|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-793 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1621.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 6 DSSDKEKCLDLFLKIGLDERTARNTVANNKVTANLTSVINEAGVTDGCSRTVGNLLYTVATKYPANALPHRPTLLQYIVS 85
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 86 SKVKTTAQLDAALSFLATTGLENLDLKTFEEACGVGIEVSTEDIKQAVSEVVEENKATILELRYRTNVGELLGYVRKRLP 165
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 166 WGDAKVAKQLVDAKLYELLGERTAADDEKPSKKKKEKPAKVEDKAPVATPEKSPEEDLNPYLIFPNPEENFKVHTEVPFS 245
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHTEVFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 246 DGSILRCCNTKALLDKHLKATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIE 325
Cdd:PLN02859 241 DGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 326 EIVQWMGWKPFKITYTSDYFQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEE 405
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 406 GKATLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHAL 485
Cdd:PLN02859 401 GKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 486 GIYQPYVWEYSRLNVSNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTLISVERL 565
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 566 EYHVREELNRTAPRAMVVLHPLKVVITNLEANSAIEVDAKKWPDAKADDASAFYKIPFSNVVYIERSDFRMKDSKDYYGL 645
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 646 APGKSAILRYAFPIKCTEVILADDNETILEIRAEYDPSKKTKPKGVLHWVSQPSPGVDPLKVEIRLFERLFLSENPAELD 725
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELE 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570378292 726 NWLGDLNPNSKVIIPGAYGVSSLRNAKVGDNFQFERLGYFVVDQDSTPEKLVFNRTVTLKDSYSKGGK 793
Cdd:PLN02859 721 DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
270-788 |
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: 594.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 270 VLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDYFQEL 348
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 349 YELAVELIKRGHAYVDHQTPDEIKEYR----EKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNYNMY 424
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIY-QPYVWEYSRLNVSNT 503
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 504 VMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDgTLISVERLEYHVREELNRTAPRAMVV 583
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQD-NNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 584 LHPLKVVITNLEAnsaiEVDAKKWPDAKADDASAFYKIPFSNVVYIERSDFRMKDSKDYYGLAPGKSAILRYAFPIKcTE 663
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 664 VILADDNETILEIRAEYD-------PSKKTKPKGVLHWVsqpsPGVDPLKVEIRLFERLFLSENPAELDNWLGDLNPNSK 736
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1570378292 737 VIIPGaYGVSSLRNAKVGDNFQFERLGYFVVD-QDSTPEKLVFNRTVTLKDSY 788
Cdd:TIGR00440 471 VIKQG-FMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
269-574 |
1.62e-160 |
|
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: 467.95 E-value: 1.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDYFQE 347
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 348 LYELAVELIKRGHAYVDHQTPDEIKEYREKKM--NSPWRDRPISESLKLF-EDMKSGLVEEGKATLRMKQDMQSDnYNMY 424
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIY-QPYVWEYSRLNV 500
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 501 SNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTLISVERLEYHVREELN 574
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
269-579 |
9.49e-144 |
|
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: 422.05 E-value: 9.49e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPFKITYTSDYFQEL 348
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 349 YELAVELIKRGHAYVDHQTpdeikeyrekkmnspwrdrpiseslklfedmksglveegkatlrmkqdmqsdnynmydlia 428
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 429 yrikftphphaGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVSNTVMSKR 508
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570378292 509 KLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVREELNRTAPR 579
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADST-IDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
266-766 |
1.08e-82 |
|
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: 271.67 E-value: 1.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 266 TGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDY 344
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGHAYVDHQTPDEIKEYREKKM--------NSPWRDRPISESlklfEDMKsglvEEG-KATLRMK-- 413
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEEL----ERML----AAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 414 ------QDMQS-----DNYNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLL 482
Cdd:COG0008 153 eegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 483 HALGIYQPyvwEYSRLNV----SNTVMSKRKlnrlvtekwvdgwddpRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGT 558
Cdd:COG0008 221 EALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 559 LI-SVERLEYHVreELNRTaPRAMVVLHPLKVVITNLEANSAIEVDA----------KKWPDAKADDASAFYK------- 620
Cdd:COG0008 282 EIfSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEElaellapelpEAGIREDLERLVPLVReraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 621 --IPFSNVVYIERSDfrMKDSKDYygLAPGKSAILryafpIKCTEVILAD----DNETIleiraeydpskktkpKGVLHW 694
Cdd:COG0008 359 elAELARFFFIERED--EKAAKKR--LAPEEVRKV-----LKAALEVLEAvetwDPETV---------------KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 695 VSQpspgvdplKVEIRlferlflsenpaeldnwLGDLNPNSKVIIPGAYGVSSLRN--AKVGDNFQFERLGYFV 766
Cdd:COG0008 415 VSA--------EAGVK-----------------DGLLFMPLRVALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-793 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1621.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 6 DSSDKEKCLDLFLKIGLDERTARNTVANNKVTANLTSVINEAGVTDGCSRTVGNLLYTVATKYPANALPHRPTLLQYIVS 85
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 86 SKVKTTAQLDAALSFLATTGLENLDLKTFEEACGVGIEVSTEDIKQAVSEVVEENKATILELRYRTNVGELLGYVRKRLP 165
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 166 WGDAKVAKQLVDAKLYELLGERTAADDEKPSKKKKEKPAKVEDKAPVATPEKSPEEDLNPYLIFPNPEENFKVHTEVPFS 245
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHTEVFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 246 DGSILRCCNTKALLDKHLKATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIE 325
Cdd:PLN02859 241 DGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 326 EIVQWMGWKPFKITYTSDYFQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEE 405
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 406 GKATLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHAL 485
Cdd:PLN02859 401 GKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 486 GIYQPYVWEYSRLNVSNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTLISVERL 565
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 566 EYHVREELNRTAPRAMVVLHPLKVVITNLEANSAIEVDAKKWPDAKADDASAFYKIPFSNVVYIERSDFRMKDSKDYYGL 645
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 646 APGKSAILRYAFPIKCTEVILADDNETILEIRAEYDPSKKTKPKGVLHWVSQPSPGVDPLKVEIRLFERLFLSENPAELD 725
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELE 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570378292 726 NWLGDLNPNSKVIIPGAYGVSSLRNAKVGDNFQFERLGYFVVDQDSTPEKLVFNRTVTLKDSYSKGGK 793
Cdd:PLN02859 721 DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
260-790 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 771.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 260 DKHLkATG--GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPF- 336
Cdd:PRK05347 19 DEDL-ASGkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 337 KITYTSDYFQELYELAVELIKRGHAYVDHQTPDEIKEYR----EKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRM 412
Cdd:PRK05347 98 ELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 413 KQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGI-YQPY 491
Cdd:PRK05347 178 KIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 492 VWEYSRLNVSNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVRE 571
Cdd:PRK05347 258 QYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSV-IDMSMLESCIRE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 572 ELNRTAPRAMVVLHPLKVVITNLEANSAIEVDAKKWPDakaDDASAFYKIPFSNVVYIERSDFRMKDSKDYYGLAPGKSA 651
Cdd:PRK05347 337 DLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPE---DPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 652 ILRYAFPIKCTEVIlADDNETILEIRAEYDP---SKKT----KPKGVLHWVSQPspgvDPLKVEIRLFERLFLSENPAEL 724
Cdd:PRK05347 414 RLRNAYVIKCEEVV-KDADGNITEIHCTYDPdtlSGNPadgrKVKGTIHWVSAA----HAVPAEVRLYDRLFTVPNPAAG 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1570378292 725 DNWLGDLNPNSKVIIpGAYGVSSLRNAKVGDNFQFERLGYFVVDQDSTPEKLVFNRTVTLKDSYSK 790
Cdd:PRK05347 489 KDFLDFLNPDSLVIK-QGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
252-791 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 617.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 252 CCNTKALLDKHLKATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWM 331
Cdd:PTZ00437 34 CRNTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 332 GWKPFKITYTSDYFQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLR 411
Cdd:PTZ00437 114 GWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 412 MKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPY 491
Cdd:PTZ00437 194 VKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 492 VWEYSRLNVSNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSdGTLISVERLEYHVRE 571
Cdd:PTZ00437 274 VWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRS-MNVIQISMLENTLRE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 572 ELNRTAPRAMVVLHPLKVVITNLEANSAIEV-DAKKWPDAKADdasafyKIPFSNVVYIERSDFRMKDS-KDYYGLAPGK 649
Cdd:PTZ00437 353 DLDERCERRLMVIDPIKVVVDNWKGEREFECpNHPRKPELGSR------KVMFTDTFYVDRSDFRTEDNnSKFYGLAPGP 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 650 SAI-LRYAFPIKCTEVILADDNETILeIRAEYDPSKKTKPKGVLHWVSQpsPGVDPlkVEIRLFERLfLSENPAELD-NW 727
Cdd:PTZ00437 427 RVVgLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSA--TACTP--VEVRLYNAL-LKDDRAAIDpEF 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 728 LGDLNPNSKVIIPGaYGVSSLRNAKVGDNFQFERLGYFVVDQDSTPEKLVFNRTVTLKDSYSKG 791
Cdd:PTZ00437 501 LKFIDEDSEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
268-792 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 603.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 268 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWK-PFKITYTSDYFQ 346
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 347 ELYELAVELIKRGHAYVDHQTPDEIKEYR----EKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNYN 422
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 423 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIY--QPYVWEYSRLNV 500
Cdd:PRK14703 190 LRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQYEFARLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 501 SNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVREELNRTAPRA 580
Cdd:PRK14703 270 GYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNST-VDIGVLEFAIRDDLNRRAPRV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 581 MVVLHPLKVVITNLEANSAIEVDAKKWPDAKADDASAfyKIPFSNVVYIERSDFRMKDSKDYYGLAPGKSAILRYAFPIK 660
Cdd:PRK14703 349 MAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLTPGREVRLRGAYIIR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 661 CTEVIlADDNETILEIRAEYDPSKKT------KPKGVLHWVSQPSpgvdPLKVEIRLFERLFLSENPAELD-NWLGDLNP 733
Cdd:PRK14703 427 CDEVV-RDADGAVTELRCTYDPESAKgedtgrKAAGVIHWVSAKH----ALPAEVRLYDRLFKVPQPEAADeDFLEFLNP 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 734 NSKVIIPGaYGVSSLRNAKVGDNFQFERLGYFVVD-QDSTPEKLVFNRTVTLKDSYSKGG 792
Cdd:PRK14703 502 DSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADpVDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
270-788 |
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: 594.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 270 VLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDYFQEL 348
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 349 YELAVELIKRGHAYVDHQTPDEIKEYR----EKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNYNMY 424
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIY-QPYVWEYSRLNVSNT 503
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 504 VMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDgTLISVERLEYHVREELNRTAPRAMVV 583
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQD-NNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 584 LHPLKVVITNLEAnsaiEVDAKKWPDAKADDASAFYKIPFSNVVYIERSDFRMKDSKDYYGLAPGKSAILRYAFPIKcTE 663
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 664 VILADDNETILEIRAEYD-------PSKKTKPKGVLHWVsqpsPGVDPLKVEIRLFERLFLSENPAELDNWLGDLNPNSK 736
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1570378292 737 VIIPGaYGVSSLRNAKVGDNFQFERLGYFVVD-QDSTPEKLVFNRTVTLKDSY 788
Cdd:TIGR00440 471 VIKQG-FMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
269-574 |
1.62e-160 |
|
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: 467.95 E-value: 1.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDYFQE 347
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 348 LYELAVELIKRGHAYVDHQTPDEIKEYREKKM--NSPWRDRPISESLKLF-EDMKSGLVEEGKATLRMKQDMQSDnYNMY 424
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIY-QPYVWEYSRLNV 500
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 501 SNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTLISVERLEYHVREELN 574
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
269-579 |
9.49e-144 |
|
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: 422.05 E-value: 9.49e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPFKITYTSDYFQEL 348
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 349 YELAVELIKRGHAYVDHQTpdeikeyrekkmnspwrdrpiseslklfedmksglveegkatlrmkqdmqsdnynmydlia 428
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 429 yrikftphphaGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVSNTVMSKR 508
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570378292 509 KLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVREELNRTAPR 579
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADST-IDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
265-768 |
8.80e-103 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 332.84 E-value: 8.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 265 ATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPFKITYTSDY 344
Cdd:PLN02907 209 AEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDY 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGlVEEGKA-TLRMKQDMQSDNYNM 423
Cdd:PLN02907 289 FPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAG-SERGLQcCVRGKLDMQDPNKSL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 424 YDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVSNT 503
Cdd:PLN02907 368 RDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 504 VMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRsDGTLISVERLEYHVREELNRTAPRAMVV 583
Cdd:PLN02907 448 LLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASK-NLNLMEWDKLWTINKKIIDPVCPRHTAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 584 LHPLKVVITNLEANSAIEVDA----KKWPDA--KAddasafykIPFSNVVYIERSDFRMKDSKDYYGLAPGKSAILRyaf 657
Cdd:PLN02907 527 LKEGRVLLTLTDGPETPFVRIiprhKKYEGAgkKA--------TTFTNRIWLDYADAEAISEGEEVTLMDWGNAIIK--- 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 658 pikcteVILADDNETILEIRAEYDPS---KKTKPKgvLHWVsqpsPGVDPLkVEIRL--FERLFLSENPAELDNWLGDLN 732
Cdd:PLN02907 596 ------EITKDEGGAVTALSGELHLEgsvKTTKLK--LTWL----PDTNEL-VPLSLveFDYLITKKKLEEDDNFLDVLN 662
|
490 500 510
....*....|....*....|....*....|....*.
gi 1570378292 733 PNSKVIIPgAYGVSSLRNAKVGDNFQFERLGYFVVD 768
Cdd:PLN02907 663 PCTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
265-777 |
3.55e-95 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 309.20 E-value: 3.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 265 ATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGwKPFKI--TYTS 342
Cdd:PTZ00402 48 AEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 343 DYFQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGlVEEGKAT-LRMKQDMQSDNY 421
Cdd:PTZ00402 127 DYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKG-SAEGQETcLRAKISVDNENK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 422 NMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVS 501
Cdd:PTZ00402 206 AMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 502 NTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSdGTLISVERLEYHVREELNRTAPRAM 581
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT-VNFMEWSKLWYFNTQILDPSVPRYT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 582 VVLHPLKVVITnLEANSAIEvDAKKWPDAKADD--ASAFYKipfSNVVYIERSDFRMKDSKDYYGLAPGKSAILRyafPI 659
Cdd:PTZ00402 365 VVSNTLKVRCT-VEGQIHLE-ACEKLLHKKVPDmgEKTYYK---SDVIFLDAEDVALLKEGDEVTLMDWGNAYIK---NI 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 660 KCT-EVILADDNETILEIRAEYdpsKKTKPKgvLHWVSQpSPgvDPLKVEIRLFERLFLSENP---AELDNWLGDLNPNS 735
Cdd:PTZ00402 437 RRSgEDALITDADIVLHLEGDV---KKTKFK--LTWVPE-SP--KAEVMELNEYDHLLTKKKPdpeESIDDIIAPVTKYT 508
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1570378292 736 KVIipgaYGVSSLRNAKVGDNFQFERLGYFVVDQDsTPEKLV 777
Cdd:PTZ00402 509 QEV----YGEEALSVLKKGDIIQLERRGYYIVDDV-TPKKVL 545
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
265-769 |
3.92e-90 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 293.45 E-value: 3.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 265 ATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPFKITYTSDY 344
Cdd:PLN03233 7 AIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNYNMY 424
Cdd:PLN03233 87 FEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVSNTV 504
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 505 MSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSdgtLISVERLEYHV--REELNRTAPRAMV 582
Cdd:PLN03233 247 LSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRR---VVNLDWAKFWAenKKEIDKRAKRFMA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 583 V--LHPLKVVITNleansaievdAKKWPDAKADDASAFYKIPFSNVVYIERSDFRMKDSKDYYGLAPGKSAILRYAFPIK 660
Cdd:PLN03233 324 IdkADHTALTVTN----------ADEEADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 661 CTEVilADDNETILEIRAEYDPSKKTkpkgvLHWVSQPSpgvDPLKVEIRLFERLFLSENPAELDNWLGDLNPNSKVIIP 740
Cdd:PLN03233 394 ISKI--DGDLEGHFIPDGDFKAAKKK-----ISWIADVS---DNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETD 463
|
490 500
....*....|....*....|....*....
gi 1570378292 741 gAYGVSSLRNAKVGDNFQFERLGYFVVDQ 769
Cdd:PLN03233 464 -VIGDAGLKTLKEHDIIQLERRGFYRVDR 491
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
265-768 |
6.76e-89 |
|
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: 290.96 E-value: 6.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 265 ATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKPFKITYTSDY 344
Cdd:TIGR00463 89 AKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNYNMY 424
Cdd:TIGR00463 169 IETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF--ETRRASYYWLLHALGIYQPYVWEYSRLNVSN 502
Cdd:TIGR00463 249 DWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 503 TVMSKRKLNRLVTEKWVdGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTLiSVERLEYHVREELNRTAPRAMV 582
Cdd:TIGR00463 329 ALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALNRKIIDEEARRYFF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 583 VLHPLKVVITNLEanSAIEVDAKKWPDakaDDASAFYKIPFSNVVYIERSDFRMKdsKDYYGLapgksailryafpIKCT 662
Cdd:TIGR00463 407 IWNPVKIEIVGLP--EPKRVERPLHPD---HPEIGERVLILRGEIYVPKDDLEEG--VEPVRL-------------MDAV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 663 EVILADDNETILEIRAEYDpskKTKPKGVLHWVsqpsPGVDPLKVEIRLFERL----FLSENPAELDnwlgdlnpnskvi 738
Cdd:TIGR00463 467 NVIYSKKELRYHSEGLEGA---RKLGKSIIHWL----PAKDAVKVKVIMPDASivegVIEADASELE------------- 526
|
490 500 510
....*....|....*....|....*....|
gi 1570378292 739 ipgaygvsslrnakVGDNFQFERLGYFVVD 768
Cdd:TIGR00463 527 --------------VGDVVQFERFGFARLD 542
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
264-778 |
9.13e-84 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 277.89 E-value: 9.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 264 KATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEK--KEYIDHIEEIVQWMGWKPFKITYT 341
Cdd:PRK04156 96 NAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 342 SDYFQELYELAVELIKRGHAYVDHQTPDEIKEYREKKMNSPWRDRPISESLKLFEDMKSGLVEEGKATLRMKQDMQSDNY 421
Cdd:PRK04156 176 SDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 422 NMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFE--TRRASYywLLHALGIYQPYVWEYSRLN 499
Cdd:PRK04156 256 SVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYDYFGWEYPETIHYGRLK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 500 VSNTVMSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVREELNRTAPR 579
Cdd:PRK04156 334 IEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 580 AMVVLHPLKVVITNLEansAIEVDAKKWPDakaDDASAFYKIPFSNVVYIERSDFRmkdskdyyglAPGKSAILRYAFPI 659
Cdd:PRK04156 413 YFFVRDPVELEIEGAE---PLEAKIPLHPD---RPERGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFNV 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 660 KCTEViladdneTILEIR---AEYDPSKKTKPKgVLHWVsqpsPGVDPLKVEIrlferlflsenpaeldnwlgdLNPNSK 736
Cdd:PRK04156 477 EITGV-------SVDKARyhsDDLEEARKNKAP-IIQWV----PEDESVPVRV---------------------LKPDGG 523
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1570378292 737 VIIpgAYGVSSLRNAKVGDNFQFERLGYFVVDqDSTPEKLVF 778
Cdd:PRK04156 524 DIE--GLAEPDVADLEVDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
266-766 |
1.08e-82 |
|
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: 271.67 E-value: 1.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 266 TGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWKP-FKITYTSDY 344
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGHAYVDHQTPDEIKEYREKKM--------NSPWRDRPISESlklfEDMKsglvEEG-KATLRMK-- 413
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEEL----ERML----AAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 414 ------QDMQS-----DNYNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLL 482
Cdd:COG0008 153 eegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 483 HALGIYQPyvwEYSRLNV----SNTVMSKRKlnrlvtekwvdgwddpRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGT 558
Cdd:COG0008 221 EALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 559 LI-SVERLEYHVreELNRTaPRAMVVLHPLKVVITNLEANSAIEVDA----------KKWPDAKADDASAFYK------- 620
Cdd:COG0008 282 EIfSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNGPYIRALDDEElaellapelpEAGIREDLERLVPLVReraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 621 --IPFSNVVYIERSDfrMKDSKDYygLAPGKSAILryafpIKCTEVILAD----DNETIleiraeydpskktkpKGVLHW 694
Cdd:COG0008 359 elAELARFFFIERED--EKAAKKR--LAPEEVRKV-----LKAALEVLEAvetwDPETV---------------KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 695 VSQpspgvdplKVEIRlferlflsenpaeldnwLGDLNPNSKVIIPGAYGVSSLRN--AKVGDNFQFERLGYFV 766
Cdd:COG0008 415 VSA--------EAGVK-----------------DGLLFMPLRVALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
11-169 |
2.39e-70 |
|
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: 227.83 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 11 EKCLDLFLKIGLDERTARNTVANNKVTANLTSVINEAGVTDGCSRTVGNLLYTVATKYPANALPHRPTLLQYIVSSKVKT 90
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 91 TAQLDAALSFLATTGLENLDLKTFEEACGVGIEVSTEDIKQAVSEVVEENKATILELRYRTNVGELLGYVRK--RLPWGD 168
Cdd:pfam04558 81 TLQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWAD 160
|
.
gi 1570378292 169 A 169
Cdd:pfam04558 161 P 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
577-768 |
1.36e-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: 174.77 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 577 APRAMVVLHPLKVVITNLEANSAIEVDAKKWPDakaDDASAFYKIPFSNVVYIERSDFRmkdskdyyGLAPGKSAILRYA 656
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPK---NPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 657 FPIKCTEVIlADDNETILEIRAEYDP---SKKTKPKG-VLHWVSQPspgvDPLKVEIRLFERLFLSENPaelDNWLgdLN 732
Cdd:pfam03950 70 YNIKVTEVV-KDEDGNVTELHCTYDGddlGGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1570378292 733 PNSKVIIPGAYGVSSLRNAKVGDNFQFERLGYFVVD 768
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
269-579 |
9.84e-44 |
|
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: 158.28 E-value: 9.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKK--EYIDHIEEIVQWMGWKPFKITYTSDYFQ 346
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 347 ELYELAVELIKRGHAYVdhqtpdeikeyrekkmnspwrdrpiseslklfedmksglveegkatlrmkqdmqsdnynmydl 426
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 427 iayrikftpHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFE--TRRASYywLLHALGIYQPYVWEYSRLNVSNTV 504
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570378292 505 MSKRKLNRLVTEKWVDGWDDPRLMTLAGLRRRGMTPTAINAFVRGIGITRSDGTlISVERLEYHVREELNRTAPR 579
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
269-557 |
3.82e-40 |
|
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: 147.62 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMGWK----PFkitYTSDY 344
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPY---RQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 345 FQELYELAVELIKRGhayvdhqtpdeikeyrekkmnspwrdrpiseslklfedmksglveegkatlrmkqdmqsdnynmy 424
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 425 dliayrikftphphagdkwcIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLHALGIYQPYVWEYSRLNVS-NT 503
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEdGT 152
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1570378292 504 VMSKRKLNRlvtekwvdgwddprlmTLAGLRRRGMTPTAINAFVRGIGITRSDG 557
Cdd:cd00418 153 KLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDG 190
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
269-359 |
8.84e-12 |
|
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: 65.69 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 269 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMG--W--KPFKITYTSDY 344
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWdeGPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 1570378292 345 FQ----ELY-ELAVELIKRG 359
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
272-362 |
1.71e-08 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 56.78 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 272 TRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMG--W-KPfkITYTSDYFqEL 348
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWdGP--VLYQSQRH-DA 84
|
90
....*....|....*
gi 1570378292 349 YELAVE-LIKRGHAY 362
Cdd:PRK05710 85 YRAALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
265-376 |
1.43e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 54.75 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570378292 265 ATGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKDRNGGCYLRYDDTNPEAEKKEYIDHIEEIVQWMG--WK--PFKITY 340
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegPDVGGE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1570378292 341 TSDYFQ----ELY-ELAVELIKRGHAYVDHQTPDEIKEYRE 376
Cdd:PLN02627 121 YGPYRQsernAIYkQYAEKLLESGHVYPCFCTDEELEAMKE 161
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
272-331 |
2.28e-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: 47.86 E-value: 2.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570378292 272 TRFPPEPNGYLHIGHAKAMFIDFGLAKD-RNGG----CYLRYDDTN-------------PEAEKKEYIDHIEEIVQWM 331
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyRKLGykvrCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
272-332 |
1.29e-04 |
|
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: 41.76 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1570378292 272 TRFPPEPnGYLHIGHAKAMfidfGLAKDRNGGCYLRYDDTNPE------AEKKEYIDHIEEIVQWMG 332
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG 63
|
|
| |
