|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
1-536 |
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: 682.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 1 MSIFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCF 80
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 81 RSLGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVEGICPHC-YEAARGDQCDACSAI 159
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCgAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 160 LDPLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKGVVEiakQKGTWRDNAIQLTERYVKEGLQDRAVSRDLPVGIP 239
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIE---ENPDIQPEVRNEVLSWLKEGLQDLSISRDFDWGIP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 240 IPvaGYEDKKIYVWIEAVTGYYSASKHWAEKTGKDD--QEFW-DKETKTYYVHGKDNIPFHSIIWPAVLLGVGEEaIPRH 316
Cdd:COG0143 238 VP--GDPGKVFYVWFDALIGYISATKGYADDRGLPEdfEKYWpAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLP-LPKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 317 IVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNRTLKFI 396
Cdd:COG0143 315 VFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 397 EKYYDGVVPKGT----IHVELKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKQR-EDDPVSCEETV 471
Cdd:COG0143 395 HKYFDGKVPEPGelteADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAkDEDPERLATVL 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 472 YNCVYLIANFANLLEPFLPFSSERVRNTLSI--VKRNWEPQNTLP---NKIDSVQPLFERIDVKQIEHEI 536
Cdd:COG0143 475 YTLLEALRILAILLKPFLPETAEKILEQLGLegDELTWEDAGWPLpagHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
3-542 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 640.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRS 82
Cdd:PRK00133 4 ILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 83 LGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVEGICPHC-YEAARGDQCDACSAILD 161
Cdd:PRK00133 84 FGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCgAEDQYGDNCEVCGATYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 162 PLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKGVVEiakQKGTWRDNAIQLTERYVKEGLQDRAVSRDLP-VGIPI 240
Cdd:PRK00133 164 PTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWIT---RSGELQPNVANKMKEWLEEGLQDWDISRDAPyFGFEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 241 PvaGYEDKKIYVWIEAVTGYYSASKHWAEKTGKDD-QEFWDKETKTYYVH--GKDNIPFHSIIWPAVLLGvGEEAIPRHI 317
Cdd:PRK00133 241 P--GAPGKVFYVWLDAPIGYISSTKNLCDKRGGLDwDEYWKKDSDTELYHfiGKDIIYFHTLFWPAMLEG-AGYRLPTNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 318 VSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPEN-RDTDFSWREFIYSHNSELLGAYGNFVNRTLKFI 396
Cdd:PRK00133 318 FAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 397 EKYYDGVVPKGTIHVELKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKQREDDPVSCEETVYNCVY 476
Cdd:PRK00133 398 NKRFDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERLQAVCSVGLN 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207602735 477 LIANFANLLEPFLPFSSERVRNTLSIVKRNWEPQNTLP--NKIDSVQPLFERIDVKQIEHEIEKLYGA 542
Cdd:PRK00133 478 LFRALAIYLKPVLPELAERAEAFLNLEELTWDDAQQPLagHPINKFKILFTRIEDKQIEALIEASKEA 545
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
3-528 |
2.41e-177 |
|
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: 510.38 E-value: 2.41e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRS 82
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 83 LGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVEGICPHC-YEAARGDQCDACSAILD 161
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCgSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 162 PLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKGVVEIAKQKGTWRDNAIQLTERYVKEGLQDRAVSRDLPV-GIPI 240
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVYwGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 241 PvaGYEDKKIYVWIEAVTGYYSASkhwAEKTG--KDDQEFW--DKETKTYYVHGKDNIPFHSIIWPAVLLGVGeEAIPRH 316
Cdd:TIGR00398 241 P--NDPNKVVYVWFDALIGYISSL---GILSGdtEDWKKWWnnDEDAELIHFIGKDIVRFHTIYWPAMLMGLG-LPLPTQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 317 IVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNRTLKFI 396
Cdd:TIGR00398 315 VFSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 397 EKYYDGVVPKGTIHVE----LKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKqREDDPVSCEETVY 472
Cdd:TIGR00398 395 KKYFNGVLPSEDITDEedkkLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWE-LFKQSPRLKELLA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207602735 473 NCVYLIANFANLLEPFLPFSSERVRNTLSIVKRNWEPQNTLPN-KIDSVQPLFERID 528
Cdd:TIGR00398 474 VCSMLIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGhKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
3-392 |
1.16e-176 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 503.36 E-value: 1.16e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRS 82
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 83 LGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVEGICPHC-YEAARGDQCDACSAILD 161
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCgSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 162 PLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKGVVEiaKQKGTWRDNAIQLTERYVKEGLQDRAVSRDLPVGIPIP 241
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIE--ENNPEWPENVKNMVLEWLKEGLKDRAISRDLDWGIPVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 242 vaGYEDKKIYVWIEAVTGYYSASKHWAEkTGKDDQEFWDKETKTYYVH--GKDNIPFHSIIWPAVLLGVGEEaIPRHIVS 319
Cdd:pfam09334 239 --GAEGKVFYVWLDAPIGYISATKELSG-NEEKWKEWWPNDPDTELVHfiGKDIIYFHTIFWPAMLLGAGYR-LPTTVFA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207602735 320 NEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNRT 392
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
3-368 |
2.76e-137 |
|
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: 400.37 E-value: 2.76e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRS 82
Cdd:cd00814 2 VLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 83 LGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPdryvegicphcyeaargdqcdacsaildp 162
Cdd:cd00814 82 LNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP----------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 163 ldllekkcklcgstpSVQETEHFYFALHTFQEQIKGVVEiAKQKGTWRDNAIQLTERYVKEGLQDRAVSRDLPV-GIPIP 241
Cdd:cd00814 133 ---------------EWREEEHYFFRLSKFQDRLLEWLE-KNPDFIWPENARNEVLSWLKEGLKDLSITRDLFDwGIPVP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 242 vaGYEDKKIYVWIEAVTGYYSASKHWAEKTGKDDqEFWDKETKTYYVHGKDNIPFHSIIWPAVLLGVGEEaIPRHIVSNE 321
Cdd:cd00814 197 --LDPGKVIYVWFDALIGYISATGYYNEEWGNSW-WWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLP-LPTRIVAHG 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1207602735 322 YLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDF 368
Cdd:cd00814 273 YLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
3-541 |
1.51e-133 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 407.24 E-value: 1.51e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAWPYANGSLHLGHI-ASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFR 81
Cdd:PLN02610 19 ILITSALPYVNNVPHLGNIiGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 82 SLGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVEGICPHC---YEAARGDQCDACSA 158
Cdd:PLN02610 99 WFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTEgcnYDSARGDQCEKCGK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 159 ILDPLDLLEKKCKLCGSTPSVQETEHFYFALHTFQEQIKGVVEIAKQKGTWRDNAIQLTERYVKEGLQDRAVSRDLPVGI 238
Cdd:PLN02610 179 LLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGWSQNAIQTTNAWLRDGLKPRCITRDLKWGV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 239 PIPVAGYEDKKIYVWIEAVTGYYSASKHWAEktgkdDQEFWDKETKT---YYVHGKDNIPFHSIIWPAVLLGVGEE-AIP 314
Cdd:PLN02610 259 PVPLEKYKDKVFYVWFDAPIGYVSITACYTP-----EWEKWWKNPENvelYQFMGKDNVPFHTVMFPSTLLGTGENwTMM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 315 RHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSI-RYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNRTL 393
Cdd:PLN02610 334 KTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVwRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFINRVL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 394 KFIEK----YYDGVVPKGT------IHVELKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKQREDD 463
Cdd:PLN02610 414 SFIAKppgaGYGSVIPDAPgaeshpLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWKLYKED 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 464 PVSCEETVYNCVYLIANFANLLEPFLP-FSSERVR------NTLSIVKRNWE------PQNTLP--NKIDSVQPLFERID 528
Cdd:PLN02610 494 KPSCAIVVKTSVGLVYLLACLLEPFMPsFSKEVLKqlnlppESLSLSDEKGEvarakrPWELVPagHKIGTPEPLFKELK 573
|
570
....*....|...
gi 1207602735 529 VKQIEHEIEKLYG 541
Cdd:PLN02610 574 DEEVEAYREKFAG 586
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
10-530 |
2.86e-114 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 348.41 E-value: 2.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRSLGFTYDC 89
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 90 YTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRyvegicphcyeaargdqcdacsaildplDLLEKK 169
Cdd:PRK11893 90 FIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTES----------------------------ELIEDG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 170 --CKLCGSTPSVQETEHFYFALHTFQEQIKGVVEiakqkgtWRDNAIQLTERY------VKEGLQDRAVSRdLPV--GIP 239
Cdd:PRK11893 142 yrCPPTGAPVEWVEEESYFFRLSKYQDKLLELYE-------ANPDFIQPASRRnevisfVKSGLKDLSISR-TNFdwGIP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 240 IPvaGYEDKKIYVWIEAVTGYYSAskhwaekTGKDDQE---------FWDKEtktyyVH--GKDNIPFHSIIWPAVLLGV 308
Cdd:PRK11893 214 VP--GDPKHVIYVWFDALTNYLTA-------LGYPDDEellaelfnkYWPAD-----VHliGKDILRFHAVYWPAFLMAA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 309 GEEaIPRHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNF 388
Cdd:PRK11893 280 GLP-LPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 389 VNRTLKFIEKYYDGVVPKGTIHVE----LKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKQREDDP 464
Cdd:PRK11893 359 AQRTLSMIAKNFDGKVPEPGALTEadeaLLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDP 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207602735 465 VSCEETVYNCVYLIANFANLLEPFLP-----------FSSERVRNTLSIVKRNWEPQNTLPNKidsvQPLFERIDVK 530
Cdd:PRK11893 439 ERLATVLYTLLEVLRGIAVLLQPVMPelaakildqlgVEEDENRDFAALSWGRLAPGTTLPKP----EPIFPRLEEE 511
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
11-539 |
2.51e-87 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 282.46 E-value: 2.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 11 YANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRSLGFTYDCY 90
Cdd:PRK12267 14 YPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDISYDKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 91 TRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVE--GICPHCyeaargdqcdacsaiLDPLDLlek 168
Cdd:PRK12267 94 IRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVdgGKCPDC---------------GREVEL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 169 kcklcgstpsVQEtEHFYFALHTFQEQIKGVVEiakqkgtwrDN--AIQ-------LTERYVKEGLQDRAVSRD-LPVGI 238
Cdd:PRK12267 156 ----------VKE-ESYFFRMSKYQDRLLEYYE---------ENpdFIQpesrkneMINNFIKPGLEDLSISRTsFDWGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 239 PIPvagyEDKK--IYVWIEAVTGYYSASKHwaektGKDDQEFWDKetktYY---VH--GKDNIPFHSIIWPAVLLGVGEE 311
Cdd:PRK12267 216 PVP----FDPKhvVYVWIDALLNYITALGY-----GSDDDELFKK----FWpadVHlvGKDILRFHAIYWPIMLMALGLP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 312 aIPRHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNR 391
Cdd:PRK12267 283 -LPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 392 TLKFIEKYYDGVVPKGT----IHVELKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPW---KQREDDP 464
Cdd:PRK12267 362 TVAMINKYFDGEIPAPGnvteFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWvlaKDEGKKE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 465 VSceETV-YNCVYLIANFANLLEPFLPFSSERVRNTLSIV--KRNWE---PQNTLP--NKIDSVQPLFERIDVKQIEHEI 536
Cdd:PRK12267 442 RL--ATVmYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEeeLTSWEsllEWGGLPagTKVAKGEPLFPRIDVEEEIAYI 519
|
...
gi 1207602735 537 EKL 539
Cdd:PRK12267 520 KEQ 522
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
11-538 |
6.48e-54 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 192.62 E-value: 6.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 11 YANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRSLGFTYDCY 90
Cdd:PLN02224 79 YVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDLDIAYDKF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 91 TRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLpdryvegicphcyeaargdqcdacsailDPLDLLEKKC 170
Cdd:PLN02224 159 IRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYK----------------------------DEKELLENNC 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 171 KLCGSTPSVQETE-HFYFALHTFQEQIKGVVEIAKQ--KGTWRDNAIQlteRYVKEGLQDRAVSRDLpVGIPIPVAGYED 247
Cdd:PLN02224 211 CPVHQMPCVARKEdNYFFALSKYQKPLEDILAQNPRfvQPSYRLNEVQ---SWIKSGLRDFSISRAL-VDWGIPVPDDDK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 248 KKIYVWIEAVTGYYSASKhwaektgkDDQEFWDKETK-------TYYVHGKDNIPFHSIIWPAVLLGVGEEaIPRHIVSN 320
Cdd:PLN02224 287 QTIYVWFDALLGYISALT--------EDNKQQNLETAvsfgwpaSLHLIGKDILRFHAVYWPAMLMSAGLE-LPKMVFGH 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 321 EYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDFSWREFIYSHNSELLGAYGNFVNRTLKFIEKYY 400
Cdd:PLN02224 358 GFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKNC 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 401 DG-VVPKGTIHVE---LKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFDEKQPWKQREDDPVSCEETVYNCVY 476
Cdd:PLN02224 438 EStLVEDSTVAAEgvpLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAKDLVI 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207602735 477 LIANF---ANLLEPFLPFSSERVRNTLSIVKRNWEPQNTLPNK---------IDSVQPLFERIDVKQIEHEIEK 538
Cdd:PLN02224 518 ILEVMrviAVALSPIAPCLSLRIYSQLGYSEDQFNSITWSDTKwgglkggqvMEQASPVFARIELNPEKEEDEK 591
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
377-500 |
7.47e-42 |
|
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: 146.48 E-value: 7.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 377 HNSELLGAYGNFVNRTLKFIEKYYDGVVPKGT----IHVELKDKVEGLYKEVGVAIEQTKFKVALETIFDAVRFANKYFD 452
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGglteEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207602735 453 EKQPWKQ-REDDPVSCEETVYNCVYLIANFANLLEPFLPFSSERVRNTL 500
Cdd:cd07957 81 ETAPWKLaKEEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
10-368 |
7.20e-40 |
|
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: 147.18 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGV-------------TAKEIADKYHEEF 76
Cdd:cd00668 9 PYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFVEEMSGEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 77 ERCFRSLGFTYDC--YTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEqaycetctqflpdryvegicphcyeaargdqcd 154
Cdd:cd00668 89 KEDFRRLGISYDWsdEYITTEPEYSKAVELIFSRLYEKGLIYRGTHP--------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 155 acsaildpldllekkcklcgstpsVQETEHFYFALHTFQEQIKGVVEIAKQKGTWRDNAIqltERYVKEGLqDRAVSRDL 234
Cdd:cd00668 136 ------------------------VRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRM---EAWLESLL-DWAISRQR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 235 PVGIPIPvagyeDKKIYVWIEAvTGYYSASKHWAEKTgKDDQEFWDKEtktYYVHGKDNIPFHSIIWPAVLLGVGEEAIP 314
Cdd:cd00668 188 YWGTPLP-----EDVFDVWFDS-GIGPLGSLGYPEEK-EWFKDSYPAD---WHLIGKDILRGWANFWITMLVALFGEIPP 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1207602735 315 RHIVSNEYLTVEK-RKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPENRDTDF 368
Cdd:cd00668 258 KNLLVHGFVLDEGgQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
4-370 |
9.21e-28 |
|
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: 113.50 E-value: 9.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 4 FIGGAWPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRSL 83
Cdd:cd00812 3 YILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 84 GFTYDcYTR----TDSEHHHETvQKVFLRLLEEGYIYKKTVEQAYCETCTQ-FLpdRYVEgicPHCYEAARGDqcdacsa 158
Cdd:cd00812 83 GFSYD-WRRefttCDPEYYKFT-QWLFLKLYEKGLAYKKEAPVNWCKLLDQwFL--KYSE---TEWKEKLLKD------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 159 iLDPLDLLekkcklcgstPSvqetehfyfalhTFQEQIKGVVEIAKQKGtWrdnaiqlteryvkeglqdravsrdlpvGI 238
Cdd:cd00812 149 -LEKLDGW----------PE------------EVRAMQENWIGCSRQRY-W---------------------------GT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 239 PIP----VAGYEDKKIYvwieavTGYYSASkHWAEKTGKDDQEFWDKETKTY-----YVHGKDNIPFH---SIIWPAVL- 305
Cdd:cd00812 178 PIPwtdtMESLSDSTWY------YARYTDA-HNLEQPYEGDLEFDREEFEYWypvdiYIGGKEHAPNHllySRFNHKALf 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207602735 306 -LGVGEEAIPRHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAPEnrDTDFSW 370
Cdd:cd00812 251 dEGLVTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPP--DADFDW 314
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
10-118 |
8.41e-20 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 93.33 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRA-KQEGVTA------------KEIADKYHEEF 76
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGLPTERKVeKYYGIRKddisreefielcRELTDEDEKKF 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207602735 77 ERCFRSLGFTYD---CYtRTDSEHHHETVQKVFLRLLEEGYIYKK 118
Cdd:PRK13208 127 RELWRRLGLSVDwslEY-QTISPEYRRISQKSFLDLYKKGLIYRA 170
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
10-368 |
2.35e-19 |
|
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: 90.00 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGtpIAIRAKQEGVTAK------------------EIADK 71
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAG--IATQVVVEKKLGIegktrhdlgreeflekcwEWKEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 72 YHEEFERCFRSLGFTYD--CYTRTDSEHHHETVQKVFLRLLEEGYIYKktveqaycetctqflpDRYVEGICPHCYEA-A 148
Cdd:cd00817 88 SGGKIREQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLIYR----------------DNRLVNWCPKLRTAiS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 149 RGDQCDACSAILDPldLLEK----KCKlcgstpsvqetehfyfalhtfqEQIKGVVEIAKQkgtwrdNAIQLT-ERYVK- 222
Cdd:cd00817 152 DIEVCSRSGDVIEP--LLKPqwfvKVK----------------------DLAKKALEAVKE------GDIKFVpERMEKr 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 223 -----EGLQDRAVSRDLPVGIPIPvagyedkkiyVWIEAVTGYYSASKHWAEKTGKDDQEFWDKETKTYYVHGKD--NIP 295
Cdd:cd00817 202 yenwlENIRDWCISRQLWWGHRIP----------AWYCKDGGHWVVAREEDEAIDKAAPEACVPCGGEELKQDEDvlDTW 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 296 FHSIIWPAVLLGVGEEA----------------------IPRHIVSNEYLTVEK----------------RKLSTSKNWA 337
Cdd:cd00817 272 FSSSLWPFSTLGWPEETkdlkkfyptsllvtghdiiffwVARMIMRGLKLTGKLpfkevylhglvrdedgRKMSKSLGNV 351
|
410 420 430
....*....|....*....|....*....|.
gi 1207602735 338 VWVPDILESYDPDSIRYFLTVNAPENRDTDF 368
Cdd:cd00817 352 IDPLDVIDGYGADALRFTLASAATQGRDINL 382
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
10-117 |
2.27e-14 |
|
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: 76.25 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGtpIAIRAKQEGVTAKEIADKY---HEEF-ERCF----- 80
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAG--IATQVKVEKKLGAEGKTKHdlgREEFrEKIWewkee 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207602735 81 ---------RSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYK 117
Cdd:TIGR00422 120 sggtiknqiKRLGASLD-WSRerfTMDEGLSKAVKEAFVRLYEKGLIYR 167
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
10-117 |
2.36e-14 |
|
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: 74.19 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQE-GVT----------------AKEIADKY 72
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElGISgkkdiekmgiaefnakCREFALRY 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207602735 73 HEEFERCFRSLGFTYD---CYtRTDSEHHHETVQKVFLRLLEEGYIYK 117
Cdd:cd00818 90 VDEQEEQFQRLGVWVDwenPY-KTMDPEYMESVWWVFKQLHEKGLLYR 136
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
10-138 |
3.32e-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: 75.52 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPI--------AIRAKQE----GVTA-----KEIADKY 72
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTeqvvekklGIKEKKTrhkyGREEfrekcREWKMEY 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207602735 73 HEEFERCFRSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVE 138
Cdd:pfam00133 112 ADEIRKQFRRLGRSID-WDReyfTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVE 179
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
9-125 |
9.49e-13 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 71.01 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 9 WPYANGS-LHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFERCFRSLGFTY 87
Cdd:PLN02563 118 FPYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSY 197
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207602735 88 DcYTR----TDSEHHHETvQKVFLRLLEEGYIYKKTVEQAYC 125
Cdd:PLN02563 198 D-WDReistTEPEYYKWT-QWIFLQLLKRGLAYQAEVPVNWC 237
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
10-128 |
5.35e-12 |
|
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: 68.54 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPI---AIRAKQ--EGVTAKEIADkyheeFERCFRSLG 84
Cdd:COG0495 42 PYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFGLPAenaAIKNGVhpAEWTYENIAN-----MRRQLKRLG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207602735 85 FTYDcYTR----TDSEHHHETvQKVFLRLLEEGYIYKKTVEQAYCETC 128
Cdd:COG0495 117 LSYD-WSReiatCDPEYYKWT-QWIFLQLYEKGLAYRKEAPVNWCPVD 162
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
16-125 |
2.07e-10 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 63.73 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 16 LHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPI-----AIRAKQE----------GVTAKE---------IADK 71
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPIlgiaeRIARGDPetielykslyGIPEEElekfkdpeyIVEY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207602735 72 YHEEFERCFRSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYC 125
Cdd:PRK12300 81 FSEEAKEDMKRIGYSID-WRReftTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYC 136
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
10-128 |
2.65e-10 |
|
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: 63.18 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHiasLLPG---DILARYYRAKGENVLYVSGSDCNGTPIAIRA-KQEGVTAKEI---------------AD 70
Cdd:COG0060 55 PYANGDIHIGH---ALNKilkDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIKKKDIekvgiaefrekcreyAL 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207602735 71 KYHEEFERCFRSLGF---------TYDcytrTDSEhhhETVQKVFLRLLEEGYIYK--KTVeqAYCETC 128
Cdd:COG0060 132 KYVDEQREDFKRLGVwgdwdnpylTMD----PEYE---ESIWWALKKLYEKGLLYKglKPV--PWCPRC 191
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
10-138 |
9.90e-10 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 61.55 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNG--TPIAIRAKQEGVTAKEIADKYHEEF-ERCF------ 80
Cdd:PRK14900 57 PNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLPGTDHAGiaTQMIVEKELKKTEKKSRHDLGREAFlERVWawkeqy 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207602735 81 --------RSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETCTQFLPDRYVE 138
Cdd:PRK14900 137 gsrigeqhKALGASLD-WQRerfTMDEGLSRAVREVFVRLHEEGLIYREKKLINWCPDCRTALSDLEVE 204
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
10-119 |
1.36e-09 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 61.17 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGtpIA-------IRAKQEGVTAKEIA------------D 70
Cdd:PTZ00419 69 PNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAG--IAtqvvvekKLMKEENKTRHDLGreeflkkvwewkD 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207602735 71 KYHEEFERCFRSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYKKT 119
Cdd:PTZ00419 147 KHGNNICNQLRRLGSSLD-WSRevfTMDEQRSKAVKEAFVRLYEDGLIYRDT 197
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
14-117 |
1.76e-09 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 60.50 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 14 GSLHLGHI--ASLLpgDILARYYRAKGENVLYVSGSDCNGtpIAIRAK------QEGVTAKEIADkyhEEF-ERCF---- 80
Cdd:PRK05729 49 GSLHMGHAlnNTLQ--DILIRYKRMQGYNTLWLPGTDHAG--IATQMVverqlaAEGKSRHDLGR---EKFlEKVWewke 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207602735 81 ----------RSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYK 117
Cdd:PRK05729 122 esggtitnqlRRLGASCD-WSRerfTMDEGLSKAVREVFVRLYEKGLIYR 170
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
10-117 |
7.25e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 58.63 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNG-------------------TPIAIRAKQEGVtAKEIAD 70
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGlpielkvlqsldqearkelTPIKLRAKAAKF-AKKTVD 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207602735 71 KYHEEFERcFRSLGFTYDCYTRTDSEhhHETVQ-KVFLRLLEEGYIYK 117
Cdd:PLN02843 120 TQRESFKR-YGVWGDWENPYLTLDPE--YEAAQiEVFGQMFLNGYIYR 164
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
14-117 |
2.25e-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: 56.98 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 14 GSLHLGHiA---SLLpgDILARYYRAKGENVLYVSGSDCNGtpIAIRAK------QEGVTAKEIADkyhEEF-ERCF--- 80
Cdd:COG0525 48 GSLHMGH-AlnnTLQ--DILIRYKRMQGYNTLWQPGTDHAG--IATQAVverqlaEEGKSRHDLGR---EKFlERVWewk 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207602735 81 -----------RSLG---------FTYDcytrtdsEHHHETVQKVFLRLLEEGYIYK 117
Cdd:COG0525 120 eesggtitnqlRRLGascdwsrerFTMD-------EGLSKAVREVFVRLYEKGLIYR 169
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
15-84 |
2.54e-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: 54.51 E-value: 2.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207602735 15 SLHLGHIASLLPGDILARYYRAKGENVLYVsgsdCNGT----PIAIRAKQEGVTAKEIADKYHEEFERCFRSLG 84
Cdd:cd00672 33 YAHIGHARTYVVFDVLRRYLEDLGYKVRYV----QNITdiddKIIKRAREEGLSWKEVADYYTKEFFEDMKALN 102
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
290-494 |
2.27e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 53.72 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 290 GKDNIP----F----HSIIWPavllgvgEEAIPRHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLTVNAp 361
Cdd:PRK12300 537 GKDLIPnhltFfifnHVAIFP-------EEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSA- 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 362 eNRDTDFSWREfiyshnsellgaygNFVNRTLKFIEKYYD---------GVVPKGTIHVELKDKVEGLYKEVGVAIEQTK 432
Cdd:PRK12300 609 -ELLQDADWRE--------------KEVESVRRQLERFYElakelieigGEEELRFIDKWLLSRLNRIIKETTEAMESFQ 673
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207602735 433 FKVALETIFDAVRfanKYFDEkqpWKQREDDPVSceetvYNCVYLIANFANLLEPFLPFSSE 494
Cdd:PRK12300 674 TRDAVQEAFYELL---NDLRW---YLRRVGEANN-----KVLREVLEIWIRLLAPFTPHLAE 724
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
17-84 |
4.11e-07 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 52.41 E-value: 4.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207602735 17 HLGHIASLLPGDILARYYRAKGENVLYVSgsdcNGT----PIAIRAKQEGVTAKEIADKYHEEFERCFRSLG 84
Cdd:COG0215 37 HIGHARTFVVFDVLRRYLRYLGYKVTYVR----NITdvddKIIKRAAEEGESIWELAERYIAAFHEDMDALG 104
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
9-77 |
7.66e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 51.99 E-value: 7.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207602735 9 WPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIairakqegvtaKEIADKYHEEFE 77
Cdd:PLN02959 53 YPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGMPI-----------KASADKLAREIQ 110
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
10-78 |
2.75e-06 |
|
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: 47.09 E-value: 2.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQEGVTAKEIADKYHEEFER 78
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKE 74
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
10-117 |
8.11e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 48.78 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQ----EGVTAKEIA------------DKYH 73
Cdd:PLN02943 97 PNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQLVVEKmlasEGIKRTDLGrdeftkrvwewkEKYG 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207602735 74 EEFERCFRSLGFTYDcYTR---TDSEHHHETVQKVFLRLLEEGYIYK 117
Cdd:PLN02943 177 GTITNQIKRLGASCD-WSRerfTLDEQLSRAVVEAFVRLHEKGLIYQ 222
|
|
| Anticodon_1 |
pfam08264 |
Anticodon-binding domain of tRNA ligase; This domain is found mainly hydrophobic tRNA ... |
416-539 |
2.03e-05 |
|
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: 44.70 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 416 KVEGLYKEVGVAIEQTKFKVALETIFDAV--RFANKYFDEKQPWKQREDDPVSCEETVYncvYLIANFANLLEPFLPFSS 493
Cdd:pfam08264 7 RLNKLIKEVTEAYENYRFNTAAQALYEFFwnDLSDWYLELIKDRLYGEEPDSRAQTTLY---EVLETLLRLLAPFMPFIT 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207602735 494 ERVRNTLSIVKRNWePQNTLPNKIDSVQPLFERIDVKQIeheIEKL 539
Cdd:pfam08264 84 EELWQKESIHLAPW-PEDAELEEAELEEAFELRQEIVQA---IRKL 125
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
3-117 |
3.76e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 46.64 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAwPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPI--------AIRAKQE----GV-----TA 65
Cdd:PLN02882 41 IFYDGP-PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVeyeidkklGIKRRDDvlkmGIdkyneEC 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207602735 66 KEIADKYHEEFE----RCFRSLGFTYDcYTRTDSEhHHETVQKVFLRLLEEGYIYK 117
Cdd:PLN02882 120 RSIVTRYSKEWEktvtRTGRWIDFEND-YKTMDPK-FMESVWWVFKQLFEKGLVYK 173
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
10-117 |
2.24e-04 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 44.12 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 10 PYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNG--TPIAIRAK---QEGVTAKEIAD--------KYHEEF 76
Cdd:PLN02381 137 PNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGiaTQVVVEKKlmrERHLTRHDIGReefvsevwKWKDEY 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207602735 77 --------ERCFRSLGFTYDCYTRtdSEHHHETVQKVFLRLLEEGYIYK 117
Cdd:PLN02381 217 ggtilnqlRRLGASLDWSRECFTM--DEQRSKAVTEAFVRLYKEGLIYR 263
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
3-128 |
3.58e-04 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 43.42 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 3 IFIGGAwPYANGSLHLGHIASLLPGDILARYYRAKGENVLYVSGSDCNGTPIAIRAKQE-GVTAKE-------------- 67
Cdd:PTZ00427 105 IFYDGP-PFATGLPHYGHLLAGIIKDCVTRYFYQCGFSVERKFGWDCHGLPIEYEIEKEnNINKKEdilkmgidvynekc 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207602735 68 --IADKYHEEF----ERCFRSLGFTYDcyTRTDSEHHHETVQKVFLRLLEEGYIYKKTVEQAYCETC 128
Cdd:PTZ00427 184 rgIVLKYSNEWvktvERIGRWIDFKND--YKTMDKTFMESVWWVFSELYKNNYVYKSFKVMPYSCKC 248
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
320-455 |
1.07e-03 |
|
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: 41.63 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 320 NEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFL-------TVnapenrdtDFSWrefiyshnsELLGAYGNFVNRt 392
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLlsahyrsPL--------DFSE---------EALEEAEKALER- 317
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207602735 393 lkfIEKYYDGVVPKGTIHVELKDKVEGLYKEVGVAIEQ---TkfKVALETIFDAVRFANKYFDEKQ 455
Cdd:COG0215 318 ---LYNALRRLEEALGAADSSAEEIEELREEFIAAMDDdfnT--PEALAVLFELVREINKALDEGE 378
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
315-369 |
1.28e-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: 40.25 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1207602735 315 RHIVSNEYLTVEKRKLSTSKNWAVWVPDILESYDPDSIRYFLtVNAPENRDTDFS 369
Cdd:cd00672 160 RYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL-LSSHYRSPLDFS 213
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
13-118 |
2.59e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 40.52 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207602735 13 NGSLHLGHIASLLPGDILARYYRAKGENVL---YVsgsdcN--GTPIAI------RAKQEGVtakeiaDKYHEEFERCFR 81
Cdd:PRK01611 123 TGPLHVGHLRSAVIGDALARILEFAGYDVTreyYV-----NdaGTQIGMliasleLLWRKAV------DISLDEIKEDLD 191
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207602735 82 SLGFTYDCYTRTDSEHHHETVQKVFLRLLEEGYIYKK 118
Cdd:PRK01611 192 RLGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLYVE 228
|
|
| |
