|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-488 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 596.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG--------PYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEERHK---AAGRDPklGYDNYDRNLTEEQKEAFRAEGRKPVIRLRMPDE 160
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtAPGKPP--RYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 161 DIVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkriGVAKftPE 240
Cdd:COG0008 155 GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL---GWEP--PE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 241 FGHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKK 320
Cdd:COG0008 230 FAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 321 ADAINADHIRMLDPKDFEQRLRAYLEShfdfpDDYPADKFAFLAtLLQTRVKTLSDAWDLSKFLVVEEDEftfDERSARR 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPE-----AGIREDLERLVP-LVRERAKTLSELAELARFFFIERED---EKAAKKR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 401 NFKEDAVAVLEATIAAVEPLseEDFVTEKLEAALqKALIEDLELKPRKAFGPVRVAVTGAQVSPPLFESMELLGRSRSLS 480
Cdd:COG0008 381 LAPEEVRKVLKAALEVLEAV--ETWDPETVKGTI-HWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFE 457
|
....*...
gi 1093476548 481 RLRKALEV 488
Cdd:COG0008 458 RLGYAIDK 465
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-484 |
3.09e-159 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 460.28 E-value: 3.09e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEG--------PYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVE-ERHKAAGRDPKLGYDNYDRNLTEEQKEAFRAEGRKPVIRLRMPDE-D 161
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLErLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEaV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 162 IVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKrigvAKfTPEF 241
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALG----WK-IPVF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 242 GHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKKA 321
Cdd:TIGR00464 229 AHLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 322 DAINADHIRMLDPKDFEQRLRAYLESHFDfPDDYPADKFAFLATLLQTRVKTLSDAWDLSKFLVveEDEFTFDERSARRN 401
Cdd:TIGR00464 309 QWLNAHYIKELPDEELFELLDPHLKSLVN-TDTLNREQLAELLLLFKERLKTLKEIAELIRLFF--EDKKEVDEDAFKKH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 402 FKEDAVAVLEATIAAVEPLseEDFVTEKLEAALqKALIEDLELKPRKAFGPVRVAVTGAQVSPPLFESMELLGRSRSLSR 481
Cdd:TIGR00464 386 LKKNVKEVLEALKKKLQAL--EEWTADEVKSAI-KQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKR 462
|
...
gi 1093476548 482 LRK 484
Cdd:TIGR00464 463 LKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-475 |
1.16e-116 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 353.66 E-value: 1.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 2 SDVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIDVGGPHGP 81
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 82 YRQSQRKDIYADVLQRLIDAGEAYEAFSTAEEVE---ERHKAAGRDPKlgYDNYDRNLTEEQKEAFRAEGRKPVIRLRMP 158
Cdd:PLN02627 124 YRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEamkEEAELKKLPPR--YTGKWATASDEEVQAELAKGTPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 159 DED-IVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkrigvaKF 237
Cdd:PLN02627 202 KEGsVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKAL------GF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 238 T-PEFGHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSmDG-DQDIFTMDEMVKAFDIHDVLSNPAR 315
Cdd:PLN02627 276 PmPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN-DGtENEIFTLEELVEKFSIDRINKSGAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 316 FDQKKADAINADHIRMLDPKDF-----EQRLRAYLESHFDFPddypadkFAFLAT-LLQTRVKTLSDA---------WDL 380
Cdd:PLN02627 355 FDSTKLKWMNGQHLRLLPEEELvklvgERWKSAGILKESDGS-------FVKEAVeLLKDGIELVTDAdkellnllsYPL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 381 SKFLVVEEDEFTFDErsarrNFKEDAVAVLEAtiaaveplseedFVTEKLEAALQ----------KALIEDLELKPRKAF 450
Cdd:PLN02627 428 AATLSSPEAKTVVED-----NFSEVADALIAA------------YDSGELAAALEeghdgwqkwvKAFGKALKRKGKRLF 490
|
490 500
....*....|....*....|....*
gi 1093476548 451 GPVRVAVTGAQVSPPLFESMELLGR 475
Cdd:PLN02627 491 MPLRVALTGKMHGPDVGESLVLLHK 515
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
4.67e-116 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the 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: 173905 [Multi-domain] Cd Length: 239 Bit Score: 341.49 E-value: 4.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIDVGGPHGPYR 83
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGeayeafstaeeveerhkaagrdpklgydnydrnlteeqkeafraegrkpvirlrmpdediv 163
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 164 fedlvrgriefkaglvpdfviarsNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKRIgvakfTPEFGH 243
Cdd:cd00808 101 ------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWE-----PPKFAH 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 244 LPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKKADA 323
Cdd:cd00808 152 LPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 1093476548 324 INADHIRM 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-322 |
3.66e-103 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 311.18 E-value: 3.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEgidvggphGPYR 83
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEE-RHKAAGRDPKlGYDNYD---RNLTEEQKEAFRAEGRKPVIRLRMPD 159
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEeREEQEALGSP-SRDRYDeenLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 160 E-DIVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKrigvaKFT 238
Cdd:pfam00749 153 EsPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 239 PEFGHLPFVMGEGNKKLSKRDPQSNLFIH--RDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARF 316
Cdd:pfam00749 228 PPFIHEYLRLNLDGTKLSKRKLSWSVDISqvKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAF 307
|
....*.
gi 1093476548 317 DQKKAD 322
Cdd:pfam00749 308 DRKKLD 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-488 |
0e+00 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 596.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEG--------PYY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEERHK---AAGRDPklGYDNYDRNLTEEQKEAFRAEGRKPVIRLRMPDE 160
Cdd:COG0008 77 QSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALREtqtAPGKPP--RYDGRCRDLSPEELERMLAAGEPPVLRFKIPEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 161 DIVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkriGVAKftPE 240
Cdd:COG0008 155 GVVFDDLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEAL---GWEP--PE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 241 FGHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKK 320
Cdd:COG0008 230 FAHLPLILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 321 ADAINADHIRMLDPKDFEQRLRAYLEShfdfpDDYPADKFAFLAtLLQTRVKTLSDAWDLSKFLVVEEDEftfDERSARR 400
Cdd:COG0008 310 LVWLNGPYIRALDDEELAELLAPELPE-----AGIREDLERLVP-LVRERAKTLSELAELARFFFIERED---EKAAKKR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 401 NFKEDAVAVLEATIAAVEPLseEDFVTEKLEAALqKALIEDLELKPRKAFGPVRVAVTGAQVSPPLFESMELLGRSRSLS 480
Cdd:COG0008 381 LAPEEVRKVLKAALEVLEAV--ETWDPETVKGTI-HWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELLGKERVFE 457
|
....*...
gi 1093476548 481 RLRKALEV 488
Cdd:COG0008 458 RLGYAIDK 465
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
4-484 |
3.09e-159 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 460.28 E-value: 3.09e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEG--------PYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVE-ERHKAAGRDPKLGYDNYDRNLTEEQKEAFRAEGRKPVIRLRMPDE-D 161
Cdd:TIGR00464 74 QSQRLDIYKKYAKELLEEGLAYRCYCSKERLErLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEaV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 162 IVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKrigvAKfTPEF 241
Cdd:TIGR00464 154 VSFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALG----WK-IPVF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 242 GHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKKA 321
Cdd:TIGR00464 229 AHLPMILDEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 322 DAINADHIRMLDPKDFEQRLRAYLESHFDfPDDYPADKFAFLATLLQTRVKTLSDAWDLSKFLVveEDEFTFDERSARRN 401
Cdd:TIGR00464 309 QWLNAHYIKELPDEELFELLDPHLKSLVN-TDTLNREQLAELLLLFKERLKTLKEIAELIRLFF--EDKKEVDEDAFKKH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 402 FKEDAVAVLEATIAAVEPLseEDFVTEKLEAALqKALIEDLELKPRKAFGPVRVAVTGAQVSPPLFESMELLGRSRSLSR 481
Cdd:TIGR00464 386 LKKNVKEVLEALKKKLQAL--EEWTADEVKSAI-KQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELIGKTESIKR 462
|
...
gi 1093476548 482 LRK 484
Cdd:TIGR00464 463 LKA 465
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-475 |
1.16e-116 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 353.66 E-value: 1.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 2 SDVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIDVGGPHGP 81
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVGGEYGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 82 YRQSQRKDIYADVLQRLIDAGEAYEAFSTAEEVE---ERHKAAGRDPKlgYDNYDRNLTEEQKEAFRAEGRKPVIRLRMP 158
Cdd:PLN02627 124 YRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEamkEEAELKKLPPR--YTGKWATASDEEVQAELAKGTPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 159 DED-IVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkrigvaKF 237
Cdd:PLN02627 202 KEGsVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKAL------GF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 238 T-PEFGHLPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSmDG-DQDIFTMDEMVKAFDIHDVLSNPAR 315
Cdd:PLN02627 276 PmPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN-DGtENEIFTLEELVEKFSIDRINKSGAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 316 FDQKKADAINADHIRMLDPKDF-----EQRLRAYLESHFDFPddypadkFAFLAT-LLQTRVKTLSDA---------WDL 380
Cdd:PLN02627 355 FDSTKLKWMNGQHLRLLPEEELvklvgERWKSAGILKESDGS-------FVKEAVeLLKDGIELVTDAdkellnllsYPL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 381 SKFLVVEEDEFTFDErsarrNFKEDAVAVLEAtiaaveplseedFVTEKLEAALQ----------KALIEDLELKPRKAF 450
Cdd:PLN02627 428 AATLSSPEAKTVVED-----NFSEVADALIAA------------YDSGELAAALEeghdgwqkwvKAFGKALKRKGKRLF 490
|
490 500
....*....|....*....|....*
gi 1093476548 451 GPVRVAVTGAQVSPPLFESMELLGR 475
Cdd:PLN02627 491 MPLRVALTGKMHGPDVGESLVLLHK 515
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
4-331 |
4.67e-116 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the 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: 173905 [Multi-domain] Cd Length: 239 Bit Score: 341.49 E-value: 4.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIDVGGPHGPYR 83
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGeayeafstaeeveerhkaagrdpklgydnydrnlteeqkeafraegrkpvirlrmpdediv 163
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 164 fedlvrgriefkaglvpdfviarsNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKRIgvakfTPEFGH 243
Cdd:cd00808 101 ------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWE-----PPKFAH 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 244 LPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKKADA 323
Cdd:cd00808 152 LPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDW 231
|
....*...
gi 1093476548 324 INADHIRM 331
Cdd:cd00808 232 LNGQYIRE 239
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
4-322 |
3.66e-103 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 311.18 E-value: 3.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEgidvggphGPYR 83
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPYY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEE-RHKAAGRDPKlGYDNYD---RNLTEEQKEAFRAEGRKPVIRLRMPD 159
Cdd:pfam00749 74 QSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEeREEQEALGSP-SRDRYDeenLHLFEEEMKKGSAEGGPATVRAKIPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 160 E-DIVFEDLVRGRIEFKAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKrigvaKFT 238
Cdd:pfam00749 153 EsPYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALG-----WEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 239 PEFGHLPFVMGEGNKKLSKRDPQSNLFIH--RDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARF 316
Cdd:pfam00749 228 PPFIHEYLRLNLDGTKLSKRKLSWSVDISqvKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAF 307
|
....*.
gi 1093476548 317 DQKKAD 322
Cdd:pfam00749 308 DRKKLD 313
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
4-331 |
3.64e-90 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the 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. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 274.73 E-value: 3.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEG--------PYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGeayeafstaeeveerhkaagrdpklgydnydrnlteeqkeafraegrkpvirlrmpdediv 163
Cdd:cd00418 74 QSDRFDLYRAYAEELIKKG------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 164 fedlvrgriefkaglvpdfviarsnGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLKRIgvakfTPEFGH 243
Cdd:cd00418 93 -------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWE-----PPRFYH 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 244 LPFVMGEGNKKLSKRDPQSNLFIHRDNGFIREGLLNYLALLGWSMDGDQDIFTMDEMVKAFDIHDVLSNPARFDQKKADA 323
Cdd:cd00418 143 FPRLLLEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADATFDWAKLEW 222
|
....*...
gi 1093476548 324 INADHIRM 331
Cdd:cd00418 223 LNREYIRE 230
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-259 |
3.56e-74 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 236.29 E-value: 3.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 1 MSDVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDegidvgGPhg 80
Cdd:PRK05710 3 MTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWD------GP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 81 PYRQSQRKDIYADVLQRLIDAGEAYEAFSTAEEVeERHKAAGRDPKLGYDNYDRNLTEeqkeafrAEGRKPVIRLRMPDE 160
Cdd:PRK05710 75 VLYQSQRHDAYRAALDRLRAQGLVYPCFCSRKEI-AAAAPAPPDGGGIYPGTCRDLLH-------GPRNPPAWRLRVPDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 161 DIVFEDLVRGRIEF-KAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkriGVAkfTP 239
Cdd:PRK05710 147 VIAFDDRLQGRQHQdLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLL---GLP--TP 221
|
250 260
....*....|....*....|
gi 1093476548 240 EFGHLPFVMGEGNKKLSKRD 259
Cdd:PRK05710 222 RYLHLPLVLNADGQKLSKQN 241
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
4-259 |
6.23e-66 |
|
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274810 Cd Length: 271 Bit Score: 213.56 E-value: 6.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGidvggphgPYR 83
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGE--------VVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEERHKAAGRdpklgYDNYDRNLTEeqkeafRAEGRKPVIRLRMPDEDIV 163
Cdd:TIGR03838 73 QSQRHALYQAALDRLLAAGLAYPCQCTRKEIAAARDGGGI-----YPGTCRNGLP------GRPGRPAAWRLRVPDGVIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 164 FEDLVRGRIEF-KAGLVPDFVIARSNGEPLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYESLkriGVAkfTPEFG 242
Cdd:TIGR03838 142 FDDRLQGPQQQdLAAAVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLL---GLP--PPRYL 216
|
250
....*....|....*..
gi 1093476548 243 HLPFVMGEGNKKLSKRD 259
Cdd:TIGR03838 217 HLPLVVNADGEKLSKQN 233
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
4-227 |
6.21e-32 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 128.82 E-value: 6.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAA--RDSEESYQAIIEALNWLGIDWDEgidvggphgP 81
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWDE---------V 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 82 YRQSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEERhKAAGRDPKlgydnyDRNLT-EEQKEAFRA-------EGrKPVI 153
Cdd:PRK04156 173 VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKEL-RDAGKPCP------HRDKSpEENLELWEKmldgeykEG-EAVV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 154 RlrmpdedivfedlVRGRIEFKAGLVPDFVIAR-------SNGE-----PLYTLVNPVDDALMEITHVLRGEDLLPSTPR 221
Cdd:PRK04156 245 R-------------VKTDLEHPNPSVRDWVAFRivktphpRVGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEK 311
|
....*.
gi 1093476548 222 QIALYE 227
Cdd:PRK04156 312 QRYIYD 317
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-256 |
4.19e-29 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 120.31 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 1 MSDVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIdvggphg 80
Cdd:TIGR00463 91 MGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVV------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 81 pyRQSQRKDIYADVLQRLIDAGEAYEAFSTAEEV-EERHKaagrdpklGYDNYDRNLT-EEQKEAFRaegrkpvirlRMP 158
Cdd:TIGR00463 164 --YQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFrELRNR--------GEACHCRDRSvEENLERWE----------EML 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 159 D-EDIVFEDLVRGRIEFKA--GLVPDFVIARSNGE------------PLYTLVNPVDDALMEITHVLRGEDLLPSTPRQI 223
Cdd:TIGR00463 224 EgKEEGGSVVVRVKTDLKHknPAIRDWVIFRIVKTphprtgdkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQE 303
|
250 260 270
....*....|....*....|....*....|...
gi 1093476548 224 ALYESLKRIgvakfTPEFGHLPFVMGEGNKKLS 256
Cdd:TIGR00463 304 YIYRYFGWE-----PPEFIHWGRLKIDDVRALS 331
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
336-486 |
5.63e-28 |
|
Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.
Pssm-ID: 466020 [Multi-domain] Cd Length: 148 Bit Score: 108.82 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 336 DFEQRLRAYLESHFDFPDDYpaDKFAFLATLLQTRVKTLSDAWDLSKFLVVEEDEFTFD--ERSARRNFKEDAVAVLEAT 413
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLDD--EYLKKVVPLLKERAETLSELAELADFFFELPLEYDEEayAKKKMKTNKEESLEVLQEL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093476548 414 IAAVEplSEEDFVTEKLEAALqKALIEDLELKPRKAFGPVRVAVTGAQVSPPLFESMELLGRSRSLSRLRKAL 486
Cdd:pfam19269 79 LPRLE--ALEDWTAEALEAAL-KALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILGKEETLARLRKAI 148
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
4-227 |
2.36e-25 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the 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. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 104.36 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSE--ESYQAIIEALNWLGIDWDEgidvggphgP 81
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDE---------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 82 YRQSQRKDIYADVLQRLIDAGEAYeafstaeeveerhkaagrdpklgydnydrnlteeqkeafraegrkpvIRLRMPDED 161
Cdd:cd09287 73 VIASDRIELYYEYARKLIEMGGAY-----------------------------------------------VHPRTGSKY 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093476548 162 IVFedlvrgriefkaglvpdfviarsngePLYTLVNPVDDALMEITHVLRGEDLLPSTPRQIALYE 227
Cdd:cd09287 106 RVW--------------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYE 145
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
4-70 |
7.52e-13 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 68.05 E-value: 7.52e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWD 70
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY 68
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
4-211 |
1.01e-12 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 70.38 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEgidvggphGPYR 83
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDV--------GPTY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEerhkaagrdpKLGYD----NYDRNLTEEQKEAFR------AEGRKPVI 153
Cdd:PTZ00402 125 SSDYMDLMYEKAEELIKKGLAYCDKTPREEMQ----------KCRFDgvptKYRDISVEETKRLWNemkkgsAEGQETCL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093476548 154 RLRMP--DEDIVFEDLVRGRIEfkagLVPDfviARSNGE----PLYTLVNPVDDALMEITHVLR 211
Cdd:PTZ00402 195 RAKISvdNENKAMRDPVIYRVN----LTPH---ARQGTKykayPTYDFCCPIIDSVEGVTHALR 251
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-116 |
8.04e-11 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 64.36 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIdvggphgpYR 83
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHL--------YY 103
|
90 100 110
....*....|....*....|....*....|...
gi 1093476548 84 QSQRKDIYADVLQRLIDAGEAYEAFSTAEEVEE 116
Cdd:PRK14703 104 ASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRE 136
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
4-211 |
3.75e-09 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 58.87 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIDVGGPHGPYR 83
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEPIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QsqrkdiYADVlqrLIDAGEAYEAfSTAEEVEERHKAAGRDPKlgydnyDRNLT-EEQKEAFR------AEGRKPVIRLR 156
Cdd:PLN03233 92 C------YAII---LIEEGLAYMD-DTPQEEMKKERADRAESK------HRNQSpEEALEMFKemcsgkEEGGAWCLRAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 157 MpdeDIVFED-LVRGRIEFKAGLVPDFviaRS----NGEPLYTLVNPVDDALMEITHVLR 211
Cdd:PLN03233 156 I---DMQSDNgTLRDPVLFRQNTTPHH---RSgtayKAYPTYDLACPIVDSIEGVTHALR 209
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
1-258 |
9.34e-09 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 57.81 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 1 MSDVRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDegidvggphg 80
Cdd:PLN02907 211 EGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD---------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 81 pyRQSQRKDIYADVL---QRLIDAGEAYeAFSTAEEVEERHKAAGRDPKLgydnydRNLTEEQKeafraegrkpvirLRM 157
Cdd:PLN02907 281 --AVTYTSDYFPQLMemaEKLIKEGKAY-VDDTPREQMRKERMDGIESKC------RNNSVEEN-------------LRL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 158 PDEDIV-----FEDLVRGRIEFKA--GLVPDFVIARSNGE------------PLYTLVNPVDDALMEITHVLRGEDLlps 218
Cdd:PLN02907 339 WKEMIAgsergLQCCVRGKLDMQDpnKSLRDPVYYRCNPTphhrigskykvyPTYDFACPFVDALEGVTHALRSSEY--- 415
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1093476548 219 TPRQIALYESLKRIGVAKF-TPEFGHLPFVmgegNKKLSKR 258
Cdd:PLN02907 416 HDRNAQYYRILEDMGLRKVhIWEFSRLNFV----YTLLSKR 452
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
7-176 |
2.11e-08 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 56.53 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 7 RFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGI--DWDEgidvggphgpYRQ 84
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDWVT----------FSS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 85 SQRKDIYADVLQrLIDAGEAYEAFSTAEEV----EERHKAAGRDPKLgydnyDRNLT--EEQKEAFRAEGRKPV-IRLRM 157
Cdd:PTZ00437 125 DYFDQLHEFAVQ-LIKDGKAYVDHSTPDELkqqrEQREDSPWRNRSV-----EENLLlfEHMRQGRYAEGEATLrVKADM 198
|
170
....*....|....*....
gi 1093476548 158 PDEDIVFEDLVRGRIEFKA 176
Cdd:PTZ00437 199 KSDNPNMRDFIAYRVKYVE 217
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-174 |
2.19e-08 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 56.69 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGidWDegidvggphgPYR 83
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WE----------PFK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 84 QSQRKDIYADVLQ---RLIDAGEAYEAFSTAEEVEERhkaagRDPKLGYDNYDR------NLTEEQKEAFRAEGrKPVIR 154
Cdd:PLN02859 333 ITYTSDYFQELYElavELIRRGHAYVDHQTPEEIKEY-----REKKMNSPWRDRpieeslKLFEDMRRGLIEEG-KATLR 406
|
170 180
....*....|....*....|..
gi 1093476548 155 LR--MPDEDIVFEDLVRGRIEF 174
Cdd:PLN02859 407 MKqdMQNDNFNMYDLIAYRIKF 428
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
4-116 |
6.51e-05 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 45.48 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093476548 4 VRVRFCPSPTGTPHVGLIRTALFNWAYARHTGGKLVFRIEDTDAARDSEESYQAIIEALNWLGIDWDEGIdvggphgpYR 83
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGEL--------RY 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 1093476548 84 QSQrkdiYADVL----QRLIDAGEAYEAFSTAEEVEE 116
Cdd:PRK05347 102 ASD----YFDQLyeyaVELIKKGKAYVDDLSAEEIRE 134
|
|
| |
