|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
21-898 |
0e+00 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 976.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 21 EKKDPKsiLPQPGKRNILITAALPYVNNVPHLGNIIGCVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTP 100
Cdd:PLN02610 5 GKSPPK--LPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 101 RELCDKYHAIHKGIYEWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLADRFVTGTCPM-- 178
Cdd:PLN02610 83 KEICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTeg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 179 CAYDDARGDQCDGCGKLINAVDLKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLdrELAKEDNRWSSNAVGITKAW 258
Cdd:PLN02610 163 CNYDSARGDQCEKCGKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYI--NETSVAGGWSQNAIQTTNAW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 259 MKLGLDPRCITRDLKWGTAVPLDGFEKKVFYVWFDAPIGYLSITKCVLGDnWTKWWKNPENVELFNFVGKDNVAFHAVMF 338
Cdd:PLN02610 241 LRDGLKPRCITRDLKWGVPVPLEKYKDKVFYVWFDAPIGYVSITACYTPE-WEKWWKNPENVELYQFMGKDNVPFHTVMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 339 PCSQLGANDNYTVVNNLCATEYLNYEDTKFSKSRGTGIFGDAAQGTEIPADIWRFYLLYMRPESQDTAFSWDDFVLKVNS 418
Cdd:PLN02610 320 PSTLLGTGENWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 419 ELLNNLGNFINRALSFVANS----FGGVVP------EMNLTNDDAEVLSEIhneCMQWDKQFDGVHLKDAVKTILNVSRL 488
Cdd:PLN02610 400 ELLNNLGNFINRVLSFIAKPpgagYGSVIPdapgaeSHPLTKKLAEKVGKL---VEQYVEAMEKVKLKQGLKTAMSISSE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 489 GNQYMQAQTPWVLMKKDeegKKRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPL------------FTPF 556
Cdd:PLN02610 477 GNAYLQESQFWKLYKED---KPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLslsdekgevaraKRPW 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 557 PIcyLKAGHKIGQPSPLFQKLDPAQIAEFKAKFGGSQ--DAQSSAPKTAEKPKQQKKQAPTKDKKGDKkmastaafvele 634
Cdd:PLN02610 554 EL--VPAGHKIGTPEPLFKELKDEEVEAYREKFAGSQadRAARAEAAEAKKLAKQLKKKALSDGGKKK------------ 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 635 qgakvisqliaqnlkkfdqakalftrnqlqrldgenkqltidvktlqhqlieletaagikqvpkpvvsctptptstpasg 714
Cdd:PLN02610 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 715 iitEAPKKEAPSTPAPSepkkakeqkkgkggaaaapVDDTIDVGRLDMRVGRIIKCEKHPDADALYVEQIDVGESAPRTV 794
Cdd:PLN02610 620 ---QGKKAGGGGKSKAA-------------------AEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTV 677
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 795 VSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCASSPD--KVEIMEVPADSKPGTPVVCPPYTHRPDEQLNPK 872
Cdd:PLN02610 678 VSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPDDVLNPK 757
|
890 900
....*....|....*....|....*.
gi 392900888 873 KKIWETVAEDLKVSAEGFAEWKGQPL 898
Cdd:PLN02610 758 KKVWETLQPDLHTNSELVACYKDVPF 783
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
34-856 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 690.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 34 KRNILITAALPYVNNVPHLGNIIGcVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKG 113
Cdd:PRK00133 1 MRKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 114 IYEWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLADRFVTGTCPMCAYDDARGDQCDGCG 193
Cdd:PRK00133 80 DFAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 194 KLINAVDLKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLDRELakednRWSSNAVGITKAWMKLGLDPRCITRDLK 273
Cdd:PRK00133 160 ATYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSG-----ELQPNVANKMKEWLEEGLQDWDISRDAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 274 W-GTAVPldGFEKKVFYVWFDAPIGYLSITKC----VLGDNWTKWWKNPENVELFNFVGKDNVAFHAVMFPCSQLGAndN 348
Cdd:PRK00133 235 YfGFEIP--GAPGKVFYVWLDAPIGYISSTKNlcdkRGGLDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGA--G 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 349 YTVVNNLCATEYLNYEDTKFSKSRGTGIFGDAAQgTEIPADIWRFYLLYMRPES-QDTAFSWDDFVLKVNSELLNNLGNF 427
Cdd:PRK00133 311 YRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYL-DHLDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKVVNF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 428 INRALSFVANSFGGVVPemnLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILNVSRLGNQYMQAQTPWVLMKKDEE 507
Cdd:PRK00133 390 ASRTAGFINKRFDGKLP---DALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 508 gkkRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPlFTPFPIcyLKAGHKIGQPSPLFQKLDPAQIAEFKA 587
Cdd:PRK00133 467 ---RLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEELT-WDDAQQ--PLAGHPINKFKILFTRIEDKQIEALIE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 588 KfggsqdaqSSAPKTAEKPKQQKKQAPTKDKKGDKkmastaafveleqgakvISqliaqnlkkFDqakalftrnqlqrld 667
Cdd:PRK00133 541 A--------SKEAAAAKAAAAAAAAPLAEEPIAET-----------------IS---------FD--------------- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 668 genkqltidvktlqhqlieletaagikqvpkpvvsctptptstpasgiiteapkkeapstpapsepkkakeqkkgkggaa 747
Cdd:PRK00133 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 748 aapvddtiDVGRLDMRVGRIIKCEKHPDADALYVEQIDVGEsAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVE 827
Cdd:PRK00133 572 --------DFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIKSAYDPEELVGKLVVMVANLAPRKMKFGV 642
|
810 820 830
....*....|....*....|....*....|
gi 392900888 828 SRAMVMCASSPDK-VEIMEVPADSKPGTPV 856
Cdd:PRK00133 643 SEGMVLAAGPGGGdLFLLEPDEGAKPGMRV 672
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
35-584 |
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: 625.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 35 RNILITAALPYVNNVPHLGNIIgCVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGI 114
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 115 YEWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLADRFVTGTCPMCAYDDARGDQCDGCGK 194
Cdd:COG0143 80 FEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 195 LINAVDLKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLDrelakEDNRWSSNAVGITKAWMKLGLDPRCITRDLKW 274
Cdd:COG0143 160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIE-----ENPDIQPEVRNEVLSWLKEGLQDLSISRDFDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 275 GtaVPLDGFEKKVFYVWFDAPIGYLSITK-----CVLGDNWTKWWKNPeNVELFNFVGKDNVAFHAVMFPCSQLGAndNY 349
Cdd:COG0143 235 G--IPVPGDPGKVFYVWFDALIGYISATKgyaddRGLPEDFEKYWPAP-DTELVHFIGKDIIRFHAIIWPAMLMAA--GL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 350 TVVNNLCATEYLNYEDTKFSKSRGTGIFGDAAqgTEI-PADIWRFYLLYMRPESQDTAFSWDDFVLKVNSELLNNLGNFI 428
Cdd:COG0143 310 PLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDL--LDRyGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 429 NRALSFVANSFGGVVPEM-NLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILNVSRLGNQYMQAQTPWVLMKkdEE 507
Cdd:COG0143 388 SRTLSMIHKYFDGKVPEPgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAK--DE 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392900888 508 GKKRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPLFTPFPICYLKAGHKIGQPSPLFQKLDPAQIAE 584
Cdd:COG0143 466 DPERLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLPAGHKIGKPEPLFPRIEDEQIEA 542
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
37-578 |
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: 577.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 37 ILITAALPYVNNVPHLGNIIgCVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIYE 116
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 117 WFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLADRFVTGTCPMCAYDDARGDQCDGCGKLI 196
Cdd:TIGR00398 80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 197 NAVDLKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLdrELAKEDNRWSSNAVGITKAWMKLGLDPRCITRDLK-WG 275
Cdd:TIGR00398 160 EPTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWI--RKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVyWG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 276 TAVPLDgfEKKVFYVWFDAPIGYLSITKCVLGD--NWTKWWKNPENVELFNFVGKDNVAFHAVMFPCSQLGAndNYTVVN 353
Cdd:TIGR00398 238 IPVPND--PNKVVYVWFDALIGYISSLGILSGDteDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGL--GLPLPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 354 NLCATEYLNYEDTKFSKSRGTGIFGDAAQgTEIPADIWRFYLLYMRPESQDTAFSWDDFVLKVNSELLNNLGNFINRALS 433
Cdd:TIGR00398 314 QVFSHGYLTVEGGKMSKSLGNVVDPSDLL-ARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 434 FVANSFGGVVP-EMNLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILNVSRLGNQYMQAQTPWVLMKKDEEGKKra 512
Cdd:TIGR00398 393 FIKKYFNGVLPsEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKE-- 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392900888 513 gtIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPLFtpfpICYLKAGHKIGQPSPLFQKLD 578
Cdd:TIGR00398 471 --LLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFELEWDF----KLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
37-431 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 549.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 37 ILITAALPYVNNVPHLGNIIGcVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIYE 116
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 117 WFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLADRFVTGTCPMCAYDDARGDQCDGCGKLI 196
Cdd:pfam09334 80 KFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 197 NAVDLKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLDRelakEDNRWSSNAVGITKAWMKLGLDPRCITRDLKWGT 276
Cdd:pfam09334 160 EPTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEE----NNPEWPENVKNMVLEWLKEGLKDRAISRDLDWGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 277 AVPldGFEKKVFYVWFDAPIGYLSITKCVLGD--NWTKWWKNPENVELFNFVGKDNVAFHAVMFPCSQLGAndNYTVVNN 354
Cdd:pfam09334 236 PVP--GAEGKVFYVWLDAPIGYISATKELSGNeeKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGA--GYRLPTT 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392900888 355 LCATEYLNYEDTKFSKSRGTGIFGDAAQGTeIPADIWRFYLLYMRPESQDTAFSWDDFVLKVNSELLNNLGNFINRA 431
Cdd:pfam09334 312 VFAHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
36-407 |
2.43e-158 |
|
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: 466.62 E-value: 2.43e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 36 NILITAALPYVNNVPHLGNIIGCVLsADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIY 115
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 116 EWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKFLadrfvtgtcpmcayddargdqcdgcgkl 195
Cdd:cd00814 80 KWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL---------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 196 inavdlkdakchmckatPEVKQSTHIFLSLDKLQQKTTEHLDRElakEDNRWSSNAVGITKAWMKLGLDPRCITRDL-KW 274
Cdd:cd00814 132 -----------------PEWREEEHYFFRLSKFQDRLLEWLEKN---PDFIWPENARNEVLSWLKEGLKDLSITRDLfDW 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 275 GTAVPLDgfEKKVFYVWFDAPIGYLSITKCVLGDNWTKWWKNPENVELFNFVGKDNVAFHAVMFPCSQLGAndNYTVVNN 354
Cdd:cd00814 192 GIPVPLD--PGKVIYVWFDALIGYISATGYYNEEWGNSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGA--GLPLPTR 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 392900888 355 LCATEYLNYEDTKFSKSRGTGIFGDAAQGTeIPADIWRFYLLYMRPESQDTAF 407
Cdd:cd00814 268 IVAHGYLTVEGKKMSKSRGNVVDPDDLLER-YGADALRYYLLRERPEGKDSDF 319
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
34-856 |
6.08e-102 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 331.38 E-value: 6.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 34 KRNILITAALPYVNNVPHLGN----IIgcvlsADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHA 109
Cdd:PRK12267 3 KKTFYITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 110 IHKGIYEWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNG------YTSsqsvdqLYCNQCEKFLADRfvtgtcpmcaydd 183
Cdd:PRK12267 78 GFKELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGdiykgeYEG------WYCVSCETFFTES------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 184 argdqcdgcgKLINavdlkDAKCHMCKATPE-VKQSTHiFLSLDKLQQKTTEHLDR--ELAKEDNRwsSNAVgiTKAWMK 260
Cdd:PRK12267 139 ----------QLVD-----GGKCPDCGREVElVKEESY-FFRMSKYQDRLLEYYEEnpDFIQPESR--KNEM--INNFIK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 261 LGLDPRCITRD-LKWGTAVPLDgfEKKVFYVWFDAPIGYLSitkcVLG------DNWTKWWknPENVELfnfVGKDNVAF 333
Cdd:PRK12267 199 PGLEDLSISRTsFDWGIPVPFD--PKHVVYVWIDALLNYIT----ALGygsdddELFKKFW--PADVHL---VGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 334 HAVMFPCsQLGANDnYTVVNNLCATEYLNYEDTKFSKSRGTGI--------FGdaaqgteipADIWRFYLLYMRPESQDT 405
Cdd:PRK12267 268 HAIYWPI-MLMALG-LPLPKKVFAHGWWLMKDGKMSKSKGNVVdpeelvdrYG---------LDALRYYLLREVPFGSDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 406 AFSWDDFVLKVNSELLNNLGNFINRALSFVANSFGGVVPEM-NLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILN 484
Cdd:PRK12267 337 DFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPAPgNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 485 VSRLGNQYMQAQTPWVLMKkDEEGKKRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPLFTPFPICY--LK 562
Cdd:PRK12267 417 LISRANKYIDETAPWVLAK-DEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLLEWggLP 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 563 AGHKIGQPSPLFQKLDpaqiaefkakfggsqdaqssaPKTAEKPKQQKKQAPTKDKKGDKKMAStaafveleqgakvisq 642
Cdd:PRK12267 496 AGTKVAKGEPLFPRID---------------------VEEEIAYIKEQMEGSAPKEPEEKEKKP---------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 643 liaqnlkkfdqakalftrnqlqrldgENKQLTIDvktlqhqlieletaagikqvpkpvvsctptptstpasgiiteapkk 722
Cdd:PRK12267 539 --------------------------EKPEITID---------------------------------------------- 546
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 723 eapstpapsepkkakeqkkgkggaaaapvddtiDVGRLDMRVGRIIKCEKHPDADALYVEQIDVGESAPRTVVSGLVRHV 802
Cdd:PRK12267 547 ---------------------------------DFDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFY 593
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 392900888 803 PLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCASSPDKVEIMEVPADSKPGTPV 856
Cdd:PRK12267 594 PPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEVPNGSKV 647
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
35-578 |
1.58e-96 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 312.59 E-value: 1.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 35 RNILITAALPYVNNVPHLGNIiGCVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGI 114
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 115 YEWFGIDFSHFGRTTTDHQTEICQDMFLKLHKNG--YTSSQSVdqLYCNQCEKFLADRFvtgtcpmcayddargdqcdgc 192
Cdd:PRK11893 80 WEALNISYDDFIRTTDPRHKEAVQEIFQRLLANGdiYLGKYEG--WYCVRCEEFYTESE--------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 193 gkLINavdlKDAKCHMCKATPEVKQSTHIFLSLDKLQQKTTEHLdreLAKEDNRWSSNAVGITKAWMKLGLDPRCITR-D 271
Cdd:PRK11893 137 --LIE----DGYRCPPTGAPVEWVEEESYFFRLSKYQDKLLELY---EANPDFIQPASRRNEVISFVKSGLKDLSISRtN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 272 LKWGTAVPLDgfEKKVFYVWFDAPIGYLSITKC-----VLGDNWTKWWknPENVelfNFVGKDNVAFHAVMFPcSQLGAN 346
Cdd:PRK11893 208 FDWGIPVPGD--PKHVIYVWFDALTNYLTALGYpddeeLLAELFNKYW--PADV---HLIGKDILRFHAVYWP-AFLMAA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 347 D---------NYtvvnnlcateYLNYEDTKFSKSRGTGIfgDAAQGTEI-PADIWRFYLLYMRPESQDTAFSWDDFVLKV 416
Cdd:PRK11893 280 GlplpkrvfaHG----------FLTLDGEKMSKSLGNVI--DPFDLVDEyGVDAVRYFLLREIPFGQDGDFSREAFINRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 417 NSELLNNLGNFINRALSFVANSFGGVVPEMN-LTNDDAEVLSEIhNECMQW-DKQFDGVHLKDAVKTILNVSRLGNQYMQ 494
Cdd:PRK11893 348 NADLANDLGNLAQRTLSMIAKNFDGKVPEPGaLTEADEALLEAA-AALLERvRAAMDNLAFDKALEAILALVRAANKYID 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 495 AQTPWVLMKKDEEgkkRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALP--LFTPFPICYLKAGHKIGQPSP 572
Cdd:PRK11893 427 EQAPWSLAKTDPE---RLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDEnrDFAALSWGRLAPGTTLPKPEP 503
|
....*.
gi 392900888 573 LFQKLD 578
Cdd:PRK11893 504 IFPRLE 509
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
755-857 |
4.07e-59 |
|
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: 196.68 E-value: 4.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 755 IDVGRLDMRVGRIIKCEKHPDADALYVEQIDVGESAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMC 834
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|....*
gi 392900888 835 ASSPD--KVEIMEVPADSKPGTPVV 857
Cdd:cd02799 81 ASNADheKVELLEPPEGAKPGERVT 105
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
416-544 |
1.52e-41 |
|
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: 148.41 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 416 VNSELLNNLGNFINRALSFVANSFGGVVPEM-NLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILNVSRLGNQYMQ 494
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFgGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392900888 495 AQTPWVLMKkdEEGKKRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQ 544
Cdd:cd07957 81 ETAPWKLAK--EEDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQ 128
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
38-615 |
2.98e-41 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 161.03 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 38 LITAALPYVNNVPHLGNIIgCVLSADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIYEW 117
Cdd:PLN02224 72 VLTTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 118 FGIDFSHFGRTTTDHQTEICQDMFLKLHKNGYTSSQSVDQLYCNQCEKfladrfvtgtcpmcaYDDARgdqcdgcgklin 197
Cdd:PLN02224 151 LDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEE---------------YKDEK------------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 198 avDLKDAKCHMCKATPEV-KQSTHIFLSLDKLQQKTTEHLDRELAKEDNRWSSNAVgitKAWMKLGLDPRCITRDL-KWG 275
Cdd:PLN02224 204 --ELLENNCCPVHQMPCVaRKEDNYFFALSKYQKPLEDILAQNPRFVQPSYRLNEV---QSWIKSGLRDFSISRALvDWG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 276 TAVPLDgfEKKVFYVWFDAPIGYLSitkCVLGDNWTKwwkNPENVELF------NFVGKDNVAFHAVMFPCSQLGANdnY 349
Cdd:PLN02224 279 IPVPDD--DKQTIYVWFDALLGYIS---ALTEDNKQQ---NLETAVSFgwpaslHLIGKDILRFHAVYWPAMLMSAG--L 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 350 TVVNNLCATEYLNYEDTKFSKSrgtgiFGDAAQGTEI----PADIWRFYLLYMRPESQDTAFSWDDFVLKVNSELLNNLG 425
Cdd:PLN02224 349 ELPKMVFGHGFLTKDGMKMGKS-----LGNTLEPFELvqkfGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 426 NFINRALSFVA-NSFGGVVPEMNLTNDDAEVLSEIHNECMQWDKQFDGVHLKDAVKTILNVSRLGNQYMQAQTPWVLMKK 504
Cdd:PLN02224 424 NLLNRTLGLLKkNCESTLVEDSTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQ 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 505 DEEGKKRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCGLPALPL----FTPFPICYLKAGHKIGQPSPLFQKLDpa 580
Cdd:PLN02224 504 GGVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFnsitWSDTKWGGLKGGQVMEQASPVFARIE-- 581
|
570 580 590
....*....|....*....|....*....|....*....
gi 392900888 581 qiaefkakFGGSQDAQSSAPKTAEKPKQQK----KQAPT 615
Cdd:PLN02224 582 --------LNPEKEEDEKKPKVGKKTGKAKvkvvEQTPT 612
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
762-855 |
2.92e-40 |
|
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: 143.15 E-value: 2.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 762 MRVGRIIKCEKHPDADALYVEQIDVGESAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCAS--SPD 839
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80
|
90
....*....|....*.
gi 392900888 840 KVEIMEVPADSKPGTP 855
Cdd:pfam01588 81 SVGLLEPPADVPPGTK 96
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
762-856 |
3.56e-39 |
|
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: 140.35 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 762 MRVGRIIKCEKHPDADALYVEQIDVGESAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCAS----S 837
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEelglE 80
|
90
....*....|....*....
gi 392900888 838 PDKVEIMEVPADSKPGTPV 856
Cdd:cd02153 81 EGSVGILELPEDAPVGDRI 99
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
756-856 |
1.04e-26 |
|
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: 104.89 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 756 DVGRLDMRVGRIIKCEKHPDADALYVEQIDVGESaPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCA 835
Cdd:cd02800 5 DFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEE-ERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAA 83
|
90 100
....*....|....*....|.
gi 392900888 836 SSPDKVEIMEVPADSKPGTPV 856
Cdd:cd02800 84 EDGGKLKLLTPDEEVEPGSRV 104
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
37-407 |
2.34e-26 |
|
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: 110.59 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 37 ILITAALPYVNNVPHLGNIIGCVLsADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEG-------------CTPREL 103
Cdd:cd00668 2 FYVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGgrkkktiwieefrEDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 104 CDKYHAIHKGIYEWFGI--DFSHFGRTTTDHQTEICQDMFLKLHKNGYtssqsvdqlycnqcekfladrfvtgtcpmcAY 181
Cdd:cd00668 81 VEEMSGEHKEDFRRLGIsyDWSDEYITTEPEYSKAVELIFSRLYEKGL------------------------------IY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 182 DDARgdqcdgcgklinavdlkdakchmckatpEVKQSTHIFLSLDKLQQKTTEHLdRELAKEDNRWSSNavgiTKAWMKL 261
Cdd:cd00668 131 RGTH----------------------------PVRITEQWFFDMPKFKEKLLKAL-RRGKIVPEHVKNR----MEAWLES 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 262 GLDpRCITRDLKWGTAVPLDgfekkVFYVWFDAPIGYLSITKCVLGDNWTK-WWKnpenvELFNFVGKDNVAFHAVMFPC 340
Cdd:cd00668 178 LLD-WAISRQRYWGTPLPED-----VFDVWFDSGIGPLGSLGYPEEKEWFKdSYP-----ADWHLIGKDILRGWANFWIT 246
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392900888 341 SQLGANDNYTVVNNLCATEYLNYEDTKFSKSRGTGIFGDAAQgTEIPADIWRFYLLYMRPESQDTAF 407
Cdd:cd00668 247 MLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVV-EKYGADALRYYLTSLAPYGDDIRL 312
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
751-856 |
1.87e-23 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 106.86 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 751 VDDTIDVGRLD-MRVGRIIKCEKHPDADALYVEQIDVGEsAPRTVVSGL--VR---HVPLDqMQNRLVVVLCNLKPAKMR 824
Cdd:COG0073 32 VEDFEKVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnVYagdKVPEA-LVGAQVPGVVNLKPRKIR 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 392900888 825 GVESRAMVMCAS----SPDKVEIMEVPADSKPGTPV 856
Cdd:COG0073 110 GVESEGMLCSAEelglGEDHDGILELPEDAPPGDDA 145
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
756-856 |
4.10e-23 |
|
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: 94.62 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 756 DVGRLDMRVGRIIKCEKHPDA-DALYVEQIDVGESAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMC 834
Cdd:cd02798 5 DFEKVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLG 84
|
90 100
....*....|....*....|...
gi 392900888 835 ASSP-DKVEIMEVPADSKPGTPV 856
Cdd:cd02798 85 ADDEgGEVVLLVPDREVPNGAKV 107
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
719-856 |
2.65e-21 |
|
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: 90.57 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 719 APKKEAPSTPAPSEPkkakeqkkgkggaaaaPVDDTI---DVGRLDMRVGRIIKCEKHPDADALYVEQIDVGESApRTVV 795
Cdd:TIGR00399 12 AKKKEKKDEGEKALE----------------PQKETItidDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIV 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392900888 796 SGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCASSPDKVEIMEVP-ADSKPGTPV 856
Cdd:TIGR00399 75 SGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPdQEAIAGERI 136
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
764-856 |
1.30e-14 |
|
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.
Pssm-ID: 239196 [Multi-domain] Cd Length: 103 Bit Score: 70.23 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 764 VGRIIKCEKHPDADALYVEQIDVGESAPRTVVSG--LVRhvpldqmQNRLVVV------LCN---LKPAKMRGVESRAMv 832
Cdd:cd02796 3 VGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGapNVR-------AGDKVVValpgavLPGglkIKKRKLRGVESEGM- 74
|
90 100
....*....|....*....|....*....
gi 392900888 833 MCASS----PDKVE-IMEVPADSKPGTPV 856
Cdd:cd02796 75 LCSAKelglGEDSDgIIELPEDAPVGTDI 103
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
759-839 |
1.51e-14 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 70.63 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 759 RLDMRVGRIIKCEKHPDADAL-YVEQIDVG-ESAPRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVMCAS 836
Cdd:PRK10089 11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFE 90
|
...
gi 392900888 837 SPD 839
Cdd:PRK10089 91 DED 93
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
764-856 |
1.23e-13 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 75.21 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 764 VGRIIKCEKHPDADALYVEQIDVGESaPRTVVSGL--VRhvpldqmQNRLVVV------LCN---LKPAKMRGVESRAMv 832
Cdd:PRK00629 47 VGKVLECEKHPNADKLRVCQVDVGEE-PLQIVCGApnVR-------AGDKVPValpgavLPGgfkIKKAKLRGVESEGM- 117
|
90 100
....*....|....*....|....*....
gi 392900888 833 MCASS----PDKVE-IMEVPADSKPGTPV 856
Cdd:PRK00629 118 LCSASelglSDDHDgIIELPEDAPVGTDA 146
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
44-303 |
1.89e-10 |
|
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: 63.80 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 44 PYVNNVPHLGNIIGCVLsADVFARYCNLRGHQTFYVGGTDEYGTATETK----ALQEGCTPR--------ELC----DKY 107
Cdd:cd00817 10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVVvekkLGIEGKTRHdlgreeflEKCwewkEES 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 108 HAIhkgIYEWF-----GIDFSHFGRTTTDHQTEICQDMFLKLHKNG--YTSSQSVdqLYCNQCEKFLADRFVtgtcpmca 180
Cdd:cd00817 89 GGK---IREQLkrlgaSVDWSREYFTMDPGLSRAVQEAFVRLYEKGliYRDNRLV--NWCPKLRTAISDIEV-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 181 yddargdqCDGCGKLInavdlkdakchmckatpEVKQSTHIFLSLDKLQQKTTEHLDRELAK---ED--NRWSSnavgit 255
Cdd:cd00817 156 --------CSRSGDVI-----------------EPLLKPQWFVKVKDLAKKALEAVKEGDIKfvpERmeKRYEN------ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 392900888 256 kaWMKlGLDPRCITRDLKWGTAVPldgfekkVFYV-----WFDAPIGYLSITK 303
Cdd:cd00817 205 --WLE-NIRDWCISRQLWWGHRIP-------AWYCkdgghWVVAREEDEAIDK 247
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
488-594 |
5.00e-09 |
|
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 437135 [Multi-domain] Cd Length: 152 Bit Score: 55.97 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 488 LGNQYMQAQTPWVLMKKDEEgkkRAGTIIGVAANIAYHVSVLLYPIMPTISATIREQCG-------------LPALPlft 554
Cdd:pfam19303 47 AGNEYLQEAAPWTTFKTDPE---AAAAQVRLALNLIRLYAVLSAPFIPDAAAAMLAAMGtddaawpddvaaaLTALP--- 120
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 392900888 555 pfpicylkAGHKIGQPSPLFQKLDPAQIAEFKAKFGGSQD 594
Cdd:pfam19303 121 --------AGHAFTVPEVLFAKITDEQREEWQERFAGTRA 152
|
|
| chap_CsaA |
TIGR02222 |
export-related chaperone protein CsaA; This model describes Bacillus subtilis CsaA, an ... |
756-856 |
1.24e-08 |
|
export-related chaperone protein CsaA; This model describes Bacillus subtilis CsaA, an export-related chaperone that interacts with the Sec system, and related proteins from a number of other bacteria and archaea. The crystal structure is known for the homodimer from Thermus thermophilus. [Protein fate, Protein folding and stabilization, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131277 [Multi-domain] Cd Length: 107 Bit Score: 53.57 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 756 DVGRLDMRVGRIIKCEKHPDA-DALYVEQIDVGES-APRTVVSGLVRHVPLDQMQNRLVVVLCNLKPAKMRGVESRAMVM 833
Cdd:TIGR02222 3 DFEKLDLRVGRIVRAEPFPEArKPAYKLWVDFGTEiGVKQSSAQITKLYKPEDLIGRLVVAVVNFPPKQIAGFLSEVLVL 82
|
90 100
....*....|....*....|....
gi 392900888 834 CA-SSPDKVEIMEVPADSKPGTPV 856
Cdd:TIGR02222 83 GViDEQGRVVLLQPDRPVPNGTKI 106
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
206-544 |
4.58e-06 |
|
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: 50.44 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 206 CHMCKATPEVKQSTHIFLSLDKLQQKTTEHLDRELAK-EDNRWSSNavgiTKAWMKlGLDPRCITRDLKWGTAVPldgfe 284
Cdd:TIGR00422 343 CWRSGTVVEPLLSKQWFVKVEKLADKALEAAEEGEIKfVPKRMEKR----YLNWLR-NIKDWCISRQLIWGHRIP----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 285 kkvfyVWFDAPIGYLSITK-CVLGDNWTKWWKNpenvelFNFVGKDNVA---FHAVMFPCSQLGANDN------------ 348
Cdd:TIGR00422 413 -----VWYCKECGEVYVAKeEPLPDDKTNTGPS------VELEQDTDVLdtwFSSSLWPFSTLGWPDEtkdlkkfyptdl 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 349 -------------YTVVNNLCATEYLNYEDT------------KFSKSRGTGI--------FGdaaqgteipADIWRFYL 395
Cdd:TIGR00422 482 lvtgydiiffwvaRMIFRSLALTGQVPFKEVyihglvrdeqgrKMSKSLGNVIdpldviekYG---------ADALRFTL 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 396 LYMRPESQDTAFSWDDfvLKVNSELLNNLGNFINRALSFVANSFGGVVPEMNLTNDDAEVLSEIHNECMQWDKQFDGVHL 475
Cdd:TIGR00422 553 ASLVTPGDDINFDWKR--VESARNFLNKLWNASRFVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRF 630
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392900888 476 KDAVKTILNV--SRLGNQYMQAQTPwVLMKKDEEGKKragtiigVAANIAYHV----SVLLYPIMPTISATIREQ 544
Cdd:TIGR00422 631 AEAAKALYEFiwNDFCDWYIELVKY-RLYNGNEAEKK-------AARDTLYYVldkaLRLLHPFMPFITEEIWQH 697
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
44-148 |
1.63e-05 |
|
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: 48.90 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 44 PYVNNVPHLGNIIGCVLSaDVFARYCNLRGHQTFYVGGTDEYGTATETK----ALQEGCT----PRElcdkyhAIHKGIY 115
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQ-DIIARYKRMKGYNVLWLPGTDHAGIATQVKvekkLGAEGKTkhdlGRE------EFREKIW 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 392900888 116 EW----------------FGIDFSHFGRTTTDHQTEICQDMFLKLHKNG 148
Cdd:TIGR00422 115 EWkeesggtiknqikrlgASLDWSRERFTMDEGLSKAVKEAFVRLYEKG 163
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
44-133 |
4.93e-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: 44.39 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 44 PYVNNVPHLGNIIGCVLsADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIYEWF---GI 120
Cdd:cd00802 6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVEYMflqAA 84
|
90
....*....|...
gi 392900888 121 DFSHFGRTTTDHQ 133
Cdd:cd00802 85 DFLLLYETECDIH 97
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
44-169 |
6.94e-05 |
|
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: 46.63 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 44 PYVNNVPHLGNIIGCVLSaDVFARYCNLRGHQTFYVGGTDEYGTATE-------------------TKALQEGCtpRELC 104
Cdd:pfam00133 32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEqvvekklgikekktrhkygREEFREKC--REWK 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392900888 105 DKYHAIHKGIYEWFG--IDFSHFGRTTTDHQTEICQDMFLKLHKNG--YTSSQSVDqlYCNQCEKFLAD 169
Cdd:pfam00133 109 MEYADEIRKQFRRLGrsIDWDREYFTMDPELEAAVWEVFVRLHDKGliYRGKKLVN--WSPALNTALSN 175
|
|
| PheT |
COG0072 |
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ... |
764-857 |
1.10e-04 |
|
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439842 [Multi-domain] Cd Length: 793 Bit Score: 45.93 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 764 VGRIIKCEKHPDADALYVEQIDVGESAPRTVVSGLVRHVPLDqmqnrLVVVLCN---------LKPAKMRGVESRAMvMC 834
Cdd:COG0072 47 VVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVGV-----VVVAAPGgavlpggfkIKKAKIRGVESSGM-LC 120
|
90 100
....*....|....*....|....*...
gi 392900888 835 AS-----SPDKVEIMEVPADSKPGTPVV 857
Cdd:COG0072 121 SEeelglGEDHDGIIVLPPDAPVGGDAR 148
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
39-149 |
1.12e-03 |
|
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: 42.23 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 39 ITAALPYVNNVPHLGNIIGCVLsADVFARYCNLRGHQTFYVGGTDEYGTATETKALQEGCTPRELCDKYHAIHKGIYEWF 118
Cdd:cd00812 4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRM 82
|
90 100 110
....*....|....*....|....*....|....
gi 392900888 119 GIDFShFGR--TTTDHQ-TEICQDMFLKLHKNGY 149
Cdd:cd00812 83 GFSYD-WRRefTTCDPEyYKFTQWLFLKLYEKGL 115
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
44-149 |
3.14e-03 |
|
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: 40.68 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900888 44 PYVNNVPHLGNIIGCVLSaDVFARYCNLRGHQTFYVGGTDEYGTATETKALQEG-------------------CtpRELC 104
Cdd:cd00818 10 PYANGLPHYGHALNKILK-DIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELgisgkkdiekmgiaefnakC--REFA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 392900888 105 DKYHAIHKGIYEWFGI--DFSHFGRTTTDHQTEICQDMFLKLHKNGY 149
Cdd:cd00818 87 LRYVDEQEEQFQRLGVwvDWENPYKTMDPEYMESVWWVFKQLHEKGL 133
|
|
| |
