|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
4-689 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1238.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 4 RRILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDF 83
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 84 DNFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFIKGECPKCGAKDQYGDSCEVCGAT 163
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 164 YQPTDLKNPYSVVSGATPVRKSSEHYFFKLsdPRCENFLRDWV--ADLAQPEATNKMREWLgeegEAKLSDWDISRDAPY 241
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKL--PRFEEFLKEWItrSGELQPNVANKMKEWL----EEGLQDWDISRDAPY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 242 FGFEIPGAPGKYFYVWLDAPVGYYASFKNLCAKR-GLDFDAWINEHSTTEQYHFIGKDILYFHTLFWPAMLKFSGHRTPT 320
Cdd:PRK00133 236 FGFEIPGAPGKVFYVWLDAPIGYISSTKNLCDKRgGLDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 321 NVFAHGFLTVDGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAKLNATMEDLDLNLDDFIARVNSDLVGKFVNIASRSA 400
Cdd:PRK00133 316 NVFAHGFLTVEGAKMSKSRGTFIWARTYLDH-LDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 401 GFLVKRFEGRVSDAALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNAFVDTEKPWDLAKDEanREKLHAAC 480
Cdd:PRK00133 395 GFINKRFDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQD--GERLQAVC 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 481 SVALEAFRLLAVYLKPILPTTVERIEAFLNVEPLTWRSIDsQLSSAKPIQPYSHLMTRVDKKQVDALVEANRQslQATAD 560
Cdd:PRK00133 473 SVGLNLFRALAIYLKPVLPELAERAEAFLNLEELTWDDAQ-QPLAGHPINKFKILFTRIEDKQIEALIEASKE--AAAAK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 561 APAAAANGAAAIEPMAETITIDDFAKIDLRVAKIVACQRVEGSNKLLQLTLDVGEGqTRNVFSGIQSAYSPEDLVGKLTV 640
Cdd:PRK00133 550 AAAAAAAAPLAEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEE-TRQVFSGIKSAYDPEELVGKLVV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1777068331 641 MVANLAPRKMKFGMSEGMVLAASAADEKaqpgLYILEPHSGAVPGMRVR 689
Cdd:PRK00133 629 MVANLAPRKMKFGVSEGMVLAAGPGGGD----LFLLEPDEGAKPGMRVK 673
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
4-548 |
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: 827.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 4 RRILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDF 83
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 84 DNFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFIKGECPKCGAKDQYGDSCEVCGAT 163
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 164 YQPTDLKNPYSVVSGATPVRKSSEHYFFKLSDprCENFLRDWVADLA--QPEATNKMREWLgEEGeakLSDWDISRDAPY 241
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSK--YQDRLLEWIEENPdiQPEVRNEVLSWL-KEG---LQDLSISRDFDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 242 fGFEIPGAPGKYFYVWLDAPVGYYASFKNLCAKRGL--DFDAWINEhSTTEQYHFIGKDILYFHTLFWPAMLKFSGHRTP 319
Cdd:COG0143 235 -GIPVPGDPGKVFYVWFDALIGYISATKGYADDRGLpeDFEKYWPA-PDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 320 TNVFAHGFLTVDGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAKlNATMEDLDLNLDDFIARVNSDLVGKFVNIASRS 399
Cdd:COG0143 313 KKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDR-YGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 400 AGFLVKRFEGRVSDA----ALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNAFVDTEKPWDLAKDEaNREK 475
Cdd:COG0143 391 LSMIHKYFDGKVPEPgeltEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDE-DPER 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777068331 476 LHAACSVALEAFRLLAVYLKPILPTTVERIEAFLNVEP--LTWRSIDSQLSSAKPIQPYSHLMTRVDKKQVDALV 548
Cdd:COG0143 470 LATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGdeLTWEDAGWPLPAGHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
6-540 |
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: 590.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 6 ILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDFDN 85
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 86 FLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFIKGECPKCGAKDQYGDSCEVCGATYQ 165
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 166 PTDLKNPYSVVSGATPVRKSSEHYFFKLsdPRCENFLRDWVADLAQP-----EATNKMREWLGEegeaKLSDWDISRDAP 240
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRL--SAFEKELEEWIRKNPESgspasNVKNKAQNWLKG----GLKDLAITRDLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 241 YFGFEIPGAPGKYFYVWLDAPVGYYASfknLCAKRGL--DFDAWINEHSTTEQYHFIGKDILYFHTLFWPAMLKFSGHRT 318
Cdd:TIGR00398 235 YWGIPVPNDPNKVVYVWFDALIGYISS---LGILSGDteDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 319 PTNVFAHGFLTVDGAKMSKSRGTFITAQSYIDtGLNPEWLRYYFAAKLNATmEDLDLNLDDFIARVNSDLVGKFVNIASR 398
Cdd:TIGR00398 312 PTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLA-RFGADILRYYLLKERPLG-KDGDFSWEDFVERVNADLANKLGNLLNR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 399 SAGFLVKRFEGRVS----DAALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNAFVDTEKPWDLAKDEANRE 474
Cdd:TIGR00398 390 TLGFIKKYFNGVLPsediTDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068331 475 KLHAACSvalEAFRLLAVYLKPILPTTVERIEAFLNVEPLTWRSidSQLSSAKPIQPYSHLMTRVD 540
Cdd:TIGR00398 470 ELLAVCS---MLIRVLSILLYPIMPKLSEKILKFLNFELEWDFK--LKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
6-399 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 565.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 6 ILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDFDN 85
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 86 FLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFIKGECPKCGAKDQYGDSCEVCGATYQ 165
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 166 PTDLKNPYSVVSGATPVRKSSEHYFFKLSDprCENFLRDWVA---DLAQPEATNKMREWLGEEgeakLSDWDISRDAPYf 242
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSK--FQDKLREWIEennPEWPENVKNMVLEWLKEG----LKDRAISRDLDW- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 243 GFEIPGAPGKYFYVWLDAPVGYYASFKNLCAkRGLDFDAWINEHSTTEQYHFIGKDILYFHTLFWPAMLKFSGHRTPTNV 322
Cdd:pfam09334 234 GIPVPGAEGKVFYVWLDAPIGYISATKELSG-NEEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777068331 323 FAHGFLTVDGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAKLNATmEDLDLNLDDFIARVNSDLVGKFVNIASRS 399
Cdd:pfam09334 313 FAHGYLTYEGGKMSKSRGNVVWPSEALDR-FPPDALRYYLARNRPET-KDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
5-374 |
2.20e-131 |
|
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: 390.35 E-value: 2.20e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 5 RILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDFD 84
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 85 NFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPdrfikgecpkcgakdqygdscevcgaty 164
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 165 qptdlknpysvvsgatpVRKSSEHYFFKLSdpRCENFLRDWV---ADLAQPE-ATNKMREWLGEEgeakLSDWDISRDAP 240
Cdd:cd00814 133 -----------------EWREEEHYFFRLS--KFQDRLLEWLeknPDFIWPEnARNEVLSWLKEG----LKDLSITRDLF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 241 YFGFEIPGAPGKYFYVWLDAPVGYYASFKNLCAKRGLDFDAWINEhstTEQYHFIGKDILYFHTLFWPAMLKFSGHRTPT 320
Cdd:cd00814 190 DWGIPVPLDPGKVIYVWFDALIGYISATGYYNEEWGNSWWWKDGW---PELVHFIGKDIIRFHAIYWPAMLLGAGLPLPT 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1777068331 321 NVFAHGFLTVDGAKMSKSRGTFITAQSYIDTGlNPEWLRYYFAAKLNATmEDLD 374
Cdd:cd00814 267 RIVAHGYLTVEGKKMSKSRGNVVDPDDLLERY-GADALRYYLLRERPEG-KDSD 318
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
1-689 |
2.53e-126 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 388.77 E-value: 2.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 1 MSERRILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHK 80
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 81 RDFDNFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFI--KGECPKCGakdqygdsce 158
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLvdGGKCPDCG---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 159 vcgatyqptdlknpysvvsgaTPVRKSSEH-YFFKLSdpRCENFLRDWVA---DLAQPEatNKMREWLG---EEGeakLS 231
Cdd:PRK12267 151 ---------------------REVELVKEEsYFFRMS--KYQDRLLEYYEenpDFIQPE--SRKNEMINnfiKPG---LE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 232 DWDISRDAPYFGFEIPGAPGKYFYVWLDAPVGYyasfknLCAkrgLDFDAWinEHSTTEQY-----HFIGKDILYFHTLF 306
Cdd:PRK12267 203 DLSISRTSFDWGIPVPFDPKHVVYVWIDALLNY------ITA---LGYGSD--DDELFKKFwpadvHLVGKDILRFHAIY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 307 WPAMLKFSGHRTPTNVFAHGFLTVDGAKMSKSRGTFITAQSYIDT-GLNPewLRYY------FAAklnatmeDLDLNLDD 379
Cdd:PRK12267 272 WPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRyGLDA--LRYYllrevpFGS-------DGDFSPEA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 380 FIARVNSDLVGKFVNIASRSAGFLVKRFEGRVSDAALGHPLMVQLREAAPQIADLYEKR----EYSKALRAVMELADAVN 455
Cdd:PRK12267 343 LVERINSDLANDLGNLLNRTVAMINKYFDGEIPAPGNVTEFDEELIALAEETLKNYEELmeelQFSRALEEVWKLISRAN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 456 AFVDTEKPWDLAKDEANREKLHAACSVALEAFRLLAVYLKPILPTTVERIEAFLNVEP--LTWRSIDS--QLSSAKPIQP 531
Cdd:PRK12267 423 KYIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEelTSWESLLEwgGLPAGTKVAK 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 532 YSHLMTRVDkkqvdalVEANRQSLQATADAPAAAANGAAAIEPMAETITIDDFAKIDLRVAKIVACQRVEGSNKLLQLTL 611
Cdd:PRK12267 503 GEPLFPRID-------VEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLEAEKVEKSDKLLKLQV 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777068331 612 DVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGMVLAASAADEkaqpgLYILEPHSGAVPGMRVR 689
Cdd:PRK12267 576 DLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGK-----LTLLTVDKEVPNGSKVK 648
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
4-540 |
2.45e-97 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 309.12 E-value: 2.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 4 RRILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDF 83
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 84 DNFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYdpvkemflpdrfikgecpkcgakdqygdsCEVCGAT 163
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 164 YQPTDL--KNPYSVVSGATPVRKSSEHYFFKLSDPrcENFLRDWVA---DLAQPEAT-NKMREWLgEEGeakLSDWDISR 237
Cdd:PRK11893 132 YTESELieDGYRCPPTGAPVEWVEEESYFFRLSKY--QDKLLELYEanpDFIQPASRrNEVISFV-KSG---LKDLSISR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 238 ---DApyfGFEIPGAPGKYFYVWLDAPVGYYAsfknlcakrGLDFDAwiNEHSTTEQY--------HFIGKDILYFHTLF 306
Cdd:PRK11893 206 tnfDW---GIPVPGDPKHVIYVWFDALTNYLT---------ALGYPD--DEELLAELFnkywpadvHLIGKDILRFHAVY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 307 WPAMLKFSGHRTPTNVFAHGFLTVDGAKMSKSRGTFITAQSYIDT-GLNPewLRYYFAAKLNATmEDLDLNLDDFIARVN 385
Cdd:PRK11893 272 WPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEyGVDA--VRYFLLREIPFG-QDGDFSREAFINRIN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 386 SDLVGKFVNIASRSAGFLVKRFEGRVSDA----ALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNAFVDTE 461
Cdd:PRK11893 349 ADLANDLGNLAQRTLSMIAKNFDGKVPEPgaltEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQ 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 462 KPWDLAKDeaNREKLHAACSVALEAFRLLAVYLKPILPTTVERIEAFLNVEPLTWRSIDS----QLSSAKPIQPYSHLMT 537
Cdd:PRK11893 429 APWSLAKT--DPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEEDENRDFAAlswgRLAPGTTLPKPEPIFP 506
|
...
gi 1777068331 538 RVD 540
Cdd:PRK11893 507 RLE 509
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
4-688 |
1.72e-94 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 309.79 E-value: 1.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 4 RRILVTSALPYANGPIHIGHLVE-YIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRD 82
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGcVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 83 FDNFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFIKGECPK--CGAKDQYGDSCEVC 160
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 161 GATYQPTDLKNPYSVVSGATPVRKSSEHYFFKLS--DPRCENFLRD------WVADLAQpeATNKmreWLgEEGeakLSD 232
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPllKDKLVEYINEtsvaggWSQNAIQ--TTNA---WL-RDG---LKP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 233 WDISRDAPYfGFEIP--GAPGKYFYVWLDAPVGYYAsfknLCAKRGLDFDAWINEHSTTEQYHFIGKDILYFHTLFWPAM 310
Cdd:PLN02610 248 RCITRDLKW-GVPVPleKYKDKVFYVWFDAPIGYVS----ITACYTPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPST 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 311 LKFSGHR--TPTNVFAHGFLTVDGAKMSKSRGTFITAQSYIDTGLNPEWLRYYFAAKLnATMEDLDLNLDDFIARVNSDL 388
Cdd:PLN02610 323 LLGTGENwtMMKTISVTEYLNYEGGKFSKSKGVGVFGNDAKDTNIPVEVWRYYLLTNR-PEVSDTLFTWADLQAKLNSEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 389 VGKFVNIASRSAGFLVKR----FEGRVSDA--ALGHPLMVQLREAAPQIADLY----EKREYSKALRAVMELADAVNAFV 458
Cdd:PLN02610 402 LNNLGNFINRVLSFIAKPpgagYGSVIPDApgAESHPLTKKLAEKVGKLVEQYveamEKVKLKQGLKTAMSISSEGNAYL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 459 DTEKPWDLAKDEanreklHAACSV----ALEAFRLLAVYLKPILPTTVERIEAFLNVEPLTWRSIDSQLSSAKPIQPYS- 533
Cdd:PLN02610 482 QESQFWKLYKED------KPSCAIvvktSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLSDEKGEVARAKRPWEl 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 534 ----HLMTRVD---KKQVDALVEANRQSL---QATADAPAAAANGAAAIEPMAETITID--------------------- 582
Cdd:PLN02610 556 vpagHKIGTPEplfKELKDEEVEAYREKFagsQADRAARAEAAEAKKLAKQLKKKALSDggkkkqgkkaggggkskaaae 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 583 ---DFAKIDLRVAKIVACQRVEGSNKLLQLTLDVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGMV 659
Cdd:PLN02610 636 reiDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMV 715
|
730 740
....*....|....*....|....*....
gi 1777068331 660 LAASAADEKAqpgLYILEPHSGAVPGMRV 688
Cdd:PLN02610 716 LAASNSDHTK---VELVEPPESAAVGERV 741
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
5-366 |
1.64e-67 |
|
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: 224.22 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 5 RILVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGL-------------TPRQL 71
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 72 IERVWTEHKRDFDNFLVSFD--NYYSTDSDENKELCQNVYLKLKEAGLIdvreveqfydpvkemflpdrfikgecpkcga 149
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLI------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 150 kdqygdscevcgatyqptdlknpysvVSGATPVRKSsEHYFFKLSDPRCEnfLRDWV--ADLAQPEATNKMREWLgeege 227
Cdd:cd00668 130 --------------------------YRGTHPVRIT-EQWFFDMPKFKEK--LLKALrrGKIVPEHVKNRMEAWL----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 228 AKLSDWDISRDApYFGFEIPGapgKYFYVWLDAPVGYYASFKNLCAKRGLdfdawinEHSTTEQYHFIGKDILYFHTLFW 307
Cdd:cd00668 176 ESLLDWAISRQR-YWGTPLPE---DVFDVWFDSGIGPLGSLGYPEEKEWF-------KDSYPADWHLIGKDILRGWANFW 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777068331 308 PAMLK-FSGHRTPTNVFAHGFLTV-DGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAKL 366
Cdd:cd00668 245 ITMLVaLFGEIPPKNLLVHGFVLDeGGQKMSKSKGNVIDPSDVVEK-YGADALRYYLTSLA 304
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
7-519 |
5.73e-51 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 187.23 E-value: 5.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 7 LVTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDFDNF 86
Cdd:PLN02224 72 VLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 87 LVSFDNYYSTDSDENKELCQNVYLKLKEAGLIDVREVEQFYdpvkemflpdrfikgeCPKCgakDQYGDSCEVcgatyqp 166
Cdd:PLN02224 152 DIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDEKEL------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 167 tdLKNPYSVVSGATPVRKSSEHYFFKLSdpRCENFLRDWVAD---LAQPE-ATNKMREWLgeegEAKLSDWDISRDAPYF 242
Cdd:PLN02224 206 --LENNCCPVHQMPCVARKEDNYFFALS--KYQKPLEDILAQnprFVQPSyRLNEVQSWI----KSGLRDFSISRALVDW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 243 GFEIPGAPGKYFYVWLDAPVGYYASFKNLCAKRGLDFDAWINEHSTteqYHFIGKDILYFHTLFWPAMLKFSGHRTPTNV 322
Cdd:PLN02224 278 GIPVPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPAS---LHLIGKDILRFHAVYWPAMLMSAGLELPKMV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 323 FAHGFLTVDGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAKLNATmEDLDLNLDDFIARVNSDLVGKFVNIASRSAGF 402
Cdd:PLN02224 355 FGHGFLTKDGMKMGKSLGNTLEPFELVQK-FGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 403 LVKRFEGRV----SDAALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNAFVDTEKPWDLAKDEA-NREKLH 477
Cdd:PLN02224 433 LKKNCESTLvedsTVAAEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGvSAEEAA 512
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1777068331 478 AACSVALEAFRLLAVYLKPILPTTVERIEAFLNVEPLTWRSI 519
Cdd:PLN02224 513 KDLVIILEVMRVIAVALSPIAPCLSLRIYSQLGYSEDQFNSI 554
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
579-689 |
7.97e-49 |
|
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.
Pssm-ID: 239199 [Multi-domain] Cd Length: 105 Bit Score: 166.52 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 579 ITIDDFAKIDLRVAKIVACQRVEGSNKLLQLTLDVGEgQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGM 658
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100 110
....*....|....*....|....*....|.
gi 1777068331 659 VLAASAADekaqpGLYILEPHSGAVPGMRVR 689
Cdd:cd02800 80 ILAAEDGG-----KLKLLTPDEEVEPGSRVS 105
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
573-689 |
1.70e-44 |
|
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: 155.66 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 573 EPMAETITIDDFAKIDLRVAKIVACQRVEGSNKLLQLTLDVGEGQtRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKF 652
Cdd:TIGR00399 26 EPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFG 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1777068331 653 GMSEGMVLAASAADEKaqpgLYILEPHSGAVPGMRVR 689
Cdd:TIGR00399 105 VKSEGMILAAEDDGKV----LFLLSPDQEAIAGERIK 137
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
377-509 |
3.03e-39 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 140.70 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 377 LDDFIARVNSDLVGKFVNIASRSAGFLVKRFEGrvsDAALGHPLMVQLREAAPQIADLYEKREYSKALRAVMELADAVNA 456
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGG---LTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1777068331 457 FVDTEKPWDLAKDEaNREKLHAACSVALEAFRLLAVYLKPILPTTVERIEAFL 509
Cdd:cd07957 78 YIDETAPWKLAKEE-DPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
589-688 |
1.18e-32 |
|
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: 121.09 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 589 LRVAKIVACQRVEGSNKLLQLTLDVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGMVLAASAADEK 668
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLE 80
|
90 100
....*....|....*....|
gi 1777068331 669 AQpGLYILEPHSGAVPGMRV 688
Cdd:cd02153 81 EG-SVGILELPEDAPVGDRI 99
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
589-687 |
5.82e-29 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 110.79 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 589 LRVAKIVACQRVEGSNKLLQLTLDVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGMVLAASAADEK 668
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80
|
90
....*....|....*....
gi 1777068331 669 aqpGLYILEPHSGAVPGMR 687
Cdd:pfam01588 81 ---SVGLLEPPADVPPGTK 96
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
576-685 |
4.11e-26 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 114.18 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 576 AETITIDDFAKID----LRVAKIVACQRVEGSNKLLQLTLDVGEGqTRNVFSGIQSAY----SPEDLVGKLTVMVANLAP 647
Cdd:COG0073 27 MAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGAPNVYagdkVPEALVGAQVPGVVNLKP 105
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1777068331 648 RKMKFGMSEGMVLaasAADEKAQPGLY--ILEPHSGAVPG 685
Cdd:COG0073 106 RKIRGVESEGMLC---SAEELGLGEDHdgILELPEDAPPG 142
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
582-688 |
1.46e-25 |
|
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: 101.15 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 582 DDFAKIDLRVAKIVACQRVEGSNKLLQLTLDVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEGMVLA 661
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|....*..
gi 1777068331 662 ASAADekaQPGLYILEPHSGAVPGMRV 688
Cdd:cd02799 81 ASNAD---HEKVELLEPPEGAKPGERV 104
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
579-688 |
1.69e-21 |
|
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.
Pssm-ID: 239197 [Multi-domain] Cd Length: 107 Bit Score: 89.99 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 579 ITIDDFAKIDLRVAKIVACQRVEGSNK-LLQLTLDVGEGQTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFGMSEG 657
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEDFPEARKpAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100 110
....*....|....*....|....*....|.
gi 1777068331 658 MVLAASAADEkaqpGLYILEPHSGAVPGMRV 688
Cdd:cd02798 81 LVLGADDEGG----EVVLLVPDREVPNGAKV 107
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
576-667 |
5.46e-17 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 77.18 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 576 AETITIDDFAKIDLRVAKIVACQRVEGSNKL-LQLTLDVGEG-QTRNVFSGIQSAYSPEDLVGKLTVMVANLAPRKMKFG 653
Cdd:PRK10089 1 METITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEEiGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGF 80
|
90
....*....|....
gi 1777068331 654 MSEGMVLAASAADE 667
Cdd:PRK10089 81 MSEVLVLGFEDEDG 94
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
13-375 |
7.24e-17 |
|
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: 83.06 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEK----EGLTPRQL-----IERVWT---EHK 80
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKklgiEGKTRHDLgreefLEKCWEwkeESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 81 RDFDNFL------VSFDNYYSTDSDENKELCQNVYLKLKEAGLIdvrevEQFYDPVKemflpdrfikgECPKCGAKDQYG 154
Cdd:cd00817 90 GKIREQLkrlgasVDWSREYFTMDPGLSRAVQEAFVRLYEKGLI-----YRDNRLVN-----------WCPKLRTAISDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 155 DSCEVCGATYQPTDLKNPY-SVVSGATPVRKSSEHYFFKLSDPRCENFLRDWVADlaqpeatnkmrewlgeegeakLSDW 233
Cdd:cd00817 154 EVCSRSGDVIEPLLKPQWFvKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLEN---------------------IRDW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 234 DISRDApYFGFEIPgapgkYFYV-----WLDAPVGYYA------SFKNLCAKRGLD---------FDA---------WIN 284
Cdd:cd00817 213 CISRQL-WWGHRIP-----AWYCkdgghWVVAREEDEAidkaapEACVPCGGEELKqdedvldtwFSSslwpfstlgWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 285 EHSTTEQYH-----FIGKDILYfhtlFWPA-M----LKFSGHRTPTNVFAHGF-LTVDGAKMSKSRGTFITAQSYIDtGL 353
Cdd:cd00817 287 ETKDLKKFYptsllVTGHDIIF----FWVArMimrgLKLTGKLPFKEVYLHGLvRDEDGRKMSKSLGNVIDPLDVID-GY 361
|
410 420
....*....|....*....|..
gi 1777068331 354 NPEWLRyYFAAKLNATMEDLDL 375
Cdd:cd00817 362 GADALR-FTLASAATQGRDINL 382
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
13-364 |
9.95e-17 |
|
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: 81.89 E-value: 9.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKE-GLTPRQLIERVWTEHKR---------- 81
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElGISGKKDIEKMGIAEFNakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 82 ------DFDNF--LVSFDNYYSTDSDENKELCQNVYLKLKEAGLIdvrevEQFYDPVkemflpdrfikgecpkcgakdqy 153
Cdd:cd00818 90 vdeqeeQFQRLgvWVDWENPYKTMDPEYMESVWWVFKQLHEKGLL-----YRGYKVV----------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 154 gdscevcgatyqptdlknPYSVVSGATPvrksseHYFFKLSDprcenfLRDWVADLAQ-----PEAT-NKMREWLGEege 227
Cdd:cd00818 142 ------------------PWPLIYRATP------QWFIRVTK------IKDRLLEANDkvnwiPEWVkNRFGNWLEN--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 228 akLSDWDISRDApYFGFEIPgapgkyfyVWldapvgYYASFKNLCAKRGLD-FDAWI-------------NEHSTTEQ-- 291
Cdd:cd00818 189 --RRDWCISRQR-YWGTPIP--------VW------YCEDCGEVLVRRVPDvLDVWFdsgsmpyaqlhypFENEDFEElf 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 292 -YHFI--GKDIL--YFHTLFWPAMLKFSghRTP-TNVFAHGF-LTVDGAKMSKSRGTFITAQSYIDT-GLNPewLRYYFA 363
Cdd:cd00818 252 pADFIleGSDQTrgWFYSLLLLSTALFG--KAPyKNVIVHGFvLDEDGRKMSKSLGNYVDPQEVVDKyGADA--LRLWVA 327
|
.
gi 1777068331 364 A 364
Cdd:cd00818 328 S 328
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
8-350 |
3.40e-16 |
|
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: 79.98 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 8 VTSALPYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPrqlieRVWTEH-----KRD 82
Cdd:cd00812 4 ILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDP-----EDWTEYnikkmKEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 83 FDNFLVSFD---NYYSTDSDENKeLCQNVYLKLKEAGLidvreveqfydpvkemflpdrfikgecpkcgakdqygdscev 159
Cdd:cd00812 79 LKRMGFSYDwrrEFTTCDPEYYK-FTQWLFLKLYEKGL------------------------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 160 cgatyqptdlknpysVVSGATPV--RKSSEHYFFKLSDPrcenflrDWvADLAQpEATNKMREWlGEEGEAKLSDW-DIS 236
Cdd:cd00812 116 ---------------AYKKEAPVnwCKLLDQWFLKYSET-------EW-KEKLL-KDLEKLDGW-PEEVRAMQENWiGCS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 237 RDApYFGFEIPgapgkYFYV---WLDAPVgYYASFknLCAKRgLDFDAWINEHSTTE---------QYHFiGKDI----- 299
Cdd:cd00812 171 RQR-YWGTPIP-----WTDTmesLSDSTW-YYARY--TDAHN-LEQPYEGDLEFDREefeywypvdIYIG-GKEHapnhl 239
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1777068331 300 ---LYFHTLFWPamLKFSGHRTPTNVFAHGFLTVDGAKMSKSRGTFITAQSYID 350
Cdd:cd00812 240 lysRFNHKALFD--EGLVTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIK 291
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
13-118 |
5.93e-14 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 75.61 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYY-VGADDtHGTPVMLRAEKE-GLTP--------RQLIERVWTEHKRD 82
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEKYyGIRKddisreefIELCRELTDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1777068331 83 FDNFL------VSFDNYYSTDSDENKELCQNVYLKLKEAGLI 118
Cdd:PRK13208 126 FRELWrrlglsVDWSLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
13-118 |
2.89e-13 |
|
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273054 [Multi-domain] Cd Length: 861 Bit Score: 73.18 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKE-GLTPRQLIERVWTEHKRD--------- 82
Cdd:TIGR00392 45 PYANGSIHLGHALNKILKDIILRYKTMQGFNVTRKPGWDTHGLPIEHKVEKKlGISGKKEISSLEIEEFREkcrefalkq 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1777068331 83 -------FDNF--LVSFDNYYSTDSDENKELCQNVYLKLKEAGLI 118
Cdd:TIGR00392 125 ieeqreqFQRLgvWGDWENPYKTMDPSYEESQWWLFKEAHEKGLL 169
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
13-96 |
8.28e-13 |
|
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: 72.03 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKE-GLTpRQLIERV---------------W 76
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVEKElGIK-KKDIEKVgiaefrekcreyalkY 133
|
90 100
....*....|....*....|...
gi 1777068331 77 TEH-KRDFDN--FLVSFDNYYST 96
Cdd:COG0060 134 VDEqREDFKRlgVWGDWDNPYLT 156
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
13-118 |
2.72e-09 |
|
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: 60.12 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKE-GLTPRQ---------LIERVWT----- 77
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKlGIKEKKtrhkygreeFREKCREwkmey 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1777068331 78 --EHKRDFDNF--LVSFDNYYSTDSDENKELCQNVYLKLKEAGLI 118
Cdd:pfam00133 112 adEIRKQFRRLgrSIDWDREYFTMDPELEAAVWEVFVRLHDKGLI 156
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
13-93 |
1.18e-08 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 58.63 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRA-------EKEGLTPRQLIERVWTEHKRDFDN 85
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVlqsldqeARKELTPIKLRAKAAKFAKKTVDT 120
|
....*...
gi 1777068331 86 FLVSFDNY 93
Cdd:PLN02843 121 QRESFKRY 128
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
13-118 |
2.49e-07 |
|
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: 54.29 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEK----EGLT----PR-QLIERV--WTEHKR 81
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEKklgaEGKTkhdlGReEFREKIweWKEESG 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1777068331 82 DFD-------NFLVSFDNYYSTDSDENKELCQNVYLKLKEAGLI 118
Cdd:TIGR00422 122 GTIknqikrlGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLI 165
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
321-362 |
4.76e-07 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 51.04 E-value: 4.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1777068331 321 NVFAH-GFLTVDGAKMSKSRGTFITAQSyIDTGLNPEWLRYYF 362
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRD-ALKKYDPEVLRLAL 201
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
302-512 |
1.23e-05 |
|
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: 48.54 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 302 FHTLFWPAMLKFsgHRTP-TNVFAHGFlTVD--GAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAAklNATMEdlDLNLD 378
Cdd:COG0060 571 FYSSLLTSTALF--GRAPyKNVLTHGF-VLDedGRKMSKSLGNVVDPQEVIDK-YGADILRLWVAS--SDYWG--DLRFS 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 379 DFIARVNSDLVGKFVNIASrsagFLVKRFEG------RVSDAALgHPL----MVQLREAAPQIADLYEKREYSKALRAVM 448
Cdd:COG0060 643 DEILKEVRDVYRRLRNTYR----FLLANLDDfdpaedAVPYEDL-PELdrwiLSRLNELIKEVTEAYDNYDFHRAYRALH 717
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777068331 449 E-LADAVNAF-VDTEKP--WDLAKDEANREklhAACSV---ALEAF-RLLAvylkPILPTTVERIEAFLNVE 512
Cdd:COG0060 718 NfCVEDLSNWyLDISKDrlYTEAADSLDRR---AAQTTlyeVLETLvRLLA----PILPFTAEEIWQNLPGE 782
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
589-686 |
3.20e-05 |
|
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: 43.27 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 589 LRVAKIVACQRVEGSNKLLQLTLDVGEGQTRNVFSGiqsaySPEDLVGKLTVmVAN----------LAPRKMKFGMSEGM 658
Cdd:cd02796 1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG-----APNVRAGDKVV-VALpgavlpgglkIKKRKLRGVESEGM 74
|
90 100 110
....*....|....*....|....*....|.
gi 1777068331 659 VlaASAAD---EKAQPGLYILEPhsGAVPGM 686
Cdd:cd02796 75 L--CSAKElglGEDSDGIIELPE--DAPVGT 101
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
259-361 |
4.13e-05 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 46.77 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 259 DAPVGY-YASFKNLCAKRGLDFdawineHSTTEQYHFIGKDILYFHTLFWPAMLKFSGHRTPTNVFAHG-FLTVDGAKMS 336
Cdd:PRK14534 208 DSPWGFgYPSWHLECAAMNLEY------FKSTLDIHLGGVDHIGVHHINEIAIAECYLNKKWCDMFVHGeFLIMEYEKMS 281
|
90 100
....*....|....*....|....*
gi 1777068331 337 KSRGTFITAQSYIDTGLNPEWLRYY 361
Cdd:PRK14534 282 KSNNNFITIKDLEDQGFSPLDFRYF 306
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
325-482 |
4.60e-05 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 46.63 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 325 HGFLTVDGAKMSKSRGTFITAQSYIDTgLNPEWLRYYFAA-----KLNATMEDLDlnlddfiarvnsdlvgkfvniASRS 399
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKK-YDPEVLRFFLLSahyrsPLDFSEEALE---------------------EAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 400 AgflVKRFEGRVSDAAlghPLMVQLREAAPQIADLYEK-REY-------SKALRAVMELADAVNAFVDTEKpwDLAKDEA 471
Cdd:COG0215 314 A---LERLYNALRRLE---EALGAADSSAEEIEELREEfIAAmdddfntPEALAVLFELVREINKALDEGE--DKAALAA 385
|
170
....*....|.
gi 1777068331 472 NREKLHAACSV 482
Cdd:COG0215 386 LAALLRALGGV 396
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
13-252 |
5.87e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 46.35 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 13 PYANGP-IHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEKEGLTPRQLIERVWTEHKRDFDNFLVSFD 91
Cdd:PLN02563 119 PYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 92 --NYYSTDSDENKELCQNVYLKLKEAGLIDVREVeqfydPVKemflpdrfikgECPKCGakdqygdscevcgatyqpTDL 169
Cdd:PLN02563 199 wdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEV-----PVN-----------WCPALG------------------TVL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 170 KNPYSV--VS--GATPV-RKSSEHYFFKLSDpRCENFLRDwVADLAQPEATNKM-REWLGEEGEAKLsdwdisrdapyfG 243
Cdd:PLN02563 245 ANEEVVdgLSerGGHPViRKPMRQWMLKITA-YADRLLED-LDDLDWPESIKEMqRNWIGRSEGAEL------------D 310
|
....*....
gi 1777068331 244 FEIPGAPGK 252
Cdd:PLN02563 311 FSVLDGEGK 319
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
13-84 |
8.50e-05 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 43.24 E-value: 8.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHET-YYVGADDTHGTpVMLRAEKEGLTPRQLIERVWTEHKRDFD 84
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVrCIALIDDAGGL-IGDPANKKGENAKAFVERWIERIKEDVE 77
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
12-42 |
1.89e-04 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 44.66 E-value: 1.89e-04
10 20 30
....*....|....*....|....*....|.
gi 1777068331 12 LPYANGPIHIGHLVEYIQTDIWVRFQRMRGH 42
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGY 71
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
199-505 |
5.40e-04 |
|
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: 43.51 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 199 ENFLRDWVadlaqPEATNKM-REWLGeegeaKLSDWDISRDApYFGFEIPgapgkyfyVWLDAPVG--YYASFKNLCAKR 275
Cdd:TIGR00422 374 EEGEIKFV-----PKRMEKRyLNWLR-----NIKDWCISRQL-IWGHRIP--------VWYCKECGevYVAKEEPLPDDK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 276 G--------------LD--FDAWINEHSTT---------EQYH-----FIGKDILYFhtlfWPA-MLKFSGHRTPT---- 320
Cdd:TIGR00422 435 TntgpsveleqdtdvLDtwFSSSLWPFSTLgwpdetkdlKKFYptdllVTGYDIIFF----WVArMIFRSLALTGQvpfk 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 321 NVFAHGFL-TVDGAKMSKSRGTFITAQSYIDT-GLNPewLRyYFAAKLNATMEDLDLNLDDFIArvNSDLVGKFVNiASR 398
Cdd:TIGR00422 511 EVYIHGLVrDEQGRKMSKSLGNVIDPLDVIEKyGADA--LR-FTLASLVTPGDDINFDWKRVES--ARNFLNKLWN-ASR 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 399 sagFLVKRFEGrvsDAALGHPLMVQ----------LREAAPQIADLYEKREYSKALRAVMELA--DAVNAFVDTEKPWDL 466
Cdd:TIGR00422 585 ---FVLMNLSD---DLELSGGEEKLsladrwilskLNRTIKEVRKALDKYRFAEAAKALYEFIwnDFCDWYIELVKYRLY 658
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1777068331 467 AKDEA-NREKLHAACSVALEAFRLLAvylkPILPTTVERI 505
Cdd:TIGR00422 659 NGNEAeKKAARDTLYYVLDKALRLLH----PFMPFITEEI 694
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
5-140 |
6.11e-04 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) 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. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 41.78 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 5 RILV--TSALPyaNGPIHIGHLVEYIQTDIWVRFQRMRGHET---YYVGadDThGTPV-ML-RAEKEGltpRQLIERVWT 77
Cdd:cd00671 1 KILVefVSANP--TGPLHVGHLRNAIIGDSLARILEFLGYDVtreYYIN--DW-GRQIgLLiLSLEKW---RKLVEESIK 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777068331 78 EHKRDFDNFLVSFDNYYStDSDENKELcQNVYLKLKEAGLIDVREVEQFYDPVKEMFLPDRFI 140
Cdd:cd00671 73 ADLETYGRLDVRFDVWFG-ESSYLGLM-GKVVELLEELGLLYEEDGALWLDLTEFGDDKDRVL 133
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
13-76 |
8.42e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 42.62 E-value: 8.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777068331 13 PYANGPIHIGHLVEYIQTDIWVRFQRMRGHETYYVGADDTHGTPVMLRAEK----EG-----LTPRQLIERVW 76
Cdd:PLN02943 97 PNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGIATQLVVEKmlasEGikrtdLGRDEFTKRVW 169
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
17-76 |
8.78e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.78 E-value: 8.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777068331 17 GPIHIGH-LVEYIQtDIWVRFQRMRGHETYYV-GADdtH-G----TPVMLRAEKEGLTPRQL-----IERVW 76
Cdd:PRK05729 49 GSLHMGHaLNNTLQ-DILIRYKRMQGYNTLWLpGTD--HaGiatqMVVERQLAAEGKSRHDLgrekfLEKVW 117
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
19-118 |
1.34e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.16 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 19 IHIGHLVEYIQTDIWVRFQRMRG---------HETyyvgaddthGTPVMLRAE--KEG-------LT-----PRQLIERV 75
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGynvlfpmafHVT---------GTPILGIAEriARGdpetielYKslygiPEEELEKF 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1777068331 76 -----WTEH-----KRDFDNFLVSFD---NYYSTDSDENKeLCQNVYLKLKEAGLI 118
Cdd:PRK12300 72 kdpeyIVEYfseeaKEDMKRIGYSIDwrrEFTTTDPEYSK-FIEWQFRKLKEKGLI 126
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
4-118 |
1.39e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 41.68 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 4 RRILV--TSALPyaNGPIHIGHLVEYIQTDIWVRFQRMRGHE---TYYVGaDdtHGTPVM-----LRAEKegltpRQLIE 73
Cdd:PRK01611 111 KKVVVeyVSANP--TGPLHVGHLRSAVIGDALARILEFAGYDvtrEYYVN-D--AGTQIGmliasLELLW-----RKAVD 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1777068331 74 RVWTEHKRDFDNFLVSFDNYYS-TDSDENKELcQNVYLKLKEAGLI 118
Cdd:PRK01611 181 ISLDEIKEDLDRLGVHFDVWFSeSELYYNGKV-DEVVEDLKEKGLL 225
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
14-84 |
1.69e-03 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 40.25 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 14 YANGP-----IHIGHLVEYIQTDIWVRFQRMRGHETYYV----GADDthgtPVMLRAEKEGLTPRQLIERVWTEHKRDFD 84
Cdd:cd00672 24 YVCGPtvydyAHIGHARTYVVFDVLRRYLEDLGYKVRYVqnitDIDD----KIIKRAREEGLSWKEVADYYTKEFFEDMK 99
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
20-76 |
3.15e-03 |
|
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: 40.80 E-value: 3.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777068331 20 HIGH-LVEYIQtDIWVRFQRMRGHETYYV-GADdtHG-----TPV--MLRaeKEGLTPRQL-----IERVW 76
Cdd:COG0525 51 HMGHaLNNTLQ-DILIRYKRMQGYNTLWQpGTD--HAgiatqAVVerQLA--EEGKSRHDLgrekfLERVW 116
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
11-76 |
6.67e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 39.99 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777068331 11 ALPYAN--GPIHIGH-LVEYIQtDIWVRFQRMRGHETYYVGADDTHG--TPV----MLrAEKEGLTPRQL-----IERVW 76
Cdd:PTZ00419 65 VLPPPNvtGYLHIGHaLTGAIQ-DSLIRYHRMKGDETLWVPGTDHAGiaTQVvvekKL-MKEENKTRHDLgreefLKKVW 142
|
|
| |
