|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
9-680 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1308.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 9 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 88
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 89 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 168
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 169 YSPTELIDPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 247
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 248 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDtTSFDEYWKKGSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 327
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 328 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFISKR 407
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 408 FDGVLAAELADPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDAdlQAICTMGLNM 487
Cdd:PRK00133 401 FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 488 FRVLMTWLKPVLPQLAARAEAFLN-SELSWDAIQQPLLAHKVNPFKALYNRIEMKQVEALVEASKE--EVKATAAPVTGP 564
Cdd:PRK00133 479 FRALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEaaAAKAAAAAAAAP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 565 LADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYpDPQPLIGRLTVMVANLAPRK 644
Cdd:PRK00133 559 LAEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIKSAY-DPEELVGKLVVMVANLAPRK 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 1454611170 645 MRFGISEGMVMAAGPGGKDIFLLSPDDGAKPGQQVK 680
Cdd:PRK00133 638 MKFGVSEGMVLAAGPGGGDLFLLEPDEGAKPGMRVK 673
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
9-547 |
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: 875.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 9 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 88
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 89 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 168
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 169 YSPTELIDPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 247
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 248 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWkKGSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 327
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 328 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFISKR 407
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 408 FDGVLAA----ELADPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDAdLQAICTM 483
Cdd:COG0143 398 FDGKVPEpgelTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1454611170 484 GLNMFRVLMTWLKPVLPQLAARAEAFLN---SELSWDAIQQPLLA-HKVNPFKALYNRIEMKQVEALV 547
Cdd:COG0143 477 LLEALRILAILLKPFLPETAEKILEQLGlegDELTWEDAGWPLPAgHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
11-539 |
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: 769.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 11 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 90
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 91 FDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 170
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 171 PTELIDPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 246
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 247 PNAPGKYFYVWLDAPIGYMGSfknLCDKRGDTTSFDEYWKKGSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFV 326
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISS---LGILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 327 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFISK 406
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 407 RFDGVLAAELA----DPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADLQAICt 482
Cdd:TIGR00398 397 YFNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVC- 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1454611170 483 mgLNMFRVLMTWLKPVLPQLAARAEAFLNSELSWDAIQQPLLAHKVNPFKALYNRIE 539
Cdd:TIGR00398 476 --SMLIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
11-400 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 628.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 11 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 90
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 91 FDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 170
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 171 PTELIDPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPN 248
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 249 APGKYFYVWLDAPIGYMGSFKNLCdkrGDTTSFDEYWKKGSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHG 328
Cdd:pfam09334 240 AEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1454611170 329 YVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 400
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR-NRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
10-375 |
5.72e-147 |
|
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: 429.64 E-value: 5.72e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 10 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFA 89
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 90 GFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 169
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 170 sptelidpksvvsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 246
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 247 PNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDttsfDEYWKKGSTaELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFV 326
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGN----SWWWKDGWP-ELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1454611170 327 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDID 375
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
9-680 |
8.34e-127 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 389.93 E-value: 8.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 9 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 88
Cdd:PRK12267 4 KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 89 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFI-KNR-------------TISQLYDPEKgmflpdrfvkgtCPKCKS 154
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIyKGEyegwycvscetffTESQLVDGGK------------CPDCGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 155 PdqygdncevcgatyspTELIDPKSvvsgatpvmrdsehFFFDLPSFSEMLQAWTRSGA---LQEQVANKMQEWF-ESGL 230
Cdd:PRK12267 152 E----------------VELVKEES--------------YFFRMSKYQDRLLEYYEENPdfiQPESRKNEMINNFiKPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 231 QQWDISRDAPYFGFEIPNAPGKYFYVWLDA------PIGYMGSfknlcdkrgDTTSFDEYWkkgsTAELyHFIGKDIVYF 304
Cdd:PRK12267 202 EDLSISRTSFDWGIPVPFDPKHVVYVWIDAllnyitALGYGSD---------DDELFKKFW----PADV-HLVGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 305 HSLFWPAMLEGSNFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYytakLSSRI---DDIDLNLEDF 381
Cdd:PRK12267 268 HAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY----LLREVpfgSDGDFSPEAL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 382 VQRVNADIVNKVVNLASRNAGFISKRFDGVLAA----ELADPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANR 457
Cdd:PRK12267 344 VERINSDLANDLGNLLNRTVAMINKYFDGEIPApgnvTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 458 YVDEQAPWVVAKQEGRDADLQAICTMGLNMFRVLMTWLKPVLPQLAAR---------AEAFLNSELSWDAIQQPllaHKV 528
Cdd:PRK12267 424 YIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKifeqlgleeELTSWESLLEWGGLPAG---TKV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 529 NPFKALYNRIEmkqVEALVEASKEEVKATAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDL 608
Cdd:PRK12267 501 AKGEPLFPRID---VEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLEAEKVEKSDKLLKLQVDL 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1454611170 609 GGEK-RNVFSGIRSAYPdPQPLIGRLTVMVANLAPRKMRFGISEGMVMAAGPGGKdIFLLSPDDGAKPGQQVK 680
Cdd:PRK12267 578 GEEEpRQIVSGIAKFYP-PEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGK-LTLLTVDKEVPNGSKVK 648
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
10-376 |
3.57e-123 |
|
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: 368.67 E-value: 3.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 10 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGI-------------TPEQM 76
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 77 IGEMSQEHQTDFAGFDISYD--NYHSTHSDENRELSELIYTRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkcks 154
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 155 pdqygdncevcgatysptelidpksvvsgatpvmRDSEHFFFDLPSFSEMLQAWTRSGA-LQEQVANKMQEWFESGLQqW 233
Cdd:cd00668 137 ----------------------------------RITEQWFFDMPKFKEKLLKALRRGKiVPEHVKNRMEAWLESLLD-W 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 234 DISRDApYFGFEIPNapgKYFYVWLDAPIGYMGSFKNLCDKRgdttsfdeyWKKGSTAELYHFIGKDIVYFHSLFWPAML 313
Cdd:cd00668 182 AISRQR-YWGTPLPE---DVFDVWFDSGIGPLGSLGYPEEKE---------WFKDSYPADWHLIGKDILRGWANFWITML 248
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1454611170 314 EGSNFR-KPTNLFVHGYVTVN-GAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDL 376
Cdd:cd00668 249 VALFGEiPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLA-PYGDDIRL 312
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
9-541 |
1.79e-105 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 329.92 E-value: 1.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 9 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 88
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 89 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckspdqygdnCEVCGAT 168
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 169 YSPTELIDPKSV--VSGATPVMRDSEHFFFDLPSFSEMLQAW--TRSGALQ-EQVANKMQEWFESGLQQWDISR---DAp 240
Cdd:PRK11893 132 YTESELIEDGYRcpPTGAPVEWVEEESYFFRLSKYQDKLLELyeANPDFIQpASRRNEVISFVKSGLKDLSISRtnfDW- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 241 yfGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWkkgsTAELyHFIGKDIVYFHSLFWPAMLEGSNFRK 320
Cdd:PRK11893 211 --GIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELLAELFNKYW----PADV-HLIGKDILRFHAVYWPAFLMAAGLPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 321 PTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRyYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 400
Cdd:PRK11893 284 PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVR-YFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 401 AGFISKRFDGVL----AAELADPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANRYVDEQAPWVVAKQEgrDAD 476
Cdd:PRK11893 363 LSMIAKNFDGKVpepgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTD--PER 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1454611170 477 LQAICTMGLNMFRVLMTWLKPVLPQLAARAEAFLNSE----LSWDAIQQPLLA--HKVNPFKALYNRIEMK 541
Cdd:PRK11893 441 LATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEedenRDFAALSWGRLApgTTLPKPEPIFPRLEEE 511
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
9-680 |
8.85e-96 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 312.87 E-value: 8.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 9 KKILVTCALPYANGSIHLGHMLEHI-QADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 87
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 88 FAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKSPDQYGDNCEVC 165
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 166 GATYSPTELIDPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQ-VANKMQ---EWFESGLQQWDISRD--- 238
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGwSQNAIQttnAWLRDGLKPRCITRDlkw 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 239 ---APYFGFEipnapGKYFYVWLDAPIGYMGSFKNLcdkrgdTTSFDEYWKKGSTAELYHFIGKDIVYFHSLFWPAMLEG 315
Cdd:PLN02610 257 gvpVPLEKYK-----DKVFYVWFDAPIGYVSITACY------TPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 316 S--NFRKPTNLFVHGYVTVNGAKMSKSRG----------TFIKASTWlnhfdadslRYYYtakLSSR--IDDIDLNLEDF 381
Cdd:PLN02610 326 TgeNWTMMKTISVTEYLNYEGGKFSKSKGvgvfgndakdTNIPVEVW---------RYYL---LTNRpeVSDTLFTWADL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 382 VQRVNADIVNKVVNLASRNAGFISKR----FDGVL--AAELADPALYKTFtdaAESIG-------EAWDSREFGKAIREI 448
Cdd:PLN02610 394 QAKLNSELLNNLGNFINRVLSFIAKPpgagYGSVIpdAPGAESHPLTKKL---AEKVGklveqyvEAMEKVKLKQGLKTA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 449 MALADVANRYVDEQAPWVVAKQegrDADLQAI---CTMGLnmFRVLMTWLKPVLPQLAARAEAFLN---SELS------- 515
Cdd:PLN02610 471 MSISSEGNAYLQESQFWKLYKE---DKPSCAIvvkTSVGL--VYLLACLLEPFMPSFSKEVLKQLNlppESLSlsdekge 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 516 -------WDAIQQpllAHKVNPFKALYNRIEMKQVEALVE----------------------------------ASKEEV 554
Cdd:PLN02610 546 varakrpWELVPA---GHKIGTPEPLFKELKDEEVEAYREkfagsqadraaraeaaeakklakqlkkkalsdggKKKQGK 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 555 KATAAPVTGPLADDPIqetitfdDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQpLIGRL 633
Cdd:PLN02610 623 KAGGGGKSKAAAEREI-------DVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGApRTVVSGLVKYIPLEE-MQNRK 694
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1454611170 634 TVMVANLAPRKMRFGISEGMVMAAGPG-GKDIFLLSPDDGAKPGQQVK 680
Cdd:PLN02610 695 VCVLCNLKPAAMRGIKSQAMVLAASNSdHTKVELVEPPESAAVGERVT 742
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
544-680 |
2.30e-59 |
|
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: 195.72 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 544 EALVEASKEE-VKATAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSA 622
Cdd:TIGR00399 1 DKKIEELKLKgAKKKEKKDEGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAGY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1454611170 623 YPdPQPLIGRLTVMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDDGAKPGQQVK 680
Cdd:TIGR00399 81 YT-PEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK 137
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
8-575 |
5.74e-58 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 206.87 E-value: 5.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 8 AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 87
Cdd:PLN02224 68 ADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 88 FAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkspDQYGDNCEVCGA 167
Cdd:PLN02224 148 WKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDEKELLEN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 168 TYSPtelidpksvVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVA---NKMQEWFESGLQQWDISRDAPYFGF 244
Cdd:PLN02224 209 NCCP---------VHQMPCVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSyrlNEVQSWIKSGLRDFSISRALVDWGI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 245 EIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTTSFDEYWKKGstaelYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNL 324
Cdd:PLN02224 280 PVPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPAS-----LHLIGKDILRFHAVYWPAMLMSAGLELPKMV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 325 FVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRiDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFI 404
Cdd:PLN02224 355 FGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 405 SKRFDGVLAAELADPALYKTFTDAAESIGEA----WDSREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADLQAI 480
Cdd:PLN02224 434 KKNCESTLVEDSTVAAEGVPLKDTVEKLVEKaqtnYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 481 -CTMGLNMFRVLMTWLKPVLPQLAARAEAFLN-----------SELSWDAIQQPLLAHKVNPfkaLYNRIEMKQvealvE 548
Cdd:PLN02224 514 dLVIILEVMRVIAVALSPIAPCLSLRIYSQLGysedqfnsitwSDTKWGGLKGGQVMEQASP---VFARIELNP-----E 585
|
570 580
....*....|....*....|....*..
gi 1454611170 549 ASKEEVKATAAPVTGPLADDPIQETIT 575
Cdd:PLN02224 586 KEEDEKKPKVGKKTGKAKVKVVEQTPT 612
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
574-680 |
3.49e-49 |
|
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: 167.29 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 574 ITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPdPQPLIGRLTVMVANLAPRKMRFGISEGM 653
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYP-PEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100
....*....|....*....|....*..
gi 1454611170 654 VMAAGPGGKdIFLLSPDDGAKPGQQVK 680
Cdd:cd02800 80 ILAAEDGGK-LKLLTPDEEVEPGSRVS 105
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
378-510 |
1.93e-39 |
|
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: 141.47 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 378 LEDFVQRVNADIVNKVVNLASRNAGFISKRFDGvlaAELADPALYKTFTDAAESIGEAWDSREFGKAIREIMALADVANR 457
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGG---LTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1454611170 458 YVDEQAPWVVAKQEGRDAdLQAICTMGLNMFRVLMTWLKPVLPQLAARAEAFL 510
Cdd:cd07957 78 YIDETAPWKLAKEEDPER-LATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
584-678 |
6.81e-29 |
|
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: 110.41 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 584 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQpLIGRLTVMVANLAPRKMRFGISEGMVMAAGP-GG 661
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEpRQIVSGAVNVYPPEE-LVGRLVVVVANLKPAKLRGVESEGMILSAEElDG 79
|
90
....*....|....*..
gi 1454611170 662 KDIFLLSPDDGAKPGQQ 678
Cdd:pfam01588 80 GSVGLLEPPADVPPGTK 96
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
551-680 |
1.65e-28 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 121.89 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 551 KEEVKATAAPVTgpLADDPIQETITFDDFAKVD----LRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYP-D 625
Cdd:COG0073 9 KEYVDLDLSPEE--LAEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYAgD 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 626 PQP--LIGRLTVMVANLAPRKMRFGISEGMVMAA---GPGGKDIFLLSPDDGAKPGQQVK 680
Cdd:COG0073 87 KVPeaLVGAQVPGVVNLKPRKIRGVESEGMLCSAeelGLGEDHDGILELPEDAPPGDDAE 146
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
584-679 |
2.90e-27 |
|
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: 106.06 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 584 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQPLIGRLTVMVANLAPRKMRFGISEGMVMAA---GP 659
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKpRQIVSGAANVYP-PEELVGKKVVVAVNLKPKKLRGVESEGMLLSAeelGL 79
|
90 100
....*....|....*....|
gi 1454611170 660 GGKDIFLLSPDDGAKPGQQV 679
Cdd:cd02153 80 EEGSVGILELPEDAPVGDRI 99
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
574-679 |
2.57e-21 |
|
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: 89.22 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 574 ITFDDFAKVDLRVALIENAE-FVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQPLIGRLTVMVANLAPRKMRFGISEG 652
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEdFPEARKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*..
gi 1454611170 653 MVMAAGPGGKDIFLLSPDDGAKPGQQV 679
Cdd:cd02798 81 LVLGADDEGGEVVLLVPDREVPNGAKV 107
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
10-362 |
6.50e-20 |
|
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: 91.16 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 10 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQM----IGEMSQehQ 85
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWteynIKKMKE--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 86 TDFAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkCKSPDQYGDNcevc 165
Cdd:cd00812 79 LKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW-------------------CKLLDQWFLK---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 166 gatYSPTELIDpksvvsgatpvmrdsehfffDLPSFSEMLQAWTrsgalqEQVANKMQEWFesglqqwDISRDApYFGFE 245
Cdd:cd00812 136 ---YSETEWKE--------------------KLLKDLEKLDGWP------EEVRAMQENWI-------GCSRQR-YWGTP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 246 IPnapgkYFYV---WLDAPIgYMGSF---KNLCDKRGDTTSFD----EYWkkgSTAELYHFiGKDIVYFH---SLFWPAM 312
Cdd:cd00812 179 IP-----WTDTmesLSDSTW-YYARYtdaHNLEQPYEGDLEFDreefEYW---YPVDIYIG-GKEHAPNHllySRFNHKA 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1454611170 313 L--EGSNFRK-PTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 362
Cdd:cd00812 249 LfdEGLVTDEpPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLY 301
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
577-679 |
1.65e-19 |
|
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: 84.20 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 577 DDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQpLIGRLTVMVANLAPRKMRfGI-SEGMV 654
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEpRTIVSGLVKFVPLEQ-MQNRLVVVLCNLKPRKMR-GVkSQGMV 78
|
90 100
....*....|....*....|....*.
gi 1454611170 655 MAAGPGGKDIF-LLSPDDGAKPGQQV 679
Cdd:cd02799 79 LCASNADHEKVeLLEPPEGAKPGERV 104
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
572-679 |
8.83e-17 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 76.41 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 572 ETITFDDFAKVDLRVALIENAEFVEGSDKL-LRLTLDLGGEkrnvfSGIR--SA----YPDPQPLIGRLTVMVANLAPRK 644
Cdd:PRK10089 2 ETITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEE-----IGVKqsSAqitpHYTPEELIGKQVVAVVNFPPKQ 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1454611170 645 MRFGISEGMVMAAGPGGKDIFLLSPDDGAKPGQQV 679
Cdd:PRK10089 77 IAGFMSEVLVLGFEDEDGEVVLLTPDRPVPNGVKL 111
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
18-362 |
1.37e-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: 75.35 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMS--------------- 81
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMGiaefnakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 82 ---QEHQTDFAGFDISYDNYHSTHSDENRElSELiytrlkengfiknRTISQLYdpEKGMflpdrfvkgtcpkckspdqy 158
Cdd:cd00818 90 vdeQEEQFQRLGVWVDWENPYKTMDPEYME-SVW-------------WVFKQLH--EKGL-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 159 gdncevcgatysptelidpksVVSGATPVM-----RDSEHFFFDLPSF-SEMLQAWTRSGALQEQVANKMQEWFEsGLQQ 232
Cdd:cd00818 134 ---------------------LYRGYKVVPwpliyRATPQWFIRVTKIkDRLLEANDKVNWIPEWVKNRFGNWLE-NRRD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 233 WDISRDApYFGFEIP----NAPGKY--------FYVWLDApiGYMGSFKNlcDKRGDTTSFDEYWKkgstaelYHFI--G 298
Cdd:cd00818 192 WCISRQR-YWGTPIPvwycEDCGEVlvrrvpdvLDVWFDS--GSMPYAQL--HYPFENEDFEELFP-------ADFIleG 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 299 KDIV--YFHSLfwpaMLEGS-NFRKP--TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 362
Cdd:cd00818 260 SDQTrgWFYSL----LLLSTaLFGKApyKNVIVHGFVlDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
18-376 |
2.42e-14 |
|
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: 75.36 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEHQ 85
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 86 TDFA------GFDISYDNYHSTHSDENRELSELIYTRLKENGFIknrtisqlydpEKGMFLPDRfvkgtCPKCKSPDQyg 159
Cdd:cd00817 90 GKIReqlkrlGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLI-----------YRDNRLVNW-----CPKLRTAIS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 160 dNCEVCGATYSPTElidpksvvsgatPVMrdSEHFFFDLPSFSEMLQAWTRSGALQ---EQVANKMQEWFESgLQQWDIS 236
Cdd:cd00817 152 -DIEVCSRSGDVIE------------PLL--KPQWFVKVKDLAKKALEAVKEGDIKfvpERMEKRYENWLEN-IRDWCIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 237 RDApYFGFEIPnapgkyfyVWLDAPIGY--------------MGSFKNLCDK---RGDT----TSFDE--------YWKK 287
Cdd:cd00817 216 RQL-WWGHRIP--------AWYCKDGGHwvvareedeaidkaAPEACVPCGGeelKQDEdvldTWFSSslwpfstlGWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 288 GsTAELYHFI-------GKDIVYfhslFWPA--MLEGSNF--RKP-TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHF 354
Cdd:cd00817 287 E-TKDLKKFYptsllvtGHDIIF----FWVArmIMRGLKLtgKLPfKEVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGY 361
|
410 420
....*....|....*....|..
gi 1454611170 355 DADSLRyYYTAKLSSRIDDIDL 376
Cdd:cd00817 362 GADALR-FTLASAATQGRDINL 382
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
18-83 |
1.18e-11 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 68.18 E-value: 1.18e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITpEQMIGEMSQE 83
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIK-KKDIEKVGIA 120
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
18-123 |
2.82e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 63.67 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNF-ICADDaHGTPIMLKAQ-QLGITP----------------EQMIGE 79
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcreltDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1454611170 80 MSQEHQTdfAGFDISYDNYHSTHSDENRELSELIYTRLKENGFI 123
Cdd:PRK13208 126 FRELWRR--LGLSVDWSLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
18-155 |
6.24e-10 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 62.43 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMSQEHQTDFAGFDISYd 96
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVeKKLGIKEKKTRHKYGREEFREKCREWKME- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1454611170 97 nYHSTHSDENRELSELI-----YTRLKEnGFIKN--RTISQLYDpeKGMFLPDRFVKGTCPKCKSP 155
Cdd:pfam00133 111 -YADEIRKQFRRLGRSIdwdreYFTMDP-ELEAAvwEVFVRLHD--KGLIYRGKKLVNWSPALNTA 172
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
18-68 |
1.82e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 60.94 E-value: 1.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQ 68
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
18-123 |
6.93e-09 |
|
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: 59.30 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEH- 84
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESg 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1454611170 85 -----QTDFAGFDISYDNYHSTHSDENRELSELIYTRLKENGFI 123
Cdd:TIGR00422 122 gtiknQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLI 165
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
295-380 |
4.69e-06 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 48.90 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 295 HFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY-YTAKLSSRID 372
Cdd:pfam01406 211 HGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFlLSVHYRSPLD 290
|
....*...
gi 1454611170 373 DIDLNLED 380
Cdd:pfam01406 291 FSEELLEQ 298
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
323-363 |
4.79e-06 |
|
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: 47.96 E-value: 4.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1454611170 323 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 363
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
298-402 |
1.34e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 48.71 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 298 GKDIVYFHSLF-------------WPAMLEgsnfrkptnlfVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYT 364
Cdd:PRK12300 537 GKDLIPNHLTFfifnhvaifpeekWPRGIV-----------VNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT 605
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1454611170 365 --AKLSSridDIDLNlEDFVQRVnADIVNKVVNLASRNAG 402
Cdd:PRK12300 606 ssAELLQ---DADWR-EKEVESV-RRQLERFYELAKELIE 640
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
323-363 |
2.42e-05 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 47.40 E-value: 2.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1454611170 323 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 363
Cdd:COG0215 251 RYWMHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
22-49 |
4.59e-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: 46.97 E-value: 4.59e-05
10 20
....*....|....*....|....*....
gi 1454611170 22 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 49
Cdd:COG0525 48 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 75
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
22-49 |
5.38e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 46.64 E-value: 5.38e-05
10 20
....*....|....*....|....*....
gi 1454611170 22 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 49
Cdd:PRK05729 49 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 76
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
18-103 |
8.06e-05 |
|
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: 43.24 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFI-CADDAHGTPIMLKAQQLGITP---EQMIGEMSQ--EHQTDFAGF 91
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIaLIDDAGGLIGDPANKKGENAKafvERWIERIKEdvEYMFLQAAD 85
|
90
....*....|..
gi 1454611170 92 DISYDNYHSTHS 103
Cdd:cd00802 86 FLLLYETECDIH 97
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
17-49 |
1.04e-04 |
|
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: 45.43 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|...
gi 1454611170 17 LPYANGSIHLGHMLEHIQADVWVRYQRMRGHEV 49
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
18-145 |
6.90e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 42.89 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 18 PYANGS-IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLG----ITPEQMIGEMSQEHQTdfAGFD 92
Cdd:PLN02563 119 PYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGthpkITTLKNIARFRSQLKS--LGFS 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1454611170 93 ISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFV 145
Cdd:PLN02563 197 YDWDREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV 249
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
18-80 |
1.63e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 42.02 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1454611170 18 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEM 80
Cdd:PLN02882 47 PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIdKKLGIKRRDDVLKM 110
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
24-155 |
5.12e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 40.24 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 24 IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQL---------------GItPEQMIGEM-------- 80
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIargdpetielykslyGI-PEEELEKFkdpeyive 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 81 --SQEHQTDF--AGFDIsyD---NYHSThsDEnrELSELI---YTRLKENGFIknrtisqlydpekgmflpdrfVKGT-- 148
Cdd:PRK12300 80 yfSEEAKEDMkrIGYSI--DwrrEFTTT--DP--EYSKFIewqFRKLKEKGLI---------------------VKGShp 132
|
170
....*....|
gi 1454611170 149 ---CPKCKSP 155
Cdd:PRK12300 133 vryCPNDNNP 142
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
298-448 |
5.18e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 40.09 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 298 GKDIVYFhslfWPA--MLEGSNFRK--P-TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRI 371
Cdd:PRK05729 480 GFDIIFF----WVArmIMMGLHFTGqvPfKDVYIHGLVrDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAA-LASPG 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 372 DDIDLNLEdfvqRVNA--DIVNKVVNlASR-----NAGFISKRFDGVLAAELADPALYKTFTDAAESIGEAWDSREFGKA 444
Cdd:PRK05729 555 RDIRFDEE----RVEGyrNFANKLWN-ASRfvlmnLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEA 629
|
....
gi 1454611170 445 IREI 448
Cdd:PRK05729 630 ARAL 633
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
304-500 |
9.54e-03 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 39.29 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 304 FHSLFWPA-MLEGSN-FRkptNLFVHGYVtV--NGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAklSSRIDDIDLNlE 379
Cdd:COG0060 571 FYSSLLTStALFGRApYK---NVLTHGFV-LdeDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS--SDYWGDLRFS-D 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1454611170 380 DFVQRVnADIVNKVVNLAsrnagfiskRFdgvLAAELA--DP----------------ALYKTfTDAAESIGEAWDSREF 441
Cdd:COG0060 644 EILKEV-RDVYRRLRNTY---------RF---LLANLDdfDPaedavpyedlpeldrwILSRL-NELIKEVTEAYDNYDF 709
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1454611170 442 GKAIREIMALA--DVANRYVDeqapwvVAKQ----EGRD--ADLQAICTMgLNMFRVLMTWLKPVLP 500
Cdd:COG0060 710 HRAYRALHNFCveDLSNWYLD------ISKDrlytEAADslDRRAAQTTL-YEVLETLVRLLAPILP 769
|
|
| |
