|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-791 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1604.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 4 KDEESRKSLDLFLKIGLDERTAQNTLANAKVTASLNAVIGEAAVANGCNKAVGNLLYTVATKFPANALIHRPTLLEYIVS 83
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 84 SKIKNAMQLDAAFAFFTSVGPENFHLNEFEKACGVGVDVSLEDIERAVAEVFEENKDAIMEQRYGINAGNLYKQIRERQP 163
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 164 WADMKSVKEVVTRKLHELLGERTAADDQKPVKKKEKPVKVEVQVNAVDAPSvPPSEEELNPFSIFPQPEENIKVHTEIFF 243
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAA-PPSEEELNPYSIFPQPEENFKVHTEVFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 244 SNGTIWRPYNTKEKLERHLNATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 323
Cdd:PLN02859 240 SDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 324 QEIVQWMGWEPFKVTYTSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIE 403
Cdd:PLN02859 320 EEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 404 EGKATLRMKQDMQSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEA 483
Cdd:PLN02859 400 EGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 484 LDLYKPYVWEYSRLNVTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSLIRLDR 563
Cdd:PLN02859 480 LGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 564 LEYHIREEMNRTAPRTMVVLHPLKVVITNLEVGSVMHLDAKKWPDAHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYG 643
Cdd:PLN02859 560 LEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 644 LAPGKSVLLRYAFPIKCTEVVYGDDKETVVEIRAEYDPSKKTKPKGVLHWVAQPSPAVEPLKVEVRLFDKLFLSENPAEL 723
Cdd:PLN02859 640 LAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAEL 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2548740356 724 DDWLADLNPHSKEVIPEAYAAPTLANAVMGDKFQFERLGYFSIDPDSSAEKLVFNRTVTLRDSYSKGG 791
Cdd:PLN02859 720 EDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
269-787 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 586.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 269 VYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDYFQDL 347
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 348 YDLSVELIRRGHAYVDHQLPEEIKEYR----EKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQDMQSDNFNMY 423
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 424 DLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLY-KPYVWEYSRLNVTNT 502
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 503 VMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSlIRLDRLEYHIREEMNRTAPRTMVV 582
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 583 LHPLKVVITNLEVGSVMhldaKKWPDAHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYGLAPGKSVLLRYAFPIKcTE 662
Cdd:TIGR00440 320 IDPVEVVIENLSDEYEL----ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 663 VVYGDDKETVVEIRAEYD-------PSKKTKPKGVLHWVaqpsPAVEPLKVEVRLFDKLFLSENPAELDDWLADLNPHSK 735
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2548740356 736 eVIPEAYAAPTLANAVMGDKFQFERLGYFSIDP-DSSAEKLVFNRTVTLRDSY 787
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
268-573 |
4.24e-148 |
|
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: 436.37 E-value: 4.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDYFQD 346
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 347 LYDLSVELIRRGHAYVDHQLPEEIKEYREK--KLNSPWRDRPIEESLKLF-DDMRRGMIEEGKATLRMKQDMQSDnFNMY 423
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 424 DLIAYRIKYTP---HPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLY-KPYVWEYSRLNV 499
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2548740356 500 TNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSLIRLDRLEYHIREEMN 573
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
268-578 |
9.51e-141 |
|
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: 414.34 E-value: 9.51e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEPFKVTYTSDYFQDL 347
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 348 YDLSVELIRRGHAYVdhqlpeeikeyrekklnspwrdrpieeslklfddmrrgmieegkatlrmkqdmqsdnfnmydlia 427
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 428 yrikytpHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNVTNTVMSKR 507
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2548740356 508 KLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNsLIRLDRLEYHIREEMNRTAPR 578
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
265-594 |
8.34e-78 |
|
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: 258.57 E-value: 8.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 265 TGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDY 343
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 344 FQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKL--------NSPWRDRPIEEslklfddmRRGMIEEG-KATLRMK-- 412
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 413 ------QDMQS-----DNFNMYDLIAYRikytphpHAGdkwciYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLL 481
Cdd:COG0008 153 eegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 482 EALDLYKPyvwEYSRLNVT----NTVMSKRKlnrlvtekwvdgwddpRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNS 557
Cdd:COG0008 221 EALGWEPP---EFAHLPLIlgpdGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350
....*....|....*....|....*....|....*...
gi 2548740356 558 LIR-LDRLEYHIreEMNRTaPRTMVVLHPLKVVITNLE 594
Cdd:COG0008 282 EIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGP 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
4-791 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1604.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 4 KDEESRKSLDLFLKIGLDERTAQNTLANAKVTASLNAVIGEAAVANGCNKAVGNLLYTVATKFPANALIHRPTLLEYIVS 83
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 84 SKIKNAMQLDAAFAFFTSVGPENFHLNEFEKACGVGVDVSLEDIERAVAEVFEENKDAIMEQRYGINAGNLYKQIRERQP 163
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 164 WADMKSVKEVVTRKLHELLGERTAADDQKPVKKKEKPVKVEVQVNAVDAPSvPPSEEELNPFSIFPQPEENIKVHTEIFF 243
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAA-PPSEEELNPYSIFPQPEENFKVHTEVFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 244 SNGTIWRPYNTKEKLERHLNATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 323
Cdd:PLN02859 240 SDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 324 QEIVQWMGWEPFKVTYTSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIE 403
Cdd:PLN02859 320 EEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 404 EGKATLRMKQDMQSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEA 483
Cdd:PLN02859 400 EGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 484 LDLYKPYVWEYSRLNVTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSLIRLDR 563
Cdd:PLN02859 480 LGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 564 LEYHIREEMNRTAPRTMVVLHPLKVVITNLEVGSVMHLDAKKWPDAHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYG 643
Cdd:PLN02859 560 LEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 644 LAPGKSVLLRYAFPIKCTEVVYGDDKETVVEIRAEYDPSKKTKPKGVLHWVAQPSPAVEPLKVEVRLFDKLFLSENPAEL 723
Cdd:PLN02859 640 LAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAEL 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2548740356 724 DDWLADLNPHSKEVIPEAYAAPTLANAVMGDKFQFERLGYFSIDPDSSAEKLVFNRTVTLRDSYSKGG 791
Cdd:PLN02859 720 EDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
263-789 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 760.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 263 NATG--AKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEPF-KVTY 339
Cdd:PRK05347 22 LASGkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 340 TSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYR----EKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQDM 415
Cdd:PRK05347 102 ASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 416 QSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDL-YKPYVWEY 494
Cdd:PRK05347 182 ASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQYEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 495 SRLNVTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDnSLIRLDRLEYHIREEMNR 574
Cdd:PRK05347 262 SRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLESCIREDLNE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 575 TAPRTMVVLHPLKVVITNLEVGSVMHLDAKKWPDahaDDASAFYKVPFTNVVYIECSDFRTKDSKDYYGLAPGKSVLLRY 654
Cdd:PRK05347 341 NAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPE---DPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRN 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 655 AFPIKCTEVVYgDDKETVVEIRAEYDP---SKKT----KPKGVLHWVAqpspAVEPLKVEVRLFDKLFLSENPAELDDWL 727
Cdd:PRK05347 418 AYVIKCEEVVK-DADGNITEIHCTYDPdtlSGNPadgrKVKGTIHWVS----AAHAVPAEVRLYDRLFTVPNPAAGKDFL 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2548740356 728 ADLNPHSKeVIPEAYAAPTLANAVMGDKFQFERLGYFSIDPDSSAEKLVFNRTVTLRDSYSK 789
Cdd:PRK05347 493 DFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
256-791 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 612.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 256 EKLERHLNA-TGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWE- 333
Cdd:PRK14703 18 EIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 334 PFKVTYTSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYR----EKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATL 409
Cdd:PRK14703 98 GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 410 RMKQDMQSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLY-- 487
Cdd:PRK14703 178 RAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWpp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 488 KPYVWEYSRLNVTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSdNSLIRLDRLEYH 567
Cdd:PRK14703 258 RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKT-NSTVDIGVLEFA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 568 IREEMNRTAPRTMVVLHPLKVVITNLEVGSVMHLDAKKWPdaHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYGLAPG 647
Cdd:PRK14703 337 IRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWP--HDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 648 KSVLLRYAFPIKCTEVVYgDDKETVVEIRAEYDPSKKT------KPKGVLHWVAqpspAVEPLKVEVRLFDKLFLSENPA 721
Cdd:PRK14703 415 REVRLRGAYIIRCDEVVR-DADGAVTELRCTYDPESAKgedtgrKAAGVIHWVS----AKHALPAEVRLYDRLFKVPQPE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2548740356 722 ELD-DWLADLNPHSKEVIpEAYAAPTLANAVMGDKFQFERLGYFSIDP-DSSAEKLVFNRTVTLRDSYSKGG 791
Cdd:PRK14703 490 AADeDFLEFLNPDSLRVA-QGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGARA 560
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
253-790 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 605.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 253 NTKEKLERHLNATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGW 332
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 333 EPFKVTYTSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMK 412
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 413 QDMQSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVW 492
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 493 EYSRLNVTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNsLIRLDRLEYHIREEM 572
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMN-VIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 573 NRTAPRTMVVLHPLKVVITNLE-VGSVMHLDAKKWPDAHADdasafyKVPFTNVVYIECSDFRTKDS-KDYYGLAPGKSV 650
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKgEREFECPNHPRKPELGSR------KVMFTDTFYVDRSDFRTEDNnSKFYGLAPGPRV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 651 L-LRYAFPIKCTEVVYGDDKETVVeIRAEYDPSKKTKPKGVLHWVAqpspAVEPLKVEVRLFDKLFLSENPAELDDWLAD 729
Cdd:PTZ00437 429 VgLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVS----ATACTPVEVRLYNALLKDDRAAIDPEFLKF 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2548740356 730 LNPHSkEVIPEAYAAPTLANAVMGDKFQFERLGYFSIDPDSSAEKLVFNRTVTLRDSYSKG 790
Cdd:PTZ00437 504 IDEDS-EVVSHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
269-787 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 586.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 269 VYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDYFQDL 347
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 348 YDLSVELIRRGHAYVDHQLPEEIKEYR----EKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQDMQSDNFNMY 423
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 424 DLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLY-KPYVWEYSRLNVTNT 502
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 503 VMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSlIRLDRLEYHIREEMNRTAPRTMVV 582
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 583 LHPLKVVITNLEVGSVMhldaKKWPDAHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYGLAPGKSVLLRYAFPIKcTE 662
Cdd:TIGR00440 320 IDPVEVVIENLSDEYEL----ATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 663 VVYGDDKETVVEIRAEYD-------PSKKTKPKGVLHWVaqpsPAVEPLKVEVRLFDKLFLSENPAELDDWLADLNPHSK 735
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2548740356 736 eVIPEAYAAPTLANAVMGDKFQFERLGYFSIDP-DSSAEKLVFNRTVTLRDSY 787
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
268-573 |
4.24e-148 |
|
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: 436.37 E-value: 4.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDYFQD 346
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 347 LYDLSVELIRRGHAYVDHQLPEEIKEYREK--KLNSPWRDRPIEESLKLF-DDMRRGMIEEGKATLRMKQDMQSDnFNMY 423
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 424 DLIAYRIKYTP---HPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLY-KPYVWEYSRLNV 499
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2548740356 500 TNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSLIRLDRLEYHIREEMN 573
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
268-578 |
9.51e-141 |
|
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: 414.34 E-value: 9.51e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEPFKVTYTSDYFQDL 347
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 348 YDLSVELIRRGHAYVdhqlpeeikeyrekklnspwrdrpieeslklfddmrrgmieegkatlrmkqdmqsdnfnmydlia 427
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 428 yrikytpHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNVTNTVMSKR 507
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2548740356 508 KLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNsLIRLDRLEYHIREEMNRTAPR 578
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
263-767 |
3.39e-99 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 323.21 E-value: 3.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 263 NATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEPFKVTYTSD 342
Cdd:PLN02907 208 GAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 343 YFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMiEEGKA-TLRMKQDMQSDNFN 421
Cdd:PLN02907 288 YFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGS-ERGLQcCVRGKLDMQDPNKS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 422 MYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNVTN 501
Cdd:PLN02907 367 LRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVY 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 502 TVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNsLIRLDRLEYHIREEMNRTAPRTMV 581
Cdd:PLN02907 447 TLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLN-LMEWDKLWTINKKIIDPVCPRHTA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 582 VLHPLKVVITnLEVG-----SVMHLDAKKWPDAhADDASAfykvpFTNVVYIECSDFRTkdskdyygLAPGKSVLLR--- 653
Cdd:PLN02907 526 VLKEGRVLLT-LTDGpetpfVRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEA--------ISEGEEVTLMdwg 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 654 YAFPIKCTEVVYGDDKETVVEIRAEYDpSKKTKPKgvLHWVaqpsPAVEPLkVEVRL--FDKLFLSENPAELDDWLADLN 731
Cdd:PLN02907 591 NAIIKEITKDEGGAVTALSGELHLEGS-VKTTKLK--LTWL----PDTNEL-VPLSLveFDYLITKKKLEEDDNFLDVLN 662
|
490 500 510
....*....|....*....|....*....|....*.
gi 2548740356 732 PHSKEVIPeAYAAPTLANAVMGDKFQFERLGYFSID 767
Cdd:PLN02907 663 PCTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
263-776 |
1.37e-93 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 304.96 E-value: 1.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 263 NATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGwEPFKV--TYT 340
Cdd:PTZ00402 47 NAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 341 SDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMiEEGKAT-LRMKQDMQSDN 419
Cdd:PTZ00402 126 SDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKISVDNEN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 420 FNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNV 499
Cdd:PTZ00402 205 KAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 500 TNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNsLIRLDRLEYHIREEMNRTAPRT 579
Cdd:PTZ00402 285 EYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN-FMEWSKLWYFNTQILDPSVPRY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 580 MVVLHPLKVVITnleVGSVMHLDA------KKWPDAhadDASAFYKvpfTNVVYIecsdfrtkDSKDYYGLAPGKSVLLR 653
Cdd:PTZ00402 364 TVVSNTLKVRCT---VEGQIHLEAcekllhKKVPDM---GEKTYYK---SDVIFL--------DAEDVALLKEGDEVTLM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 654 -----YAFPIKcTEVVYGDDKETVVEIRAEYDpSKKTKPKgvLHWVAQpSPAVEPLkvEVRLFDKLFLSENP---AELDD 725
Cdd:PTZ00402 427 dwgnaYIKNIR-RSGEDALITDADIVLHLEGD-VKKTKFK--LTWVPE-SPKAEVM--ELNEYDHLLTKKKPdpeESIDD 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2548740356 726 WLADLNPHSKEVIPEAyAAPTLANavmGDKFQFERLGYFSIDPDSSAEKLV 776
Cdd:PTZ00402 500 IIAPVTKYTQEVYGEE-ALSVLKK---GDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
255-767 |
1.33e-87 |
|
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: 287.87 E-value: 1.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 255 KEKLERHL-NATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWE 333
Cdd:TIGR00463 79 KRKGLRELpGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 334 PFKVTYTSDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQ 413
Cdd:TIGR00463 159 WDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 414 DMQSDNFNMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEF--ETRRASYYWLLEALDLYKPYV 491
Cdd:TIGR00463 239 DLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 492 WEYSRLNVTNTVMSKRKLNRLVTEKWVdGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSLiRLDRLEYHIREE 571
Cdd:TIGR00463 319 WGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALNRKI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 572 MNRTAPRTMVVLHPLKVVITNLEvGSVMHLDAKkwpdaHADD-ASAFYKVPFTNVVYIECSDFRTKdsKDYYGLAPGKSV 650
Cdd:TIGR00463 397 IDEEARRYFFIWNPVKIEIVGLP-EPKRVERPL-----HPDHpEIGERVLILRGEIYVPKDDLEEG--VEPVRLMDAVNV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 651 LLRyafpiKCTEVVYGDDKETVveiraeydpskKTKPKGVLHWVaqpsPAVEPLKVEVRLFDKL----FLSENPAELDdw 726
Cdd:TIGR00463 469 IYS-----KKELRYHSEGLEGA-----------RKLGKSIIHWL----PAKDAVKVKVIMPDASivegVIEADASELE-- 526
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2548740356 727 ladlnphskevipeayaaptlanavMGDKFQFERLGYFSID 767
Cdd:TIGR00463 527 -------------------------VGDVVQFERFGFARLD 542
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
264-767 |
8.16e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 284.59 E-value: 8.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 264 ATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEPFKVTYTSDY 343
Cdd:PLN03233 7 AIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 344 FQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQDMQSDNFNMY 423
Cdd:PLN03233 87 FEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 424 DLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNVTNTV 503
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 504 MSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRsdnSLIRLDRLEY--HIREEMNRTAPRTMV 581
Cdd:PLN03233 247 LSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASR---RVVNLDWAKFwaENKKEIDKRAKRFMA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 582 V--LHPLKVVITNlevgsvmhldAKKWPDAHADDASAFYKVPFTNVVYIECSDFRTKDSKDYYGLAPGKS-VLLRYAFpI 658
Cdd:PLN03233 324 IdkADHTALTVTN----------ADEEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDiVLLRWGV-I 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 659 KCTEVvyGDDKETVVEIRAEYDPSKKTkpkgvLHWVAQPSPAVEPLKVEvrlFDKLFLSENPAELDDWLADLNPHSK--- 735
Cdd:PLN03233 393 EISKI--DGDLEGHFIPDGDFKAAKKK-----ISWIADVSDNIPVVLSE---FDNLIIKEKLEEDDKFEDFINPDTLaet 462
|
490 500 510
....*....|....*....|....*....|..
gi 2548740356 736 EVIPEAyAAPTLANAvmgDKFQFERLGYFSID 767
Cdd:PLN03233 463 DVIGDA-GLKTLKEH---DIIQLERRGFYRVD 490
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
263-777 |
8.73e-82 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 272.50 E-value: 8.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 263 NATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEK--KEYIDHIQEIVQWMGWEPFKVTYT 340
Cdd:PRK04156 96 NAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 341 SDYFQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKLNSPWRDRPIEESLKLFDDMRRGMIEEGKATLRMKQDMQSDNF 420
Cdd:PRK04156 176 SDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 421 NMYDLIAYRIKYTPHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFE--TRRASYywLLEALDLYKPYVWEYSRLN 498
Cdd:PRK04156 256 SVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYDYFGWEYPETIHYGRLK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 499 VTNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSlIRLDRLEYHIREEMNRTAPR 578
Cdd:PRK04156 334 IEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 579 TMVVLHPLKVVITNLEvgsvmHLDAKkwPDAHADDAS-AFYKVPFTNVVYIECSDFRtkdskdyyglAPGKSVLLRYAFP 657
Cdd:PRK04156 413 YFFVRDPVELEIEGAE-----PLEAK--IPLHPDRPErGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 658 IKCTEVVYGddkeTVVEIRAEYDPSKKTKPKgVLHWVaqpsPAVEPLKVEVrlfdklflsenpaelddwladLNPHSKEV 737
Cdd:PRK04156 476 VEITGVSVD----KARYHSDDLEEARKNKAP-IIQWV----PEDESVPVRV---------------------LKPDGGDI 525
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2548740356 738 ipEAYAAPTLANAVMGDKFQFERLGYFSIDpDSSAEKLVF 777
Cdd:PRK04156 526 --EGLAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
265-594 |
8.34e-78 |
|
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: 258.57 E-value: 8.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 265 TGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-FKVTYTSDY 343
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 344 FQDLYDLSVELIRRGHAYVDHQLPEEIKEYREKKL--------NSPWRDRPIEEslklfddmRRGMIEEG-KATLRMK-- 412
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 413 ------QDMQS-----DNFNMYDLIAYRikytphpHAGdkwciYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLL 481
Cdd:COG0008 153 eegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 482 EALDLYKPyvwEYSRLNVT----NTVMSKRKlnrlvtekwvdgwddpRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNS 557
Cdd:COG0008 221 EALGWEPP---EFAHLPLIlgpdGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350
....*....|....*....|....*....|....*...
gi 2548740356 558 LIR-LDRLEYHIreEMNRTaPRTMVVLHPLKVVITNLE 594
Cdd:COG0008 282 EIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGP 316
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
12-166 |
2.41e-64 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461353 Cd Length: 161 Bit Score: 212.04 E-value: 2.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 12 LDLFLKIGLDERTAQNTLANAKVTASLNAVIGEAAVANGCNKAVGNLLYTVATKFPANALIHRPTLLEYIVSSKIKNAMQ 91
Cdd:pfam04558 4 IELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTTLQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2548740356 92 LDAAFAFFTSVGPENFHLNEFEKACGVGVDVSLEDIERAVAEVFEENKDAIMEQRYGINAGNLYKQIR--ERQPWAD 166
Cdd:pfam04558 84 VDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRklPELKWAD 160
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
576-767 |
1.16e-50 |
|
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: 175.15 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 576 APRTMVVLHPLKVVITNLEVGSVMHLDAKKWPDahaDDASAFYKVPFTNVVYIECSDFRtkdskdyyGLAPGKSVLLRYA 655
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPK---NPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 656 FPIKCTEVVYgDDKETVVEIRAEYDP---SKKTKPKG-VLHWVaqpsPAVEPLKVEVRLFDKLFLSENPaelDDWLadLN 731
Cdd:pfam03950 70 YNIKVTEVVK-DEDGNVTELHCTYDGddlGGARKVKGkIIHWV----SASDAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 2548740356 732 PHSKEVIPEAYAAPTLANAVMGDKFQFERLGYFSID 767
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
268-578 |
2.65e-40 |
|
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: 148.65 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEK--KEYIDHIQEIVQWMGWEPFKVTYTSDYFQ 345
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRpdPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 346 DLYDLSVELIRRGHAYVdhqlpeeikeyrekklnspwrdrpieeslklfddmrrgmieegkatlrmkqdmqsdnfnmydl 425
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 426 iayrikytpHPHAGDKWCIYPSYDYSHCIVDSLENITHSLCTLEFE--TRRASYywLLEALDLYKPYVWEYSRLNVTNTV 503
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2548740356 504 MSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGVTSTAINTFIRGIGITRSDNSlIRLDRLEYHIREEMNRTAPR 578
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
268-579 |
7.19e-39 |
|
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: 144.15 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMG--WEPfKVTYTSDYFQ 345
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDE-GPYRQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 346 DLYDLSVELIRRGhayvdhqlpeeikeyrekklnspwrdrpieeslklfddmrrgmieegkatlrmkqdmqsdnfnmydl 425
Cdd:cd00418 80 LYRAYAEELIKKG------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 426 iayrikytphphagdkwcIYPSYDYSHCIVDSLENITHSLCTLEFETRRASYYWLLEALDLYKPYVWEYSRLNV-TNTVM 504
Cdd:cd00418 93 ------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKL 154
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2548740356 505 SKRKLNRlvtekwvdgwddprlmTLAGLRRRGVTSTAINTFIRGIGITRSDN-SLIRLDRLEYHIREEMNRTAPRT 579
Cdd:cd00418 155 SKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGhELFTLEEMIAAFSVERVNSADAT 214
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
268-334 |
2.96e-11 |
|
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: 64.14 E-value: 2.96e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2548740356 268 KVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMGWEP 334
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDW 67
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
271-361 |
5.92e-11 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 64.10 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 271 TRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMG--WEPfKVTYTSDYFqDLY 348
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DAY 85
|
90
....*....|....
gi 2548740356 349 DLSVE-LIRRGHAY 361
Cdd:PRK05710 86 RAALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
264-409 |
1.05e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.52 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 264 ATGAKVYTRFPPEPNGYLHIGHAKAMFIDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIQEIVQWMG--WE-------- 333
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegpdvgge 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 334 --PFKVTYTSDYFQDLYDlsvELIRRGHAY----VDHQLpEEIKEYREKKLNSP-----WRDR----------------- 385
Cdd:PLN02627 121 ygPYRQSERNAIYKQYAE---KLLESGHVYpcfcTDEEL-EAMKEEAELKKLPPrytgkWATAsdeevqaelakgtpyty 196
|
170 180
....*....|....*....|....*...
gi 2548740356 386 ----PIEESLKLfDDMRRGMIEEGKATL 409
Cdd:PLN02627 197 rfrvPKEGSVKI-DDLIRGEVSWNTDTL 223
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
271-330 |
3.10e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 47.47 E-value: 3.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2548740356 271 TRFPPEPNGYLHIGHAKAMFIDFGLAKE-----RGGCCYLRFDDTN-------------PEAEKKEYIDHIQEIVQWM 330
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
271-363 |
1.26e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 44.84 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2548740356 271 TRFPPEPnGYLHIGHAKAMfidfGLAKERGGCCYLRFDDTNPE------AEKKEYIDHIQEIVQWMGwepfkvtytsDYF 344
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG----------EDF 66
|
90
....*....|....*....
gi 2548740356 345 QDLYDLSVELIRRGHAYVD 363
Cdd:cd02156 67 QQNRELYRWVKDNITLPVD 85
|
|
| |
