFYVWLDAPIGYIsSTKNLCDkrGGLDWDEYWKKdsdtelYHFIGKDIIYFHTLFW 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 272 QAMLMSVG--LPNtiQVVIHGFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSP-FEDSDFTEDKFKEAYNA 348
Cdd:PRK00133 303 PAMLEGAGyrLPT--NVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPEtIDDLDFNWEDFQQRVNS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 349 NLANGLGNLVSR----IMKMF---VAYEVAEDKkkfIFNDFKsfevmvrgESYKEYREMMNNFEFGKVMD--FAWGKIGe 419
Cdd:PRK00133 381 ELVGKVVNFASRtagfINKRFdgkLPDALADPE---LLEEFE--------AAAEKIAEAYEAREFRKALReiMALADFA- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 420 iDKQIQETQPFKLIKTDKEKAiDEVARLVGELW-SIANLLTPFMPETSHKI--------------KEAIRANKI--PEPL 482
Cdd:PRK00133 449 -NKYVDDNEPWKLAKQDGERL-QAVCSVGLNLFrALAIYLKPVLPELAERAeaflnleeltwddaQQPLAGHPInkFKIL 526
|
....*
gi 1277159303 483 FLRKE 487
Cdd:PRK00133 527 FTRIE 531
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
5-337 |
6.64e-69 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 222.68 E-value: 6.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKG------EIIQNYCDSC--- 75
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGgrkkktIWIEEFREDPkef 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 76 ADNFRKLQST----LNLSNDA--FIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKycvgcelektdsdledgkcpDHP 149
Cdd:cd00668 81 VEEMSGEHKEdfrrLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPVR--------------------ITE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 150 NleieiieeenYFFRLSKYQDKLLDFYEKNPsfVLPEKRFNEAKKFVESGLsDFSISRlkeKMPWGVQVPDDqdhVMYVW 229
Cdd:cd00668 141 Q----------WFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLL-DWAISR---QRYWGTPLPED---VFDVW 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 230 FDALVNYISTLGWPEDDKKFQAFWPG-VQLAGKDNLRQQAVMWQAMLMSVGLPNTIQ-VVIHGFIT-SGGKKMSKTVGNV 306
Cdd:cd00668 202 FDSGIGPLGSLGYPEEKEWFKDSYPAdWHLIGKDILRGWANFWITMLVALFGEIPPKnLLVHGFVLdEGGQKMSKSKGNV 281
|
330 340 350
....*....|....*....|....*....|.
gi 1277159303 307 INPFETVDGYGTDALRYYLAREVSPFEDSDF 337
Cdd:cd00668 282 IDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
4-337 |
1.32e-40 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 149.70 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 4 GKFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGL----KVYRKAQEKG-------------- 65
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIatqvVVEKKLGIEGktrhdlgreeflek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 66 --EIIQNYCDSCADNFRKLQSTLNLSNDAFirTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCelEKTDSDLE-- 141
Cdd:cd00817 81 cwEWKEESGGKIREQLKRLGASVDWSREYF--TMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKL--RTAISDIEvc 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 142 -DGKCPDHPNLeieiieEENYFFRLSKYQDKLLDFYEKNPSFVLPEKRFNEAKKFVESgLSDFSISRlkeKMPWGVQVP- 219
Cdd:cd00817 157 sRSGDVIEPLL------KPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLEN-IRDWCISR---QLWWGHRIPa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 220 ------------------------------------DDQDhVMYVWFDALVNYISTLGWPEDDKKFQAFWPG-VQLAGKD 262
Cdd:cd00817 227 wyckdgghwvvareedeaidkaapeacvpcggeelkQDED-VLDTWFSSSLWPFSTLGWPEETKDLKKFYPTsLLVTGHD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 263 NLRqqavMWQA--MLMSVGLPNTI---QVVIHGFI-TSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSD 336
Cdd:cd00817 306 IIF----FWVArmIMRGLKLTGKLpfkEVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRDIN 381
|
.
gi 1277159303 337 F 337
Cdd:cd00817 382 L 382
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
8-469 |
6.10e-36 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 141.84 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 8 ITTTLPYVNANPHLGHAFELV-EADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQSTL 86
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 87 NLSNDAFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSdLEDGKCPdhpnleieiIEEENYFFRLS 166
Cdd:PLN02610 101 DISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADR-LVEGTCP---------TEGCNYDSARG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 167 KYQD---KLLDFYE-KNPSFVL----PEKR-----F-------NEAKKFVES---------------------GLSDFSI 205
Cdd:PLN02610 171 DQCEkcgKLLNPTElIDPKCKVckntPRIRdtdhlFlelpllkDKLVEYINEtsvaggwsqnaiqttnawlrdGLKPRCI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 206 SR-LKekmpWGVQVPDD--QDHVMYVWFDALVNYIS-TLGWPEDdkkFQAFWPG------VQLAGKDNLRQQAVMWQAML 275
Cdd:PLN02610 251 TRdLK----WGVPVPLEkyKDKVFYVWFDAPIGYVSiTACYTPE---WEKWWKNpenvelYQFMGKDNVPFHTVMFPSTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 276 MSVGLPNTIQVVIH--GFITSGGKKMSKTVGnvinpfetVDGYGTDA---------LRYYLAREVSPFEDSDFTEDKFKE 344
Cdd:PLN02610 324 LGTGENWTMMKTISvtEYLNYEGGKFSKSKG--------VGVFGNDAkdtnipvevWRYYLLTNRPEVSDTLFTWADLQA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 345 AYNANLANGLGNLVSRIMkMFVAYEVAEDKKKFIFN--DFKSFEVMVR-----GESYKEYREMMNNFEFGKVMDFAWGKI 417
Cdd:PLN02610 396 KLNSELLNNLGNFINRVL-SFIAKPPGAGYGSVIPDapGAESHPLTKKlaekvGKLVEQYVEAMEKVKLKQGLKTAMSIS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1277159303 418 GEIDKQIQETQPFKLIKTDKEKAIDEVARLVGELWSIANLLTPFMPETSHKI 469
Cdd:PLN02610 475 SEGNAYLQESQFWKLYKEDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEV 526
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
13-334 |
2.71e-28 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 114.64 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 13 PYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEK-----GEIIQNY--------CDSCADNF 79
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElgisgKKDIEKMgiaefnakCREFALRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 80 RKLQStlnlsnDAFIR------------TTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVgcELEKTDSdledgkcpd 147
Cdd:cd00818 90 VDEQE------EQFQRlgvwvdwenpykTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPWPL--IYRATPQ--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 148 hpnleieiieeenYFFRLSKYQDKLLDFYEKN---PSFVlpEKRFneaKKFVEsGLSDFSISRLKEkmpWGVQVP----D 220
Cdd:cd00818 153 -------------WFIRVTKIKDRLLEANDKVnwiPEWV--KNRF---GNWLE-NRRDWCISRQRY---WGTPIPvwycE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 221 DQDH--------VMYVWFDALVNYISTLGWPEDDKKFQAFWPG-VQLAGKDNLRqqAVMWQAMLMSVGLPNTI---QVVI 288
Cdd:cd00818 211 DCGEvlvrrvpdVLDVWFDSGSMPYAQLHYPFENEDFEELFPAdFILEGSDQTR--GWFYSLLLLSTALFGKApykNVIV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1277159303 289 HGFITSG-GKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFED 334
Cdd:cd00818 289 HGFVLDEdGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
3-469 |
7.88e-25 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 108.22 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 3 KGKFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEK-GEIIQNYCDSCADNFRK 81
Cdd:TIGR00422 32 KPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEKKlGAEGKTKHDLGREEFRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 82 LQSTLNLSNDAFIR-----------------TTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGC-------ELEKTD 137
Cdd:TIGR00422 112 KIWEWKEESGGTIKnqikrlgasldwsrerfTMDEGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLntaisdiEVEYKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 138 SD---------LEDGK---------------------------------------------------------------- 144
Cdd:TIGR00422 192 VKgklyyirypLANGSkdylvvattrpetmfgdtavavhpederykhligkkvilpltgrkipiiadeyvdmefgtgavk 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 145 -CPDH-PN--------------------------------------------------LEIEIIEEEN------------ 160
Cdd:TIGR00422 272 vTPAHdFNdyewgkrhnlefinildedgllnenagkyqgltrfearkkivedlkeeglLVKIEPHTHNvgtcwrsgtvve 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 161 ------YFFRLSKYQDKLLD-FYEKNPSFVlPEKRFNEAKKFVESgLSDFSISRlkeKMPWGVQVP---DDQDHVMYV-- 228
Cdd:TIGR00422 352 pllskqWFVKVEKLADKALEaAEEGEIKFV-PKRMEKRYLNWLRN-IKDWCISR---QLIWGHRIPvwyCKECGEVYVak 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 229 --------------------------WFDALVNYISTLGWPEDDKKFQAFWP-GVQLAGKDNLRqqavMWQA--MLMSVG 279
Cdd:TIGR00422 427 eeplpddktntgpsveleqdtdvldtWFSSSLWPFSTLGWPDETKDLKKFYPtDLLVTGYDIIF----FWVArmIFRSLA 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 280 LPNTI---QVVIHGFI-TSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFKeaYNANLANGLG 355
Cdd:TIGR00422 503 LTGQVpfkEVYIHGLVrDEQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVE--SARNFLNKLW 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 356 NlVSRIMKMfvayevAEDKKKFIFNDFKSFEVMVR------GESYKEYREMMNNFEFGK----VMDFAWGKIgeIDKQIQ 425
Cdd:TIGR00422 581 N-ASRFVLM------NLSDDLELSGGEEKLSLADRwilsklNRTIKEVRKALDKYRFAEaakaLYEFIWNDF--CDWYIE 651
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1277159303 426 ETQPFKLIKTDKEK--AIDEvarLVGELWSIANLLTPFMPETSHKI 469
Cdd:TIGR00422 652 LVKYRLYNGNEAEKkaARDT---LYYVLDKALRLLHPFMPFITEEI 694
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
5-339 |
7.48e-24 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 101.56 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRKLQS 84
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 85 TLNLSND--AFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVgcelektdsdLEDgkcpdhpnleieiieeeNYF 162
Cdd:cd00812 81 RMGFSYDwrREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWCK----------LLD-----------------QWF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 163 FRLS--KYQDKLLDFYEKNPSFvlPEKRFNEAKKFVesglsDFSISR-LKEKMPWgvqvpddqDHVMYVWFDA------- 232
Cdd:cd00812 134 LKYSetEWKEKLLKDLEKLDGW--PEEVRAMQENWI-----GCSRQRyWGTPIPW--------TDTMESLSDStwyyary 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 233 LVNYISTLGWP----EDDKKFQAFWP-GVQLAGKDnlrqQAVM-------WQAMLMSVGLPNTI---QVVIHGFITSGGK 297
Cdd:cd00812 199 TDAHNLEQPYEgdleFDREEFEYWYPvDIYIGGKE----HAPNhllysrfNHKALFDEGLVTDEppkGLIVQGMVLLEGE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1277159303 298 KMSKTVGNVINPFETVDGYGTDALRYYLAREVSPfeDSDFTE 339
Cdd:cd00812 275 KMSKSKGNVVTPDEAIKKYGADAARLYILFAAPP--DADFDW 314
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
202-480 |
1.72e-20 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 95.06 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 202 DFSISRlkeKMPWGVQVP----------------------------DDQDhVMYVWFDALVNYISTLGWPEDDKKFQAFW 253
Cdd:PRK14900 415 DWCISR---QLWWGHQIPawycpdghvtvaretpeacstcgkaelrQDED-VLDTWFSSGLWPFSTMGWPEQTDTLRTFY 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 254 P-GVQLAGKDNLrqqaVMWQAMLMSVGL------PNTiQVVIHGFI-TSGGKKMSKTVGNVINPFETVDGYGTDALRYYL 325
Cdd:PRK14900 491 PtSVMETGHDII----FFWVARMMMMGLhfmgevPFR-TVYLHPMVrDEKGQKMSKTKGNVIDPLVITEQYGADALRFTL 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 326 AREVSPFEDSDFTEDKFkEAYNAnLANGLGNlVSR--IMKMFVAYEVAEDKKKFIFNDFKSFEVMVRGESYKEYREMMNN 403
Cdd:PRK14900 566 AALTAQGRDIKLAKERI-EGYRA-FANKLWN-ASRfaLMNLSGYQERGEDPARLARTPADRWILARLQRAVNETVEALEA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 404 FEFGK----VMDFAWGKIgeIDKQIqETQPFKLIKTDKEKAIDEVARLVGELWSIANLLTPFMP----ETSHKIKEAIRA 475
Cdd:PRK14900 643 FRFNDaanaVYAFVWHEL--CDWYI-ELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPfiteELWHVLRAQVGA 719
|
....*
gi 1277159303 476 NKIPE 480
Cdd:PRK14900 720 SAWAD 724
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
346-473 |
2.16e-20 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 86.77 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 346 YNANLANGLGNLVSRIMKM------FV--AYEVAEDKKKFIFNDFKsfevmvrgESYKEYREMMNNFEFGKVMDFAWGKI 417
Cdd:cd07957 1 INSELANNLGNLVNRTLNMaskyfgGVvpEFGGLTEEDEELLEEAE--------ELLEEVAEAMEELEFRKALEEIMELA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1277159303 418 GEIDKQIQETQPFKLIKTDKEKAIDEVARLVGE-LWSIANLLTPFMPETSHKIKEAI 473
Cdd:cd07957 73 RAANKYIDETAPWKLAKEEDPERLATVLYVLLElLRILAILLSPFMPETAEKILDQL 129
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
238-463 |
2.28e-18 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 88.24 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 238 STLGWPEDDKKFQAFWPGvqlagkdnlrqqAVM---------WQA-MLMSvGLPNTIQ-----VVIHGFI-TSGGKKMSK 301
Cdd:PRK05729 457 STLGWPEKTEDLKRFYPT------------SVLvtgfdiiffWVArMIMM-GLHFTGQvpfkdVYIHGLVrDEQGRKMSK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 302 TVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFkEAYnANLANGLGNlVSR--IMKMFVAYEVAEDKK---- 375
Cdd:PRK05729 524 SKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFDEERV-EGY-RNFANKLWN-ASRfvLMNLEGADVGELPDPeels 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 376 ---KFIFNDFKSFEvmvrgesyKEYREMMNNFEFGKVM----DFAWG----------KIGEIDKQIQETQpFKLIKTdke 438
Cdd:PRK05729 601 ladRWILSRLNRTV--------AEVTEALDKYRFDEAAralyEFIWNefcdwylelaKPVLQEAAKRATR-ATLAYV--- 668
|
250 260
....*....|....*....|....*
gi 1277159303 439 kaIDEVARlvgelwsianLLTPFMP 463
Cdd:PRK05729 669 --LEQILR----------LLHPFMP 681
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
237-463 |
4.07e-17 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 84.33 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 237 ISTLGWPEDDKKFQAFWPGvqlagkdnlrqqAVM---------WQA-MLMSvGLPNTIQ-----VVIHGFI-TSGGKKMS 300
Cdd:COG0525 458 FSTLGWPEKTEDLKYFYPT------------SVLvtgfdiiffWVArMIMM-GLHFTGEvpfkdVYIHGLVrDEQGRKMS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 301 KTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEDKFkEAYnANLANGLGNlVSRIMKMFVayevaEDKKKFIFN 380
Cdd:COG0525 525 KSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIKFDEERV-EGY-RNFANKLWN-ASRFVLMNL-----EGFDPGLDP 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 381 DFKSFEVMVR------GESYKEYREMMNNFEFG----KVMDFAWG----------KI---GEIDKQIQETQpfkliktdk 437
Cdd:COG0525 597 DPEELSLADRwilsrlNKTIAEVTEALEKYRFDeaaqALYDFVWNefcdwylelaKPrlyGGDEAAKRETR--------- 667
|
250 260
....*....|....*....|....*.
gi 1277159303 438 ekaidevARLVGELWSIANLLTPFMP 463
Cdd:COG0525 668 -------ATLVYVLEQILRLLHPFMP 686
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
204-326 |
7.09e-16 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 80.76 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 204 SISRLKEKMPWGVQVPDDQDhVMYVWFDALVNYISTLGWPEDDKK-FQAFWPGVQL-AGKDNLrqqaVMWQAMLMSVGLP 281
Cdd:PLN02943 486 ALEKAREKYGKDVEIYQDPD-VLDTWFSSALWPFSTLGWPDVSAEdFKKFYPTTVLeTGHDIL----FFWVARMVMMGIE 560
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1277159303 282 NT-----IQVVIHGFI-TSGGKKMSKTVGNVINPFETVDGYGTDALRYYLA 326
Cdd:PLN02943 561 FTgtvpfSYVYLHGLIrDSQGRKMSKTLGNVIDPLDTIKEFGTDALRFTLA 611
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
200-326 |
3.23e-15 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 78.22 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 200 LSDFSISRLKEKMPWGVQVPDdqdhVMYVWFDALVNYISTLGWPEDD-KKFQAFWPG-VQLAGKDNLRqqavMW-QAMLM 276
Cdd:pfam00133 465 LHREAKDKLGYGKGTLEQDED----VLDTWFSSGSWPFSTLGWPFVNtEEFKKFFPAdMLLEGSDQTR----GWfYRMIM 536
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1277159303 277 -SVGLPNTI---QVVIHGFITSG-GKKMSKTVGNVINPFETVDGYGTDALRYYLA 326
Cdd:pfam00133 537 lSTALTGSVpfkNVLVHGLVRDEqGRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
274-352 |
1.81e-11 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 66.64 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 274 MLMSVGLPNTI---QVVIHGFITSG-GKKMSKTVGNVINPFETVDGYGTDALRYYLAReVSPFEDSDFTEDKFKE---AY 346
Cdd:COG0060 575 LLTSTALFGRApykNVLTHGFVLDEdGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS-SDYWGDLRFSDEILKEvrdVY 653
|
90
....*....|....*.
gi 1277159303 347 N----------ANLAN 352
Cdd:COG0060 654 RrlrntyrfllANLDD 669
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
6-142 |
5.52e-11 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 64.83 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 6 FYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEK-G------------EIIQNYC 72
Cdd:PRK13208 40 YSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLPTERKVEKYyGirkddisreefiELCRELT 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277159303 73 DSCADNFRKLQSTLNLSND--AFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCELEKTDSDLED 142
Cdd:PRK13208 120 DEDEKKFRELWRRLGLSVDwsLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIAQAEVEY 191
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
221-321 |
1.52e-10 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 63.87 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 221 DQDhVMYVWFDALVNYISTLGWPEDDKKFQAFWPGVQL-AGKDNLrqqaVMWQA-MLM-SVGLPNTI---QVVIHGFI-T 293
Cdd:PTZ00419 506 DED-VLDTWFSSGLFPFSTLGWPDQTDDLQRFFPTSLLeTGSDIL----FFWVArMVMmSLHLTDKLpfkTVFLHAMVrD 580
|
90 100
....*....|....*....|....*...
gi 1277159303 294 SGGKKMSKTVGNVINPFETVDGYGTDAL 321
Cdd:PTZ00419 581 SQGEKMSKSKGNVIDPLEVIEGISLQDL 608
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
2-132 |
2.34e-10 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 62.81 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 2 KKGKFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGL----KVYRKAQEKG------------ 65
Cdd:pfam00133 21 GKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLpteqVVEKKLGIKEkktrhkygreef 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277159303 66 -----EIIQNYCDSCADNFRKLQSTLNLSNDAFirTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCVGCE 132
Cdd:pfam00133 101 rekcrEWKMEYADEIRKQFRRLGRSIDWDREYF--TMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALN 170
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
221-414 |
2.93e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 62.52 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 221 DQDhVMYVWFD-ALVNYISTlGWPEDDKKFQAFWPgVQLA--GKDNLRqqavMW--QAMLMSVGLPNTI---QVVIHGFI 292
Cdd:PRK13208 454 ETD-VMDTWATsSITPLIVT-GWERDEDLFEKVFP-MDLRpqGHDIIR----TWlfYTILRAYLLTGKLpwkNIMISGMV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 293 TS-GGKKMSKTVGNVINPFETVDGYGTDALRYYLArEVSPFEDSDFTEDKFKEAYnaNLANGLGNlVSRIMKMFVAYEVA 371
Cdd:PRK13208 527 LDpDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDTPFDEKQVKIGR--RLLTKLWN-ASRFVLHFSADPEP 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1277159303 372 EDKK------KFIFNDFKSFEvmvrgesyKEYREMMNNFEFGKVMD----FAW 414
Cdd:PRK13208 603 DKAEvlepldRWILAKLAKVV--------EKATEALENYDFAKALEeiesFFW 647
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
8-73 |
7.26e-10 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 57.10 E-value: 7.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277159303 8 ITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCD 73
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVE 66
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
217-321 |
3.21e-09 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 59.53 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 217 QVPDdqdhVMYVWFDALVNYISTLGWPEDDKKFQAFWPGVQL-AGKDNLrqqaVMWQA--MLMSVGLPNTI---QVVIHG 290
Cdd:PLN02381 575 QDPD----VLDTWFSSGLFPLSVLGWPDDTDDLKAFYPTSVLeTGHDIL----FFWVArmVMMGMQLGGDVpfrKVYLHP 646
|
90 100 110
....*....|....*....|....*....|..
gi 1277159303 291 FITSG-GKKMSKTVGNVINPFETVDGYGTDAL 321
Cdd:PLN02381 647 MIRDAhGRKMSKSLGNVIDPLEVINGISLEGL 678
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
285-406 |
1.90e-08 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 56.80 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 285 QVVIHGFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSDFTEdkfkeaynaNLANGLGNLVSRI--- 361
Cdd:PRK12300 564 GIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWRE---------KEVESVRRQLERFyel 634
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1277159303 362 MKMFVAYEVaEDKKKFIfnDfKSFEVMVRgESYKEYREMMNNFEF 406
Cdd:PRK12300 635 AKELIEIGG-EEELRFI--D-KWLLSRLN-RIIKETTEAMESFQT 674
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
288-378 |
1.18e-07 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 53.95 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 288 IH-GFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLA----RevSPFedsDFTEDKFKEAYNA--NLANGLGNLVSR 360
Cdd:COG0215 254 MHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahyR--SPL---DFSEEALEEAEKAleRLYNALRRLEEA 328
|
90
....*....|....*....
gi 1277159303 361 IMK-MFVAYEVAEDKKKFI 378
Cdd:COG0215 329 LGAaDSSAEEIEELREEFI 347
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
2-141 |
6.14e-07 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 52.32 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 2 KKGKFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLK----VYRKAQEKGEIIQ-------- 69
Cdd:PTZ00419 58 SGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGIAtqvvVEKKLMKEENKTRhdlgreef 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 70 ---------NYCDSCADNFRKLQSTLNLSNDAFirTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYCvgCELEKTDSDL 140
Cdd:PTZ00419 138 lkkvwewkdKHGNNICNQLRRLGSSLDWSREVF--TMDEQRSKAVKEAFVRLYEDGLIYRDTRLVNWC--CYLKTAISDI 213
|
.
gi 1277159303 141 E 141
Cdd:PTZ00419 214 E 214
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
226-409 |
1.87e-06 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 50.54 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 226 MYVWFD------ALVNYISTLGWPEDdkkfqafwpgVQLAGKDNLRQqavmW--QAMLMSV---GLPNTIQVVIHGFI-T 293
Cdd:PLN02843 541 MDVWFDsgsswaGVLGSREGLSYPAD----------LYLEGSDQHRG----WfqSSLLTSVatkGKAPYKSVLTHGFVlD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 294 SGGKKMSKTVGNVINPFETVDG---------YGTDALRYYLArevspfeDSDFTED---------KFKEAY---NANLAN 352
Cdd:PLN02843 607 EKGFKMSKSLGNVVDPRLVIEGgknqkqepaYGADVLRLWVA-------SVDYTGDvligpqilkQMSDIYrklRGTLRY 679
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 353 GLGNLVSRIMKMFVAYEvaedkkkfifnDFKSFE--VMVRGES-YKEYREMMNNFEFGKV 409
Cdd:PLN02843 680 LLGNLHDWKPDNAVPYE-----------DLPSIDkyALFQLENvVNEIEESYDNYQFFKI 728
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
298-335 |
7.28e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 48.67 E-value: 7.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1277159303 298 KMSKTVGNVINPFETVDGYGTDALRYYlarE--VSPFEDS 335
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRLY---EmfMGPLRDS 759
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
284-335 |
2.63e-05 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 46.97 E-value: 2.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1277159303 284 IQVVIHGFITSGGKKMSKTVGNVINPFETVDGYGTDALRYYL--ArevSPFEDS 335
Cdd:COG0495 575 LEVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEmfA---GPPERD 625
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
5-46 |
4.28e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 46.22 E-value: 4.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1277159303 5 KFYITTTLPYVNANPHLGHAFELVEADIIARFHRGLGDDVFF 46
Cdd:PLN02959 46 KFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLL 87
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
294-325 |
1.85e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 44.33 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|..
gi 1277159303 294 SGGKKMSKTVGNVINPFETVDGYGTDALRYYL 325
Cdd:PLN02882 610 EDGKKMSKSLKNYPDPNEVIDKYGADALRLYL 641
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
20-65 |
1.18e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 41.63 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1277159303 20 HLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGL----KVYRKAQEKG 65
Cdd:PRK05729 52 HMGHALNNTLQDILIRYKRMQGYNTLWLPGTDHAGIatqmVVERQLAAEG 101
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
3-173 |
1.37e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 41.35 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 3 KGKFYITTTLPY-VNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGLKVYRKAQEKGEIIQNYCDSCADNFRK 81
Cdd:PLN02563 109 KPKFYVLDMFPYpSGAGLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 82 LQSTLNLSND--AFIRTTDNHHKESAQEFWRRSFQAGDIYKKNYKIKYC-----VGCELEKTDSDLEDGkcpDHPnleIE 154
Cdd:PLN02563 189 QLKSLGFSYDwdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCpalgtVLANEEVVDGLSERG---GHP---VI 262
|
170
....*....|....*....
gi 1277159303 155 IIEEENYFFRLSKYQDKLL 173
Cdd:PLN02563 263 RKPMRQWMLKITAYADRLL 281
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
292-390 |
1.63e-03 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 41.11 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 292 ITSGGKKMSKTVGNVINPFETVDGYGTDALRYYLAREVSPFEDSdfteDKFKEaynanlaNGLGNLV-SRIMKM-----F 365
Cdd:PTZ00427 714 LASDGKKMSKRLKNYPDPLYILDKYGADSLRLYLINSVAVRAEN----LKFQE-------KGVNEVVkSFILPFyhsfrF 782
|
90 100 110
....*....|....*....|....*....|..
gi 1277159303 366 VAYEVAE----DKKKFIFND---FKSFEVMVR 390
Cdd:PTZ00427 783 FSQEVTRyeclNKKQFLFNTdyiYKNDNIMDQ 814
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
13-82 |
3.73e-03 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 40.06 E-value: 3.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277159303 13 PYVNANPHLGHAFELVEADIIARFHRGLGDDVFFNTGTDEHGL----KVYRKAQEKGEIIQNYcdsCADNFRKL 82
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLpielKVEKELGIKKKDIEKV---GIAEFREK 125
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
19-144 |
4.33e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 39.85 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 19 PHLGHAFELVEADIIARFHRGLGDDVFFN-----TGT------------DEHGLKVYRKAQEKGEiiqnycdscaDNFRK 81
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPmafhvTGTpilgiaeriargDPETIELYKSLYGIPE----------EELEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277159303 82 LQSTLNL----SNDAfirttdnhhKESAQEF-----WRRSFQAGD-------------------IYKKNYKIKYCVGCEL 133
Cdd:PRK12300 71 FKDPEYIveyfSEEA---------KEDMKRIgysidWRREFTTTDpeyskfiewqfrklkekglIVKGSHPVRYCPNDNN 141
|
170
....*....|.
gi 1277159303 134 EKTDSDLEDGK 144
Cdd:PRK12300 142 PVGDHDLLDGE 152
|
|
| |
