|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
1-659 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 1038.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 1 MEKirPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTE 80
Cdd:PRK12267 1 MMK--KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 81 IKRIWDLMNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQLVD-GKCPDCGRPVTPAKE 159
Cdd:PRK12267 79 FKELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVDgGKCPDCGREVELVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 160 EAYFFKMSKYAPRLIDYINTHPEFIQPVSRKNEMMNNFLLPGLQDLCVSRTSFTWGIPVSFDPKHVTYVWLDALTNYITG 239
Cdd:PRK12267 159 ESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPGLEDLSISRTSFDWGIPVPFDPKHVVYVWIDALLNYITA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 240 IGYDCDGNssEQFNKLWPADLHLIGKDIIRFHTIYWPIFLMALDLPLPKQVFGHPWLLQGDGKMSKSKGNVIYADDLVDL 319
Cdd:PRK12267 239 LGYGSDDD--ELFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 320 FGVDAVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRTISMSNKYFGGVVTKTGAAEEVDDDLKAVVTATKA 399
Cdd:PRK12267 317 YGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPAPGNVTEFDEELIALAEETLK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 400 KVAAKMEELRVADAMTEIFGLFKRCNKYIDETMPWALAKDEAKKDRLEEVLYNLVESITIGACLLESFMPETTEKILAQL 479
Cdd:PRK12267 397 NYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 480 N--AEKRSYEELDQFGLYVSGNKVTDqPQILFQRLDVKevmEKVEVIQAKQKAAMAAASQEEEKEeeavidlEPKEEITF 557
Cdd:PRK12267 477 GleEELTSWESLLEWGGLPAGTKVAK-GEPLFPRIDVE---EEIAYIKEQMEGSAPKEPEEKEKK-------PEKPEITI 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 558 EDFGKMQFQVGEIISCEPVKKSKKLLCFQVKVGS-QVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLC 636
Cdd:PRK12267 546 DDFDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEeEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILA 625
|
650 660
....*....|....*....|...
gi 1473291936 637 AEDaEGNVCLMTPEKAMPAGAEI 659
Cdd:PRK12267 626 AED-DGKLTLLTVDKEVPNGSKV 647
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
6-521 |
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: 753.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 6 PKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIW 85
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 86 DLMNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESqLVDGKCP----------------- 148
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDR-YVEGTCPkcgaedaygdqcencga 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 149 -------------DCGRPVTPAKEEAYFFKMSKYAPRLIDYINTHPEfIQPvSRKNEMMNnFLLPGLQDLCVSRTsFTWG 215
Cdd:COG0143 160 tleptelinprsaISGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQP-EVRNEVLS-WLKEGLQDLSISRD-FDWG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 216 IPVSFDPKHVTYVWLDALTNYITG-IGYDCDGNSSEQFNKLWPAD----LHLIGKDIIRFHTIYWPIFLMALDLPLPKQV 290
Cdd:COG0143 236 IPVPGDPGKVFYVWFDALIGYISAtKGYADDRGLPEDFEKYWPAPdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 291 FGHPWLLQGDGKMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRTISMSN 370
Cdd:COG0143 316 FAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 371 KYFGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCNKYIDETMPWALAKDEaKKDRLEEVL 450
Cdd:COG0143 396 KYFDGKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDE-DPERLATVL 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1473291936 451 YNLVESITIGACLLESFMPETTEKILAQLNAE--KRSYEELDQfgLYVSGNKVTdQPQILFQRLDVKEVMEKV 521
Cdd:COG0143 475 YTLLEALRILAILLKPFLPETAEKILEQLGLEgdELTWEDAGW--PLPAGHKIG-KPEPLFPRIEDEQIEALL 544
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
7-515 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 751.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 7 KYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWD 86
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 87 LMNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQLVDGK--CPDCGRPVTPAKEEAYFF 164
Cdd:PRK11893 82 ALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIEDGyrCPPTGAPVEWVEEESYFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 165 KMSKYAPRLIDYINTHPEFIQPVSRKNEMMNnFLLPGLQDLCVSRTSFTWGIPVSFDPKHVTYVWLDALTNYITGIGYDC 244
Cdd:PRK11893 162 RLSKYQDKLLELYEANPDFIQPASRRNEVIS-FVKSGLKDLSISRTNFDWGIPVPGDPKHVIYVWFDALTNYLTALGYPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 245 DGNSS-EQFNKLWPADLHLIGKDIIRFHTIYWPIFLMALDLPLPKQVFGHPWLLQGDGKMSKSKGNVIYADDLVDLFGVD 323
Cdd:PRK11893 241 DEELLaELFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 324 AVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRTISMSNKYFGGVVTKTGAAEEVDDDLKAVVTATKAKVAA 403
Cdd:PRK11893 321 AVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERVRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 404 KMEELRVADAMTEIFGLFKRCNKYIDETMPWALAKDeaKKDRLEEVLYNLVESITIGACLLESFMPETTEKILAQLNAEK 483
Cdd:PRK11893 401 AMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKT--DPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEE 478
|
490 500 510
....*....|....*....|....*....|....
gi 1473291936 484 RSYEELDQF--GLYVSGNKVTdQPQILFQRLDVK 515
Cdd:PRK11893 479 DENRDFAALswGRLAPGTTLP-KPEPIFPRLEEE 511
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
8-513 |
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: 588.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 8 YYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWDL 87
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 88 MNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQlVDGKCPDC----------------- 150
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRY-VEGTCPKCgsedargdhcevcgrhl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 151 -------------GRPVTPAKEEAYFFKMSKYAPRLIDYINTHPEFIQPVSRKNEMMNNFLLPGLQDLCVSRTSFTWGIP 217
Cdd:TIGR00398 160 eptelinprckicGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 218 VSFDPKHVTYVWLDALTNYITGIGYDcdGNSSEQFNKLWPAD-----LHLIGKDIIRFHTIYWPIFLMALDLPLPKQVFG 292
Cdd:TIGR00398 240 VPNDPNKVVYVWFDALIGYISSLGIL--SGDTEDWKKWWNNDedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 293 HPWLLQGDGKMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRTISMSNKY 372
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 373 FGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCNKYIDETMPWALAKDEakkDRLEEVLYN 452
Cdd:TIGR00398 398 FNGVLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQS---PRLKELLAV 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473291936 453 LVESITIGACLLESFMPETTEKILAQLNAEKrsyeELDQFGLYVSGNKVTDqPQILFQRLD 513
Cdd:TIGR00398 475 CSMLIRVLSILLYPIMPKLSEKILKFLNFEL----EWDFKLKLLEGHKLNK-AEPLFSKIE 530
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
7-659 |
1.38e-177 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 520.48 E-value: 1.38e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 7 KYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWD 86
Cdd:PRK00133 3 KILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 87 LMNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFftesqLVD----GKCP---------D---- 149
Cdd:PRK00133 83 GFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMF-----LPDrfvkGTCPkcgaedqygDncev 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 150 CGRPVTPA----------------KE-EAYFFKMSKYAPRLIDYInTHPEFIQPVSRKneMMNNFLLPGLQDLCVSRTSF 212
Cdd:PRK00133 158 CGATYSPTelinpksaisgatpvlKEsEHFFFKLPRFEEFLKEWI-TRSGELQPNVAN--KMKEWLEEGLQDWDISRDAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 213 TWGIPVSFDPKHVTYVWLDAltnyitGIGYD------CDGNSSEQFNKLWPAD-----LHLIGKDIIRFHTIYWPIFLMA 281
Cdd:PRK00133 235 YFGFEIPGAPGKVFYVWLDA------PIGYIsstknlCDKRGGLDWDEYWKKDsdtelYHFIGKDIIYFHTLFWPAMLEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 282 LDLPLPKQVFGHPWL-LQGDgKMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDGV-ITWELLVERMNSDLANTLG 359
Cdd:PRK00133 309 AGYRLPTNVFAHGFLtVEGA-KMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLdFNWEDFQQRVNSELVGKVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 360 NLVNRTISMSNKYFGGVVtktgAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCNKYIDETMPWALAKD 439
Cdd:PRK00133 388 NFASRTAGFINKRFDGKL----PDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 440 EAKkdRLEEVLYNLVESITIGACLLESFMPETTEKILAQLNAEKRSYEELDQFglyVSGNKVTDqPQILFQRLDVKEVME 519
Cdd:PRK00133 464 DGE--RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEELTWDDAQQP---LAGHPINK-FKILFTRIEDKQIEA 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 520 KVEVIQAKQKAAMAAASQEEEKeeeaviDLEP-KEEITFEDFGKMQFQVGEIISCEPVKKSKKLLCFQVKVGSQVRQIVS 598
Cdd:PRK00133 538 LIEASKEAAAAKAAAAAAAAPL------AEEPiAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFS 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473291936 599 GIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLCAEDAEGNVCLMTPEKAMPAGAEI 659
Cdd:PRK00133 612 GIKSAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGGDLFLLEPDEGAKPGMRV 672
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
7-339 |
1.74e-169 |
|
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: 486.65 E-value: 1.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 7 KYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWD 86
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 87 LMNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQlvdgkcpdcgrpvtpaKEEAYFFKM 166
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPEWR----------------EEEHYFFRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 167 SKYAPRLIDYINTHPEFIQPVSRKNEMMnNFLLPGLQDLCVSRTSFTWGIPVSFDPKHVTYVWLDALTNYITGIGYDCD- 245
Cdd:cd00814 145 SKFQDRLLEWLEKNPDFIWPENARNEVL-SWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDALIGYISATGYYNEe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 246 GNSSEQFNKLWPADLHLIGKDIIRFHTIYWPIFLMALDLPLPKQVFGHPWLLQGDGKMSKSKGNVIYADDLVDLFGVDAV 325
Cdd:cd00814 224 WGNSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADAL 303
|
330
....*....|....
gi 1473291936 326 RYFVLHEMPFENDG 339
Cdd:cd00814 304 RYYLLRERPEGKDS 317
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
8-365 |
2.02e-154 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 450.97 E-value: 2.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 8 YYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWDL 87
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 88 MNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQlVDGKCP-------------DCGRPV 154
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRY-VEGTCPhcgsedargdqceNCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 155 TPA-----------------KEEAYFFKMSKYAPRLIDYIN-THPEfiqPVSRKNEMMNNFLLPGLQDLCVSRTsFTWGI 216
Cdd:pfam09334 160 EPTelinpkcvicgttpevkETEHYFFDLSKFQDKLREWIEeNNPE---WPENVKNMVLEWLKEGLKDRAISRD-LDWGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 217 PVSFDPKHVTYVWLDALTNYITGIGYDCDGNssEQFNKLWPAD-----LHLIGKDIIRFHTIYWPIFLMALDLPLPKQVF 291
Cdd:pfam09334 236 PVPGAEGKVFYVWLDAPIGYISATKELSGNE--EKWKEWWPNDpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVF 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473291936 292 GHPWLLQGDGKMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRT 365
Cdd:pfam09334 314 AHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
8-522 |
9.99e-118 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 364.81 E-value: 9.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 8 YYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWDL 87
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 88 MNTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQLVDGK-CPDCGRPVTPAKEEAYFFKM 166
Cdd:PLN02224 151 LDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLENNcCPVHQMPCVARKEDNYFFAL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 167 SKYAPRLIDYINTHPEFIQPVSRKNEmMNNFLLPGLQDLCVSRTSFTWGIPVSFDPKHVTYVWLDALTNYITGIGYDCDG 246
Cdd:PLN02224 231 SKYQKPLEDILAQNPRFVQPSYRLNE-VQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWFDALLGYISALTEDNKQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 247 NSSEQFNKL-WPADLHLIGKDIIRFHTIYWPIFLMALDLPLPKQVFGHPWLLQGDGKMSKSKGNVIYADDLVDLFGVDAV 325
Cdd:PLN02224 310 QNLETAVSFgWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 326 RYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVNRTISMSNKYFGG--VVTKTGAAEEVddDLKAVVTATKAKVAA 403
Cdd:PLN02224 390 RYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKNCEStlVEDSTVAAEGV--PLKDTVEKLVEKAQT 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 404 KMEELRVADAMTEIFGLFKRCNKYIDETMPWALAK------DEAKKDrleevLYNLVESITIGACLLESFMPETTEKILA 477
Cdd:PLN02224 468 NYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKqggvsaEEAAKD-----LVIILEVMRVIAVALSPIAPCLSLRIYS 542
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1473291936 478 QLNAEKRSYEEL---DQFGLYVSGNKVTDQPQILFQRLDVKEVMEKVE 522
Cdd:PLN02224 543 QLGYSEDQFNSItwsDTKWGGLKGGQVMEQASPVFARIELNPEKEEDE 590
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
7-338 |
2.97e-81 |
|
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: 259.66 E-value: 2.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 7 KYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGI-------------TPKEF 73
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 74 VDNVSTEIKRIWDLMNTSYD--KFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGlyctpcesfftesqlvdgkcpdcg 151
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 152 rpvtpAKEEAYFFKMSKYAPRLIDYINTHPefIQPVSRKNEMMNnfLLPGLQDLCVSRTSFtWGIPVsfdPKHVTYVWLD 231
Cdd:cd00668 137 -----RITEQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEA--WLESLLDWAISRQRY-WGTPL---PEDVFDVWFD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 232 ALTNYITGIGYDCDgnsSEQFNKLWPADLHLIGKDIIRFHTIYWPIFLMALDLPLP-KQVFGHPWLLQGDG-KMSKSKGN 309
Cdd:cd00668 204 SGIGPLGSLGYPEE---KEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGEIPpKNLLVHGFVLDEGGqKMSKSKGN 280
|
330 340
....*....|....*....|....*....
gi 1473291936 310 VIYADDLVDLFGVDAVRYFVLHEMPFEND 338
Cdd:cd00668 281 VIDPSDVVEKYGADALRYYLTSLAPYGDD 309
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
10-659 |
1.66e-78 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 266.26 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 10 ITTAIAYTSGKPHIGNTYEIVL-ADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWDLM 88
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 89 NTSYDKFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTEsQLVDGKCPDCG----------------- 151
Cdd:PLN02610 101 DISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLAD-RLVEGTCPTEGcnydsargdqcekcgkl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 152 -------RP------VTPAKEEA--YFFKMSKYAPRLIDYINTHPefIQPVSRKN--EMMNNFLLPGLQDLCVSRtSFTW 214
Cdd:PLN02610 180 lnpteliDPkckvckNTPRIRDTdhLFLELPLLKDKLVEYINETS--VAGGWSQNaiQTTNAWLRDGLKPRCITR-DLKW 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 215 GIPV---SFDPKhVTYVWLDALTNYITgigydCDGNSSEQFNKLW--PADLHL---IGKDIIRFHTIYWPIFLMAL--DL 284
Cdd:PLN02610 257 GVPVpleKYKDK-VFYVWFDAPIGYVS-----ITACYTPEWEKWWknPENVELyqfMGKDNVPFHTVMFPSTLLGTgeNW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 285 PLPKQVFGHPWLLQGDGKMSKSKGNVIYADDLVDL-FGVDAVRYFVLHEMPFENDGVITWELLVERMNSDLANTLGNLVN 363
Cdd:PLN02610 331 TMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTnIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFIN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 364 RTISM----SNKYFGGVVTKTGAAE--EVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCNKYIDETMPWALA 437
Cdd:PLN02610 411 RVLSFiakpPGAGYGSVIPDAPGAEshPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWKLY 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 438 KDEakKDRLEEVLYNLVESITIGACLLESFMPETTEKILAQLNAEKRSYEELDQFG----------LYVSGNKVtDQPQI 507
Cdd:PLN02610 491 KED--KPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGevarakrpweLVPAGHKI-GTPEP 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 508 LFQRLDVKEV-------------------MEKVEVIQAKQKAAMAAASQEEEKEEEAVIDLEPKEEITFE-DFGKMQFQV 567
Cdd:PLN02610 568 LFKELKDEEVeayrekfagsqadraaraeAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREiDVSRLDIRV 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 568 GEIISCEPVKKSKKLLCFQVKVG-SQVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLCAEDAEGN-VC 645
Cdd:PLN02610 648 GLIVKAEKHPDADSLYVEEIDVGeGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTkVE 727
|
730
....*....|....
gi 1473291936 646 LMTPekamPAGAEI 659
Cdd:PLN02610 728 LVEP----PESAAV 737
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
351-479 |
3.79e-51 |
|
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: 173.06 E-value: 3.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 351 NSDLANTLGNLVNRTISMSNKYFGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCNKYIDE 430
Cdd:cd07957 2 NSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYIDE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1473291936 431 TMPWALAKDEaKKDRLEEVLYNLVESITIGACLLESFMPETTEKILAQL 479
Cdd:cd07957 82 TAPWKLAKEE-DPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
555-660 |
1.90e-43 |
|
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: 151.50 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 555 ITFEDFGKMQFQVGEIISCEPVKKSKKLLCFQVKVGSQVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGML 634
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMI 80
|
90 100
....*....|....*....|....*.
gi 1473291936 635 LCAEDaEGNVCLMTPEKAMPAGAEIC 660
Cdd:cd02800 81 LAAED-GGKLKLLTPDEEVEPGSRVS 105
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
6-328 |
6.12e-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: 150.86 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 6 PKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEE-AGITPK--------EFVDN 76
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKkLGIEGKtrhdlgreEFLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 77 V-------STEIKRIWDLMNTSYD--KFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESffTESQL-Vdgk 146
Cdd:cd00817 81 CwewkeesGGKIREQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRT--AISDIeV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 147 CPDCGRPVTPAKEEAYFFKMSKYAPRLID-----YINTHPEFiqpvsrkneMMNNFL--LPGLQDLCVSRTSFtWG--IP 217
Cdd:cd00817 156 CSRSGDVIEPLLKPQWFVKVKDLAKKALEavkegDIKFVPER---------MEKRYEnwLENIRDWCISRQLW-WGhrIP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 218 VSFDPKhVTYVWLD-----ALTNYITGIGYDCDGNSSEQ---------------------------FNKLWPADLHLIGK 265
Cdd:cd00817 226 AWYCKD-GGHWVVAreedeAIDKAAPEACVPCGGEELKQdedvldtwfssslwpfstlgwpeetkdLKKFYPTSLLVTGH 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473291936 266 DIIRFhtiyWpIFLMAL-------DLPLpKQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYF 328
Cdd:cd00817 305 DIIFF----W-VARMIMrglkltgKLPF-KEVYLHGLVRDEDGrKMSKSLGNVIDPLDVIDGYGADALRFT 369
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
548-660 |
4.05e-39 |
|
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: 140.64 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 548 DLEPKEEITFEDFGKMQFQVGEIISCEPVKKSKKLLCFQVKVGSQVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAG 627
Cdd:TIGR00399 25 LEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFG 104
|
90 100 110
....*....|....*....|....*....|...
gi 1473291936 628 MMSEGMLLCAEDAEGNVCLMTPEKAMPAGAEIC 660
Cdd:TIGR00399 105 VKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK 137
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-343 |
2.72e-38 |
|
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: 144.31 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 7 KYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWD 86
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 87 LMNTSYD--KFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCtpcesfftesqlvdgkcpdcgrpvtpAKEEAYFF 164
Cdd:cd00812 81 RMGFSYDwrREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWC--------------------------KLLDQWFL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 165 KMS--KYAPRLIDYINThPEFIQPVSRKneMMNNFllpglqdLCVSRTSFtWG--IPVSF------DPKHVTYVWLDAlt 234
Cdd:cd00812 135 KYSetEWKEKLLKDLEK-LDGWPEEVRA--MQENW-------IGCSRQRY-WGtpIPWTDtmeslsDSTWYYARYTDA-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 235 NYITGIGYDCDGNSSEQFNKLWPADLHLIGKDIIRFH---TIYWPIFLMALDLPL---PKQVFGHPWLLQGDGKMSKSKG 308
Cdd:cd00812 202 HNLEQPYEGDLEFDREEFEYWYPVDIYIGGKEHAPNHllySRFNHKALFDEGLVTdepPKGLIVQGMVLLEGEKMSKSKG 281
|
330 340 350
....*....|....*....|....*....|....*
gi 1473291936 309 NVIYADDLVDLFGVDAVRYFVLHEMPFENDgvITW 343
Cdd:cd00812 282 NVVTPDEAIKKYGADAARLYILFAAPPDAD--FDW 314
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
16-338 |
2.27e-36 |
|
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: 139.29 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 16 YTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEA-GITPKEFVDNVSTE-------------- 80
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElGISGKKDIEKMGIAefnakcrefalryv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 81 ------IKR--IWDLMNTSYdkfiRTTDADHEAQVQKIFKKLYDQGDIYKGY----YEGLYctpcesfftesqlvdgkcp 148
Cdd:cd00818 91 deqeeqFQRlgVWVDWENPY----KTMDPEYMESVWWVFKQLHEKGLLYRGYkvvpWPLIY------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 149 dcgRPVtpakeEAYFFKMSKYAPRLIDYINT---HPEFIQpvSRKNEMMNNfllpgLQDLCVSRTSFtWGIPV------S 219
Cdd:cd00818 148 ---RAT-----PQWFIRVTKIKDRLLEANDKvnwIPEWVK--NRFGNWLEN-----RRDWCISRQRY-WGTPIpvwyceD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 220 FDPKHVTY------VWLDALTNYITGIGYDcdgNSSEQFNKLWPADLHLIGKDIIR--FHTiywpifLMAL-----DLPL 286
Cdd:cd00818 212 CGEVLVRRvpdvldVWFDSGSMPYAQLHYP---FENEDFEELFPADFILEGSDQTRgwFYS------LLLLstalfGKAP 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1473291936 287 PKQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFEND 338
Cdd:cd00818 283 YKNVIVHGFVLDEDGrKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
565-659 |
1.20e-33 |
|
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: 123.78 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 565 FQVGEIISCEPVKKSKKLLCFQVKVGS-QVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLCAED---A 640
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEeKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEElglE 80
|
90
....*....|....*....
gi 1473291936 641 EGNVCLMTPEKAMPAGAEI 659
Cdd:cd02153 81 EGSVGILELPEDAPVGDRI 99
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
552-656 |
7.02e-30 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 125.74 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 552 KEEITFEDFGKMQ----FQVGEIISCEPVKKSKKLLCFQVKVGSQVRQIVSGIKAYY----KPEDTIGMKVMVLTNLKPA 623
Cdd:COG0073 27 MAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYagdkVPEALVGAQVPGVVNLKPR 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1473291936 624 KLAGMMSEGMLLCA------EDAEGnvcLMTPEKAMPAG 656
Cdd:COG0073 107 KIRGVESEGMLCSAeelglgEDHDG---ILELPEDAPPG 142
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
555-659 |
1.77e-28 |
|
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: 109.64 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 555 ITFEDFGKMQFQVGEIISCEP-VKKSKKLLCFQVKVGS-QVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEG 632
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEDfPEARKPAYKLKVDFGEiGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*..
gi 1473291936 633 MLLCAEDAEGNVCLMTPEKAMPAGAEI 659
Cdd:cd02798 81 LVLGADDEGGEVVLLVPDREVPNGAKV 107
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
552-660 |
5.83e-27 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 105.30 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 552 KEEITFEDFGKMQFQVGEIISCEPVKKSKKLlCFQVKV--GSQ--VRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAG 627
Cdd:PRK10089 1 METITYEDFEKVDIRVGTIVEAEPFPEARKP-AYKLWIdfGEEigVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAG 79
|
90 100 110
....*....|....*....|....*....|...
gi 1473291936 628 MMSEGMLLCAEDAEGNVCLMTPEKAMPAGAEIC 660
Cdd:PRK10089 80 FMSEVLVLGFEDEDGEVVLLTPDRPVPNGVKLV 112
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
567-657 |
3.13e-26 |
|
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: 102.71 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 567 VGEIISCEPVKKSKKLLCFQVKVGS-QVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLCAEDAEG-NV 644
Cdd:pfam01588 3 VGKVVEAERHPNADKLLVCKVDVGEeEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGgSV 82
|
90
....*....|...
gi 1473291936 645 CLMTPEKAMPAGA 657
Cdd:pfam01588 83 GLLEPPADVPPGT 95
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
6-480 |
4.88e-26 |
|
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: 114.00 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 6 PKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEE-AGITPKEFVDnVSTE--IK 82
Cdd:TIGR00422 33 PPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEKkLGAEGKTKHD-LGREefRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 83 RIWDLMNTSYDKFIRT-------TDADHEA---------QVQKIFKKLYDQGDIYKGYYEGLYCTPCES----------- 135
Cdd:TIGR00422 112 KIWEWKEESGGTIKNQikrlgasLDWSRERftmdeglskAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTaisdieveyke 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 136 -------------FFTESQLV----------------------------------------------------------- 143
Cdd:TIGR00422 192 vkgklyyiryplaNGSKDYLVvattrpetmfgdtavavhpederykhligkkvilpltgrkipiiadeyvdmefgtgavk 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 144 --------------------------DGK------------------------------------------CPDCGRPVT 155
Cdd:TIGR00422 272 vtpahdfndyewgkrhnlefinildeDGLlnenagkyqgltrfearkkivedlkeegllvkiephthnvgtCWRSGTVVE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 156 PAKEEAYFFKMSKYAPRLIDYI-NTHPEFIqPVSRKNEMMNnfLLPGLQDLCVSRTSFtWG--IPVSFDPKHVTYV--WL 230
Cdd:TIGR00422 352 PLLSKQWFVKVEKLADKALEAAeEGEIKFV-PKRMEKRYLN--WLRNIKDWCISRQLI-WGhrIPVWYCKECGEVYvaKE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 231 DALTNYITGIGYDCD------------------------GNSSEQFNKLWPADLHLIGKDIIRFHTIYWPIFLMALDLPL 286
Cdd:TIGR00422 428 EPLPDDKTNTGPSVEleqdtdvldtwfssslwpfstlgwPDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQV 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 287 P-KQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDGVITWELLveRMNSDLANTLGNlVNR 364
Cdd:TIGR00422 508 PfKEVYIHGLVRDEQGrKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRV--ESARNFLNKLWN-ASR 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 365 TISMSNKYFGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIF----GLFkrCNKYIDETMPWALAKDE 440
Cdd:TIGR00422 585 FVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYefiwNDF--CDWYIELVKYRLYNGNE 662
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1473291936 441 AKKDRLEEVLYNLVESITIgacLLESFMPETTEKILAQLN 480
Cdd:TIGR00422 663 AEKKAARDTLYYVLDKALR---LLHPFMPFITEEIWQHFK 699
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
558-659 |
6.32e-23 |
|
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: 93.83 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 558 EDFGKMQFQVGEIISCEPVKKSKKLLCFQVKVG-SQVRQIVSGIKAYYKPEDTIGMKVMVLTNLKPAKLAGMMSEGMLLC 636
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGeEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|....
gi 1473291936 637 AEDAE-GNVCLMTPekamPAGAEI 659
Cdd:cd02799 81 ASNADhEKVELLEP----PEGAKP 100
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
5-475 |
4.02e-19 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 91.79 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 5 RPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEA-GITP------------K 71
Cdd:PRK13208 37 KPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLPTERKVEKYyGIRKddisreefielcR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 72 EFVDNVSTEIKRIWDLMNTSYD--KFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCE--------------- 134
Cdd:PRK13208 117 ELTDEDEKKFRELWRRLGLSVDwsLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCEtaiaqaeveyrereg 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 135 -----SFFTES------------------------------QLV------------------------------------ 143
Cdd:PRK13208 197 klnyiKFPVEDgeeieiattrpellpacvavvvhpdderykHLVgktaivplfgvevpiladplvdpdfgtgavmictfg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 144 ---------------------DGK------------------------------------------CPDCGRPVTPAKEE 160
Cdd:PRK13208 277 dktdvtwwrelnlptriiideDGRmteaagklagltieearkkivedlksggllgkqepikhnvkfCERCDTPLEILVTR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 161 AYFFKMSKYAPRLIDY---INTHPEFIqpvsrKNEMMNnfLLPGLQ-DLCVSRTSFtWGIPVSF---------------- 220
Cdd:PRK13208 357 QWFIKVLDLKEELLERgkeINWYPEHM-----RVRLEN--WIEGLNwDWCISRQRY-FGTPIPVwyckdcghpilpdeed 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 221 ---DP---------------------KHVTYVWLD-ALT-NYITGIGYDcdgnsSEQFNKLWPADLHLIGKDIIR---FH 271
Cdd:PRK13208 429 lpvDPtkdeppgykcpqcgspgfegeTDVMDTWATsSITpLIVTGWERD-----EDLFEKVFPMDLRPQGHDIIRtwlFY 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 272 TIywpifL--MALDLPLP-KQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFEnDGVITWELLV 347
Cdd:PRK13208 504 TI-----LraYLLTGKLPwKNIMISGMVLDPDGkKMSKSKGNVVTPEELLEKYGADAVRYWAASARLGS-DTPFDEKQVK 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 348 ErmNSDLANTLGNlVNRTISMsnkyFGGVVTKTGAA--EEVD----DDLKAVV-TATKAkvaakMEELRVADAMTEIFGL 420
Cdd:PRK13208 578 I--GRRLLTKLWN-ASRFVLH----FSADPEPDKAEvlEPLDrwilAKLAKVVeKATEA-----LENYDFAKALEEIESF 645
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473291936 421 FKR--CNKYIDetmpwaLAKDEAKKDRLEE-------VLYNLVESITIgacLLESFMPETTEKI 475
Cdd:PRK13208 646 FWHvfCDDYLE------LVKSRAYGEDEEEeqksaryTLYTVLDTLLR---LLAPFLPFITEEV 700
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
5-179 |
4.69e-16 |
|
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: 82.02 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 5 RPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGqkieLKAEEA----GITPKEF-VDNVST 79
Cdd:COG0495 32 KPKYYVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFG----LPAENAaiknGVHPAEWtYENIAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 80 ---EIKRiwdlMNTSYD--KFIRTTDAD---HEaqvQKIFKKLYDQGDIYKGyyEGL--YCTPC------EsfftesQLV 143
Cdd:COG0495 108 mrrQLKR----LGLSYDwsREIATCDPEyykWT---QWIFLQLYEKGLAYRK--EAPvnWCPVDqtvlanE------QVI 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1473291936 144 DGKCPDCGRPVTPAKEEAYFFKMSKYAPRLIDYINT 179
Cdd:COG0495 173 DGRCWRCGAPVEKKELPQWFLKITDYADELLDDLDK 208
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
2-135 |
1.94e-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: 79.76 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 2 EKIRPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAE-EAGITPKEFVDNVSTE 80
Cdd:pfam00133 19 RKGKPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEkKLGIKEKKTRHKYGRE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1473291936 81 ----------------IKRIWDLMNTSYDkFIR---TTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCES 135
Cdd:pfam00133 99 efrekcrewkmeyadeIRKQFRRLGRSID-WDReyfTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNT 171
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
10-88 |
1.28e-12 |
|
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: 65.58 E-value: 1.28e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1473291936 10 ITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEFVDNVSTEIKRIWDLM 88
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEYM 79
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
16-135 |
1.59e-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: 70.88 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 16 YTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEA-GITPK-------------------EFVD 75
Cdd:COG0060 56 YANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVEKElGIKKKdiekvgiaefrekcreyalKYVD 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1473291936 76 NVSTEIKRI-----WDlmnTSYdkfiRTTDADHEAQVQKIFKKLYDQGDIYKGY---YeglYCTPCES 135
Cdd:COG0060 136 EQREDFKRLgvwgdWD---NPY----LTMDPEYEESIWWALKKLYEKGLLYKGLkpvP---WCPRCGT 193
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
5-174 |
7.80e-12 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 68.70 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 5 RPKYYITTAIAYTSGKP-HIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEAGITPKEF----VDNVST 79
Cdd:PLN02563 109 KPKFYVLDMFPYPSGAGlHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITtlknIARFRS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 80 EIKRiwdlMNTSYD--KFIRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCESFFTESQLVDGKCPDCGRPVTPA 157
Cdd:PLN02563 189 QLKS----LGFSYDwdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDGLSERGGHPVIRK 264
|
170
....*....|....*..
gi 1473291936 158 KEEAYFFKMSKYAPRLI 174
Cdd:PLN02563 265 PMRQWMLKITAYADRLL 281
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
19-125 |
7.98e-12 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 68.59 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 19 GKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHG---Q-KIELKAEEAGITPK-----EFVDNV-------STEIK 82
Cdd:PRK05729 49 GSLHMGHALNNTLQDILIRYKRMQGYNTLWLPGTDHAGiatQmVVERQLAAEGKSRHdlgreKFLEKVwewkeesGGTIT 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1473291936 83 RIWDLMNTSYD----KFirTTDAD-HEAqVQKIFKKLYDQGDIYKGYY 125
Cdd:PRK05729 129 NQLRRLGASCDwsreRF--TMDEGlSKA-VREVFVRLYEKGLIYRGKR 173
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
567-639 |
3.60e-10 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 63.27 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 567 VGEIISCEPVKKSKKL-LCfQVKVGSQVRQIVSG---IKAyykpedtiGMKVMV---------LTNLKPAKLAGMMSEGM 633
Cdd:PRK00629 47 VGKVLECEKHPNADKLrVC-QVDVGEEPLQIVCGapnVRA--------GDKVPValpgavlpgGFKIKKAKLRGVESEGM 117
|
....*.
gi 1473291936 634 lLCAED 639
Cdd:PRK00629 118 -LCSAS 122
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
291-450 |
5.24e-10 |
|
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: 62.04 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 291 FGHPW--------LLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYFVL--H---EMPFendgviTWELL------VERm 350
Cdd:COG0215 245 TGKPFarywmhngFLTVNGeKMSKSLGNFFTVRDLLKKYDPEVLRFFLLsaHyrsPLDF------SEEALeeaekaLER- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 351 nsdLANTLGNLVnrtismsnkyfggvvtktgAAEEVDDDLKAVVTATKAKVAAKMEE-LRVADAMTEIFGLFKRCNKYID 429
Cdd:COG0215 318 ---LYNALRRLE-------------------EALGAADSSAEEIEELREEFIAAMDDdFNTPEALAVLFELVREINKALD 375
|
170 180
....*....|....*....|..
gi 1473291936 430 ETMPWALAKDEAKK-DRLEEVL 450
Cdd:COG0215 376 EGEDKAALAALAALlRALGGVL 397
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
565-639 |
1.10e-09 |
|
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: 55.98 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 565 FQVGEIISCEPVKKSKKLLCFQVKVGS-QVRQIVSGikAyykPEDTIGMKVMV------LTN---LKPAKLAGMMSEGMl 634
Cdd:cd02796 1 VVVGKVLEVEPHPNADKLNVCKVDIGEnKPLQIVCG--A---PNVRAGDKVVValpgavLPGglkIKKRKLRGVESEGM- 74
|
....*
gi 1473291936 635 LCAED 639
Cdd:cd02796 75 LCSAK 79
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
145-490 |
1.57e-09 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 61.16 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 145 GKCPDCGRPVTPAKEEAYFFKMSKYAPRLIDYINTHPEFIQPVSRKNEMMNnfLLPGLQDLCVSRtSFTWG--IPVSFDP 222
Cdd:PRK14900 358 GRCQRSATILEPLLSDQWYVRIEPLARPAIEAVEQGRTRFIPEQWTNTYMA--WMRNIHDWCISR-QLWWGhqIPAWYCP 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 223 K-HVTY------------------------VWLDALTNYITGIGYDCDGNSSEQFnklWPADLHLIGKDIIRFhtiyWPI 277
Cdd:PRK14900 435 DgHVTVaretpeacstcgkaelrqdedvldTWFSSGLWPFSTMGWPEQTDTLRTF---YPTSVMETGHDIIFF----WVA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 278 FLMAL------DLPLpKQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRyFVLHEMPFENDGVitwELLVERM 350
Cdd:PRK14900 508 RMMMMglhfmgEVPF-RTVYLHPMVRDEKGqKMSKTKGNVIDPLVITEQYGADALR-FTLAALTAQGRDI---KLAKERI 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 351 NS--DLANTLGN-----LVNrtisMSNKYFGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLF-- 421
Cdd:PRK14900 583 EGyrAFANKLWNasrfaLMN----LSGYQERGEDPARLARTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFVwh 658
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1473291936 422 KRCNKYIDETMPWALAKDEAKKDRLEEVlynLVESITIGACLLESFMPETTEKILAQLNAEKRSYEELD 490
Cdd:PRK14900 659 ELCDWYIELAKEALASEDPEARRSVQAV---LVHCLQTSYRLLHPFMPFITEELWHVLRAQVGASAWAD 724
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
19-125 |
1.12e-08 |
|
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: 58.52 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 19 GKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHG---Q-KIE--LKAEeaGITPK-----EFvdnvsteIKRIWD- 86
Cdd:COG0525 48 GSLHMGHALNNTLQDILIRYKRMQGYNTLWQPGTDHAGiatQaVVErqLAEE--GKSRHdlgreKF-------LERVWEw 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1473291936 87 -------------LMNTSYD----KFirTTDAD-HEAqVQKIFKKLYDQGDIYKGYY 125
Cdd:COG0525 119 keesggtitnqlrRLGASCDwsreRF--TMDEGlSKA-VREVFVRLYEKGLIYRGKR 172
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
253-361 |
1.29e-08 |
|
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: 58.17 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 253 NKLWPADLHLIGKDIIR--FHTiywpifLMAL-----DLPlP-KQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFGVD 323
Cdd:COG0060 552 ELHFPADFYLEGSDQTRgwFYS------SLLTstalfGRA-PyKNVLTHGFVLDEDGrKMSKSLGNVVDPQEVIDKYGAD 624
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1473291936 324 AVRYFVLHEmPFENDGVITWELLVERmnSD----LANT----LGNL 361
Cdd:COG0060 625 ILRLWVASS-DYWGDLRFSDEILKEV--RDvyrrLRNTyrflLANL 667
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
16-123 |
1.30e-08 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 58.24 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 16 YTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKA-------EEAGITP-----------KEFVDNV 77
Cdd:PLN02843 42 YANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVlqsldqeARKELTPiklrakaakfaKKTVDTQ 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1473291936 78 STEIKR--IWDLMNTSYdkfiRTTDADHEAQVQKIFKKLYDQGDIYKG 123
Cdd:PLN02843 122 RESFKRygVWGDWENPY----LTLDPEYEAAQIEVFGQMFLNGYIYRG 165
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
250-482 |
2.29e-08 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 57.57 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 250 EQFNKLWPADLHLIGKDIIRFH-TIYwpIFLMALDLP---LPKQ--VFGhpWLLQGDGKMSKSKGNVIYADDLVDLFGVD 323
Cdd:PRK12300 523 EEFLYWYPVDWRHSGKDLIPNHlTFF--IFNHVAIFPeekWPRGivVNG--FVLLEGKKMSKSKGNVIPLRKAIEEYGAD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 324 AVRYFVLH--EMPFENDgvitWellvermNSDLANTLGNLVNRTISMSNKyfggVVTKTGAAEEVDDDL-------KAVV 394
Cdd:PRK12300 599 VVRLYLTSsaELLQDAD----W-------REKEVESVRRQLERFYELAKE----LIEIGGEEELRFIDKwllsrlnRIIK 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 395 TATKAkvaakMEELRVADAMTEIFGLFKrcnKYIDetmpWALAK-DEAKKDRLEEVLYNLVEsitigacLLESFMPETTE 473
Cdd:PRK12300 664 ETTEA-----MESFQTRDAVQEAFYELL---NDLR----WYLRRvGEANNKVLREVLEIWIR-------LLAPFTPHLAE 724
|
....*....
gi 1473291936 474 KILAQLNAE 482
Cdd:PRK12300 725 ELWHKLGGE 733
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
298-479 |
2.73e-07 |
|
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: 53.90 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 298 QGDGKMSKSKGNVIYADDLVDLFGVDAVRYFVLHEMPFENDgvITWellvermnsdlaNTLG-----NLVNRTISMSNKY 372
Cdd:COG0495 585 GGIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPPERD--LEW------------SDSGvegayRFLNRVWRLVVDE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 373 FGGVVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRvadamteiFglfkrcNKYIDETMPW--ALAKDEAKKDRLEEVL 450
Cdd:COG0495 651 AEALKLDVADLSEADKELRRALHKTIKKVTEDIERLR--------F------NTAIAALMELvnALYKAKDSGEADRAVL 716
|
170 180
....*....|....*....|....*....
gi 1473291936 451 YNLVESITIgacLLESFMPETTEKILAQL 479
Cdd:COG0495 717 REALETLVL---LLAPFAPHIAEELWERL 742
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
21-134 |
4.87e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 52.95 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 21 PHIGNTYEIVLADSIARFKRQQGYDVFF-----QTGT------------DEhgQKIELKAEEAGI---------TPKEFV 74
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFpmafhVTGTpilgiaeriargDP--ETIELYKSLYGIpeeelekfkDPEYIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1473291936 75 DNVSTEIKRIWDLMNTSYD---KFiRTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPCE 134
Cdd:PRK12300 79 EYFSEEAKEDMKRIGYSIDwrrEF-TTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDN 140
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
302-409 |
2.01e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 51.36 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 302 KMSKSKGNVIYADDLVDLFGVDAVRyfvLHEM---PFENdgVITWELL-VERMNSDLANTLgnlvnRTISMSNKYFGGVV 377
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLR---LYEMfmgPLRD--SKTWSTSgVEGVHRFLGRTW-----RLVVGAPLPDGSFR 792
|
90 100 110
....*....|....*....|....*....|...
gi 1473291936 378 TKTGAA-EEVDDDLKAVVTATKAKVAAKMEELR 409
Cdd:PLN02563 793 DGTVVTdEEPSLEQLRLLHKCIAKVTEEIESTR 825
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
302-328 |
1.34e-05 |
|
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: 48.51 E-value: 1.34e-05
10 20
....*....|....*....|....*....
gi 1473291936 302 KMSKSKGNVIyaD--DLVDLFGVDAVRYF 328
Cdd:COG0525 522 KMSKSKGNVI--DplDLIDKYGADALRFT 548
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
348-468 |
7.83e-05 |
|
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: 42.49 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 348 ERMNSDLAntLGNLVNRTISMSNKYFGG--VVTKTGAAEEVDDDLKAVVTATKAKVAAKMEELRVADAMTEIFGLFKRCN 425
Cdd:cd07375 2 ERLKQARA--FLNRLYRLLSFFRKALGGtqPKWDNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1473291936 426 KYIDETMPWALAKDEAkkdrlEEVLYNLVESITIGACLLESFM 468
Cdd:cd07375 80 WYLDELKPALQTEELR-----EAVLAVLRAALVVLTKLLAPFT 117
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
19-122 |
2.27e-04 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 44.61 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 19 GKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHG-------QKIELKAEeaGITP-----KEFV-----------D 75
Cdd:PTZ00419 73 GYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGiatqvvvEKKLMKEE--NKTRhdlgrEEFLkkvwewkdkhgN 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1473291936 76 NVSTEIKRIWDLMNTSYDKFirTTDADHEAQVQKIFKKLYDQGDIYK 122
Cdd:PTZ00419 151 NICNQLRRLGSSLDWSREVF--TMDEQRSKAVKEAFVRLYEDGLIYR 195
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
18-125 |
3.09e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 44.16 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 18 SGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEE---------AGITPKEFVDNV----------- 77
Cdd:PLN02943 100 TGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQLVVEKmlasegikrTDLGRDEFTKRVwewkekyggti 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1473291936 78 STEIKRIWDLMNTSYDKFirTTDADHEAQVQKIFKKLYDQGDIYKGYY 125
Cdd:PLN02943 180 TNQIKRLGASCDWSRERF--TLDEQLSRAVVEAFVRLHEKGLIYQGSY 225
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
251-327 |
5.78e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 251 QFNKLWPADLHLIGKDIIRFH---TIYWPIFLMALDlPLPKQVF--GHpwLLQGDGKMSKSKGNVIYADDLVDLFGVDAV 325
Cdd:PLN02959 665 EFEYWYPFDLRVSGKDLIQNHltfAIYNHTAIWAEE-HWPRGFRcnGH--LMLNSEKMSKSTGNFLTLRQAIEEFSADAT 741
|
..
gi 1473291936 326 RY 327
Cdd:PLN02959 742 RF 743
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
21-89 |
9.77e-04 |
|
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: 41.03 E-value: 9.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 21 PHIGNTYEIVLADSIARFKRQQGYDVFF-QTGTDEhGQKIELKAEEAGITPKEFVDNVSTEIKRIWDLMN 89
Cdd:cd00672 34 AHIGHARTYVVFDVLRRYLEDLGYKVRYvQNITDI-DDKIIKRAREEGLSWKEVADYYTKEFFEDMKALN 102
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
247-311 |
1.73e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 41.53 E-value: 1.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473291936 247 NSSEQFNKLWPADLHLIGKDIIRFhtiyW--PIFLMALDL--PLP-KQVFGHPWLLQGDG-KMSKSKGNVI 311
Cdd:PTZ00419 528 DQTDDLQRFFPTSLLETGSDILFF----WvaRMVMMSLHLtdKLPfKTVFLHAMVRDSQGeKMSKSKGNVI 594
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
248-348 |
2.10e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 41.46 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 248 SSEQFNKLWPADLHLIGKDIIRFhtiyW--PIFLMALDL--PLP-KQVFGHPWLLQGDG-KMSKSKGNVIYADDLVDLFG 321
Cdd:PLN02943 527 SAEDFKKFYPTTVLETGHDILFF----WvaRMVMMGIEFtgTVPfSYVYLHGLIRDSQGrKMSKTLGNVIDPLDTIKEFG 602
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 322 VDAVRY---------------------------------FVLHEMPFENDgVITWELLVE 348
Cdd:PLN02943 603 TDALRFtlalgtagqdlnlsterltsnkaftnklwnagkFVLQNLPSQSD-TSAWEHILA 661
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
290-330 |
2.93e-03 |
|
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: 39.48 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1473291936 290 VFGHPW--------LLQGDG-KMSKSKGNVIYADDLVDLFGVDAVRYFVL 330
Cdd:cd00672 153 ATGKPFarywlhtgHLTIDGeKMSKSLGNFITVRDALKKYDPEVLRLALL 202
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
397-475 |
3.08e-03 |
|
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 400523 [Multi-domain] Cd Length: 141 Bit Score: 38.54 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 397 TKAKVAAKMEELRVADAMTEIFGLF--KRCNKYIDETMPWAlaKDEAKKDRLEEVLYNLVESITIgacLLESFMPETTEK 474
Cdd:pfam08264 11 LIKEVTEAYENYRFNTAAQALYEFFwnDLSDWYLELIKDRL--YGEEPDSRAQTTLYEVLETLLR---LLAPFMPFITEE 85
|
.
gi 1473291936 475 I 475
Cdd:pfam08264 86 L 86
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
5-124 |
3.71e-03 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 40.65 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 5 RPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAE-----EAGIT-----PKEFV 74
Cdd:PLN02381 127 KPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEkklmrERHLTrhdigREEFV 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473291936 75 D-----------NVSTEIKRIWDLMNTSYDKFirTTDADHEAQVQKIFKKLYDQGDIYKGY 124
Cdd:PLN02381 207 SevwkwkdeyggTILNQLRRLGASLDWSRECF--TMDEQRSKAVTEAFVRLYKEGLIYRDI 265
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
288-328 |
6.54e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 39.41 E-value: 6.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1473291936 288 KQVFGHP--------W-LLQGDGKMSKSKGNVIYADDLVDLFGVDAVRYF 328
Cdd:PRK00750 257 REILGGEppepfvyeLfLDKKGEKISKSKGNVITIEDWLEYAPPESLRLF 306
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
288-328 |
6.81e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 39.23 E-value: 6.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1473291936 288 KQVFGHP--------W-LLQGDGKMSKSKGNVIYADDLVDLFGVDAVRYF 328
Cdd:cd00674 252 REIFGGEppvpvmyeFiGLKGGGKMSSSKGNVITPSDWLEVAPPEVLRYL 301
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
299-330 |
8.25e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 39.37 E-value: 8.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1473291936 299 GDG-KMSKSKGNVIYADDLVD-----------------LFGVDAVRYFVL 330
Cdd:PRK01611 318 GEGvKMSTRAGNVVTLDDLLDeavgrarelieekeiaeAVGIDAVRYFDL 367
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
5-133 |
9.13e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 39.32 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473291936 5 RPKYYITTAIAYTSGKPHIGNTYEIVLADSIARFKRQQGYDVFFQTGTDEHGQKIELKAEEA-GITPKEFV-----DNVS 78
Cdd:PLN02882 37 LPEYIFYDGPPFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIDKKlGIKRRDDVlkmgiDKYN 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1473291936 79 TEIKRI-------WDLMNTSYDKFI------RTTDADHEAQVQKIFKKLYDQGDIYKGYYEGLYCTPC 133
Cdd:PLN02882 117 EECRSIvtryskeWEKTVTRTGRWIdfendyKTMDPKFMESVWWVFKQLFEKGLVYKGFKVMPYSTAC 184
|
|
| |
