|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
5-666 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 1252.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 5 EEKNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQ 84
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 85 ELWKKLEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQLEEvykdesgkviGGKAP-SG 163
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVD----------GGKCPdCG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 164 NEVELVKEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMINNFIKPGLEDLAVSRTTFDWGIKVPGNPKHVVYVWID 243
Cdd:PRK12267 151 REVELVKEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPGLEDLSISRTSFDWGIPVPFDPKHVVYVWID 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 244 ALSNYITALGYNTDNDTKFQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLPKMVFGHGWILMKDGKMSKSKGNVVDP 323
Cdd:PRK12267 231 ALLNYITALGYGSDDDELFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 324 YMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRTVAMINKYFNGEIPAyQGDVTPFDKTLVD 403
Cdd:PRK12267 311 EELVDRYGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPA-PGNVTEFDEELIA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 404 FKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYIDETAPWALAKEEEKRAELASVMTHLAENLRIIAVLLQPFLTRTP 483
Cdd:PRK12267 390 LAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 484 GEIFLQLGLqEENLKKWDSIYGYGEIPAGTTvVKKGTPIFPRLDAKEEVAFIQDEMKGsaPAPSAATAEVAALETPQIGI 563
Cdd:PRK12267 470 KKIFEQLGL-EEELTSWESLLEWGGLPAGTK-VAKGEPLFPRIDVEEEIAYIKEQMEG--SAPKEPEEKEKKPEKPEITI 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 564 EDFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEGMILS 643
Cdd:PRK12267 546 DDFDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILA 625
|
650 660
....*....|....*....|...
gi 2279656840 644 GEKDGKLSVIEASSDLPNGAKVK 666
Cdd:PRK12267 626 AEDDGKLTLLTVDKEVPNGSKVK 648
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
8-535 |
0e+00 |
|
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: 772.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 8 NTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELW 87
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 88 KKLEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTET---------QLEEVYKDESGKVIGG 158
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRyvegtcpkcGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 159 KAP----------SGNEVELVKEESYFFRMSKYADRLVEYYNSHPEfILPEsRKNEMInNFIKPGLEDLAVSRtTFDWGI 228
Cdd:COG0143 161 LEPtelinprsaiSGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQPE-VRNEVL-SWLKEGLQDLSISR-DFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 229 KVPGNPKHVVYVWIDALSNYITAL-GYNTDN--DTKFQKYWPAD----VQIVGKEIVRFHTIYWPIMLMALDLPLPKMVF 301
Cdd:COG0143 237 PVPGDPGKVFYVWFDALIGYISATkGYADDRglPEDFEKYWPAPdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 302 GHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRTVAMINK 381
Cdd:COG0143 317 AHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 382 YFNGEIPAYqGDVTPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYIDETAPWALAKeEEKRAELASVM 461
Cdd:COG0143 397 YFDGKVPEP-GELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK-DEDPERLATVL 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279656840 462 THLAENLRIIAVLLQPFLTRTPGEIFLQLGLQEENLkKWDSIygYGEIPAGTTvVKKGTPIFPRLDAKEEVAFI 535
Cdd:COG0143 475 YTLLEALRILAILLKPFLPETAEKILEQLGLEGDEL-TWEDA--GWPLPAGHK-IGKPEPLFPRIEDEQIEALL 544
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
8-529 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 770.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 8 NTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELW 87
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 88 KKLEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQLEEvykdesgkviGGK--APSGNE 165
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIE----------DGYrcPPTGAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 166 VELVKEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMInNFIKPGLEDLAVSRTTFDWGIKVPGNPKHVVYVWIDAL 245
Cdd:PRK11893 151 VEWVEEESYFFRLSKYQDKLLELYEANPDFIQPASRRNEVI-SFVKSGLKDLSISRTNFDWGIPVPGDPKHVIYVWFDAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 246 SNYITALGYNTDNDT---KFQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLPKMVFGHGWILMKDGKMSKSKGNVVD 322
Cdd:PRK11893 230 TNYLTALGYPDDEELlaeLFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVID 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 323 PYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRTVAMINKYFNGEIPAyQGDVTPFDKTLV 402
Cdd:PRK11893 310 PFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPE-PGALTEADEALL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 403 DFKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYIDETAPWALAKEEEKRaeLASVMTHLAENLRIIAVLLQPFLTRT 482
Cdd:PRK11893 389 EAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPER--LATVLYTLLEVLRGIAVLLQPVMPEL 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2279656840 483 PGEIFLQLGLQEENLKKWDSIyGYGEIPAGTTvVKKGTPIFPRLDAK 529
Cdd:PRK11893 467 AAKILDQLGVEEDENRDFAAL-SWGRLAPGTT-LPKPEPIFPRLEEE 511
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
10-527 |
0e+00 |
|
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: 617.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 10 FYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWKK 89
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 90 LEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETqleevYKDESGKVIGGKAP-------- 161
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDR-----YVEGTCPKCGSEDArgdhcevc 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 162 ----------------SGNEVELVKEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMINNFIKPGLEDLAVSRTTFD 225
Cdd:TIGR00398 156 grhleptelinprckiCGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 226 WGIKVPGNPKHVVYVWIDALSNYITALGYNTDNDTKFQKYWPAD-----VQIVGKEIVRFHTIYWPIMLMALDLPLPKMV 300
Cdd:TIGR00398 236 WGIPVPNDPNKVVYVWFDALIGYISSLGILSGDTEDWKKWWNNDedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 301 FGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRTVAMIN 380
Cdd:TIGR00398 316 FSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 381 KYFNGEIPAYQGDvTPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYIDETAPWALAKEEEKRAELASV 460
Cdd:TIGR00398 396 KYFNGVLPSEDIT-DEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAV 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279656840 461 MTHLaenLRIIAVLLQPFLTRTPGEIFLQLGLQEEnlkkWDSIYGygeiPAGTTVVKKGTPIFPRLD 527
Cdd:TIGR00398 475 CSML---IRVLSILLYPIMPKLSEKILKFLNFELE----WDFKLK----LLEGHKLNKAEPLFSKIE 530
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
9-351 |
2.98e-175 |
|
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: 501.29 E-value: 2.98e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 9 TFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWK 88
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 89 KLEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTetqleevykdesgkviggkapsgnevEL 168
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP--------------------------EW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 169 VKEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMInNFIKPGLEDLAVSRTTFDWGIKVPGNPKHVVYVWIDALSNY 248
Cdd:cd00814 135 REEEHYFFRLSKFQDRLLEWLEKNPDFIWPENARNEVL-SWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDALIGY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 249 ITALGYNTD---NDTKFQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLPKMVFGHGWILMKDGKMSKSKGNVVDPYM 325
Cdd:cd00814 214 ISATGYYNEewgNSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDD 293
|
330 340
....*....|....*....|....*.
gi 2279656840 326 LIDRYGLDALRYYLLREVPFGSDGLF 351
Cdd:cd00814 294 LLERYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
10-375 |
3.20e-167 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 483.72 E-value: 3.20e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 10 FYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWKK 89
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 90 LEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQL---------EEVYKD---------E 151
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVegtcphcgsEDARGDqcencgrhlE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 152 SGKVIGGK-APSGNEVELVKEESYFFRMSKYADRLVEYYNSHPEfiLPESRKNEMINNFIKPGLEDLAVSRtTFDWGIKV 230
Cdd:pfam09334 161 PTELINPKcVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNP--EWPENVKNMVLEWLKEGLKDRAISR-DLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 231 PGNPKHVVYVWIDALSNYITALGYNTDNDTKFQKYWPAD-----VQIVGKEIVRFHTIYWPIMLMALDLPLPKMVFGHGW 305
Cdd:pfam09334 238 PGAEGKVFYVWLDAPIGYISATKELSGNEEKWKEWWPNDpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGY 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 306 ILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRT 375
Cdd:pfam09334 318 LTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
12-666 |
8.72e-151 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 451.91 E-value: 8.72e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 12 ITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWKKLE 91
Cdd:PRK00133 6 VTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 92 ISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYsvsDEE--------YFTET----QLEEVYKDES---GKVI 156
Cdd:PRK00133 86 ISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLY---DPEkgmflpdrFVKGTcpkcGAEDQYGDNCevcGATY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 157 ggkAP----------SGNEVELVKEESYFFRMSKYADRLVEYYNSHPEfiLPESRKNeMINNFIKPGLEDLAVSRTTfDW 226
Cdd:PRK00133 163 ---SPtelinpksaiSGATPVLKESEHFFFKLPRFEEFLKEWITRSGE--LQPNVAN-KMKEWLEEGLQDWDISRDA-PY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 227 -GIKVPGNPKHVVYVWIDALSNYI--TALGYNTDNDTKFQKYWPAD-----VQIVGKEIVRFHTIYWPIMLMALDLPLPK 298
Cdd:PRK00133 236 fGFEIPGAPGKVFYVWLDAPIGYIssTKNLCDKRGGLDWDEYWKKDsdtelYHFIGKDIIYFHTLFWPAMLEGAGYRLPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 299 MVFGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGL-FTPEDFVDRVNYDLANDLGNLLNRTVA 377
Cdd:PRK00133 316 NVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLdFNWEDFQQRVNSELVGKVVNFASRTAG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 378 MINKYFNGEIPAYQGDvtpfDKTLVDFKNSVVlDYEKSMDHMQFSVALNQLWSLISRTNKYIDETAPWALAKEEEKRAel 457
Cdd:PRK00133 396 FINKRFDGKLPDALAD----PELLEEFEAAAE-KIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 458 ASVMTHLAENLRIIAVLLQPFLTRTPGEIFLQLGLQEenlKKWDSIygyGEIPAGTTVvKKGTPIFPRLDaKEEVAFIQD 537
Cdd:PRK00133 469 QAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE---LTWDDA---QQPLAGHPI-NKFKILFTRIE-DKQIEALIE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 538 EMKGSAPAPSAATAEVAALET----PQIGIEDFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKlRQVLSGIAEFYEP 613
Cdd:PRK00133 541 ASKEAAAAKAAAAAAAAPLAEepiaETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEET-RQVFSGIKSAYDP 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2279656840 614 ENLIGKKVIVVSNLKPVKLRGLMSEGMILS-GEKDGKLSVIEASSDLPNGAKVK 666
Cdd:PRK00133 620 EELVGKLVVMVANLAPRKMKFGVSEGMVLAaGPGGGDLFLLEPDEGAKPGMRVK 673
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-540 |
6.40e-121 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 373.28 E-value: 6.40e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 5 EEKNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQ 84
Cdd:PLN02224 66 DEADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 85 ELWKKLEISNTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQLEEvykdesgkvigGKAPSGN 164
Cdd:PLN02224 146 TLWKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLE-----------NNCCPVH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 165 EVELV--KEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEmINNFIKPGLEDLAVSRTTFDWGIKVPGNPKHVVYVWI 242
Cdd:PLN02224 215 QMPCVarKEDNYFFALSKYQKPLEDILAQNPRFVQPSYRLNE-VQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 243 DALSNYITALGYNTDN---DTKFQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLPKMVFGHGWiLMKDG-KMSKSKG 318
Cdd:PLN02224 294 DALLGYISALTEDNKQqnlETAVSFGWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGF-LTKDGmKMGKSLG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 319 NVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFVDRVNYDLANDLGNLLNRTVAMINKYFNGEI---PAYQGDVT 395
Cdd:PLN02224 373 NTLEPFELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKNCESTLvedSTVAAEGV 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 396 PFDKTLVDFKNSVVLDYEksmdHMQFSVALNQLWSLISRTNKYIDETAPWALAKEEEKRAELASV-MTHLAENLRIIAVL 474
Cdd:PLN02224 453 PLKDTVEKLVEKAQTNYE----NLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAKdLVIILEVMRVIAVA 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279656840 475 LQPFLTRTPGEIFLQLGLQEENLKK--WdSIYGYGEIPAGtTVVKKGTPIFPRLDAKEEVAfiQDEMK 540
Cdd:PLN02224 529 LSPIAPCLSLRIYSQLGYSEDQFNSitW-SDTKWGGLKGG-QVMEQASPVFARIELNPEKE--EDEKK 592
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
9-348 |
2.21e-73 |
|
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: 239.24 E-value: 2.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 9 TFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQ-------------EY 75
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRKKktiwieefredpkEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 76 VDEIAEGFQELWKKLEIS--NTDFIRTTQDRHKTSVAKIFEQLVEQGDIYLGEYEGwysvsdeeyftetqleevykdesg 153
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISydWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 154 kviggkapsgnevelVKEESYFFRMSKYADRLVEYYNSHPefILPESRKNEMINNFikPGLEDLAVSRTTFdWGIKVPGn 233
Cdd:cd00668 137 ---------------RITEQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWL--ESLLDWAISRQRY-WGTPLPE- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 234 pkHVVYVWIDALSNYITALGYNTDNDtKFQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLP-KMVFGHGWILMKDG- 311
Cdd:cd00668 196 --DVFDVWFDSGIGPLGSLGYPEEKE-WFKDSYPADWHLIGKDILRGWANFWITMLVALFGEIPpKNLLVHGFVLDEGGq 272
|
330 340 350
....*....|....*....|....*....|....*..
gi 2279656840 312 KMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSD 348
Cdd:cd00668 273 KMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDD 309
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
12-665 |
2.28e-71 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 247.00 E-value: 2.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 12 ITTPIYYPSGKAHIGHAYTTV-AGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWKKL 90
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 91 EISNTDFIRTTQdRHKTSVAK-IFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQLEEV-------YKDESGKVIGGKAPS 162
Cdd:PLN02610 101 DISFDKFGRTST-PQQTEICQaIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTcptegcnYDSARGDQCEKCGKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 163 GNEVELVKE--------------ESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMINNFIKPGLEDLAVSRTtFDWGI 228
Cdd:PLN02610 180 LNPTELIDPkckvckntprirdtDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPRCITRD-LKWGV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 229 KVP--GNPKHVVYVWIDALSNY--ITAlGYNTDndtkFQKYW--PADV---QIVGKEIVRFHTIYWPIMLMALdlplpkm 299
Cdd:PLN02610 259 PVPleKYKDKVFYVWFDAPIGYvsITA-CYTPE----WEKWWknPENVelyQFMGKDNVPFHTVMFPSTLLGT------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 300 vfGHGWILMK-----------DGKMSKSKGnvvdpymlIDRYGLDA---------LRYYLLREVPFGSDGLFTPEDFVDR 359
Cdd:PLN02610 327 --GENWTMMKtisvteylnyeGGKFSKSKG--------VGVFGNDAkdtnipvevWRYYLLTNRPEVSDTLFTWADLQAK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 360 VNYDLANDLGNLLNRTVAMI----NKYFNGEIP-AYQGDVTPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISR 434
Cdd:PLN02610 397 LNSELLNNLGNFINRVLSFIakppGAGYGSVIPdAPGAESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 435 TNKYIDETAPWALAKEEekRAELASVMTHLAENLRIIAVLLQPFLTRTPGEIFLQLGLQEENLKKWDSIygyGEI----- 509
Cdd:PLN02610 477 GNAYLQESQFWKLYKED--KPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEK---GEVarakr 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 510 -----PAGTTVVKKGtPIFPRLDaKEEVAF-----------------------IQDEMKGSAPAPSAATAE---VAALET 558
Cdd:PLN02610 552 pwelvPAGHKIGTPE-PLFKELK-DEEVEAyrekfagsqadraaraeaaeakkLAKQLKKKALSDGGKKKQgkkAGGGGK 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 559 PQIGIE---DFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGL 635
Cdd:PLN02610 630 SKAAAEreiDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGI 709
|
730 740 750
....*....|....*....|....*....|..
gi 2279656840 636 MSEGMIL--SGEKDGKLSVIEAssdlPNGAKV 665
Cdd:PLN02610 710 KSQAMVLaaSNSDHTKVELVEP----PESAAV 737
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
561-666 |
4.83e-48 |
|
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.
Pssm-ID: 239199 [Multi-domain] Cd Length: 105 Bit Score: 163.83 E-value: 4.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 561 IGIEDFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKlRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEGM 640
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEE-RQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100
....*....|....*....|....*.
gi 2279656840 641 ILSGEKDGKLSVIEASSDLPNGAKVK 666
Cdd:cd02800 80 ILAAEDGGKLKLLTPDEEVEPGSRVS 105
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
360-490 |
8.42e-46 |
|
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: 158.81 E-value: 8.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 360 VNYDLANDLGNLLNRTVAMINKYFNGEIPAYqGDVTPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYI 439
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEF-GGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2279656840 440 DETAPWALAKeEEKRAELASVMTHLAENLRIIAVLLQPFLTRTPGEIFLQL 490
Cdd:cd07957 80 DETAPWKLAK-EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
559-666 |
1.16e-40 |
|
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273059 [Multi-domain] Cd Length: 137 Bit Score: 144.88 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 559 PQIGIEDFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKlRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSE 638
Cdd:TIGR00399 30 ETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSE 108
|
90 100
....*....|....*....|....*....
gi 2279656840 639 GMILSGEKDGK-LSVIEASSDLPNGAKVK 666
Cdd:TIGR00399 109 GMILAAEDDGKvLFLLSPDQEAIAGERIK 137
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
8-351 |
7.93e-39 |
|
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: 147.78 E-value: 7.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 8 NTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG--------QKIQAKAKERG-ISEQEYVDE 78
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGiatqvvveKKLGIEGKTRHdLGREEFLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 79 IAE-------GFQELWKKLEISnTDFIR---TTQDRHKTSVAKIFEQLVEQGDIYLGEYE-GW-----YSVSDEEYFtet 142
Cdd:cd00817 81 CWEwkeesggKIREQLKRLGAS-VDWSReyfTMDPGLSRAVQEAFVRLYEKGLIYRDNRLvNWcpklrTAISDIEVC--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 143 qleevykDESGKVIggkapsgnevELVKEESYFFRMSKYADRLVEYYNSHPEFILPESRKNEMiNNFIKpGLEDLAVSRT 222
Cdd:cd00817 157 -------SRSGDVI----------EPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRY-ENWLE-NIRDWCISRQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 223 TFdWGIKVPgnpkhVVYV-----WIDALSNY------------------------------------ITALGYnTDNDTK 261
Cdd:cd00817 218 LW-WGHRIP-----AWYCkdgghWVVAREEDeaidkaapeacvpcggeelkqdedvldtwfssslwpFSTLGW-PEETKD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 262 FQKYWPADVQIVGKEIVRFHTIYWPIMLMALDLPLP-KMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYL 339
Cdd:cd00817 291 LKKFYPTSLLVTGHDIIFFWVARMIMRGLKLTGKLPfKEVYLHGLVRDEDGrKMSKSLGNVIDPLDVIDGYGADALRFTL 370
|
410
....*....|..
gi 2279656840 340 LREVPFGSDGLF 351
Cdd:cd00817 371 ASAATQGRDINL 382
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
571-665 |
3.61e-35 |
|
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.
Pssm-ID: 239066 [Multi-domain] Cd Length: 99 Bit Score: 128.41 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 571 LRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEGMILS----GEK 646
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSaeelGLE 80
|
90
....*....|....*....
gi 2279656840 647 DGKLSVIEASSDLPNGAKV 665
Cdd:cd02153 81 EGSVGILELPEDAPVGDRI 99
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
10-351 |
4.40e-32 |
|
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: 126.59 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 10 FYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWKK 89
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 90 L--------EISNTD--FIRTTQdrhktsvaKIFEQLVEQGDIYLGEYEGWYSVSDEEYFTETQLEEvYKDESGKVIGGK 159
Cdd:cd00812 82 MgfsydwrrEFTTCDpeYYKFTQ--------WLFLKLYEKGLAYKKEAPVNWCKLLDQWFLKYSETE-WKEKLLKDLEKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 160 ApsgnevelvkeesyffrmskyadrlveyynshpefILPESRKNeMINNFIkpgledlAVSRTTFdWGIKVPgnpkhvvy 239
Cdd:cd00812 153 D-----------------------------------GWPEEVRA-MQENWI-------GCSRQRY-WGTPIP-------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 240 vW---IDALSN-------YITA-------LGYNTDNDTKFQKYWPADVQIVGKEIVRFH---TIYWPIMLMALDLPL--- 296
Cdd:cd00812 181 -WtdtMESLSDstwyyarYTDAhnleqpyEGDLEFDREEFEYWYPVDIYIGGKEHAPNHllySRFNHKALFDEGLVTdep 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2279656840 297 PKMVFGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLF 351
Cdd:cd00812 260 PKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDADFDW 314
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
571-664 |
4.76e-31 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 116.57 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 571 LRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEGMILSGE--KDG 648
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80
|
90
....*....|....*.
gi 2279656840 649 KLSVIEASSDLPNGAK 664
Cdd:pfam01588 81 SVGLLEPPADVPPGTK 96
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
18-348 |
5.19e-30 |
|
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: 121.19 E-value: 5.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 18 YPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKA-KERGISEQEYVDEI-AEGFQELWKKLEISNT 95
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMgIAEFNAKCREFALRYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 96 D-----FIRTT-----QDRHKT-------SVAKIFEQLVEQGDIYLGEYEGWYSVsdeeyftetqleeVYKdesgkvigg 158
Cdd:cd00818 91 DeqeeqFQRLGvwvdwENPYKTmdpeymeSVWWVFKQLHEKGLLYRGYKVVPWPL-------------IYR--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 159 kapsgnevelvKEESYFFRMSKYADRLVEYYNS---HPEFIlpESRKNEMINNfikpgLEDLAVSRTTFdWGIKVP---- 231
Cdd:cd00818 149 -----------ATPQWFIRVTKIKDRLLEANDKvnwIPEWV--KNRFGNWLEN-----RRDWCISRQRY-WGTPIPvwyc 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 232 --GNPKHVVY------VWIDALSNYITALGYNTDNDtKFQKYWPADVQIVGKEIVR--FHTiywpimLMAL-----DLPL 296
Cdd:cd00818 210 edCGEVLVRRvpdvldVWFDSGSMPYAQLHYPFENE-DFEELFPADFILEGSDQTRgwFYS------LLLLstalfGKAP 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2279656840 297 PKMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSD 348
Cdd:cd00818 283 YKNVIVHGFVLDEDGrKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
5-497 |
5.21e-30 |
|
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: 126.71 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 5 EEKNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG--------QKIQAKAKERG-ISEQEY 75
Cdd:TIGR00422 30 SNKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGiatqvkveKKLGAEGKTKHdLGREEF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 76 VDEI-------AEGFQELWKKLEISnTDFIR---TTQDRHKTSVAKIFEQLVEQGDIYLGEYE-GW-----YSVSDEE-- 137
Cdd:TIGR00422 110 REKIwewkeesGGTIKNQIKRLGAS-LDWSRerfTMDEGLSKAVKEAFVRLYEKGLIYRGEYLvNWdpklnTAISDIEve 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 138 ---------YFT------------------ETQL----------EEVYKDESGKVI-----GGKAP-------------- 161
Cdd:TIGR00422 189 ykevkgklyYIRyplangskdylvvattrpETMFgdtavavhpeDERYKHLIGKKVilpltGRKIPiiadeyvdmefgtg 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 162 -----------------------------------------------------------------------------SGN 164
Cdd:TIGR00422 269 avkvtpahdfndyewgkrhnlefinildedgllnenagkyqgltrfearkkivedlkeegllvkiephthnvgtcwrSGT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 165 EVELVKEESYFFRMSKYADRLVE-YYNSHPEFIlPESRKNEMINNFIKpgLEDLAVSRTTFdWGIKVP---GNPKHVVYV 240
Cdd:TIGR00422 349 VVEPLLSKQWFVKVEKLADKALEaAEEGEIKFV-PKRMEKRYLNWLRN--IKDWCISRQLI-WGHRIPvwyCKECGEVYV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 241 -WIDALSNYITALGYNT--------------------------DNDTKFQKYWPADVQIVGKEIVRFHTIYWPIMLMALD 293
Cdd:TIGR00422 425 aKEEPLPDDKTNTGPSVeleqdtdvldtwfssslwpfstlgwpDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 294 LPLP-KMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDFvdRVNYDLANDLGNL 371
Cdd:TIGR00422 505 GQVPfKEVYIHGLVRDEQGrKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRV--ESARNFLNKLWNA 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 372 LNrtVAMINKYFNGEIPAYQGDVTPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQL----WSLISrtNKYIDETAPWAL 447
Cdd:TIGR00422 583 SR--FVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALyefiWNDFC--DWYIELVKYRLY 658
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2279656840 448 AKEEEKRAELASVMTHLAENLRIIAVLLQPFLTRtpgEIFLQLGLQEENL 497
Cdd:TIGR00422 659 NGNEAEKKAARDTLYYVLDKALRLLHPFMPFITE---EIWQHFKEGADSI 705
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
564-665 |
1.37e-28 |
|
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.
Pssm-ID: 239198 [Multi-domain] Cd Length: 105 Bit Score: 110.01 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 564 EDFDKVDLRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEGMILS 643
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|..
gi 2279656840 644 GEKDGKLSViEAsSDLPNGAKV 665
Cdd:cd02799 81 ASNADHEKV-EL-LEPPEGAKP 100
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
553-666 |
4.52e-28 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 120.34 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 553 VAALETPQIGIEDFDKVD----LRVAEVKQVEKVKKADKLLCFQLDLGEGkLRQVLSGIAEFYE----PENLIGKKVIVV 624
Cdd:COG0073 22 AEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGAPNVYAgdkvPEALVGAQVPGV 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2279656840 625 SNLKPVKLRGLMSEGMILSgEKDGKLS-----VIEASSDLPNGAKVK 666
Cdd:COG0073 101 VNLKPRKIRGVESEGMLCS-AEELGLGedhdgILELPEDAPPGDDAE 146
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
561-665 |
3.71e-26 |
|
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.
Pssm-ID: 239197 [Multi-domain] Cd Length: 107 Bit Score: 103.09 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 561 IGIEDFDKVDLRVAEVKQVEKVKKA-DKLLCFQLDLGEGKLRQVLSGIAEFYEPENLIGKKVIVVSNLKPVKLRGLMSEG 639
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*..
gi 2279656840 640 MILSGE-KDGKLSVIEASSDLPNGAKV 665
Cdd:cd02798 81 LVLGADdEGGEVVLLVPDREVPNGAKV 107
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
5-479 |
6.79e-22 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 100.65 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 5 EEKNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG----QKIQakaKERGISEQEY----- 75
Cdd:PRK13208 35 ERKPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGlpteRKVE---KYYGIRKDDIsreef 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 76 -------VDEIAEGFQELWKKLEISnTDFIRTTQDRHKTSVAKI---FEQLVEQGDIYLG-------------------- 125
Cdd:PRK13208 112 ielcrelTDEDEKKFRELWRRLGLS-VDWSLEYQTISPEYRRISqksFLDLYKKGLIYRAeapvlwcprcetaiaqaeve 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 126 --EYEGWY-----SVSDEEYFT-ET---QL------------EEVYK--------------------------------- 149
Cdd:PRK13208 191 yrEREGKLnyikfPVEDGEEIEiATtrpELlpacvavvvhpdDERYKhlvgktaivplfgvevpiladplvdpdfgtgav 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 150 -------------------------DESGKVIGGKAP--------------------------------------SGNEV 166
Cdd:PRK13208 271 mictfgdktdvtwwrelnlptriiiDEDGRMTEAAGKlagltieearkkivedlksggllgkqepikhnvkfcerCDTPL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 167 ELVKEESYFFRMSKYADRLVEYYNS---HPEFIlpesRKNemINNFIKpGLE-DLAVSRTTFdWGIKVP-------GNP- 234
Cdd:PRK13208 351 EILVTRQWFIKVLDLKEELLERGKEinwYPEHM----RVR--LENWIE-GLNwDWCISRQRY-FGTPIPvwyckdcGHPi 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 235 --------------------------------KHVVYVWID-ALSNYItALGYNTDNDtKFQKYWPADVQIVGKEIVR-- 279
Cdd:PRK13208 423 lpdeedlpvdptkdeppgykcpqcgspgfegeTDVMDTWATsSITPLI-VTGWERDED-LFEKVFPMDLRPQGHDIIRtw 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 280 -FHTIywpIMLMALDLPLP-KMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPfGSDGLFTPEDF 356
Cdd:PRK13208 501 lFYTI---LRAYLLTGKLPwKNIMISGMVLDPDGkKMSKSKGNVVTPEELLEKYGADAVRYWAASARL-GSDTPFDEKQV 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 357 vdRVNYDLANDLGNllnrtvamINKY---FNGEIPAYQGDVT-PFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQL---- 428
Cdd:PRK13208 577 --KIGRRLLTKLWN--------ASRFvlhFSADPEPDKAEVLePLDRWILAKLAKVVEKATEALENYDFAKALEEIesff 646
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2279656840 429 WSLIsrTNKYIDetapwaLAK-----EEEKRAELASVMThLAENLRIIAVLLQPFL 479
Cdd:PRK13208 647 WHVF--CDDYLE------LVKsraygEDEEEEQKSARYT-LYTVLDTLLRLLAPFL 693
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
559-665 |
2.24e-18 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 81.03 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 559 PQIGIEDFDKVDLRVAEVKQVEKVKKADKL-LCFQLDLGE--GKLRQVLSgIAEFYEPENLIGKKVIVVSNLKPVKLRGL 635
Cdd:PRK10089 2 ETITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEeiGVKQSSAQ-ITPHYTPEELIGKQVVAVVNFPPKQIAGF 80
|
90 100 110
....*....|....*....|....*....|.
gi 2279656840 636 MSEGMILSGE-KDGKLSVIEASSDLPNGAKV 665
Cdd:PRK10089 81 MSEVLVLGFEdEDGEVVLLTPDRPVPNGVKL 111
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
250-503 |
3.48e-15 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 79.65 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 250 TALGYNTDNDTkFQKYWPADVQIVGKEIVRFhtiyW--PIMLMAL----DLPLpKMVFGHGWILMKDG-KMSKSKGNVVD 322
Cdd:PRK14900 475 STMGWPEQTDT-LRTFYPTSVMETGHDIIFF----WvaRMMMMGLhfmgEVPF-RTVYLHPMVRDEKGqKMSKTKGNVID 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 323 PYMLIDRYGLDALRYYLLREVPFGSDGLFTpedfVDRV-NYD-LANDLGNLLNRTVAMINKYFNGEIPAYQGDVTPFDKT 400
Cdd:PRK14900 549 PLVITEQYGADALRFTLAALTAQGRDIKLA----KERIeGYRaFANKLWNASRFALMNLSGYQERGEDPARLARTPADRW 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 401 LVDFKNSVVLDYEKSMDHMQFSVALNQLWSLI--SRTNKYIdETAPWALAKE-EEKRAELASVMTHlaeNLRIIAVLLQP 477
Cdd:PRK14900 625 ILARLQRAVNETVEALEAFRFNDAANAVYAFVwhELCDWYI-ELAKEALASEdPEARRSVQAVLVH---CLQTSYRLLHP 700
|
250 260
....*....|....*....|....*.
gi 2279656840 478 FLTRTPGEIFLQLGLQEENLKKWDSI 503
Cdd:PRK14900 701 FMPFITEELWHVLRAQVGASAWADSV 726
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
257-495 |
1.13e-14 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 77.84 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 257 DNDTKFQKYWPADVQIVGKEIVRFhtiyWPI--MLMAL----DLPLpKMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDR 329
Cdd:PRK05729 463 EKTEDLKRFYPTSVLVTGFDIIFF----WVArmIMMGLhftgQVPF-KDVYIHGLVRDEQGrKMSKSKGNVIDPLDLIDK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 330 YGLDALRYYLLREVPFGSDGLFTPEdfvdRV----NYdlANDLGNlLNRTVAMinkyfNGEIPAYQGDVTPFDKTLVDfK 405
Cdd:PRK05729 538 YGADALRFTLAALASPGRDIRFDEE----RVegyrNF--ANKLWN-ASRFVLM-----NLEGADVGELPDPEELSLAD-R 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 406 ------NSVVLDYEKSMDHMQFSVALNQLWSLIsrTNKYID---ETAPWALAKEEEK--RAELASVmthLAENLRiiavL 474
Cdd:PRK05729 605 wilsrlNRTVAEVTEALDKYRFDEAARALYEFI--WNEFCDwylELAKPVLQEAAKRatRATLAYV---LEQILR----L 675
|
250 260
....*....|....*....|....
gi 2279656840 475 LQ---PFLTRtpgEIFLQLGLQEE 495
Cdd:PRK05729 676 LHpfmPFITE---ELWQKLAPLGI 696
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
240-340 |
1.32e-14 |
|
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: 77.07 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 240 VWIDALSNYITALGYNTDNDTKFQKYWPADVQIVGKEIVRFHtIYWPIML-MALDLPLP-KMVFGHGWILMKDG-KMSKS 316
Cdd:pfam00133 489 TWFSSGSWPFSTLGWPFVNTEEFKKFFPADMLLEGSDQTRGW-FYRMIMLsTALTGSVPfKNVLVHGLVRDEQGrKMSKS 567
|
90 100
....*....|....*....|....
gi 2279656840 317 KGNVVDPYMLIDRYGLDALRYYLL 340
Cdd:pfam00133 568 LGNVIDPLDVIDKYGADALRLWLA 591
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
12-180 |
4.31e-14 |
|
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: 69.82 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 12 ITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAEGFQELWkkle 91
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 92 isntdfirttqDRHKTSVAKIFEQLVEQGDIYLGEYEGWYSVSdeeyFTETQLEEVYkdesgkviGGKAPSGNEVELVKE 171
Cdd:cd00802 77 -----------EYMFLQAADFLLLYETECDIHLGGSDQLGHIE----LGLELLKKAG--------GPARPFGLTFGRVMG 133
|
....*....
gi 2279656840 172 EsYFFRMSK 180
Cdd:cd00802 134 A-DGTKMSK 141
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
300-478 |
4.65e-13 |
|
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: 72.78 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 300 VFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEdfvdRV----NYdlANDLGNLLnR 374
Cdd:COG0525 509 VYIHGLVRDEQGrKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIKFDEE----RVegyrNF--ANKLWNAS-R 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 375 TVAMinkyfNGEIPAYQGDVTPFDKTLVD------FkNSVVLDYEKSMDHMQFSVALNQLWSLIsrTNKYID---ETAPW 445
Cdd:COG0525 582 FVLM-----NLEGFDPGLDPDPEELSLADrwilsrL-NKTIAEVTEALEKYRFDEAAQALYDFV--WNEFCDwylELAKP 653
|
170 180 190
....*....|....*....|....*....|....*...
gi 2279656840 446 ALAKEEEK-----RAELASVmthLAENLRiiavLLQPF 478
Cdd:COG0525 654 RLYGGDEAakretRATLVYV---LEQILR----LLHPF 684
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
298-350 |
2.62e-12 |
|
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: 70.11 E-value: 2.62e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2279656840 298 KMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYLLR-----EVPFGSDGL 350
Cdd:COG0060 588 KNVLTHGFVLDEDGrKMSKSLGNVVDPQEVIDKYGADILRLWVASsdywgDLRFSDEIL 646
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
571-662 |
5.03e-11 |
|
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.
Pssm-ID: 239196 [Multi-domain] Cd Length: 103 Bit Score: 59.83 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 571 LRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGIAEFYEpenliGKKVIVVSN---------LKPVKLRGLMSEGMI 641
Cdd:cd02796 1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVRA-----GDKVVVALPgavlpgglkIKKRKLRGVESEGML 75
|
90 100
....*....|....*....|....*...
gi 2279656840 642 -------LSGEKDGklsVIEASSDLPNG 662
Cdd:cd02796 76 csakelgLGEDSDG---IIELPEDAPVG 100
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
4-210 |
1.07e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 64.84 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 4 PEEKNT----FYITTPIYYPSGKA-HIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERG----ISEQE 74
Cdd:PLN02563 102 PDDVDTskpkFYVLDMFPYPSGAGlHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGthpkITTLK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 75 YVDEIAE-----GFQELWKKlEISNTD--FIRTTQdrhktsvaKIFEQLVEQGDIYLGEYE-GWYSVsdeeyftetqLEE 146
Cdd:PLN02563 182 NIARFRSqlkslGFSYDWDR-EISTTEpeYYKWTQ--------WIFLQLLKRGLAYQAEVPvNWCPA----------LGT 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279656840 147 VYKDEsgKVIGGKAPSGNE-VELVKEESYFFRMSKYADRLVEYYNshpEFILPESRKnEMINNFI 210
Cdd:PLN02563 243 VLANE--EVVDGLSERGGHpVIRKPMRQWMLKITAYADRLLEDLD---DLDWPESIK-EMQRNWI 301
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
18-187 |
5.06e-10 |
|
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: 62.76 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 18 YPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTD------EhgqkiQAkAKERGISEQEYVDE-IA---EGFQEL- 86
Cdd:COG0495 43 YPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDafglpaE-----NA-AIKNGVHPAEWTYEnIAnmrRQLKRLg 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 87 ----WKKlEISNTD--FIRTTQdrhktsvaKIFEQLVEQGDIYLGEYEGWYSVSDeeyftETQL--EEvykdesgkVIGG 158
Cdd:COG0495 117 lsydWSR-EIATCDpeYYKWTQ--------WIFLQLYEKGLAYRKEAPVNWCPVD-----QTVLanEQ--------VIDG 174
|
170 180 190
....*....|....*....|....*....|
gi 2279656840 159 KA-PSGNEVELVKEESYFFRMSKYADRLVE 187
Cdd:COG0495 175 RCwRCGAPVEKKELPQWFLKITDYADELLD 204
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
2-340 |
1.45e-09 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 59.69 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 2 VLPEEKNTFYITTPIYYpsGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERGISEQEYVDEIAE 81
Cdd:pfam01406 4 PLHQGKVTMYVCGPTVY--DYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 82 GFQELWKKLEISNTDF-IRTTQdrHKTSVAKIFEQLVEQGDIYLGEyegwysvSDEEYFTETQLEEvYKDESGKVIGG-K 159
Cdd:pfam01406 82 AYTKDMDALNVLPPDLePRVTE--HIDEIIEFIERLIKKGYAYVSD-------NGDVYFDVSSFPD-YGKLSGQNLEQlE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 160 APSGNEVELVKEESYFF---RMSKYADrlveyynshPEFILPesrkneminnfikpgledlavsrttfdWGIKVPGnpkh 236
Cdd:pfam01406 152 AGARGEVSEGKRDPLDFalwKASKEGE---------PSWDSP---------------------------WGKGRPG---- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 237 vvyvW-ID--ALSNYItaLGYNTD-----NDTKFQKYwpadvqivGKEIVrfhtiywpiMLMAL-DLPLPKMVFGHGWIL 307
Cdd:pfam01406 192 ----WhIEcsAMARKY--LGDQIDihgggIDLAFPHH--------ENEIA---------QSEAAfDKQLANYWLHNGHVM 248
|
330 340 350
....*....|....*....|....*....|...
gi 2279656840 308 MKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLL 340
Cdd:pfam01406 249 IDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLL 281
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
299-478 |
3.46e-09 |
|
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: 60.06 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 299 MVFGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLrevpFGSDglftPED--------------FVDRVnYDL 364
Cdd:COG0495 576 EVGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEM----FAGP----PERdlewsdsgvegayrFLNRV-WRL 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 365 ANDLGNLLNRTVAminkyfngeipayqgDVTPFDKTLVDFKNSVVLDYEKSMDHMQFSVAlnqlwslISR----TNkyid 440
Cdd:COG0495 647 VVDEAEALKLDVA---------------DLSEADKELRRALHKTIKKVTEDIERLRFNTA-------IAAlmelVN---- 700
|
170 180 190
....*....|....*....|....*....|....*...
gi 2279656840 441 etapwALAKEEEKRAELASVMthlAENLRIIAVLLQPF 478
Cdd:COG0495 701 -----ALYKAKDSGEADRAVL---REALETLVLLLAPF 730
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
23-125 |
2.10e-08 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 54.89 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 23 AHIGHAYTTVAGDAMARYKRLKGYDVFY---LTGTDEhgqKIQAKAKERGISEQEYVDEIAEGFQELWKKLEISNTDFIr 99
Cdd:cd00672 34 AHIGHARTYVVFDVLRRYLEDLGYKVRYvqnITDIDD---KIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDVV- 109
|
90 100
....*....|....*....|....*.
gi 2279656840 100 tTQDRHKTSVAKIFEQLVEQGDIYLG 125
Cdd:cd00672 110 -PRVWHIECSAMAMKYLGETFDIHGG 134
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
7-123 |
5.05e-08 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 56.55 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 7 KNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG---QKIQAKA--KERGISEQEYVDE--I 79
Cdd:PTZ00419 59 GKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGiatQVVVEKKlmKEENKTRHDLGREefL 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2279656840 80 AEGFQelWKKLEISN-TDFIR-------------TTQDRHKTSVAKIFEQLVEQGDIY 123
Cdd:PTZ00419 139 KKVWE--WKDKHGNNiCNQLRrlgssldwsrevfTMDEQRSKAVKEAFVRLYEDGLIY 194
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
552-666 |
5.36e-08 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 56.33 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 552 EVAALETPQigiEDFDKVdlRVAEVKQVEKVKKADKL-LCfQLDLGEGKLrQVLSG---IAEfyepenliGKKVIV---- 623
Cdd:PRK00629 31 EVEGVEDVA---AGLSGV--VVGKVLECEKHPNADKLrVC-QVDVGEEPL-QIVCGapnVRA--------GDKVPValpg 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2279656840 624 -----VSNLKPVKLRGLMSEGMI-------LSGEKDGklsVIEASSDLPNGAKVK 666
Cdd:PRK00629 96 avlpgGFKIKKAKLRGVESEGMLcsaselgLSDDHDG---IIELPEDAPVGTDAR 147
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
254-340 |
6.21e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 56.27 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 254 YNTDNDTKFQKYWPADVQIVGKEIVR--FHTiywpimLMAL-----DLPLPKMVFGHGWILMKDG-KMSKSKGNVVDPYM 325
Cdd:PLN02882 554 YPFENKELFEKNFPADFVAEGLDQTRgwFYT------LMVLstalfDKPAFKNLICNGLVLAEDGkKMSKSLKNYPDPNE 627
|
90
....*....|....*
gi 2279656840 326 LIDRYGLDALRYYLL 340
Cdd:PLN02882 628 VIDKYGADALRLYLI 642
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
411-478 |
8.76e-08 |
|
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 437135 [Multi-domain] Cd Length: 152 Bit Score: 51.73 E-value: 8.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279656840 411 DYEKSMDHMQF---SVALNQLWSLisrTNKYIDETAPWALAKEEEkraELASVMTHLAENL-RIIAVLLQPF 478
Cdd:pfam19303 24 AYEGHMEAMEVrkaAAELRAIWVA---GNEYLQEAAPWTTFKTDP---EAAAAQVRLALNLiRLYAVLSAPF 89
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
23-90 |
9.02e-08 |
|
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: 55.11 E-value: 9.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279656840 23 AHIGHAYTTVAGDAMARYKRLKGYDVFY---LTGTDEhgqKIQAKAKERGISEQEYVDEIAEGFQELWKKL 90
Cdd:COG0215 36 AHIGHARTFVVFDVLRRYLRYLGYKVTYvrnITDVDD---KIIKRAAEEGESIWELAERYIAAFHEDMDAL 103
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
163-339 |
1.44e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 54.95 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 163 GNEVELVKEESYFFRMSKYADRLVEYYNSHPEFILPEsrKNEMINNFIKPGLEDLAVSRTTFdWGIKVPgnpkhvvyVWI 242
Cdd:PLN02943 399 GEVIEPLVSKQWFVTMEPLAEKALKAVENGELTIIPE--RFEKIYNHWLSNIKDWCISRQLW-WGHRIP--------VWY 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 243 ----DALSNYITA----------------------------------------LGYNTDNDTKFQKYWPADVQIVGKEIV 278
Cdd:PLN02943 468 ivgkDCEEDYIVArsaeealekarekygkdveiyqdpdvldtwfssalwpfstLGWPDVSAEDFKKFYPTTVLETGHDIL 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279656840 279 RFHTIYWPIMLMALDLPLP-KMVFGHGWILMKDG-KMSKSKGNVVDPYMLIDRYGLDALRYYL 339
Cdd:PLN02943 548 FFWVARMVMMGIEFTGTVPfSYVYLHGLIRDSQGrKMSKTLGNVIDPLDTIKEFGTDALRFTL 610
|
|
| pheT_bact |
TIGR00472 |
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ... |
562-666 |
4.20e-07 |
|
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273097 [Multi-domain] Cd Length: 797 Bit Score: 53.45 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 562 GIEDFDKVD--LRVAEVKQVEKVKKADKLLCFQLDLGEGKLRQVLSGiaefyEPENLIGKKVIVVSN---------LKPV 630
Cdd:TIGR00472 35 AVIPFSKPLkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG-----APNVEAGKKVAVALPgaklpnglkIKKS 109
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2279656840 631 KLRGLMSEGMI-------LSGEKDGklsVIEASSDLPNGAKVK 666
Cdd:TIGR00472 110 KLRGVESEGMLcseselgLDEKSDG---IIVLDEDAPLGTDIA 149
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
173-490 |
7.66e-07 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 52.66 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 173 SYFFRMSKYADRLVEyyNSHPEFILPESRKNEMINNFIKPGlEDLAVSRTTFdWGIKVP--------------------- 231
Cdd:PTZ00427 530 AWFIRVSNSTNELVK--NNETTYWIPAHIKEKKFHNWIKDA-KDWCISRNRY-WGTPIPiwadekmetvicvesikhlee 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 232 --------------------GNPK-----------HVVYVWIDALSNYITALGYNTDNDTK-FQKYWPADVQIVGKEIVR 279
Cdd:PTZ00427 606 lsgvknindlhrhfidhieiKNPKgktypklkripEVFDCWFESGSMPYAKVHYPFSTEKEdFHKIFPADFIAEGLDQTR 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 280 --FHTIYWPIMLMALDLPLpKMVFGHGWILMKDGK-MSKSKGNVVDPYMLIDRYGLDALRYYLLREVPFGSDGLFTPEDF 356
Cdd:PTZ00427 686 gwFYTLLVISTLLFDKAPF-KNLICNGLVLASDGKkMSKRLKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQEKG 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 357 VDRVNYDLANDLGNLLnrtvaminKYFNGEIPAYQgdVTPFDKTLVD----FKNSVVLD------YEKSMDHMQFSVALN 426
Cdd:PTZ00427 765 VNEVVKSFILPFYHSF--------RFFSQEVTRYE--CLNKKQFLFNtdyiYKNDNIMDqwifssVQSLTKSVHTEMKAY 834
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 427 QLWSLISRTNKYIDETAPWALAKEEEK-RAELASVMTHLAEN-----LRIIAVLLQPFLTRTPGEIFLQL 490
Cdd:PTZ00427 835 KLYNVLPKLLQFIENLTNWYIRLNRDRmRGSLGEENCLQSLCttyrtLHLFTVLMAPFTPFITEYIYQQL 904
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
18-136 |
1.28e-06 |
|
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: 51.62 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 18 YPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKA-KERGISEQEYVD-----------EIAEGFQE 85
Cdd:COG0060 56 YANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIKKKDIEKvgiaefrekcrEYALKYVD 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279656840 86 LWKKleisntDFIR------------TTQDRHKTSVAKIFEQLVEQGDIylgeYEG----WYSVSDE 136
Cdd:COG0060 136 EQRE------DFKRlgvwgdwdnpylTMDPEYEESIWWALKKLYEKGLL----YKGlkpvPWCPRCG 192
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
298-495 |
3.01e-06 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 50.54 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 298 KMVFGHGWILMKDG-KMSKSKGNVVDPYMLID---------RYGLDALRYYlLREVPFGSDGLFTPEdfVDRVNYDLAND 367
Cdd:PLN02843 596 KSVLTHGFVLDEKGfKMSKSLGNVVDPRLVIEggknqkqepAYGADVLRLW-VASVDYTGDVLIGPQ--ILKQMSDIYRK 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 368 LGNLLNRTVAMINKYFNGEIPAYQgDVTPFDKTLVDFKNSVVLDYEKSMDHMQFS--VALNQLWSLISRTNKYIDeTAPW 445
Cdd:PLN02843 673 LRGTLRYLLGNLHDWKPDNAVPYE-DLPSIDKYALFQLENVVNEIEESYDNYQFFkiFQILQRFTIVDLSNFYLD-VAKD 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2279656840 446 ALAKEEEKRAELASVMTHLAENLRIIAVLLQPFLTRTPGEIFLQLGLQEE 495
Cdd:PLN02843 751 RLYVGGTTSFTRRSCQTVLAAHLLSLLRAIAPILPHLAEDAWQNLPFQED 800
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
24-54 |
3.88e-06 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 50.25 E-value: 3.88e-06
10 20 30
....*....|....*....|....*....|....*.
gi 2279656840 24 HIGHAYTTVAGDAMARYKRLKGYDV-----FYLTGT 54
Cdd:PRK12300 2 HVGHGRTYTIGDVIARYKRMRGYNVlfpmaFHVTGT 37
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
7-123 |
8.90e-06 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 49.13 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 7 KNTFYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG---QKIQAK-------------AKERGI 70
Cdd:PLN02381 127 KPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGiatQVVVEKklmrerhltrhdiGREEFV 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2279656840 71 SE-----QEYVDEIAEGFQELWKKLEISNTDFirTTQDRHKTSVAKIFEQLVEQGDIY 123
Cdd:PLN02381 207 SEvwkwkDEYGGTILNQLRRLGASLDWSRECF--TMDEQRSKAVTEAFVRLYKEGLIY 262
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
303-341 |
1.32e-05 |
|
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: 48.17 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2279656840 303 HGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLR 341
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLS 294
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
252-335 |
1.33e-05 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 48.46 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 252 LGYNTDNDtKFQKYWPADVQIVGKEIVRFhtiyW--PIMLMALDL--PLP-KMVFGHGWILMKDG-KMSKSKGNVVDPYM 325
Cdd:PTZ00419 524 LGWPDQTD-DLQRFFPTSLLETGSDILFF----WvaRMVMMSLHLtdKLPfKTVFLHAMVRDSQGeKMSKSKGNVIDPLE 598
|
90
....*....|
gi 2279656840 326 LIDRYGLDAL 335
Cdd:PTZ00419 599 VIEGISLQDL 608
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
10-155 |
1.37e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 48.40 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 10 FYITTPIYYPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHG-------QKIQAKA--KERGISEQEYVDEIA 80
Cdd:PLN02943 90 FVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGiatqlvvEKMLASEgiKRTDLGRDEFTKRVW 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 81 EgfqelWKKL---EISNT--------DFIR---TTQDRHKTSVAKIFEQLVEQGDIYLGEYEGWYS------VSDeeyft 140
Cdd:PLN02943 170 E-----WKEKyggTITNQikrlgascDWSRerfTLDEQLSRAVVEAFVRLHEKGLIYQGSYMVNWSpnlqtaVSD----- 239
|
170
....*....|....*
gi 2279656840 141 etqLEEVYKDESGKV 155
Cdd:PLN02943 240 ---LEVEYSEEPGTL 251
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
18-68 |
1.78e-05 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 48.23 E-value: 1.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2279656840 18 YPSGKAHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAK------AKER 68
Cdd:PLN02843 42 YANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKvlqsldQEAR 98
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
296-478 |
2.92e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 47.56 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 296 LPKMVFGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALRYYLLrevpfGSDGLFTPEDFvdrvNYDLANDLGNLLNRT 375
Cdd:PRK12300 561 WPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT-----SSAELLQDADW----REKEVESVRRQLERF 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 376 VAMINKYFNGEIPAYQGDVtpfDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISrtnKYIDetapWALAKEEEKRA 455
Cdd:PRK12300 632 YELAKELIEIGGEEELRFI---DKWLLSRLNRIIKETTEAMESFQTRDAVQEAFYELL---NDLR----WYLRRVGEANN 701
|
170 180
....*....|....*....|...
gi 2279656840 456 ELasvmthLAENLRIIAVLLQPF 478
Cdd:PRK12300 702 KV------LREVLEIWIRLLAPF 718
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
260-425 |
5.42e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 46.60 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 260 TKFQKYWPADVQIVGKEIVRFH---TIYWPIMLMALDlPLPKMVFGHGWILMKDGKMSKSKGNVVDPYMLIDRYGLDALR 336
Cdd:PLN02959 664 QEFEYWYPFDLRVSGKDLIQNHltfAIYNHTAIWAEE-HWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATR 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 337 YYLlrevpfgSDGlftpEDFVDRVNY--DLANDLGNLLNRTVAMINKYFNGEIPAYQGDVTPF-DKTLVDFKNSVVLDYE 413
Cdd:PLN02959 743 FAL-------ADA----GDGVDDANFvfETANAAILRLTKEIAWMEEVLAAESSLRTGPPSTYaDRVFENEINIAIAETE 811
|
170
....*....|..
gi 2279656840 414 KSMDHMQFSVAL 425
Cdd:PLN02959 812 KNYEAMMFREAL 823
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
249-335 |
1.09e-04 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 45.66 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 249 ITALGYNTDNDtKFQKYWPADVQIVGKEIVRFHTIYWPIMLMAL--DLPLPKmVFGHGWILMKDG-KMSKSKGNVVDPYM 325
Cdd:PLN02381 591 LSVLGWPDDTD-DLKAFYPTSVLETGHDILFFWVARMVMMGMQLggDVPFRK-VYLHPMIRDAHGrKMSKSLGNVIDPLE 668
|
90
....*....|
gi 2279656840 326 LIDRYGLDAL 335
Cdd:PLN02381 669 VINGISLEGL 678
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
312-338 |
1.33e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 45.20 E-value: 1.33e-04
10 20
....*....|....*....|....*..
gi 2279656840 312 KMSKSKGNVVDPYMLIDRYGLDALRYY 338
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRLY 749
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
23-69 |
1.87e-03 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 41.46 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2279656840 23 AHIGHAYTTVAGDAMARYKRLKGYDVFYLTGTDEHGQKIQAKAKERG 69
Cdd:PLN02946 94 SHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELG 140
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
365-479 |
5.61e-03 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 37.10 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279656840 365 ANDLGNLLNRTVAMINKYFNGEIPAYQGDV-TPFDKTLVDFKNSVVLDYEKSMDHMQFSVALNQLWSLISRTNKYIDETA 443
Cdd:cd07375 7 ARAFLNRLYRLLSFFRKALGGTQPKWDNELlEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELNWYLDELK 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 2279656840 444 PWALAKEeekraELASVMTHLAENLRIIAVLLQPFL 479
Cdd:cd07375 87 PALQTEE-----LREAVLAVLRAALVVLTKLLAPFT 117
|
|
| |
