|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-476 |
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: 575.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 1 MAIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIE 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 81 QHREAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNEsIQWNDL 160
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 161 VRGPMNWTGKDLgGDMVIARrapANeiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPL 240
Cdd:COG0008 162 VRGEITFPNPNL-RDPVLYR---AD--GYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 241 ILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSIPDGmDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKWLN 320
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-QEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 321 SQTIHDSSSEEILKAVEPLFNKEGWDlpnlEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPLLNQDAINQLEIEGAKDSL 400
Cdd:COG0008 315 GPYIRALDDEELAELLAPELPEAGIR----EDLERLVPLVRERAKTLSELAELARFFFIEREDEKAAKKRLAPEEVRKVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238687201 401 KILLKQIDtsKINKLTVEHAKKLINDAAVFGGFKKGLIMKSLRAALLGCLQGPDVINSWILLseiNQDKS--RIERCL 476
Cdd:COG0008 391 KAALEVLE--AVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELL---GKERVfeRLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-462 |
0e+00 |
|
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: 544.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNESIQWNDLVR 162
Cdd:TIGR00464 82 KKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 163 GPMNWTGKDLgGDMVIARRApaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPLIL 242
Cdd:TIGR00464 162 GEITFQNSEL-DDFVILRSD-----GSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 243 NAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSiPDGMDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKWLNSQ 322
Cdd:TIGR00464 236 DEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWS-PPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 323 TIHDSSSEEILKAVEP-LFNKEGWDLPNLEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPL-LNQDAINQLEIEGAKDSL 400
Cdd:TIGR00464 315 YIKELPDEELFELLDPhLKSLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKeVDEDAFKKHLKKNVKEVL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238687201 401 KILLKQIdtSKINKLTVEHAKKLINDAAVFGGFKKGLIMKSLRAALLGCLQGPDVINSWILL 462
Cdd:TIGR00464 395 EALKKKL--QALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-473 |
3.09e-137 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 405.66 E-value: 3.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 2 AIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPII------- 74
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygpy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 75 -QSNRIEQHREAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNE 153
Cdd:PLN02627 125 rQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 154 SIQWNDLVRGPMNWTgKDLGGDMVIARrapANeiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP 233
Cdd:PLN02627 205 SVKIDDLIRGEVSWN-TDTLGDFVLLR---SN--GQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 234 KFAHTPLILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSipDGMD-EKFTIEESSKVFDFDRVNKAGAKFD 312
Cdd:PLN02627 279 RFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN--DGTEnEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 313 WEKLKWLNSQTIHDSSSEEILKAVEPLFNKEG-WDLPNLEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPLLnqdaiNQL 391
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGiLKESDGSFVKEAVELLKDGIELVTDADKELLNLLSYPLA-----ATL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 392 EIEGAKDSLK--------ILLKQIDTSKINKLTVEHA---KKLINDAAVFGGFK-KGLIMkSLRAALLGCLQGPDVINSW 459
Cdd:PLN02627 432 SSPEAKTVVEdnfsevadALIAAYDSGELAAALEEGHdgwQKWVKAFGKALKRKgKRLFM-PLRVALTGKMHGPDVGESL 510
|
490
....*....|....
gi 238687201 460 ILLSEINQDKSRIE 473
Cdd:PLN02627 511 VLLHKAGTPDSVTE 524
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-318 |
1.42e-118 |
|
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: 350.08 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKP--PRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNESIQWNDL 160
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 161 VRGPMNWTGKDLggDMVIARRAPaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPL 240
Cdd:pfam00749 162 VRGRIKFTPQEI--HDRTGVKWD----GYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 241 ILNAEGKKLSKRDGVTS--ISDFKEMGYTSKAMSNYMTLLGWSiPDGMDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKW 318
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWT-PEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-325 |
3.56e-117 |
|
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: 343.41 E-value: 3.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 2 AIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWD--------AEPI 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDegpdvggpYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 74 IQSNRIEQHREAIKYLLEKGlayrcftteeelaamreeqksrnkpprydnrhrslsteeesnflsegrtavirfriddne 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 154 siqwndlvrgpmnwtgkdlggdmviarrapaneIGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP 233
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 234 KFAHTPLILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSIPDGmDEKFTIEESSKVFDFDRVNKAGAKFDW 313
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-EEFFTLEELIELFDLERVSKSPAIFDP 226
|
330
....*....|..
gi 238687201 314 EKLKWLNSQTIH 325
Cdd:cd00808 227 EKLDWLNGQYIR 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-476 |
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: 575.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 1 MAIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIE 80
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 81 QHREAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNEsIQWNDL 160
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELERMLAAGEPPVLRFKIPEEG-VVFDDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 161 VRGPMNWTGKDLgGDMVIARrapANeiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPL 240
Cdd:COG0008 162 VRGEITFPNPNL-RDPVLYR---AD--GYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 241 ILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSIPDGmDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKWLN 320
Cdd:COG0008 236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDD-QEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 321 SQTIHDSSSEEILKAVEPLFNKEGWDlpnlEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPLLNQDAINQLEIEGAKDSL 400
Cdd:COG0008 315 GPYIRALDDEELAELLAPELPEAGIR----EDLERLVPLVRERAKTLSELAELARFFFIEREDEKAAKKRLAPEEVRKVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238687201 401 KILLKQIDtsKINKLTVEHAKKLINDAAVFGGFKKGLIMKSLRAALLGCLQGPDVINSWILLseiNQDKS--RIERCL 476
Cdd:COG0008 391 KAALEVLE--AVETWDPETVKGTIHWVSAEAGVKDGLLFMPLRVALTGRTVEPSLFDVLELL---GKERVfeRLGYAI 463
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
3-462 |
0e+00 |
|
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: 544.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:TIGR00464 2 VRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNESIQWNDLVR 162
Cdd:TIGR00464 82 KKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNLHEEEIENKLAKGIPPVVRFKIPQEAVVSFNDQVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 163 GPMNWTGKDLgGDMVIARRApaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPLIL 242
Cdd:TIGR00464 162 GEITFQNSEL-DDFVILRSD-----GSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 243 NAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSiPDGMDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKWLNSQ 322
Cdd:TIGR00464 236 DEDGKKLSKRDGATSIMQFKEQGYLPEALINYLALLGWS-PPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLNAH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 323 TIHDSSSEEILKAVEP-LFNKEGWDLPNLEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPL-LNQDAINQLEIEGAKDSL 400
Cdd:TIGR00464 315 YIKELPDEELFELLDPhLKSLVNTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDKKeVDEDAFKKHLKKNVKEVL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238687201 401 KILLKQIdtSKINKLTVEHAKKLINDAAVFGGFKKGLIMKSLRAALLGCLQGPDVINSWILL 462
Cdd:TIGR00464 395 EALKKKL--QALEEWTADEVKSAIKQIAEELGLKGKKVFMPLRLALTGKGHGPDLAQILELI 454
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-473 |
3.09e-137 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 405.66 E-value: 3.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 2 AIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPII------- 74
Cdd:PLN02627 45 PVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEGPDVggeygpy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 75 -QSNRIEQHREAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNE 153
Cdd:PLN02627 125 rQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAELAKGTPYTYRFRVPKEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 154 SIQWNDLVRGPMNWTgKDLGGDMVIARrapANeiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP 233
Cdd:PLN02627 205 SVKIDDLIRGEVSWN-TDTLGDFVLLR---SN--GQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 234 KFAHTPLILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSipDGMD-EKFTIEESSKVFDFDRVNKAGAKFD 312
Cdd:PLN02627 279 RFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN--DGTEnEIFTLEELVEKFSIDRINKSGAVFD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 313 WEKLKWLNSQTIHDSSSEEILKAVEPLFNKEG-WDLPNLEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPLLnqdaiNQL 391
Cdd:PLN02627 357 STKLKWMNGQHLRLLPEEELVKLVGERWKSAGiLKESDGSFVKEAVELLKDGIELVTDADKELLNLLSYPLA-----ATL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 392 EIEGAKDSLK--------ILLKQIDTSKINKLTVEHA---KKLINDAAVFGGFK-KGLIMkSLRAALLGCLQGPDVINSW 459
Cdd:PLN02627 432 SSPEAKTVVEdnfsevadALIAAYDSGELAAALEEGHdgwQKWVKAFGKALKRKgKRLFM-PLRVALTGKMHGPDVGESL 510
|
490
....*....|....
gi 238687201 460 ILLSEINQDKSRIE 473
Cdd:PLN02627 511 VLLHKAGTPDSVTE 524
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
3-318 |
1.42e-118 |
|
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: 350.08 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEQKSRNKP--PRYDNRHRSLSTEEESNFLSEGRTAVIRFRIDDNESIQWNDL 160
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQEALGSPsrDRYDEENLHLFEEEMKKGSAEGGPATVRAKIPMESPYVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 161 VRGPMNWTGKDLggDMVIARRAPaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPL 240
Cdd:pfam00749 162 VRGRIKFTPQEI--HDRTGVKWD----GYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 241 ILNAEGKKLSKRDGVTS--ISDFKEMGYTSKAMSNYMTLLGWSiPDGMDEKFTIEESSKVFDFDRVNKAGAKFDWEKLKW 318
Cdd:pfam00749 236 RLNLDGTKLSKRKLSWSvdISQVKGWGDPREATLNGLRRRGWT-PEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
2-325 |
3.56e-117 |
|
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: 343.41 E-value: 3.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 2 AIKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWD--------AEPI 73
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDegpdvggpYGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 74 IQSNRIEQHREAIKYLLEKGlayrcftteeelaamreeqksrnkpprydnrhrslsteeesnflsegrtavirfriddne 153
Cdd:cd00808 81 RQSERLEIYRKYAEKLLEKG------------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 154 siqwndlvrgpmnwtgkdlggdmviarrapaneIGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP 233
Cdd:cd00808 101 ---------------------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 234 KFAHTPLILNAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSIPDGmDEKFTIEESSKVFDFDRVNKAGAKFDW 313
Cdd:cd00808 148 KFAHLPLILNPDGKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDG-EEFFTLEELIELFDLERVSKSPAIFDP 226
|
330
....*....|..
gi 238687201 314 EKLKWLNSQTIH 325
Cdd:cd00808 227 EKLDWLNGQYIR 238
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
3-324 |
9.28e-93 |
|
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: 280.90 E-value: 9.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGlayrcftteeelaamreeqksrnkpprydnrhrslsteeesnflsegrtavirfriddnesiqwndlvr 162
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 163 gpmnwtgkdlggdmviarrapaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPLIL 242
Cdd:cd00418 93 -------------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 243 NAEGKKLSKRDGVTSISDFKEMGYTSKAMSNYMTLLGWSIPDGMDEkFTIEESSKVFDFDRVNKAGAKFDWEKLKWLNSQ 322
Cdd:cd00418 148 LEDGTKLSKRKLNTTLRALRRRGYLPEALRNYLALIGWSKPDGHEL-FTLEEMIAAFSVERVNSADATFDWAKLEWLNRE 226
|
..
gi 238687201 323 TI 324
Cdd:cd00418 227 YI 228
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
6-302 |
1.67e-84 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 262.09 E-value: 1.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQHREA 85
Cdd:PRK05710 9 RFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHDAYRAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 86 IKYLLEKGLAYRCFTTEEELAAMReeQKSRNKPPRYDNRHRSLSteeesnfLSEGRTAVIRFRIDDnESIQWNDLVRGPM 165
Cdd:PRK05710 89 LDRLRAQGLVYPCFCSRKEIAAAA--PAPPDGGGIYPGTCRDLL-------HGPRNPPAWRLRVPD-AVIAFDDRLQGRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 166 NwtgKDLG---GDMVIARRapaneigDPL--YNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPL 240
Cdd:PRK05710 159 H---QDLAlavGDFVLRRA-------DGLfaYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238687201 241 ILNAEGKKLSKRDGVTSISDfkemGYTSKAMSNYMTLLGWSiPDGMDEKFTIEESSKVFDFD 302
Cdd:PRK05710 229 VLNADGQKLSKQNGAPALDA----AGPLPVLAAALRFLGQP-PPAADASVEELLAQAVAHWD 285
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-287 |
1.70e-80 |
|
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: 250.92 E-value: 1.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQHREA 85
Cdd:TIGR03838 4 RFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALYQAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 86 IKYLLEKGLAYRCFTTEEELAAMREEQksrnkpPRYDNRHRSLSTEeesnflSEGRTAVIRFRIDDNEsIQWNDLVRGPM 165
Cdd:TIGR03838 84 LDRLLAAGLAYPCQCTRKEIAAARDGG------GIYPGTCRNGLPG------RPGRPAAWRLRVPDGV-IAFDDRLQGPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 166 NWTGKDLGGDMVIARRApaneiGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPLILNAE 245
Cdd:TIGR03838 151 QQDLAAAVGDFVLRRAD-----GLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNAD 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 238687201 246 GKKLSKRDGVTSISDFKEMGYTSKAmsnyMTLLGWSIPDGMD 287
Cdd:TIGR03838 226 GEKLSKQNGAPALDDSRPLPALLAA----LRFLGLPPPPELA 263
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
5-251 |
9.48e-45 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 164.64 E-value: 9.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 5 VRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKE--RSQEEYKENILEGLDWLGLTWDaEPIIQSNRIEQH 82
Cdd:PRK04156 104 MRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLEIY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEQKS---RNKPPRyDNRhrslstEEESNFLS----EGRtAVIRFRIDDNESi 155
Cdd:PRK04156 183 YEYARKLIEMGGAYVCTCDPEEFKELRDAGKPcphRDKSPE-ENL------ELWEKMLDgeykEGE-AVVRVKTDLEHP- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 156 qwNDLVRgpmnwtgkdlggDMVIAR--RAPANEIGD-----PLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKAL 228
Cdd:PRK04156 254 --NPSVR------------DWVAFRivKTPHPRVGDkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYF 319
|
250 260
....*....|....*....|...
gi 238687201 229 GLTLPKFAHTPlILNAEGKKLSK 251
Cdd:PRK04156 320 GWEYPETIHYG-RLKIEGFVLST 341
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
6-237 |
1.97e-42 |
|
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: 158.06 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDaEPIIQSNRIEQHREA 85
Cdd:TIGR00463 97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVVYQSDRIETYYDY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 86 IKYLLEKGLAYRCFTTEEElaaMREEQKSRNKPPrydnrHRSLSTEEE-------SNFLSEGRTAVIRFRIDDNESiqwN 158
Cdd:TIGR00463 176 TRKLIEMGKAYVCDCRPEE---FRELRNRGEACH-----CRDRSVEENlerweemLEGKEEGGSVVVRVKTDLKHK---N 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 159 DLVRgpmnwtgkdlggDMVIAR--RAPANEIGD-----PLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLT 231
Cdd:TIGR00463 245 PAIR------------DWVIFRivKTPHPRTGDkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWE 312
|
....*.
gi 238687201 232 LPKFAH 237
Cdd:TIGR00463 313 PPEFIH 318
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
3-251 |
3.53e-35 |
|
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: 130.93 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQE--EYKENILEGLDWLGLTWDaEPIIQSNRIE 80
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWD-EVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 81 QHREAIKYLLEKGLAYrcftteeelaamreeqksrnKPPRYDNRHRSlsteeesnflsegrtavirfriddnesiqWndl 160
Cdd:cd09287 81 LYYEYARKLIEMGGAY--------------------VHPRTGSKYRV-----------------------------W--- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 161 vrgpmnwtgkdlggdmviarrapaneigdPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLPKFAHTPl 240
Cdd:cd09287 109 -----------------------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWG- 158
|
250
....*....|.
gi 238687201 241 ILNAEGKKLSK 251
Cdd:cd09287 159 RLKIEGGKLST 169
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
3-252 |
1.10e-23 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 103.94 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPiIQSNRIEQH 82
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVS-FTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMREEqksrnkppRYDNRHRSLSTEEESNFLS-------EGRTAVIRFRID---DN 152
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERAD--------RAESKHRNQSPEEALEMFKemcsgkeEGGAWCLRAKIDmqsDN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 153 ESIQwnDLVRGPMNWTGKDLGGDMVIARrapaneigdPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTL 232
Cdd:PLN03233 163 GTLR--DPVLFRQNTTPHHRSGTAYKAY---------PTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR 231
|
250 260
....*....|....*....|
gi 238687201 233 PKFaHTPLILNAEGKKLSKR 252
Cdd:PLN03233 232 PRI-HAFARMNFMNTVLSKR 250
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
6-328 |
2.33e-22 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 100.04 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQHREA 85
Cdd:PTZ00402 56 RFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLMYEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 86 IKYLLEKGLAYRCFTTEEELaamreeQKSR--NKPPRYdnrhRSLSTEEESNFLS-------EGRTAVIRFRID-DNEsi 155
Cdd:PTZ00402 136 AEELIKKGLAYCDKTPREEM------QKCRfdGVPTKY----RDISVEETKRLWNemkkgsaEGQETCLRAKISvDNE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 156 qwNDLVRGPMNWTgkdlgGDMVIARRAPANEIGDPLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP-- 233
Cdd:PTZ00402 204 --NKAMRDPVIYR-----VNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPiv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 234 -KFAHtpliLNAEGKKLSKRDgVTSISDFKEM-GYTSKAMSNYMTLLGWSIPDGMDEKFTIEES-SKVFDFdrvnkagak 310
Cdd:PTZ00402 277 eDFSR----LNMEYSVMSKRK-LTQLVDTHVVdGWDDPRFPTVRALVRRGLKMEALRQFVQEQGmSKTVNF--------- 342
|
330
....*....|....*...
gi 238687201 311 FDWEKLKWLNSQTIHDSS 328
Cdd:PTZ00402 343 MEWSKLWYFNTQILDPSV 360
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
3-96 |
7.40e-16 |
|
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: 76.91 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90
....*....|....
gi 238687201 83 REAIKyLLEKGLAY 96
Cdd:cd00807 82 EYAEQ-LIKKGKAY 94
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
6-279 |
1.08e-14 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 76.68 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQHREA 85
Cdd:PRK14703 35 RFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERMYAY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 86 IKYLLEKGLAYRCFTTEEELAAMREEQKSRNKPPRYDNRhrslSTEEESNFLSEGR-------TAVIRFRIDDNESiqwN 158
Cdd:PRK14703 115 AEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDR----SVEENLDLFRRMRagefpdgAHVLRAKIDMSSP---N 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 159 DLVRGPMnwtgkdlggdMVIARRAPANEIGD-----PLYNLVVVIDDGYMGITHVIRGEDHIANTAKQILLYKALGLTLP 233
Cdd:PRK14703 188 MKLRDPL----------LYRIRHAHHYRTGDewciyPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPP 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238687201 234 K-----FAHtpliLNAEGKKLSKR-------DGVTS---------ISDFKEMGYTSKAMSNYMTLLG 279
Cdd:PRK14703 258 RprqyeFAR----LALGYTVMSKRklrelveEGYVSgwddprmptIAGQRRRGVTPEAIRDFADQIG 320
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
3-210 |
9.12e-14 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 73.61 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAePIIQSNRIEQH 82
Cdd:PLN02907 214 VCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA-VTYTSDYFPQL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEElaaMREEQKSrnkppRYDNRHRSLSTEEESNFLSE-------GRTAVIRFRID---DN 152
Cdd:PLN02907 293 MEMAEKLIKEGKAYVDDTPREQ---MRKERMD-----GIESKCRNNSVEENLRLWKEmiagserGLQCCVRGKLDmqdPN 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238687201 153 ESIqwndlvRGPmnwtgkdlggdmvIARR---APANEIGD-----PLYNLVVVIDDGYMGITHVIR 210
Cdd:PLN02907 365 KSL------RDP-------------VYYRcnpTPHHRIGSkykvyPTYDFACPFVDALEGVTHALR 411
|
|
| Anticodon_2 |
pfam19269 |
Anticodon binding domain; This entry represents the anticodon binding domain found at the ... |
331-476 |
1.75e-13 |
|
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: 67.60 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 331 EILKAVEPLFNKEGWDLPNLEWSLKLIELIKPSMTLLTDSVEQSRFFFEDPL-----LNQDAINQLEIEGAKDSLKILLK 405
Cdd:pfam19269 1 ELAELALPYLEEAGLDGLDDEYLKKVVPLLKERAETLSELAELADFFFELPLeydeeAYAKKKMKTNKEESLEVLQELLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238687201 406 QIdtSKINKLTVEHAKKLINDAAVFGGFKKGLIMKSLRAALLGCLQGPDVINSWILLSeinQDKS--RIERCL 476
Cdd:pfam19269 81 RL--EALEDWTAEALEAALKALAEELGVKNGKVMWPLRVALTGKTVSPGLFEIMEILG---KEETlaRLRKAI 148
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
3-109 |
3.38e-13 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 71.67 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 3 IKVRLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGLTWDAEPIIQSNRIEQH 82
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGELRYASDYFDQL 109
|
90 100
....*....|....*....|....*..
gi 238687201 83 REAIKYLLEKGLAYRCFTTEEELAAMR 109
Cdd:PRK05347 110 YEYAVELIKKGKAYVDDLSAEEIREYR 136
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
6-156 |
6.04e-12 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 67.70 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGltWDAEPI-IQSNRIEQHRE 84
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMG--WKPDWVtFSSDYFDQLHE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 85 AIKYLLEKGLAYRCFTTEEELAAMREEqksrnkppRYDNRHRSLSTEEE---SNFLSEGR----TAVIRFRID---DNES 154
Cdd:PTZ00437 133 FAVQLIKDGKAYVDHSTPDELKQQREQ--------REDSPWRNRSVEENlllFEHMRQGRyaegEATLRVKADmksDNPN 204
|
..
gi 238687201 155 IQ 156
Cdd:PTZ00437 205 MR 206
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-118 |
3.07e-11 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 65.94 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238687201 6 RLAPSPTGKLHIGTARTALFNWLFARKNNGSFLIRIEDTDKERSQEEYKENILEGLDWLGltWDAEPII-QSNRIEQHRE 84
Cdd:PLN02859 268 RFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPFKITyTSDYFQELYE 345
|
90 100 110
....*....|....*....|....*....|....*..
gi 238687201 85 AIKYLLEKGLAYRCFTTEEELAAMREEQKS---RNKP 118
Cdd:PLN02859 346 LAVELIRRGHAYVDHQTPEEIKEYREKKMNspwRDRP 382
|
|
| |
