|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-798 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1579.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 9 KAPALQLEKLLALGLDQRTAENALVNSKVTANLAAVIAEAGI-GGCDKSVGNLLYAVATKYPNNALVHRPALIDYIVSMK 87
Cdd:PLN02859 3 ANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVtNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 88 IKNPVQLDAALSFLTNAGPDPLDTGKFEEACGVGVVVSIEEIHSTVTKVLHGNMEAILEQRYHINVGNLCGQVRKRHPWG 167
Cdd:PLN02859 83 IKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 168 DAKATKEEIEKRLAEILGPKTEADNVKPVKTKKGKPAKAEEKVVAVVTAAPPSEDLNPYSHFPEPAENNKVHTEIFFSDG 247
Cdd:PLN02859 163 DPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHTEVFFSDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 248 NIWRAHNTKEILEKHLRATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEI 327
Cdd:PLN02859 243 SVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 328 VHWLGWEPFKVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGA 407
Cdd:PLN02859 323 VEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 408 ATLRMKQDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGL 487
Cdd:PLN02859 403 ATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 488 YQPYVWEYSRLNISHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLIPFERLEY 567
Cdd:PLN02859 483 YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRLEH 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 568 HIREELNKTASRAMVVLHPLKVVITNLEDGKVIDLDGKKWPDAPADEASSYYKVPFSRTVYIEKTDFRLEDSKDYYGLAP 647
Cdd:PLN02859 563 HIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAP 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 648 GKSALLRYAFPIKCTEVIYGDNPEDIVEIRAEYDPSKTLKPKGVLHWVAEPAPGVEPLKVEVRLFEKLFLSENPAGLDDk 727
Cdd:PLN02859 643 GKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELED- 721
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123970636 728 eleekWLGDLNPQSKEVVKGAYAVPSLAAAVVGDKFQFERLGYFAVDTDSTPEELVFNRTVTLRDSYGKVG 798
Cdd:PLN02859 722 -----WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
270-794 |
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: 582.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 270 VTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDYFQAL 348
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 349 YEHAVELIRKGLAYVDHQTAEQIRKDRETNTD----SPWRDRPIEESLQLFEDMRRGLIAEGAATLRMKQDMQNDTRNMY 424
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLY-QPYVWEYSRLNISHN 503
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 504 IMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSlIPFERLEYHIREELNKTASRAMVV 583
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 584 LHPLKVVITNLE-DGKVIDLdgkkwPDAPADEASSYYKVPFSRTVYIEKTDFRLEDSKDYYGLAPGKSALLRYAFPIKcT 662
Cdd:TIGR00440 320 IDPVEVVIENLSdEYELATI-----PNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-A 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 663 EVIYGDNPEDIVEIRAEYD-------PSKTLKPKGVLHWVaepaPGVEPLKVEVRLFEKLFLSENPAGLDDkeleekWLG 735
Cdd:TIGR00440 394 ERVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDD------FLS 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 736 DLNPQSKeVVKGAYAVPSLAAAVVGDKFQFERLGYFAVDT-DSTPEELVFNRTVTLRDSY 794
Cdd:TIGR00440 464 VINPESL-VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
269-574 |
3.10e-144 |
|
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: 426.74 E-value: 3.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDYFQA 347
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 348 LYEHAVELIRKGLAYVDHQTAEQIRKDRETNT--DSPWRDRPIEESLQLF-EDMRRGLIAEGAATLRMKQDMQNDTrNMY 424
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPY-VFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 425 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLY-QPYVWEYSRLNI 500
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2123970636 501 SHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLIPFERLEYHIREELN 574
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
269-579 |
4.02e-135 |
|
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: 400.09 E-value: 4.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEPFKVTYTSDYFQAL 348
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 349 YEHAVELIRKGLAYVDHQTaeqirkdretntdspwrdrpieeslqlfedmrrgliaegaatlrmkqdmqndtrnmydlia 428
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 429 yrikftphphaGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNISHNIMSKR 508
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123970636 509 KLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNsLIPFERLEYHIREELNKTASR 579
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
266-772 |
1.29e-85 |
|
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: 279.76 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 266 TGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDY 344
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 345 FQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNT--------DSPWRDRPIEEslqlfedmRRGLIAEG-AATLRMK-- 413
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 414 ------QDM-----QNDTRNMYDLIAYRikftphpHAGdkwciYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVL 482
Cdd:COG0008 153 eegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 483 VALGLYQPyvwEYSRLNISHN----IMSKRKlnrlvtekwvdgwddpRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNS 558
Cdd:COG0008 221 EALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 559 LI-PFERLEYHIreELNKTaSRAMVVLHPLKVVITN------LEDGKVIDLdgkKWPDAPADEASSYYK--VPFSRT--- 626
Cdd:COG0008 282 EIfSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAEL---LAPELPEAGIREDLErlVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 627 -----------VYIEKTDfrLEDSKDYygLAPGKSALLryafpIKCTeviygdnpEDIVEIRAEYDPsKTLkpKGVLHWV 695
Cdd:COG0008 356 tlselaelarfFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP-ETV--KGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123970636 696 AEPApgveplkvEVRlfeklflsenpaglddkeleekwLGDLNPQSKEVVKGAYAVPSLA--AAVVGDKFQFERLGYFA 772
Cdd:COG0008 416 SAEA--------GVK-----------------------DGLLFMPLRVALTGRTVEPSLFdvLELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-798 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1579.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 9 KAPALQLEKLLALGLDQRTAENALVNSKVTANLAAVIAEAGI-GGCDKSVGNLLYAVATKYPNNALVHRPALIDYIVSMK 87
Cdd:PLN02859 3 ANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVtNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 88 IKNPVQLDAALSFLTNAGPDPLDTGKFEEACGVGVVVSIEEIHSTVTKVLHGNMEAILEQRYHINVGNLCGQVRKRHPWG 167
Cdd:PLN02859 83 IKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 168 DAKATKEEIEKRLAEILGPKTEADNVKPVKTKKGKPAKAEEKVVAVVTAAPPSEDLNPYSHFPEPAENNKVHTEIFFSDG 247
Cdd:PLN02859 163 DPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPPSEEELNPYSIFPQPEENFKVHTEVFFSDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 248 NIWRAHNTKEILEKHLRATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEI 327
Cdd:PLN02859 243 SVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 328 VHWLGWEPFKVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGA 407
Cdd:PLN02859 323 VEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 408 ATLRMKQDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGL 487
Cdd:PLN02859 403 ATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 488 YQPYVWEYSRLNISHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLIPFERLEY 567
Cdd:PLN02859 483 YQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRLEH 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 568 HIREELNKTASRAMVVLHPLKVVITNLEDGKVIDLDGKKWPDAPADEASSYYKVPFSRTVYIEKTDFRLEDSKDYYGLAP 647
Cdd:PLN02859 563 HIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAP 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 648 GKSALLRYAFPIKCTEVIYGDNPEDIVEIRAEYDPSKTLKPKGVLHWVAEPAPGVEPLKVEVRLFEKLFLSENPAGLDDk 727
Cdd:PLN02859 643 GKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELED- 721
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123970636 728 eleekWLGDLNPQSKEVVKGAYAVPSLAAAVVGDKFQFERLGYFAVDTDSTPEELVFNRTVTLRDSYGKVG 798
Cdd:PLN02859 722 -----WLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
256-797 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 760.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 256 KEILEKHLrATG--GKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGW 333
Cdd:PRK05347 15 RQIIDEDL-ASGkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 334 EPF-KVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNT----DSPWRDRPIEESLQLFEDMRRGLIAEGAA 408
Cdd:PRK05347 94 DWSgELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTepgkNSPYRDRSVEENLDLFERMRAGEFPEGSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 409 TLRMKQDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGL- 487
Cdd:PRK05347 174 VLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 488 YQPYVWEYSRLNISHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDnSLIPFERLEY 567
Cdd:PRK05347 254 PHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 568 HIREELNKTASRAMVVLHPLKVVITNLEDGKVIDLDGkkwPDAPADEASSYYKVPFSRTVYIEKTDFRLEDSKDYYGLAP 647
Cdd:PRK05347 333 CIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEA---PNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 648 GKSALLRYAFPIKCTEVIYGDNPEdIVEIRAEYDPsKTL--------KPKGVLHWV-AEPApgvepLKVEVRLFEKLFLS 718
Cdd:PRK05347 410 GKEVRLRNAYVIKCEEVVKDADGN-ITEIHCTYDP-DTLsgnpadgrKVKGTIHWVsAAHA-----VPAEVRLYDRLFTV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123970636 719 ENPAGLDDkeleekWLGDLNPQSKeVVKGAYAVPSLAAAVVGDKFQFERLGYFAVDTDSTPEELVFNRTVTLRDSYGKV 797
Cdd:PRK05347 483 PNPAAGKD------FLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
257-799 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 595.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 257 EILEKHLRA-TGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWE- 334
Cdd:PRK14703 18 EIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 335 PFKVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRET----NTDSPWRDRPIEESLQLFEDMRRGLIAEGAATL 410
Cdd:PRK14703 98 GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTvtepGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 411 RMKQDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLY-- 488
Cdd:PRK14703 178 RAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWpp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 489 QPYVWEYSRLNISHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSdNSLIPFERLEYH 568
Cdd:PRK14703 258 RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKT-NSTVDIGVLEFA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 569 IREELNKTASRAMVVLHPLKVVITNLEDGKVIDLDGKKWPDAPADEASSyyKVPFSRTVYIEKTDFRLEDSKDYYGLAPG 648
Cdd:PRK14703 337 IRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 649 KSALLRYAFPIKCTEVIYGDNpEDIVEIRAEYDP------SKTLKPKGVLHWVAepapGVEPLKVEVRLFEKLFLSENPA 722
Cdd:PRK14703 415 REVRLRGAYIIRCDEVVRDAD-GAVTELRCTYDPesakgeDTGRKAAGVIHWVS----AKHALPAEVRLYDRLFKVPQPE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123970636 723 GLDdkeleEKWLGDLNPQSKEVVKGaYAVPSLAAAVVGDKFQFERLGYFAVD-TDSTPEELVFNRTVTLRDSYGKVGG 799
Cdd:PRK14703 490 AAD-----EDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADpVDSRPDALVFNRIITLKDTWGARAR 561
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
254-796 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 594.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 254 NTKEILEKHLRATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGW 333
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 334 EPFKVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGAATLRMK 413
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 414 QDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVW 493
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 494 EYSRLNISHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNsLIPFERLEYHIREEL 573
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMN-VIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 574 NKTASRAMVVLHPLKVVITNLEDGKVIDLdgkkwPDAPADEASSYYKVPFSRTVYIEKTDFRLEDS-KDYYGLAPGKSAL 652
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKGEREFEC-----PNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNnSKFYGLAPGPRVV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 653 -LRYAFPIKCTEVIYGDNPEDIVeIRAEYDPSKTLKPKGVLHWVAEPApgvePLKVEVRLFEKLfLSENPAGLDdkeleE 731
Cdd:PTZ00437 430 gLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSATA----CTPVEVRLYNAL-LKDDRAAID-----P 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123970636 732 KWLGDLNPQSKEVVKGaYAVPSLAAAVVGDKFQFERLGYFAVDTDSTPEELVFNRTVTLRDSYGK 796
Cdd:PTZ00437 499 EFLKFIDEDSEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEK 562
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
270-794 |
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: 582.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 270 VTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDYFQAL 348
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 349 YEHAVELIRKGLAYVDHQTAEQIRKDRETNTD----SPWRDRPIEESLQLFEDMRRGLIAEGAATLRMKQDMQNDTRNMY 424
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLY-QPYVWEYSRLNISHN 503
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 504 IMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSlIPFERLEYHIREELNKTASRAMVV 583
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 584 LHPLKVVITNLE-DGKVIDLdgkkwPDAPADEASSYYKVPFSRTVYIEKTDFRLEDSKDYYGLAPGKSALLRYAFPIKcT 662
Cdd:TIGR00440 320 IDPVEVVIENLSdEYELATI-----PNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-A 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 663 EVIYGDNPEDIVEIRAEYD-------PSKTLKPKGVLHWVaepaPGVEPLKVEVRLFEKLFLSENPAGLDDkeleekWLG 735
Cdd:TIGR00440 394 ERVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDD------FLS 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 736 DLNPQSKeVVKGAYAVPSLAAAVVGDKFQFERLGYFAVDT-DSTPEELVFNRTVTLRDSY 794
Cdd:TIGR00440 464 VINPESL-VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
269-574 |
3.10e-144 |
|
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: 426.74 E-value: 3.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDYFQA 347
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 348 LYEHAVELIRKGLAYVDHQTAEQIRKDRETNT--DSPWRDRPIEESLQLF-EDMRRGLIAEGAATLRMKQDMQNDTrNMY 424
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESPY-VFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 425 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLY-QPYVWEYSRLNI 500
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2123970636 501 SHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLIPFERLEYHIREELN 574
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
269-579 |
4.02e-135 |
|
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: 400.09 E-value: 4.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEPFKVTYTSDYFQAL 348
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 349 YEHAVELIRKGLAYVDHQTaeqirkdretntdspwrdrpieeslqlfedmrrgliaegaatlrmkqdmqndtrnmydlia 428
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 429 yrikftphphaGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNISHNIMSKR 508
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123970636 509 KLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNsLIPFERLEYHIREELNKTASR 579
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
265-774 |
1.84e-95 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 313.58 E-value: 1.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 265 ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEPFKVTYTSDY 344
Cdd:PLN02907 209 AEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDY 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 345 FQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDM----RRGLiaegAATLRMKQDMQNDT 420
Cdd:PLN02907 289 FPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMiagsERGL----QCCVRGKLDMQDPN 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 421 RNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNI 500
Cdd:PLN02907 365 KSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 501 SHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNsLIPFERLEYHIREELNKTASRA 580
Cdd:PLN02907 445 VYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLN-LMEWDKLWTINKKIIDPVCPRH 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 581 MVVLHPLKVVITnLEDGK-----VIDLDGKKWPDApADEASSyykvpFSRTVYIEKTDFRLedskdyygLAPGKSALLR- 654
Cdd:PLN02907 524 TAVLKEGRVLLT-LTDGPetpfvRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEA--------ISEGEEVTLMd 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 655 --YAFPIKCTEVIYGDNPEDIVEIRAEYDpSKTLKPKgvLHWVAEpapgVEPLkVEVRLFEKLFLsenpagLDDKELEE- 731
Cdd:PLN02907 589 wgNAIIKEITKDEGGAVTALSGELHLEGS-VKTTKLK--LTWLPD----TNEL-VPLSLVEFDYL------ITKKKLEEd 654
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2123970636 732 -KWLGDLNPQSKeVVKGAYAVPSLAAAVVGDKFQFERLGYFAVD 774
Cdd:PLN02907 655 dNFLDVLNPCTK-KETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
265-783 |
1.23e-93 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 305.35 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 265 ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGwEPFKV--TYTS 342
Cdd:PTZ00402 48 AEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 343 DYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGlIAEGAAT-LRMKQDMQNDTR 421
Cdd:PTZ00402 127 DYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKG-SAEGQETcLRAKISVDNENK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 422 NMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNIS 501
Cdd:PTZ00402 206 AMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 502 HNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNsLIPFERLEYHIREELNKTASRAM 581
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN-FMEWSKLWYFNTQILDPSVPRYT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 582 VVLHPLKVVIT-----NLEDGKviDLDGKKWPDApadEASSYYKvpfSRTVYIEKTDFRLEDSKDYYGL----------- 645
Cdd:PTZ00402 365 VVSNTLKVRCTvegqiHLEACE--KLLHKKVPDM---GEKTYYK---SDVIFLDAEDVALLKEGDEVTLmdwgnayikni 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 646 -APGKSALLRYAfpikcteviygdnpeDIVeIRAEYDPSKTlkpKGVLHWVAEpAPGVEPLkvEVRLFEKLFLSENPagl 724
Cdd:PTZ00402 437 rRSGEDALITDA---------------DIV-LHLEGDVKKT---KFKLTWVPE-SPKAEVM--ELNEYDHLLTKKKP--- 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2123970636 725 DDKELEEKWLGDLNPQSKEVvkgaYAVPSLAAAVVGDKFQFERLGYFAVDTDSTPEELV 783
Cdd:PTZ00402 492 DPEESIDDIIAPVTKYTQEV----YGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
265-774 |
2.01e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 286.52 E-value: 2.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 265 ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEPFKVTYTSDY 344
Cdd:PLN03233 7 AIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 345 FQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGAATLRMKQDMQNDTRNMY 424
Cdd:PLN03233 87 FEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 425 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNISHNI 504
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 505 MSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLiPFERLEYHIREELNKTASRAMVV- 583
Cdd:PLN03233 247 LSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNL-DWAKFWAENKKEIDKRAKRFMAId 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 584 -LHPLKVVITNLEDGKviDLDGKKWPDAPADEASSYYKVPFSRTVYIEKTDFRledskdyyGLAPGKS-ALLRYAFpIKC 661
Cdd:PLN03233 326 kADHTALTVTNADEEA--DFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTE--------DIQLGEDiVLLRWGV-IEI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 662 TEvIYGDnpediveIRAEYDPSKTLK-PKGVLHWVAEPAPGVEPLKVEvrlFEKLFLSEnpaglddkELEE--KWLGDLN 738
Cdd:PLN03233 395 SK-IDGD-------LEGHFIPDGDFKaAKKKISWIADVSDNIPVVLSE---FDNLIIKE--------KLEEddKFEDFIN 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 2123970636 739 P--QSKEVVKGAYAVPSLAAAvvgDKFQFERLGYFAVD 774
Cdd:PLN03233 456 PdtLAETDVIGDAGLKTLKEH---DIIQLERRGFYRVD 490
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
266-772 |
1.29e-85 |
|
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: 279.76 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 266 TGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLGWEP-FKVTYTSDY 344
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 345 FQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNT--------DSPWRDRPIEEslqlfedmRRGLIAEG-AATLRMK-- 413
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRFKip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 414 ------QDM-----QNDTRNMYDLIAYRikftphpHAGdkwciYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVL 482
Cdd:COG0008 153 eegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 483 VALGLYQPyvwEYSRLNISHN----IMSKRKlnrlvtekwvdgwddpRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNS 558
Cdd:COG0008 221 EALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 559 LI-PFERLEYHIreELNKTaSRAMVVLHPLKVVITN------LEDGKVIDLdgkKWPDAPADEASSYYK--VPFSRT--- 626
Cdd:COG0008 282 EIfSLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAEL---LAPELPEAGIREDLErlVPLVRErak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 627 -----------VYIEKTDfrLEDSKDYygLAPGKSALLryafpIKCTeviygdnpEDIVEIRAEYDPsKTLkpKGVLHWV 695
Cdd:COG0008 356 tlselaelarfFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP-ETV--KGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2123970636 696 AEPApgveplkvEVRlfeklflsenpaglddkeleekwLGDLNPQSKEVVKGAYAVPSLA--AAVVGDKFQFERLGYFA 772
Cdd:COG0008 416 SAEA--------GVK-----------------------DGLLFMPLRVALTGRTVEPSLFdvLELLGKERVFERLGYAI 463
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
256-774 |
3.97e-81 |
|
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: 270.54 E-value: 3.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 256 KEILEKHLR----ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWL 331
Cdd:TIGR00463 76 KEKKRKGLRelpgAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 332 GWEPFKVTYTSDYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGAATLR 411
Cdd:TIGR00463 156 GVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 412 MKQDMQNDTRNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEF--DVRRPSYYWVLVALGLYQ 489
Cdd:TIGR00463 236 VKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 490 PYVWEYSRLNISHNIMSKRKLNRLVTEKWVdGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSLiPFERLEYHI 569
Cdd:TIGR00463 316 FIHWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 570 REELNKTASRAMVVLHPLKVVITNLEDGKVIDLdgKKWPDAPadeASSYYKVPFSRTVYIEKTDFrlEDSKDYYGLapgk 649
Cdd:TIGR00463 394 RKIIDEEARRYFFIWNPVKIEIVGLPEPKRVER--PLHPDHP---EIGERVLILRGEIYVPKDDL--EEGVEPVRL---- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 650 sallryafpIKCTEVIYGDNPEDIVEIRAEYDPSKTlkpKGVLHWVAEPapgvEPLKVEVRLFEKLfLSENPAGLDDKEL 729
Cdd:TIGR00463 463 ---------MDAVNVIYSKKELRYHSEGLEGARKLG---KSIIHWLPAK----DAVKVKVIMPDAS-IVEGVIEADASEL 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2123970636 730 EekwlgdlnpqskevvkgayavpslaaavVGDKFQFERLGYFAVD 774
Cdd:TIGR00463 526 E----------------------------VGDVVQFERFGFARLD 542
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
265-784 |
1.71e-77 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 260.94 E-value: 1.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 265 ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEK--KEYIDHIQEIVHWLGWEPFKVTYTS 342
Cdd:PRK04156 97 AEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 343 DYFQALYEHAVELIRKGLAYVDHQTAEQIRKDRETNTDSPWRDRPIEESLQLFEDMRRGLIAEGAATLRMKQDMQNDTRN 422
Cdd:PRK04156 177 DRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 423 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCMVDSLENITHSLCTLEFDV--RRPSYywVLVALGLYQPYVWEYSRLNI 500
Cdd:PRK04156 257 VRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--IYDYFGWEYPETIHYGRLKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 501 SHNIMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSlIPFERLEYHIREELNKTASRA 580
Cdd:PRK04156 335 EGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANRY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 581 MVVLHPLKVVITNLEDGKVidldgkKWPDAPADEASSYYKVPFSRTVYIEKTDFRLEdskdyyglapGKSALLRYAFPIK 660
Cdd:PRK04156 414 FFVRDPVELEIEGAEPLEA------KIPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------GKMVRLMDLFNVE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 661 CTEViygdNPEDIVEIRAEYDPSKTLKPKgVLHWVAEPapgvEPLKVEVRlfeklflseNPAGLDDKELEEKWLGDLNpq 740
Cdd:PRK04156 478 ITGV----SVDKARYHSDDLEEARKNKAP-IIQWVPED----ESVPVRVL---------KPDGGDIEGLAEPDVADLE-- 537
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2123970636 741 skevvkgayavpslaaavVGDKFQFERLGYFAVDtDSTPEELVF 784
Cdd:PRK04156 538 ------------------VDDIVQFERFGFVRID-SVEDDEVVA 562
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
15-169 |
4.34e-60 |
|
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: 200.48 E-value: 4.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 15 LEKLLALGLDQRTAENALVNSKVTANLAAVIAEAGI-GGCDKSVGNLLYAVATKYPNNALVHRPALIDYIVSMKIKNPVQ 93
Cdd:pfam04558 4 IELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVeSGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTTLQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2123970636 94 LDAALSFLTNAGPDPLDTGKFEEACGVGVVVSIEEIHSTVTKVLHGNMEAILEQRYHINVGNLCGQVRK--RHPWGDA 169
Cdd:pfam04558 84 VDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
577-774 |
5.45e-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: 173.23 E-value: 5.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 577 ASRAMVVLHPLKVVITNLEDGKVIDLdgkKWPDAPADEASSYYKVPFSRTVYIEKTDFRledskdyyGLAPGKSALLRYA 656
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETA---EVPNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 657 FPIKCTEVIYGDNpEDIVEIRAEYDP---SKTLKPKG-VLHWVAEPapgvEPLKVEVRLFEKLFLSENpaglddkelEEK 732
Cdd:pfam03950 70 YNIKVTEVVKDED-GNVTELHCTYDGddlGGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDED---------DAD 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2123970636 733 WLgdLNPQSKEVVKGAYAVPSLAAAVVGDKFQFERLGYFAVD 774
Cdd:pfam03950 136 FL--LNPDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
269-579 |
4.82e-42 |
|
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: 153.28 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEK--KEYIDHIQEIVHWLGWEPFKVTYTSDYFQ 346
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRpdPEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 347 ALYEHAVELIRKGLAYVdhqtaeqirkdretntdspwrdrpieeslqlfedmrrgliaegaatlrmkqdmqndtrnmydl 426
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 427 iayrikftpHPHAGDKWCIYPSYDYAHCMVDSLENITHSL--CTLEFDVRRPSYywVLVALGLYQPYVWEYSRLNISHNI 504
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLrgKDHIDNTEKQRY--IYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123970636 505 MSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSAAAINSFIRGMGITRSDNSlIPFERLEYHIREELNKTASR 579
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
269-595 |
5.69e-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: 147.23 E-value: 5.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLG--WEPfKVTYTSDYFQ 346
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDE-GPYRQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 347 ALYEHAVELIRKGlayvdhqtaeqirkdretntdspwrdrpieeslqlfedmrrgliaegaatlrmkqdmqndtrnmydl 426
Cdd:cd00418 80 LYRAYAEELIKKG------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 427 iayrikftphphagdkwcIYPSYDYAHCMVDSLENITHSLCTLEFDVRRPSYYWVLVALGLYQPYVWEYSRLNISHN-IM 505
Cdd:cd00418 93 ------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGtKL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 506 SKRKLNRlvtekwvdgwddprllTLAGLRRRGVSAAAINSFIRGMGITRSDNSLIPFerleyhiREELNKTASRAMVVLH 585
Cdd:cd00418 155 SKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGHELFT-------LEEMIAAFSVERVNSA 211
|
330
....*....|
gi 2123970636 586 PLKVVITNLE 595
Cdd:cd00418 212 DATFDWAKLE 221
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
269-359 |
7.17e-14 |
|
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: 71.85 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 269 KVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLG--WE--PFKVTYTSDY 344
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWDegPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 2123970636 345 FQ----ALY-EHAVELIRKG 359
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
271-362 |
1.08e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 72.58 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 271 TTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLG--WEPfKVTYTSDYFqAL 348
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DA 84
|
90
....*....|....*
gi 2123970636 349 YEHAVE-LIRKGLAY 362
Cdd:PRK05710 85 YRAALDrLRAQGLVY 99
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
172-252 |
5.27e-13 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; 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: 461352 [Multi-domain] Cd Length: 87 Bit Score: 65.02 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 172 TKEEIEKRLAEILGPKTEADNVKPVKTKKGKPAKAEEKVVAvvTAAPPSEDLNPYS--------HFPEPAENNKVHTEIF 243
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKK--KKAPIEEEENKRSmfsegflgKFHKPGENPKTDGYVV 78
|
....*....
gi 2123970636 244 FSDGNIWRA 252
Cdd:pfam04557 79 TEHTMRLLK 87
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
271-374 |
5.52e-07 |
|
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: 49.79 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 271 TTRFPPEPNGYLHIGHAKAMFIDFGLAKERN-----GNCYLRFDDTNPEAEKkeyidhiQEIVHWLGWEPFkVTYTSDYF 345
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGLIGD-------PANKKGENAKAF-VERWIERI 72
|
90 100 110
....*....|....*....|....*....|
gi 2123970636 346 QALYEHAVE-LIRKGLAYVDHQTAEQIRKD 374
Cdd:cd00802 73 KEDVEYMFLqAADFLLLYETECDIHLGGSD 102
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
271-327 |
3.21e-06 |
|
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: 46.38 E-value: 3.21e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 271 TTRFPPEPnGYLHIGHAKAMfidfGLAKERNGNCYLRFDDTNPEAEKK---EYIDHIQEI 327
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVKVWQdphELEERKESI 55
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
265-362 |
4.54e-06 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 50.13 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123970636 265 ATGGKVTTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGNCYLRFDDTNPEAEKKEYIDHIQEIVHWLG--WE--PFKVTY 340
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegPDVGGE 120
|
90 100
....*....|....*....|....*..
gi 2123970636 341 TSDYFQ----ALY-EHAVELIRKGLAY 362
Cdd:PLN02627 121 YGPYRQsernAIYkQYAEKLLESGHVY 147
|
|
| |
