|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
6-676 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1282.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDF 85
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 86 AGFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 166 YSPTELIDPKSAVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 244
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 245 DAPGKYFYVWLDAPIGYMGSFKNLCDKRGDLDFDEFWRKDSTTELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHG 324
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGGLDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAHG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 325 YVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRF 404
Cdd:PRK00133 322 FLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKRF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 405 GGKLAASLADPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANRYVDEQAPWVVAKQEGRDAdlQAICSMGINLF 484
Cdd:PRK00133 402 DGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNLF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 485 RVLMTYLKPVLPSLTERAEAFLN-GELSWEGIQQPLLDHTVNPFKALFNRIDLDKVNDMVNASKEDMA--ASQAPVSGPL 561
Cdd:PRK00133 480 RALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEAAAakAAAAAAAAPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 562 ADDPIQETITFDDFAKVDMRIALIKSADLVDGSDKLLKLQLDLGGESRQIFSGIRSAYpDPKLLEGRLTIMVANLAPRKM 641
Cdd:PRK00133 560 AEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIKSAY-DPEELVGKLVVMVANLAPRKM 638
|
650 660 670
....*....|....*....|....*....|....*
gi 491103850 642 RFGISEGMVMAAGPGGKEIFLLSPDSGAQPGMQVK 676
Cdd:PRK00133 639 KFGVSEGMVLAAGPGGGDLFLLEPDEGAKPGMRVK 673
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
6-543 |
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: 874.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDF 85
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 86 AGFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 166 YSPTELIDPKSAVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 244
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 245 DAPGKYFYVWLDAPIGYMGSFKNLCDKRG-DLDFDEFWrKDSTTELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 323
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGlPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 324 GYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 404 FGGKLAA----SLADPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANRYVDEQAPWVVAKQEGRDAdLQAICSM 479
Cdd:COG0143 398 FDGKVPEpgelTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491103850 480 GINLFRVLMTYLKPVLPSLTERAEAFLNGE---LSWEGIQQPLL-DHTVNPFKALFNRIDLDKVNDMV 543
Cdd:COG0143 477 LLEALRILAILLKPFLPETAEKILEQLGLEgdeLTWEDAGWPLPaGHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
9-535 |
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: 751.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 9 LVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDFAGF 88
Cdd:TIGR00398 2 LITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 89 GISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSP 168
Cdd:TIGR00398 82 NISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 169 TELIDPKSAVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 244
Cdd:TIGR00398 162 TELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 245 DAPGKYFYVWLDAPIGYMGSfknLCDKRGDL-DFDEFWRKDSTTELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 323
Cdd:TIGR00398 242 NDPNKVVYVWFDALIGYISS---LGILSGDTeDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 324 GYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:TIGR00398 319 GYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 404 FGGKLAASLA----DPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSM 479
Cdd:TIGR00398 398 FNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVCSM 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 491103850 480 ginLFRVLMTYLKPVLPSLTERAEAFLNGELSWEGIQQPLLDHTVNPFKALFNRID 535
Cdd:TIGR00398 478 ---LIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
9-396 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 629.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 9 LVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDFAGF 88
Cdd:pfam09334 2 LVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 89 GISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSP 168
Cdd:pfam09334 82 NISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 169 TELIDPKSAVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPDA 246
Cdd:pfam09334 162 TELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 247 PGKYFYVWLDAPIGYMGSFKNLCDKrgDLDFDEFWRKDSTTELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHGYV 326
Cdd:pfam09334 241 EGKVFYVWLDAPIGYISATKELSGN--EEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGYL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 327 TVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAkLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 396
Cdd:pfam09334 319 TYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR-NRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
7-371 |
1.86e-144 |
|
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: 423.10 E-value: 1.86e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 7 KLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDFA 86
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 87 GFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 166
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 167 sptelidpksavsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 243
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 244 PDAPGKYFYVWLDAPIGYMGSFKNLCDKRGDLDfdefWRKDSTTELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 323
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGNSW----WWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAH 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 491103850 324 GYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKlSSRIDDID 371
Cdd:cd00814 272 GYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
7-372 |
3.70e-116 |
|
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: 350.57 E-value: 3.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 7 KLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIK-------------PEEM 73
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGRkkktiwieefredPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 74 IAEMSQEHQQDFAGFGISYD--NYHSTHSDENRELSSLIYGRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkcks 151
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 152 pdqygdncevcgatysptelidpksavsgatpvmRDSEHFFFDLPSFSEMLQAWTRSGA-LQEQVANKMQEWFESGLQqW 230
Cdd:cd00668 137 ----------------------------------RITEQWFFDMPKFKEKLLKALRRGKiVPEHVKNRMEAWLESLLD-W 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 231 DISRDApYFGFEIPdapGKYFYVWLDAPIGYMGSFKNLCDKRgdldfdefWRKDSTTELYHFIGKDIVYFHSLFWPAMLE 310
Cdd:cd00668 182 AISRQR-YWGTPLP---EDVFDVWFDSGIGPLGSLGYPEEKE--------WFKDSYPADWHLIGKDILRGWANFWITMLV 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491103850 311 GSNFR-KPTNLFVHGYVTVN-GAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKLsSRIDDIDL 372
Cdd:cd00668 250 ALFGEiPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLA-PYGDDIRL 312
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
6-676 |
1.62e-105 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 334.46 E-value: 1.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDF 85
Cdd:PRK12267 4 KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 86 AGFGISYDNYHSTHSDENRELSSLIYGRLKENGFI-KNR-------------TISQLYDPEKgmflpdrfvkgtCPKCKs 151
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIyKGEyegwycvscetffTESQLVDGGK------------CPDCG- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 152 pdqygdncevcgatySPTELIDPKSavsgatpvmrdsehFFFDLPSFSEMLQAWTRSGA---LQEQVANKMQEWF-ESGL 227
Cdd:PRK12267 151 ---------------REVELVKEES--------------YFFRMSKYQDRLLEYYEENPdfiQPESRKNEMINNFiKPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 228 QQWDISRDAPYFGFEIPDAPGKYFYVWLDA------PIGYMGSfknlcdkrGDLDFDEFWRKDsttelYHFIGKDIVYFH 301
Cdd:PRK12267 202 EDLSISRTSFDWGIPVPFDPKHVVYVWIDAllnyitALGYGSD--------DDELFKKFWPAD-----VHLVGKDILRFH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 302 SLFWPAMLEGSNFRKPTNLFVHGYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYyaakLSSRI---DDIDLNLEDFV 378
Cdd:PRK12267 269 AIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY----LLREVpfgSDGDFSPEALV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 379 QRVNADIVNKVVNLASRNAGFINKRFGGKLAASLA----DPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANRY 454
Cdd:PRK12267 345 ERINSDLANDLGNLLNRTVAMINKYFDGEIPAPGNvtefDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANKY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 455 VDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPSLTER---------AEAFLNGELSWEGIQqplLDHTVN 525
Cdd:PRK12267 425 IDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKifeqlgleeELTSWESLLEWGGLP---AGTKVA 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 526 PFKALFNRIDLDKvndMVNASKEDMAASQAPVSGPLADDPIQETITFDDFAKVDMRIALIKSADLVDGSDK-LLKLQLDL 604
Cdd:PRK12267 502 KGEPLFPRIDVEE---EIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLEAEKVEKSDKlLKLQVDLG 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491103850 605 GGESRQIFSGIRSAYPdPKLLEGRLTIMVANLAPRKMRFGISEGMVMAAGPGGKeIFLLSPDSGAQPGMQVK 676
Cdd:PRK12267 579 EEEPRQIVSGIAKFYP-PEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGK-LTLLTVDKEVPNGSKVK 648
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
6-537 |
1.56e-98 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 311.82 E-value: 1.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDF 85
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 86 AGFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckspdqygdnCEVCGAT 165
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 166 YSPTELIDPK--SAVSGATPVMRDSEHFFFDLPSFSEMLQAW--TRSGALQ-EQVANKMQEWFESGLQQWDISR---DAp 237
Cdd:PRK11893 132 YTESELIEDGyrCPPTGAPVEWVEEESYFFRLSKYQDKLLELyeANPDFIQpASRRNEVISFVKSGLKDLSISRtnfDW- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 238 yfGFEIPDAPGKYFYVWLDAPIGYM-GSFKNLCDKRGDLDFDEFWRKDSttelyHFIGKDIVYFHSLFWPAMLEGSNFRK 316
Cdd:PRK11893 211 --GIPVPGDPKHVIYVWFDALTNYLtALGYPDDEELLAELFNKYWPADV-----HLIGKDILRFHAVYWPAFLMAAGLPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 317 PTNLFVHGYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYaAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 396
Cdd:PRK11893 284 PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFL-LREIPFGQDGDFSREAFINRINADLANDLGNLAQRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 397 AGFINKRFGGKL----AASLADPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANRYVDEQAPWVVAKQEgrDAD 472
Cdd:PRK11893 363 LSMIAKNFDGKVpepgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTD--PER 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491103850 473 LQAICSMGINLFRVLMTYLKPVLPSLTERAEAFLNGE---------LSWEGIQQpllDHTVNPFKALFNRIDLD 537
Cdd:PRK11893 441 LATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEedenrdfaaLSWGRLAP---GTTLPKPEPIFPRLEEE 511
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
6-676 |
7.10e-84 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 281.28 E-value: 7.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGSIHLGHMLEHI-QADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQD 84
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 85 FAGFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKSPDQYGDNCEVC 162
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 163 GATYSPTELIDPKSAVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQ-VANKMQ---EWFESGLQQWDISRD--- 235
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGwSQNAIQttnAWLRDGLKPRCITRDlkw 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 236 ---APYFGFEipdapGKYFYVWLDAPIGYMGSFKNLCDkrgdlDFDEFWRKDSTTELYHFIGKDIVYFHSLFWPAMLEGS 312
Cdd:PLN02610 257 gvpVPLEKYK-----DKVFYVWFDAPIGYVSITACYTP-----EWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLGT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 313 --NFRKPTNLFVHGYVTVNGAKMSKSRGTFIKAG-TYLQHLDADCLRYYYaakLSSR--IDDIDLNLEDFVQRVNADIVN 387
Cdd:PLN02610 327 geNWTMMKTISVTEYLNYEGGKFSKSKGVGVFGNdAKDTNIPVEVWRYYL---LTNRpeVSDTLFTWADLQAKLNSELLN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 388 KVVNLASRNAGFINKRFGGKLAASLADP------ALYQTFTDAADSIAEAY-ASRES---GRAIREIMALADLANRYVDE 457
Cdd:PLN02610 404 NLGNFINRVLSFIAKPPGAGYGSVIPDApgaeshPLTKKLAEKVGKLVEQYvEAMEKvklKQGLKTAMSISSEGNAYLQE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 458 QAPWVVAKQegrDADLQAI---CSMGinLFRVLMTYLKPVLPSLTERAEAFLN------------GELS-----WE---- 513
Cdd:PLN02610 484 SQFWKLYKE---DKPSCAIvvkTSVG--LVYLLACLLEPFMPSFSKEVLKQLNlppeslslsdekGEVArakrpWElvpa 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 514 ----GIQQPLL----DHTVNPFKALF--------------------NRIDLDKVNDmVNASKEDMAASQAPVSGPLADDP 565
Cdd:PLN02610 559 ghkiGTPEPLFkelkDEEVEAYREKFagsqadraaraeaaeakklaKQLKKKALSD-GGKKKQGKKAGGGGKSKAAAERE 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 566 IqetitfdDFAKVDMRIALIKSADL-VDGSDKLLKLQLDLGGESRQIFSGIRSAYPDPKlLEGRLTIMVANLAPRKMRFG 644
Cdd:PLN02610 638 I-------DVSRLDIRVGLIVKAEKhPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEE-MQNRKVCVLCNLKPAAMRGI 709
|
730 740 750
....*....|....*....|....*....|...
gi 491103850 645 ISEGMVMAAGPG-GKEIFLLSPDSGAQPGMQVK 676
Cdd:PLN02610 710 KSQAMVLAASNSdHTKVELVEPPESAAVGERVT 742
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-537 |
7.16e-53 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 192.62 E-value: 7.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 5 AKKLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQD 84
Cdd:PLN02224 68 ADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 85 FAGFGISYDNYHSTHSDENRELSSLIYGRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkspDQYGDNCEVCGA 164
Cdd:PLN02224 148 WKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDEKELLEN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 165 TYSPtelidpksaVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVA---NKMQEWFESGLQQWDISRDAPYFGF 241
Cdd:PLN02224 209 NCCP---------VHQMPCVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSyrlNEVQSWIKSGLRDFSISRALVDWGI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 242 EIPDAPGKYFYVWLDAPIGYMGSFKNlCDKRGDLDFDEFWRKDSTtelYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLF 321
Cdd:PLN02224 280 PVPDDDKQTIYVWFDALLGYISALTE-DNKQQNLETAVSFGWPAS---LHLIGKDILRFHAVYWPAMLMSAGLELPKMVF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 322 VHGYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKLSSRiDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFIN 401
Cdd:PLN02224 356 GHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLK 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 402 KRFGGKLAASLADPALYQTFTDAADSIAEA----YASRESGRAIREIMALADLANRYVDEQAPWVVAKQEGRDADLQAI- 476
Cdd:PLN02224 435 KNCESTLVEDSTVAAEGVPLKDTVEKLVEKaqtnYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAKd 514
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491103850 477 CSMGINLFRVLMTYLKPVLPSLTERAEAFLN-----------GELSWEGIQQPLLDHTVNPfkaLFNRIDLD 537
Cdd:PLN02224 515 LVIILEVMRVIAVALSPIAPCLSLRIYSQLGysedqfnsitwSDTKWGGLKGGQVMEQASP---VFARIELN 583
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
538-676 |
1.36e-41 |
|
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: 147.57 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 538 KVNDMVNASKEDMAAsqaPVSGPLADDPIQETITFDDFAKVDMRIALIKSADLVDGSDKLLKLQLDLGGESRQIFSGIRS 617
Cdd:TIGR00399 3 KIEELKLKGAKKKEK---KDEGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491103850 618 AYPdPKLLEGRLTIMVANLAPRKMRFGISEGMVMAAGPGGKEIFLLSPDSGAQPGMQVK 676
Cdd:TIGR00399 80 YYT-PEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK 137
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
374-506 |
1.47e-38 |
|
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: 138.78 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 374 LEDFVQRVNADIVNKVVNLASRNAGFINKRFGGKLAAslaDPALYQTFTDAADSIAEAYASRESGRAIREIMALADLANR 453
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTEE---DEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491103850 454 YVDEQAPWVVAKQEGRDAdLQAICSMGINLFRVLMTYLKPVLPSLTERAEAFL 506
Cdd:cd07957 78 YIDETAPWKLAKEEDPER-LATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
570-676 |
2.60e-34 |
|
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: 126.08 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 570 ITFDDFAKVDMRIALIKSADLVDGSDKLLKLQLDLGGESRQIFSGIRSAYPdPKLLEGRLTIMVANLAPRKMRFGISEGM 649
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYP-PEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100
....*....|....*....|....*..
gi 491103850 650 VMAAGPGGKeIFLLSPDSGAQPGMQVK 676
Cdd:cd02800 80 ILAAEDGGK-LKLLTPDEEVEPGSRVS 105
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-358 |
8.33e-18 |
|
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: 84.99 E-value: 8.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 7 KLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQDFA 86
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 87 GFGISYdnyhsthsDENRELSSL----------IYGRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkCKSPDQYG 156
Cdd:cd00812 81 RMGFSY--------DWRREFTTCdpeyykftqwLFLKLYEKGLAYKKEAPVNW-------------------CKLLDQWF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 157 DNcevcgatYSPTELIDpksavsgatpvmrdsehfffDLPSFSEMLQAWTrsgalqEQVANKMQEWFesglqqwDISRDA 236
Cdd:cd00812 134 LK-------YSETEWKE--------------------KLLKDLEKLDGWP------EEVRAMQENWI-------GCSRQR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 237 pYFGFEIP---------DApGKYFYVWLDA---PIGYMGSFKNLCDKrgdldFDEFWRKDstteLYHFiGKDIVYFH--- 301
Cdd:cd00812 174 -YWGTPIPwtdtmeslsDS-TWYYARYTDAhnlEQPYEGDLEFDREE-----FEYWYPVD----IYIG-GKEHAPNHlly 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 302 SLFWPAML--EGSNFRK-PTNLFVHGYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYY 358
Cdd:cd00812 242 SRFNHKALfdEGLVTDEpPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLY 301
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
607-674 |
9.01e-18 |
|
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: 78.82 E-value: 9.01e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491103850 607 ESRQIFSGIRSAYPDPKLLeGRLTIMVANLAPRKMRFGISEGMVMAAGP-GGKEIFLLSPDSGAQPGMQ 674
Cdd:pfam01588 29 EPRQIVSGAVNVYPPEELV-GRLVVVVANLKPAKLRGVESEGMILSAEElDGGSVGLLEPPADVPPGTK 96
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
607-675 |
1.53e-16 |
|
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: 75.25 E-value: 1.53e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491103850 607 ESRQIFSGIRSAYPdPKLLEGRLTIMVANLAPRKMRFGISEGMVMAA---GPGGKEIFLLSPDSGAQPGMQV 675
Cdd:cd02153 29 KPRQIVSGAANVYP-PEELVGKKVVVAVNLKPKKLRGVESEGMLLSAeelGLEEGSVGILELPEDAPVGDRI 99
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
15-358 |
1.55e-15 |
|
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: 78.43 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKA-QQMGIKPEEMIAEMS--------------- 78
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMGiaefnakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 79 -QEHQQDFAGFGI--SYDNYHSTHSDENRELSSLIYGRLKENGfiknrtisQLYDPEKGMFLPdrfvkgtcpkckspdqy 155
Cdd:cd00818 90 vDEQEEQFQRLGVwvDWENPYKTMDPEYMESVWWVFKQLHEKG--------LLYRGYKVVPWP----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 156 gdncevcgatyspteLIdpksavsgatpvMRDSEHFFFDLPSF-SEMLQAWTRSGALQEQVANKMQEWFEsGLQQWDISR 234
Cdd:cd00818 145 ---------------LI------------YRATPQWFIRVTKIkDRLLEANDKVNWIPEWVKNRFGNWLE-NRRDWCISR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 235 DApYFGFEIP----DAPGKY--------FYVWLDApiGYMgSFKNLCDKRGDLDFDEFWRKDSTTElyhfiGKDIV--YF 300
Cdd:cd00818 197 QR-YWGTPIPvwycEDCGEVlvrrvpdvLDVWFDS--GSM-PYAQLHYPFENEDFEELFPADFILE-----GSDQTrgWF 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491103850 301 HSLfwpaMLEGS-NFRKP--TNLFVHGYV-TVNGAKMSKSRGTFIKAGTYLQHLDADCLRYY 358
Cdd:cd00818 268 YSL----LLLSTaLFGKApyKNVIVHGFVlDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
561-672 |
5.15e-15 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 78.74 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 561 LADDPIQETITFDDFAKVD----MRIALIKSADLVDGSDKLLKLQLDLGGESRQIFSGIRSAYPD---PKLLEGRLTIMV 633
Cdd:COG0073 21 LAEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYAGdkvPEALVGAQVPGV 100
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491103850 634 ANLAPRKMRFGISEGMVMAA---GPGGKEIFLLSPDSGAQPG 672
Cdd:COG0073 101 VNLKPRKIRGVESEGMLCSAeelGLGEDHDGILELPEDAPPG 142
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
15-372 |
5.88e-13 |
|
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: 71.12 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQ-QMGIKPE-----------EMIAEMSQEHQ 82
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 83 ----QDFAGFGISYD--NYHSTHSDENRELSSLIYGRLKENGFIknrtisqlydpEKGMFLPDRfvkgtCPKCKSPDQyg 156
Cdd:cd00817 90 gkirEQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLI-----------YRDNRLVNW-----CPKLRTAIS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 157 dNCEVCGATYSPTElidpksavsgatPVMrdSEHFFFDLPSFSEMLQAWTRSGALQ---EQVANKMQEWFESgLQQWDIS 233
Cdd:cd00817 152 -DIEVCSRSGDVIE------------PLL--KPQWFVKVKDLAKKALEAVKEGDIKfvpERMEKRYENWLEN-IRDWCIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 234 RDApYFGFEIPdapgkyfyVWLDAPIGY--------------MGSFKNLCDK---RGDLD-----FDEF--------WRK 283
Cdd:cd00817 216 RQL-WWGHRIP--------AWYCKDGGHwvvareedeaidkaAPEACVPCGGeelKQDEDvldtwFSSSlwpfstlgWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 284 DSTTELYHF------IGKDIVYfhslFWPA--MLEGSNF--RKP-TNLFVHGYV-TVNGAKMSKSRGTFI-------KAG 344
Cdd:cd00817 287 ETKDLKKFYptsllvTGHDIIF----FWVArmIMRGLKLtgKLPfKEVYLHGLVrDEDGRKMSKSLGNVIdpldvidGYG 362
|
410 420
....*....|....*....|....*...
gi 491103850 345 tylqhldADCLRyYYAAKLSSRIDDIDL 372
Cdd:cd00817 363 -------ADALR-FTLASAATQGRDINL 382
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
570-675 |
6.15e-12 |
|
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: 62.64 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 570 ITFDDFAKVDMRIALIKSADL------------VD-GsdkllklqldlGGESRQIFSGIrSAYPDPKLLEGRLTIMVANL 636
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEDfpearkpayklkVDfG-----------EIGVKQSSAQI-TKYYKPEELIGRQVVAVVNF 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 491103850 637 APRKMRFGISEGMVMAAGPGGKEIFLLSPDSGAQPGMQV 675
Cdd:cd02798 69 PPKQIAGVLSEVLVLGADDEGGEVVLLVPDREVPNGAKV 107
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
573-675 |
2.21e-11 |
|
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: 60.70 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 573 DDFAKVDMRIALIKSA--------------DLVDGsdkllklqldlggESRQIFSGIRSAYPdPKLLEGRLTIMVANLAP 638
Cdd:cd02799 1 VDPSRLDIRVGKILKVrkhpdadslyveeiDLGEE-------------EPRTIVSGLVKFVP-LEQMQNRLVVVLCNLKP 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 491103850 639 RKMRfGI-SEGMVMAAGPGGKEIF-LLSPDSGAQPGMQV 675
Cdd:cd02799 67 RKMR-GVkSQGMVLCASNADHEKVeLLEPPEGAKPGERV 104
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
15-80 |
2.92e-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: 67.03 E-value: 2.92e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKA-QQMGIKPEEmIAEMSQE 80
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIKKKD-IEKVGIA 120
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
15-120 |
9.79e-11 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 65.21 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHF-ICADDaHGTPIMLKAQ-QMGIKP------------EEMIAEMSQE 80
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcRELTDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491103850 81 HQQDFAGFGISYD--NYHSTHSDENRELSSLIYGRLKENGFI 120
Cdd:PRK13208 126 FRELWRRLGLSVDwsLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
15-152 |
1.92e-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: 63.97 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKA-QQMGIKPEEMIAEMS--------------- 78
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVeKKLGIKEKKTRHKYGreefrekcrewkmey 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491103850 79 -QEHQQDFAGFGISYD--NYHSTHSDENRELSSLIYGRLKENGFIknrtisqlYDPEKGMFLpdrfvkgtCPKCKSP 152
Cdd:pfam00133 112 aDEIRKQFRRLGRSIDwdREYFTMDPELEAAVWEVFVRLHDKGLI--------YRGKKLVNW--------SPALNTA 172
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
15-65 |
4.59e-10 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 62.87 E-value: 4.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQ 65
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
15-151 |
4.26e-08 |
|
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: 56.61 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQ-QMGIKPE-----------EMIAEMSQEH- 81
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESg 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491103850 82 ---QQDFAGFGISYDnyhstHSDENRELSSLIYGRLKEnGFIKnrtisqLYdpEKGMFLPDRFVKGTCPKCKS 151
Cdd:TIGR00422 122 gtiKNQIKRLGASLD-----WSRERFTMDEGLSKAVKE-AFVR------LY--EKGLIYRGEYLVNWDPKLNT 180
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
568-672 |
8.70e-08 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 50.98 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 568 ETITFDDFAKVDMRIALIKSADLVDgsdkllklqldlggESR------QI-FS---GIR--SA----YPDPKLLEGRLTI 631
Cdd:PRK10089 2 ETITYEDFEKVDIRVGTIVEAEPFP--------------EARkpayklWIdFGeeiGVKqsSAqitpHYTPEELIGKQVV 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 491103850 632 MVANLAPRKMRFGISEGMVMAAGPGGKEIFLLSPDSGAQPG 672
Cdd:PRK10089 68 AVVNFPPKQIAGFMSEVLVLGFEDEDGEVVLLTPDRPVPNG 108
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
21-152 |
5.77e-06 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 49.87 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 21 IHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKA--------QQMGI------KPEEMIAEM--------- 77
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAeriargdpETIELykslygIPEEELEKFkdpeyivey 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 78 -SQEHQQDFAGFGISYD---NYHSThsDEnrELSSLI---YGRLKENGFIknrtisqlydpekgmflpdrfVKGT----- 145
Cdd:PRK12300 81 fSEEAKEDMKRIGYSIDwrrEFTTT--DP--EYSKFIewqFRKLKEKGLI---------------------VKGShpvry 135
|
....*..
gi 491103850 146 CPKCKSP 152
Cdd:PRK12300 136 CPNDNNP 142
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
196-594 |
9.02e-06 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 49.22 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 196 PSFSEMLQAWTRsgALQEQVANKMQEWFESgLQQWDISRDApYFGFEIPD--APGKYFYVWLDAPigymgSFKNLCDK-- 271
Cdd:PRK14900 385 PAIEAVEQGRTR--FIPEQWTNTYMAWMRN-IHDWCISRQL-WWGHQIPAwyCPDGHVTVARETP-----EACSTCGKae 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 272 -RGDLDFDEFWRK------------DSTTELYHF-------IGKDIVYFhslfWPA--MLEGSNFRKPT---NLFVHGYV 326
Cdd:PRK14900 456 lRQDEDVLDTWFSsglwpfstmgwpEQTDTLRTFyptsvmeTGHDIIFF----WVArmMMMGLHFMGEVpfrTVYLHPMV 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 327 -TVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAkLSSRIDDIDLNlEDFVQRVNAdIVNKVVNlASRNA-----GFI 400
Cdd:PRK14900 532 rDEKGQKMSKTKGNVIDPLVITEQYGADALRFTLAA-LTAQGRDIKLA-KERIEGYRA-FANKLWN-ASRFAlmnlsGYQ 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 401 NK-RFGGKLAASLAD----PALYQTFTDAADSIaEAYASRESGRAIREIMaLADLANRYVDEQAPWVVAKQEGRDADLQA 475
Cdd:PRK14900 608 ERgEDPARLARTPADrwilARLQRAVNETVEAL-EAFRFNDAANAVYAFV-WHELCDWYIELAKEALASEDPEARRSVQA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 476 ICsmgINLFRVLMTYLKPVLPSLTE----------RAEAFLNGELSWEGIQQPLLDHTVNP-FKALFNRID-LDKVNDMV 543
Cdd:PRK14900 686 VL---VHCLQTSYRLLHPFMPFITEelwhvlraqvGASAWADSVLAAEYPRKGEADEAAEAaFRPVLGIIDaVRNIRGEM 762
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 491103850 544 NASKEDMAASQAPVSGPLADDPIQETITFDDFAKVdMRIALIKSADLVDGS 594
Cdd:PRK14900 763 GIPWKVKLGAQAPVEIAVADPALRDLLQAGELARV-HRVAGVEGSRLVVAA 812
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
291-362 |
2.55e-05 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 46.59 E-value: 2.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491103850 291 HFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH-GYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAK 362
Cdd:pfam01406 211 HGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSV 283
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
19-46 |
6.90e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 46.25 E-value: 6.90e-05
10 20
....*....|....*....|....*....
gi 491103850 19 GSIHLGHMLEH-IQaDIWVRYQRMRGNEV 46
Cdd:PRK05729 49 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 76
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
19-46 |
6.92e-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: 46.20 E-value: 6.92e-05
10 20
....*....|....*....|....*....
gi 491103850 19 GSIHLGHMLEH-IQaDIWVRYQRMRGNEV 46
Cdd:COG0525 48 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 75
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
6-93 |
7.91e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 45.97 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 6 KKLLVTCALPYANGS-IHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQMGIKPEEMIAEMSQEHQQD 84
Cdd:PLN02563 110 PKFYVLDMFPYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQ 189
|
....*....
gi 491103850 85 FAGFGISYD 93
Cdd:PLN02563 190 LKSLGFSYD 198
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
319-466 |
1.14e-04 |
|
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: 45.09 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 319 NLFVH-GYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYaakLSS--RiDDIDLNLEDFVQRVNAdiVNKVVNLASR 395
Cdd:COG0215 251 RYWMHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL---LSAhyR-SPLDFSEEALEEAEKA--LERLYNALRR 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491103850 396 nagfINKRFGGKLAASLADPALYQTFTDAAD---SIAEAYAsresgrairEIMALADLANRYVDEQAPWVVAKQ 466
Cdd:COG0215 325 ----LEEALGAADSSAEEIEELREEFIAAMDddfNTPEALA---------VLFELVREINKALDEGEDKAALAA 385
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
294-398 |
1.18e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 45.63 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 294 GKDIVYFHSLF-------------WPAMLEgsnfrkptnlfVHGYVTVNGAKMSKSRG---TFIKAgtyLQHLDADCLRY 357
Cdd:PRK12300 537 GKDLIPNHLTFfifnhvaifpeekWPRGIV-----------VNGFVLLEGKKMSKSKGnviPLRKA---IEEYGADVVRL 602
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 491103850 358 YYA--AKLSSridDIDLNlEDFVQRVnADIVNKVVNLASRNAG 398
Cdd:PRK12300 603 YLTssAELLQ---DADWR-EKEVESV-RRQLERFYELAKELIE 640
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
15-86 |
2.08e-04 |
|
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: 42.08 E-value: 2.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFI-CADDAHGTpIMLKAQQMGIKPEEMIAEMSQEHQQDFA 86
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIaLIDDAGGL-IGDPANKKGENAKAFVERWIERIKEDVE 77
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
300-509 |
3.49e-04 |
|
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: 43.92 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 300 FHSLFWPA-MLEGSN-FRkptNLFVHGYVtV--NGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAklSSRIDDIdlnle 375
Cdd:COG0060 571 FYSSLLTStALFGRApYK---NVLTHGFV-LdeDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS--SDYWGDL----- 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 376 dfvqRVNADIVNkvvnlasRNAGFINK-----RFggkLAASLADpalyqtFTDAADSIA--------------------- 429
Cdd:COG0060 640 ----RFSDEILK-------EVRDVYRRlrntyRF---LLANLDD------FDPAEDAVPyedlpeldrwilsrlnelike 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 430 --EAYASRESGRAIREIMALA--DLANRYV----DEQapWVVAKQEGRDADLQAIcsmginLFRVLMTYLK---PVLPSL 498
Cdd:COG0060 700 vtEAYDNYDFHRAYRALHNFCveDLSNWYLdiskDRL--YTEAADSLDRRAAQTT------LYEVLETLVRllaPILPFT 771
|
250
....*....|.
gi 491103850 499 TERAEAFLNGE 509
Cdd:COG0060 772 AEEIWQNLPGE 782
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-93 |
1.17e-03 |
|
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: 42.35 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 14 LPYANGSIHLGHMLEHIQADIWVRYQRMRGNEV-H---FicadDAHGTPIMLKAQQMGIKPEEM----IAEMSQEHQQdf 85
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVlHpmgW----DAFGLPAENAAIKNGVHPAEWtyenIANMRRQLKR-- 114
|
....*...
gi 491103850 86 agFGISYD 93
Cdd:COG0495 115 --LGLSYD 120
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
7-84 |
1.22e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 42.36 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491103850 7 KLLVTCALPYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKA-------QQMGIKP-----EEMI 74
Cdd:PLN02959 46 KFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLLPFAFHCTGMPIKASAdklareiQQYGNPPvfpeeDEDE 125
|
90
....*....|
gi 491103850 75 AEMSQEHQQD 84
Cdd:PLN02959 126 AAAVAAAKAE 135
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
15-73 |
1.88e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 41.46 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491103850 15 PYANGSIHLGHMLEHIQADIWVRYQRMRGNEVHFICADDAHGTPIMLKAQQM----GIKPEEM 73
Cdd:PLN02943 97 PNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQLVVEKMlaseGIKRTDL 159
|
|
| |
