|
Name |
Accession |
Description |
Interval |
E-value |
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
1-544 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 833.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 1 MSMLLGDHPELRSRAREIASLAARVVEQVNSMPAGEQKRLLSEQYPELARFEEQREKGDKGLPPLPGAVEGRVKLRFAPN 80
Cdd:PRK04156 30 MGKIMGENPELRSKAKEIIPIVKEVVEEVNSLSLEEQRERLEELAPELLEEEEEKKEEKKGLPPLPNAEKGKVVMRFAPN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 81 PDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLREAYDLIRQDLKWLGVSWDEEYIQSLRMEVFYSVARRA 160
Cdd:PRK04156 110 PSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 161 IERGCAYVDNCGREG-KELLSRGEYCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRHPNPSLRDWVAMRIIdte 239
Cdd:PRK04156 190 IEMGGAYVCTCDPEEfKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIV--- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 240 KHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGFILSKSKIRK 319
Cdd:PRK04156 267 KTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRLKIEGFVLSTSKIRK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 320 LLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADRIMYVEDPVEMEV 399
Cdd:PRK04156 347 GIEE--GEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFVRDPVELEI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 400 ELAqvECRAAEIPFHPSRPQRKRRITLCtGDKVLLTREDAVE-GRQLRLMGLSNFTVSQ---GILREVDPSLEYARRMKL 475
Cdd:PRK04156 425 EGA--EPLEAKIPLHPDRPERGEREIPV-GGKVYVSSDDLEAeGKMVRLMDLFNVEITGvsvDKARYHSDDLEEARKNKA 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 476 PIVQWVKKGGEASVEVLEPvelELRRHQGYAEDAIRGYGVDSRLQFVRYGFVRVDSVEDGVYRVIYTHK 544
Cdd:PRK04156 502 PIIQWVPEDESVPVRVLKP---DGGDIEGLAEPDVADLEVDDIVQFERFGFVRIDSVEDDEVVAYFAHK 567
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-544 |
6.70e-161 |
|
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: 469.69 E-value: 6.70e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 1 MSMLLGDHPELRSRAREIASLAARVVEQVNSMPAGEQKRLLSEqypeLARFEEQREKGDKGLPPLPGAVEGRVKLRFAPN 80
Cdd:TIGR00463 26 MGAVMSNNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMKR----LGLDIKKKEKKRKGLRELPGAKMGEVVMRFAPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 81 PDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTktPLREAYDLIRQDLKWLGVSWDEEYIQSLRMEVFYSVARRA 160
Cdd:TIGR00463 102 PSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRR--VDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 161 IERGCAYVDNCGREG-KELLSRGEYCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRHPNPSLRDWVAMRIIDTe 239
Cdd:TIGR00463 180 IEMGKAYVCDCRPEEfRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKT- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 240 khPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGF-ILSKSKIR 318
Cdd:TIGR00463 259 --PHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVrALSTSSAR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 319 KLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADRIMYVEDPVEME 398
Cdd:TIGR00463 337 KGILR--GEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 399 VELAQvECRAAEIPFHPSRPQRKRRITLCTGDkVLLTREDAVEGRQ-LRLMGLSNFTVSQGILREVDPSLEYARRMKLPI 477
Cdd:TIGR00463 415 IVGLP-EPKRVERPLHPDHPEIGERVLILRGE-IYVPKDDLEEGVEpVRLMDAVNVIYSKKELRYHSEGLEGARKLGKSI 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300666188 478 VQWVKKGGEASVEVLEPvelELRRHQGYAEDAIRGYGVDSRLQFVRYGFVRVDSVEDGVYRVIYTHK 544
Cdd:TIGR00463 493 IHWLPAKDAVKVKVIMP---DASIVEGVIEADASELEVGDVVQFERFGFARLDSADKDGMVFVYTHP 556
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
72-387 |
2.46e-138 |
|
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: 399.80 E-value: 2.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 72 RVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLREAYDLIRQDLKWLGVSWDEEYIQSLRME 151
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVdncgregkellsrgeycptrdlgpednlelfekmlegefyegeavvrmktdprhpnpslrdwv 231
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 232 amriidtekhpHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGFI 311
Cdd:cd09287 98 -----------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300666188 312 LSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADR 387
Cdd:cd09287 167 LSTSKIRKGIES--GEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
69-398 |
5.41e-86 |
|
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: 273.98 E-value: 5.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 69 VEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE-YIQS 147
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTE--EAVDAILEDLRWLGLDWDEGpYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 148 LRMEVFYSVARRAIERGCAYVDNCGREG-----KELLSRGE---Y-CPTRDLGPEdnlELFEKMLEGEfyegEAVVRMKT 218
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEElealrETQTAPGKpprYdGRCRDLSPE---ELERMLAAGE----PPVLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 219 DPRH-------------PNPSLRDWVAMRiidTEKhphplvgsrylvWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQ 285
Cdd:COG0008 152 PEEGvvfddlvrgeitfPNPNLRDPVLYR---ADG------------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 286 LAVYRCMGWRPPyfiHFGRLKL----EGFILSKSKirklleerpGEFmgyddprfgTIAGLRRRGVLAEAIRQIILEVGV 361
Cdd:COG0008 217 IWLYEALGWEPP---EFAHLPLilgpDGTKLSKRK---------GAV---------TVSGLRRRGYLPEAIRNYLALLGW 275
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 300666188 362 KPTDAT--ISWANLAAANrkllD-ERADRIMYVEDPVEME 398
Cdd:COG0008 276 SKSDDQeiFSLEELIEAF----DlDRVSRSPAVFDPVKLV 311
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
73-383 |
8.68e-83 |
|
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: 260.33 E-value: 8.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 73 VKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE-YIQSLRME 151
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETP--EFEESILEDLKWLGIKWDYGpYYQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVDNCG----REGKELLSRGEyCPTRDLGPEDNLELF-EKMLEGEFYEGEAVVRMKTDPRHPnPS 226
Cdd:pfam00749 80 IYYKYAEELIKKGKAYVCFCTpeelEEEREEQEALG-SPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 227 LRDWVAMRIIDTEKHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIH-FGRL 305
Cdd:pfam00749 158 FRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHeYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 306 KLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGV-KPTDATISWANLAAANRKLLDE 383
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDI--SQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGViKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
1-544 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 833.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 1 MSMLLGDHPELRSRAREIASLAARVVEQVNSMPAGEQKRLLSEQYPELARFEEQREKGDKGLPPLPGAVEGRVKLRFAPN 80
Cdd:PRK04156 30 MGKIMGENPELRSKAKEIIPIVKEVVEEVNSLSLEEQRERLEELAPELLEEEEEKKEEKKGLPPLPNAEKGKVVMRFAPN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 81 PDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLREAYDLIRQDLKWLGVSWDEEYIQSLRMEVFYSVARRA 160
Cdd:PRK04156 110 PSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDPEAYDMILEDLKWLGVKWDEVVIQSDRLEIYYEYARKL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 161 IERGCAYVDNCGREG-KELLSRGEYCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRHPNPSLRDWVAMRIIdte 239
Cdd:PRK04156 190 IEMGGAYVCTCDPEEfKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRDWVAFRIV--- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 240 KHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGFILSKSKIRK 319
Cdd:PRK04156 267 KTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRLKIEGFVLSTSKIRK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 320 LLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADRIMYVEDPVEMEV 399
Cdd:PRK04156 347 GIEE--GEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINRKLIDPIANRYFFVRDPVELEI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 400 ELAqvECRAAEIPFHPSRPQRKRRITLCtGDKVLLTREDAVE-GRQLRLMGLSNFTVSQ---GILREVDPSLEYARRMKL 475
Cdd:PRK04156 425 EGA--EPLEAKIPLHPDRPERGEREIPV-GGKVYVSSDDLEAeGKMVRLMDLFNVEITGvsvDKARYHSDDLEEARKNKA 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 476 PIVQWVKKGGEASVEVLEPvelELRRHQGYAEDAIRGYGVDSRLQFVRYGFVRVDSVEDGVYRVIYTHK 544
Cdd:PRK04156 502 PIIQWVPEDESVPVRVLKP---DGGDIEGLAEPDVADLEVDDIVQFERFGFVRIDSVEDDEVVAYFAHK 567
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-544 |
6.70e-161 |
|
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: 469.69 E-value: 6.70e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 1 MSMLLGDHPELRSRAREIASLAARVVEQVNSMPAGEQKRLLSEqypeLARFEEQREKGDKGLPPLPGAVEGRVKLRFAPN 80
Cdd:TIGR00463 26 MGAVMSNNPELRKKAKEVLEAVEAAVEEVNSLSPEEQKELMKR----LGLDIKKKEKKRKGLRELPGAKMGEVVMRFAPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 81 PDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTktPLREAYDLIRQDLKWLGVSWDEEYIQSLRMEVFYSVARRA 160
Cdd:TIGR00463 102 PSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRR--VDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 161 IERGCAYVDNCGREG-KELLSRGEYCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRHPNPSLRDWVAMRIIDTe 239
Cdd:TIGR00463 180 IEMGKAYVCDCRPEEfRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKT- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 240 khPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGF-ILSKSKIR 318
Cdd:TIGR00463 259 --PHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVrALSTSSAR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 319 KLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADRIMYVEDPVEME 398
Cdd:TIGR00463 337 KGILR--GEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 399 VELAQvECRAAEIPFHPSRPQRKRRITLCTGDkVLLTREDAVEGRQ-LRLMGLSNFTVSQGILREVDPSLEYARRMKLPI 477
Cdd:TIGR00463 415 IVGLP-EPKRVERPLHPDHPEIGERVLILRGE-IYVPKDDLEEGVEpVRLMDAVNVIYSKKELRYHSEGLEGARKLGKSI 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300666188 478 VQWVKKGGEASVEVLEPvelELRRHQGYAEDAIRGYGVDSRLQFVRYGFVRVDSVEDGVYRVIYTHK 544
Cdd:TIGR00463 493 IHWLPAKDAVKVKVIMP---DASIVEGVIEADASELEVGDVVQFERFGFARLDSADKDGMVFVYTHP 556
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
72-387 |
2.46e-138 |
|
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: 399.80 E-value: 2.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 72 RVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLREAYDLIRQDLKWLGVSWDEEYIQSLRME 151
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVdncgregkellsrgeycptrdlgpednlelfekmlegefyegeavvrmktdprhpnpslrdwv 231
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 232 amriidtekhpHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGFI 311
Cdd:cd09287 98 -----------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300666188 312 LSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADR 387
Cdd:cd09287 167 LSTSKIRKGIES--GEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
69-398 |
5.41e-86 |
|
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: 273.98 E-value: 5.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 69 VEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE-YIQS 147
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTE--EAVDAILEDLRWLGLDWDEGpYYQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 148 LRMEVFYSVARRAIERGCAYVDNCGREG-----KELLSRGE---Y-CPTRDLGPEdnlELFEKMLEGEfyegEAVVRMKT 218
Cdd:COG0008 79 DRFDIYYEYAEKLIEKGKAYVCFCTPEElealrETQTAPGKpprYdGRCRDLSPE---ELERMLAAGE----PPVLRFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 219 DPRH-------------PNPSLRDWVAMRiidTEKhphplvgsrylvWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQ 285
Cdd:COG0008 152 PEEGvvfddlvrgeitfPNPNLRDPVLYR---ADG------------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 286 LAVYRCMGWRPPyfiHFGRLKL----EGFILSKSKirklleerpGEFmgyddprfgTIAGLRRRGVLAEAIRQIILEVGV 361
Cdd:COG0008 217 IWLYEALGWEPP---EFAHLPLilgpDGTKLSKRK---------GAV---------TVSGLRRRGYLPEAIRNYLALLGW 275
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 300666188 362 KPTDAT--ISWANLAAANrkllD-ERADRIMYVEDPVEME 398
Cdd:COG0008 276 SKSDDQeiFSLEELIEAF----DlDRVSRSPAVFDPVKLV 311
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
73-383 |
8.68e-83 |
|
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: 260.33 E-value: 8.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 73 VKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE-YIQSLRME 151
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETP--EFEESILEDLKWLGIKWDYGpYYQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVDNCG----REGKELLSRGEyCPTRDLGPEDNLELF-EKMLEGEFYEGEAVVRMKTDPRHPnPS 226
Cdd:pfam00749 80 IYYKYAEELIKKGKAYVCFCTpeelEEEREEQEALG-SPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 227 LRDWVAMRIIDTEKHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIH-FGRL 305
Cdd:pfam00749 158 FRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHeYLRL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 306 KLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGV-KPTDATISWANLAAANRKLLDE 383
Cdd:pfam00749 238 NLDGTKLSKRKLSWSVDI--SQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGViKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
71-544 |
1.38e-66 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 229.99 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 71 GRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDE-EYIQSLR 149
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDT--EYVEAIKDDVRWLGFDWGEhLYYASDY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 150 MEVFYSVARRAIERGCAYVDNCGREG-KELlsRGEY------CPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRH 222
Cdd:PRK14703 108 FERMYAYAEQLIKMGLAYVDSVSEEEiREL--RGTVtepgtpSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 223 PNPSLRDWVAMRIidteKH-PHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTekqlAVY-----RCMGWRP 296
Cdd:PRK14703 186 PNMKLRDPLLYRI----RHaHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNR----AIYdwvldHLGPWPP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 297 -PYFIHFGRLKLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAA 375
Cdd:PRK14703 258 rPRQYEFARLALGYTVMSKRKLRELVEE--GYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 376 ANRKLLDERADRIMYVEDPVEMEVE-LAQVECRAAEIPFHPSRPQRKRRITLCTGDKVLLTREDAVE-----------GR 443
Cdd:PRK14703 336 AIRDDLNRRAPRVMAVLDPLKVVIEnLPAGKVEELDLPYWPHDVPKEGSRKVPFTRELYIERDDFSEdppkgfkrltpGR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 444 QLRLMGLSNFTV------SQGILREVDPSLEYARRMKLP-------IVQWVKKGGEASVEV--------------LEPVE 496
Cdd:PRK14703 416 EVRLRGAYIIRCdevvrdADGAVTELRCTYDPESAKGEDtgrkaagVIHWVSAKHALPAEVrlydrlfkvpqpeaADEDF 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 300666188 497 LE------LRRHQGYAEDAIRGYGVDSRLQFVRYG-FVR--VDSVEDG-VYRVIYTHK 544
Cdd:PRK14703 496 LEflnpdsLRVAQGRVEPAVRDDPADTRYQFERQGyFWAdpVDSRPDAlVFNRIITLK 553
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
53-452 |
2.47e-58 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 204.43 E-value: 2.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 53 EQREKGDKGLppLPGAVEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLREAydLIRQD 132
Cdd:PTZ00402 35 NANEENDKLQ--LTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ--AILDD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 133 LKWLGVSWDE-EYIQSLRMEVFYSVARRAIERGCAYVDNCGREGKElLSRGEYCPT--RDLGPEDNLELFEKMLEGEFYE 209
Cdd:PTZ00402 111 LATLGVSWDVgPTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQ-KCRFDGVPTkyRDISVEETKRLWNEMKKGSAEG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 210 GEAVVRMKTDPRHPNPSLRDWVAMRIIDTekhPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVY 289
Cdd:PTZ00402 190 QETCLRAKISVDNENKAMRDPVIYRVNLT---PHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFC 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 290 RCMGWRPPYFIHFGRLKLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATIS 369
Cdd:PTZ00402 267 DALGIRKPIVEDFSRLNMEYSVMSKRKLTQLVDT--HVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFME 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 370 WANLAAANRKLLDERADRIMYVEDP--VEMEVElAQVECRAAEIPFHPSRPQRKRRiTLCTGDKVLLTREDAV---EGRQ 444
Cdd:PTZ00402 345 WSKLWYFNTQILDPSVPRYTVVSNTlkVRCTVE-GQIHLEACEKLLHKKVPDMGEK-TYYKSDVIFLDAEDVAllkEGDE 422
|
....*...
gi 300666188 445 LRLMGLSN 452
Cdd:PTZ00402 423 VTLMDWGN 430
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
65-445 |
5.43e-58 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 201.78 E-value: 5.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 65 LPGAVEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDP-RTKTPLREAydlIRQDLKWLGVSWDEE 143
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPsKEKAEFEES---IIEDLGKIEIKPDSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 144 YIQSLRMEVFYSVARRAIERGCAYVDNCGRE--GKELLSRGEyCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPR 221
Cdd:PLN03233 81 SFTSDYFEPIRCYAIILIEEGLAYMDDTPQEemKKERADRAE-SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 222 HPNPSLRDWVAMRIIDTekhPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIH 301
Cdd:PLN03233 160 SDNGTLRDPVLFRQNTT---PHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 302 FGRLKLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLL 381
Cdd:PLN03233 237 FARMNFMNTVLSKRKLTWFVDN--GHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEI 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 382 DERADRIMYVE--DPVEMEVELAQVECRAA--EIPFHPSRPQ-RKRRITLCtgDKVLLTREDaVEGRQL 445
Cdd:PLN03233 315 DKRAKRFMAIDkaDHTALTVTNADEEADFAfsETDCHPKDPGfGKRAMRIC--DEVLLEKAD-TEDIQL 380
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
71-530 |
4.55e-57 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 200.21 E-value: 4.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 71 GRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPLReaYDLIRQDLKWLG-----VSWDEEYI 145
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVY--IDAIMEMVKWMGwkpdwVTFSSDYF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 146 QSLrmevfYSVARRAIERGCAYVD-NCGREGKELLSRGEYCPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMKTDPRHPN 224
Cdd:PTZ00437 128 DQL-----HEFAVQLIKDGKAYVDhSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 225 PSLRDWVAMRIIDTEkHPHplVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMG-WRpPYFIHFG 303
Cdd:PTZ00437 203 PNMRDFIAYRVKYVE-HPH--AKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNlWR-PHVWEFS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 304 RLKLEGFILSKSKIRKLLeeRPGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDE 383
Cdd:PTZ00437 279 RLNVTGSLLSKRKINVLV--RKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 384 RADRIMYVEDPVEMEVELAQVEcRAAEIPFHPSRPQRKRRITLCTgDKVLLTRED-AVEGRQLRLMGLS----------- 451
Cdd:PTZ00437 357 RCERRLMVIDPIKVVVDNWKGE-REFECPNHPRKPELGSRKVMFT-DTFYVDRSDfRTEDNNSKFYGLApgprvvglkys 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 452 ------NFTVS---QGILREVDPSLEYARRMKLPIvQWVKKGGEASVEV-------------LEPVELEL------RRHQ 503
Cdd:PTZ00437 435 gnvvckGFEVDaagQPSVIHVDIDFERKDKPKTNI-SWVSATACTPVEVrlynallkddraaIDPEFLKFidedseVVSH 513
|
490 500
....*....|....*....|....*..
gi 300666188 504 GYAEDAIRGYGVDSRLQFVRYGFVRVD 530
Cdd:PTZ00437 514 GYAEKGIENAKHFESVQAERFGYFVVD 540
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
58-452 |
5.11e-57 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 203.03 E-value: 5.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 58 GDKGLPP--LPGAVEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTplREAYDLIRQDLKW 135
Cdd:PLN02907 197 KDKGSFEvdLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKES--DEFVENILKDIET 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 136 LGVSWDE-----EYIQSLrMEvfysVARRAIERGCAYVDNCGREG--KELLsRGEYCPTRDLGPEDNLELFEKMLEGEFY 208
Cdd:PLN02907 275 LGIKYDAvtytsDYFPQL-ME----MAEKLIKEGKAYVDDTPREQmrKERM-DGIESKCRNNSVEENLRLWKEMIAGSER 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 209 EGEAVVRMKTDPRHPNPSLRDWVAMRIIDTekhPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAV 288
Cdd:PLN02907 349 GLQCCVRGKLDMQDPNKSLRDPVYYRCNPT---PHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRI 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 289 YRCMGWRPPYFIHFGRLKLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATI 368
Cdd:PLN02907 426 LEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDN--GKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLM 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 369 SWANLAAANRKLLDERADRIMYVED-----------PVEMEVELaqvecraaeIPFHPSRPQRKRRITLCTgDKVLLTRE 437
Cdd:PLN02907 504 EWDKLWTINKKIIDPVCPRHTAVLKegrvlltltdgPETPFVRI---------IPRHKKYEGAGKKATTFT-NRIWLDYA 573
|
410
....*....|....*...
gi 300666188 438 DAV---EGRQLRLMGLSN 452
Cdd:PLN02907 574 DAEaisEGEEVTLMDWGN 591
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
71-437 |
8.29e-57 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 199.17 E-value: 8.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 71 GRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSW-DEEYIQSLR 149
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQ--EYVDSIKEDVRWLGFDWsGELRYASDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 150 MEVFYSVARRAIERGCAYVD------------NCGREGKEllSrgeycPTRDLGPEDNLELFEKMLEGEFYEGEAVVRMK 217
Cdd:PRK05347 106 FDQLYEYAVELIKKGKAYVDdlsaeeireyrgTLTEPGKN--S-----PYRDRSVEENLDLFERMRAGEFPEGSAVLRAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 218 TDPRHPNPSLRDWVAMRIIdteKHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTE------KQLAVyRC 291
Cdd:PRK05347 179 IDMASPNINMRDPVLYRIR---HAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPlydwvlDNLPI-PP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 292 mgwrPPYFIHFGRLKLEGFILSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWA 371
Cdd:PRK05347 255 ----HPRQYEFSRLNLTYTVMSKRKLKQLVEE--KHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMS 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300666188 372 NLAAANRKLLDERADRIMYVEDPVEMEVE---LAQVEcrAAEIPFHPSRPQRKRRitlctgdKVLLTRE 437
Cdd:PRK05347 329 MLESCIREDLNENAPRAMAVLDPLKLVITnypEGQVE--ELEAPNHPEDPEMGTR-------EVPFSRE 388
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
72-383 |
6.05e-52 |
|
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: 176.89 E-value: 6.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 72 RVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPrtKTPLREAYDLIRQDLKWLGVSWDEE-YIQSLRM 150
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDP--ERSRPEYVESILEDLKWLGLDWDEGpYRQSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 151 EVFYSVARRAIERGcayvdncgregkellsrgeycptrdlgpednlelfekmlegefyegeavvrmktdprhpnpslrdw 230
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 231 vamriidtekhphplvgsrylVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLE-G 309
Cdd:cd00418 93 ---------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEdG 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 310 FILSKSKIRklleerpgefmgyddprfGTIAGLRRRGVLAEAIRQIILEVGVK-----------------------PTDA 366
Cdd:cd00418 152 TKLSKRKLN------------------TTLRALRRRGYLPEALRNYLALIGWSkpdghelftleemiaafsvervnSADA 213
|
330
....*....|....*..
gi 300666188 367 TISWANLAAANRKLLDE 383
Cdd:cd00418 214 TFDWAKLEWLNREYIRE 230
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
72-387 |
1.15e-49 |
|
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: 171.28 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 72 RVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEEYIQSLRME 151
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEE--EYVDSIKEDVKWLGIKPYKVTYASDYFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVdncgregkellsrgeycptrdlgpednlelfekmlegefyegeavvrmktdprhpnpslrdwv 231
Cdd:cd00807 79 QLYEYAEQLIKKGKAYV--------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 232 amriidtekhpHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFGRLKLEGFI 311
Cdd:cd00807 96 -----------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTV 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300666188 312 LSKSKIRKLLEErpGEFMGYDDPRFGTIAGLRRRGVLAEAIRQIILEVGVKPTDATISWANLAAANRKLLDERADR 387
Cdd:cd00807 165 MSKRKLLQLVDE--GYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
50-394 |
5.01e-46 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 172.64 E-value: 5.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 50 RFEEQREKGDKGLPplpgAVEGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTplREAYDLI 129
Cdd:PLN02859 246 RPSNTKEILEKHLK----ATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEK--KEYIDHI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 130 RQDLKWLG-----VSWDEEYIQSLrmevfYSVARRAIERGCAYVDN-CGREGKELLSRGEYCPTRDLGPEDNLELFEKML 203
Cdd:PLN02859 320 EEIVEWMGwepfkITYTSDYFQEL-----YELAVELIRRGHAYVDHqTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMR 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 204 EGEFYEGEAVVRMKTDPRHPNPSLRDWVAMRIIDTekhPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLrgkeHQLNTE 283
Cdd:PLN02859 395 RGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFT---PHPHAGDKWCIYPSYDYAHCIVDSLENITHSL----CTLEFE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 284 KQLAVY----RCMGWRPPYFIHFGRLKLEGFILSKSKIRKLLEERPGEfmGYDDPRFGTIAGLRRRGVLAEAIRQIILEV 359
Cdd:PLN02859 468 TRRASYywllDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVD--GWDDPRLLTLAGLRRRGVTPTAINAFCRGI 545
|
330 340 350
....*....|....*....|....*....|....*.
gi 300666188 360 GVKPTD-ATISWANLAAANRKLLDERADRIMYVEDP 394
Cdd:PLN02859 546 GITRSDnSLIRMDRLEHHIREELNKTAPRTMVVLHP 581
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
73-352 |
1.25e-42 |
|
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: 158.67 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 73 VKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE-YIQSLRME 151
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIE--EAEEAILEGLKWLGISWDEGpYYQSQRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 152 VFYSVARRAIERGCAYVDNCG-----REGKELLSRGEycPTRDLGPEDNLElfEKMLEGEFYEGEA-VVRMKTdPRHPNP 225
Cdd:TIGR00464 80 IYKKYAKELLEEGLAYRCYCSkerleRLREEQKANKE--TPRYDGRCRNLH--EEEIENKLAKGIPpVVRFKI-PQEAVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 226 SLRDWVAMRIIDTEKHPHPLVGSRYLVWPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHFgrl 305
Cdd:TIGR00464 155 SFNDQVRGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHL--- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 300666188 306 kleGFILSKSkiRKLLEERPGEfmgyddprfGTIAGLRRRGVLAEAI 352
Cdd:TIGR00464 232 ---PMILDED--GKKLSKRDGA---------TSIMQFKEQGYLPEAL 264
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
73-368 |
4.69e-38 |
|
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: 140.03 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 73 VKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTPlrEAYDLIRQDLKWLGVSWDEE--------- 143
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVP--EAEEAILEALKWLGLDWDEGpdvggpygp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 144 YIQSLRMEVFYSVARRAIERGcayvdncgregkellsrgeycptrdlgpeDNLelfekmlegefyegeavvrmktdprhp 223
Cdd:cd00808 80 YRQSERLEIYRKYAEKLLEKG-----------------------------DGF--------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 224 npslrdwvamriidtekhphplvgsrylvwPTYNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPPYFIHfg 303
Cdd:cd00808 104 ------------------------------PTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAH-- 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300666188 304 rLKLegfIL--SKSKIRKlleeRPGEFmgyddprfgTIAGLRRRGVLAEAIRQIILEVGVKPTDATI 368
Cdd:cd00808 152 -LPL---ILnpDGKKLSK----RKGDT---------SISDYREEGYLPEALLNYLALLGWSPPDGEE 201
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
70-301 |
7.56e-33 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 131.79 E-value: 7.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 70 EGRVKLRFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTDPRTKTplREAYDLIRQDLKWLGVSWDE------- 142
Cdd:PLN02627 43 GGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARST--KESEEAVLRDLKWLGLDWDEgpdvgge 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 143 --EYIQSLRMEVFYSVARRAIERGCAYVDNCGREgkELLSRGEYCPTRDLGPE--------DNLELFEKMLEGEFY---- 208
Cdd:PLN02627 121 ygPYRQSERNAIYKQYAEKLLESGHVYPCFCTDE--ELEAMKEEAELKKLPPRytgkwataSDEEVQAELAKGTPYtyrf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 209 ---EGEAV---------VRMKTDprhpnpSLRDWVAMRiidtekhphplvgSRYLvwPTYNFAVSVDDHMMEITHVLRGK 276
Cdd:PLN02627 199 rvpKEGSVkiddlirgeVSWNTD------TLGDFVLLR-------------SNGQ--PVYNFCVAVDDATMGITHVIRAE 257
|
250 260
....*....|....*....|....*
gi 300666188 277 EHQLNTEKQLAVYRCMGWRPPYFIH 301
Cdd:PLN02627 258 EHLPNTLRQALIYKALGFPMPRFAH 282
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
385-530 |
2.81e-27 |
|
tRNA synthetases class I (E and Q), anti-codon binding 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: 427609 [Multi-domain] Cd Length: 175 Bit Score: 108.13 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 385 ADRIMYVEDPVEMEVE-LAQVECRAAEIPFHPSRPQR-KRRITLctGDKVLLTREDA---VEGRQLRLMGLSNFTVS--- 456
Cdd:pfam03950 1 APRYMAVLDPVKVVIEnYPEGQEETAEVPNHPKNPELgTRKVPF--SREIYIEREDFkrlAPGEEVRLMDAYNIKVTevv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 457 ---QGILREV----DP-SLEYARRMKLPIVQWVKKGGEASVE----------------VLEPVELElRRHQGYAEDAIRG 512
Cdd:pfam03950 79 kdeDGNVTELhctyDGdDLGGARKVKGKIIHWVSASDAVPAEvrlydrlfkdeddadfLLNPDSLK-VLTEGLAEPALAN 157
|
170
....*....|....*...
gi 300666188 513 YGVDSRLQFVRYGFVRVD 530
Cdd:pfam03950 158 LKPGDIVQFERIGYFRVD 175
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
76-315 |
3.55e-24 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 102.62 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 76 RFAPNPDFVIHMGNARPAIVNHEYARMYKGRMVLRFEDTD-PRTKtplREAYDLIRQDLKWLGVSWDEEYI-QSLRMEVF 153
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDpPREV---PGAADAILADLEWLGLHWDGPVLyQSQRHDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 154 YSVARRAIERGCAYVDNCGRegKELLSRgeycPTRDLGPednlelfekmleGEFYEGeaVVRMKTDPRHPNPSLRdwvaM 233
Cdd:PRK05710 86 RAALDRLRAQGLVYPCFCSR--KEIAAA----APAPPDG------------GGIYPG--TCRDLLHGPRNPPAWR----L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300666188 234 RIIDTEKHPHPLVGSRYLVWPT----------------YNFAVSVDDHMMEITHVLRGKEHQLNTEKQLAVYRCMGWRPP 297
Cdd:PRK05710 142 RVPDAVIAFDDRLQGRQHQDLAlavgdfvlrradglfaYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTP 221
|
250 260
....*....|....*....|
gi 300666188 298 YFIHfGRLKL--EGFILSKS 315
Cdd:PRK05710 222 RYLH-LPLVLnaDGQKLSKQ 240
|
|
| |
