|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-790 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1600.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 1 MVKEDSNVLDLFLKIGLDEKTAKNTLANNKVTTNLTAVIHEAAVIDGCDRAVGNLLYTVATKFPANALNHRPTLLQYIVS 80
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 81 TKIKTPAQLEAAFAFLASTASENLKAHDFEEACGVGVEVSKEDIERAVSEVFEEKKTNILEQRYRINVGELFGHVRKKLP 160
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 161 WADPKVVKEVVDLKLYKLLGERTAADNEKPVKKKKekpaktEDKAKVEE----TSAPKQSEEELNPYLIFPTPEENYKVH 236
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKK------EKPAKVEEkkvaVAAAPPSEEELNPYSIFPQPEENFKVH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 237 TEIYFSDRPVLRACNSKELLEKHLKVTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKE 316
Cdd:PLN02859 235 TEVFFSDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 317 YIDHIKEIVGWMGWEPFKITYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMK 396
Cdd:PLN02859 315 YIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 397 KGMIDEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 476
Cdd:PLN02859 395 RGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 477 WLLDALGLYQPFVWEYSRLNVSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSM 556
Cdd:PLN02859 475 WLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 557 IQLSRLEYHIREELNKTAARTLVVLNPLKVVITNIEAGLVMDLDAKKWPEAPADDASSFYKVPFSRVVYIERTDFRLKDS 636
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 637 KDYYGLAPGKSVLLRYAYPIKCTDVILADDKETVLEIRAEYDPSKTIKPKGVLHWVAEPSPGVDPLKVEVRLFDRLFCSE 716
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 717 NPAELDDWLGDLSPESKVVIQNAYAVPSVSKATLGDKFQFERLGYFAVDKDSTSEKLVFNRTVTLRDNYAKGGK 790
Cdd:PLN02859 715 NPAELEDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-785 |
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: 578.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 267 VLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEP-FKITYTSDYFQDL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 346 YELAVELIRRGHAYVDHQTPDEVKEYR----EKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNFNMY 421
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 422 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLY-QPFVWEYSRLNVSNT 500
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 501 VMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSmIQLSRLEYHIREELNKTAARTLVV 580
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 581 LNPLKVVITNIEAglvmDLDAKKWPEAPADDASSFYKVPFSRVVYIERTDFRLKDSKDYYGLAPGKSVLLRYAYPIKCTD 660
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 661 ViLADDKETVLEIRAEYD-------PSKTIKPKGVLHWVaepsPGVDPLKVEVRLFDRLFCSENPAELDDWLGDLSPESk 733
Cdd:TIGR00440 396 V-EKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPES- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 565354490 734 VVIQNAYAVPSVSKATLGDKFQFERLGYFAVD-KDSTSEKLVFNRTVTLRDNY 785
Cdd:TIGR00440 470 LVIKQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
266-571 |
9.79e-151 |
|
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: 442.91 E-value: 9.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEP-FKITYTSDYFQD 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 345 LYELAVELIRRGHAYVDHQTPDEVKEYREKKM--NSPWRDRPIEESLRLFDE-MKKGMIDEGKATLRMKQDMQNDnFNMY 421
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 422 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLY-QPFVWEYSRLNV 497
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 498 SNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSMIQLSRLEYHIREELN 571
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-576 |
3.78e-139 |
|
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: 410.10 E-value: 3.78e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEPFKITYTSDYFQDL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 346 YELAVELIRRGHAYVDHQTpdevkeyrekkmnspwrdrpieeslrlfdemkkgmidegkatlrmkqdmqndnfnmydlia 425
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 426 yrikftphphaGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLYQPFVWEYSRLNVSNTVMSKR 505
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565354490 506 KLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDsSMIQLSRLEYHIREELNKTAAR 576
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKAD-STIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-763 |
1.01e-84 |
|
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: 277.06 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 263 TGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--W--EPFkitYT 338
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 339 SDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKM--------NSPWRDRPIEEslrlfdemKKGMIDEG-KATLRM 409
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 410 K--------QDM-----QNDNFNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 476
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 477 WLLDALGLYQPfvwEYSRLNV----SNTVMSKRKlnrlvtenwvdgwddpRLMTLAGLRRRGVTSTAINAFVRGIGITRS 552
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 553 DSSMIQ-LSRLEYHIR-EELNKTAArtlvVLNPLKVVITNIEAGLVMDLDAKK---WPEAPADDASSFYK--VPFSR--- 622
Cdd:COG0008 279 DDQEIFsLEELIEAFDlDRVSRSPA----VFDPVKLVWLNGPYIRALDDEELAellAPELPEAGIREDLErlVPLVRera 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 623 -----------VVYIERTDfrLKDSKDYygLAPGKSVLLryaypIKCTdviladdkETVLEIRAEYDPsKTIkpKGVLHW 691
Cdd:COG0008 355 ktlselaelarFFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP-ETV--KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 692 VAEpspgvdplKVEVRlfdrlfcsenpaelddwLGDLSPESKVVIQNAYAVPSVSK--ATLGDKFQFERLGYFA 763
Cdd:COG0008 415 VSA--------EAGVK-----------------DGLLFMPLRVALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-790 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1600.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 1 MVKEDSNVLDLFLKIGLDEKTAKNTLANNKVTTNLTAVIHEAAVIDGCDRAVGNLLYTVATKFPANALNHRPTLLQYIVS 80
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 81 TKIKTPAQLEAAFAFLASTASENLKAHDFEEACGVGVEVSKEDIERAVSEVFEEKKTNILEQRYRINVGELFGHVRKKLP 160
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 161 WADPKVVKEVVDLKLYKLLGERTAADNEKPVKKKKekpaktEDKAKVEE----TSAPKQSEEELNPYLIFPTPEENYKVH 236
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKK------EKPAKVEEkkvaVAAAPPSEEELNPYSIFPQPEENFKVH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 237 TEIYFSDRPVLRACNSKELLEKHLKVTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKE 316
Cdd:PLN02859 235 TEVFFSDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 317 YIDHIKEIVGWMGWEPFKITYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMK 396
Cdd:PLN02859 315 YIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 397 KGMIDEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 476
Cdd:PLN02859 395 RGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 477 WLLDALGLYQPFVWEYSRLNVSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSM 556
Cdd:PLN02859 475 WLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 557 IQLSRLEYHIREELNKTAARTLVVLNPLKVVITNIEAGLVMDLDAKKWPEAPADDASSFYKVPFSRVVYIERTDFRLKDS 636
Cdd:PLN02859 555 IRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 637 KDYYGLAPGKSVLLRYAYPIKCTDVILADDKETVLEIRAEYDPSKTIKPKGVLHWVAEPSPGVDPLKVEVRLFDRLFCSE 716
Cdd:PLN02859 635 KDYYGLAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 717 NPAELDDWLGDLSPESKVVIQNAYAVPSVSKATLGDKFQFERLGYFAVDKDSTSEKLVFNRTVTLRDNYAKGGK 790
Cdd:PLN02859 715 NPAELEDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
265-787 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 767.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 265 GKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEPF-KITYTSDYFQ 343
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 344 DLYELAVELIRRGHAYVDHQTPDEVKEYR----EKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNFN 419
Cdd:PRK05347 108 QLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNIN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 420 MYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGL-YQPFVWEYSRLNVS 498
Cdd:PRK05347 188 MRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIpPHPRQYEFSRLNLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 499 NTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDsSMIQLSRLEYHIREELNKTAARTL 578
Cdd:PRK05347 268 YTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLESCIREDLNENAPRAM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 579 VVLNPLKVVITNIEAGLVMDLDAKKWPEapaDDASSFYKVPFSRVVYIERTDFRLKDSKDYYGLAPGKSVLLRYAYPIKC 658
Cdd:PRK05347 347 AVLDPLKLVITNYPEGQVEELEAPNHPE---DPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVPGKEVRLRNAYVIKC 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 659 TDVIlADDKETVLEIRAEYDP-------SKTIKPKGVLHWVAEPspgvDPLKVEVRLFDRLFCSENPAELDDWLGDLSPE 731
Cdd:PRK05347 424 EEVV-KDADGNITEIHCTYDPdtlsgnpADGRKVKGTIHWVSAA----HAVPAEVRLYDRLFTVPNPAAGKDFLDFLNPD 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 565354490 732 SKVVIQnAYAVPSVSKATLGDKFQFERLGYFAVDKDSTSEKLVFNRTVTLRDNYAK 787
Cdd:PRK05347 499 SLVIKQ-GFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
229-788 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 618.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 229 PEENYKVHTEIYFSDRPVLRACNSKELLEKHLKVTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDT 308
Cdd:PTZ00437 14 PELETKRDLSLLQTGRPVPGCRNTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 309 NPEAEKKEYIDHIKEIVGWMGWEPFKITYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEES 388
Cdd:PTZ00437 94 NPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 389 LRLFDEMKKGMIDEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF 468
Cdd:PTZ00437 174 LLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 469 ETRRASYYWLLDALGLYQPFVWEYSRLNVSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIG 548
Cdd:PTZ00437 254 ETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 549 ITRSdSSMIQLSRLEYHIREELNKTAARTLVVLNPLKVVITNIEAGLVMDLdakkwPEAPADDASSFYKVPFSRVVYIER 628
Cdd:PTZ00437 334 ITRS-MNVIQISMLENTLREDLDERCERRLMVIDPIKVVVDNWKGEREFEC-----PNHPRKPELGSRKVMFTDTFYVDR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 629 TDFRLKDS-KDYYGLAPGKSVL-LRYAYPIKCTDVILADDKETVLeIRAEYDPSKTIKPKGVLHWVAEpsPGVDPlkVEV 706
Cdd:PTZ00437 408 SDFRTEDNnSKFYGLAPGPRVVgLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSA--TACTP--VEV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 707 RLFDRLFCSENPAELDDWLGDLSPESKVViQNAYAVPSVSKATLGDKFQFERLGYFAVDKDSTSEKLVFNRTVTLRDNYA 786
Cdd:PTZ00437 483 RLYNALLKDDRAAIDPEFLKFIDEDSEVV-SHGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKE 561
|
..
gi 565354490 787 KG 788
Cdd:PTZ00437 562 KA 563
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
254-789 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 608.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 254 ELLEKHLKV-TGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWE- 331
Cdd:PRK14703 18 EIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 332 PFKITYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYR----EKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATL 407
Cdd:PRK14703 98 GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 408 RMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLY-- 485
Cdd:PRK14703 178 RAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWpp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 486 QPFVWEYSRLNVSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDsSMIQLSRLEYH 565
Cdd:PRK14703 258 RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTN-STVDIGVLEFA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 566 IREELNKTAARTLVVLNPLKVVITNIEAGLVMDLDAKKWPEAPADDASSfyKVPFSRVVYIERTDFRLKDSKDYYGLAPG 645
Cdd:PRK14703 337 IRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 646 KSVLLRYAYPIKCTDVIlADDKETVLEIRAEYDP------SKTIKPKGVLHWVAEPSpgvdPLKVEVRLFDRLFCSENPA 719
Cdd:PRK14703 415 REVRLRGAYIIRCDEVV-RDADGAVTELRCTYDPesakgeDTGRKAAGVIHWVSAKH----ALPAEVRLYDRLFKVPQPE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565354490 720 ELD-DWLGDLSPESKVVIQNaYAVPSVSKATLGDKFQFERLGYFAVDK-DSTSEKLVFNRTVTLRDNYAKGG 789
Cdd:PRK14703 490 AADeDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
267-785 |
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: 578.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 267 VLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEP-FKITYTSDYFQDL 345
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 346 YELAVELIRRGHAYVDHQTPDEVKEYR----EKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNFNMY 421
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 422 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLY-QPFVWEYSRLNVSNT 500
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 501 VMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSmIQLSRLEYHIREELNKTAARTLVV 580
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 581 LNPLKVVITNIEAglvmDLDAKKWPEAPADDASSFYKVPFSRVVYIERTDFRLKDSKDYYGLAPGKSVLLRYAYPIKCTD 660
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 661 ViLADDKETVLEIRAEYD-------PSKTIKPKGVLHWVaepsPGVDPLKVEVRLFDRLFCSENPAELDDWLGDLSPESk 733
Cdd:TIGR00440 396 V-EKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPES- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 565354490 734 VVIQNAYAVPSVSKATLGDKFQFERLGYFAVD-KDSTSEKLVFNRTVTLRDNY 785
Cdd:TIGR00440 470 LVIKQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
266-571 |
9.79e-151 |
|
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: 442.91 E-value: 9.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEP-FKITYTSDYFQD 344
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 345 LYELAVELIRRGHAYVDHQTPDEVKEYREKKM--NSPWRDRPIEESLRLFDE-MKKGMIDEGKATLRMKQDMQNDnFNMY 421
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFEEeMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 422 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLY-QPFVWEYSRLNV 497
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 498 SNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSMIQLSRLEYHIREELN 571
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
266-576 |
3.78e-139 |
|
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: 410.10 E-value: 3.78e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEPFKITYTSDYFQDL 345
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 346 YELAVELIRRGHAYVDHQTpdevkeyrekkmnspwrdrpieeslrlfdemkkgmidegkatlrmkqdmqndnfnmydlia 425
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 426 yrikftphphaGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLYQPFVWEYSRLNVSNTVMSKR 505
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 565354490 506 KLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDsSMIQLSRLEYHIREELNKTAAR 576
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKAD-STIDWDKLEACVRKDLNPTAPR 238
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
249-774 |
9.79e-99 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 318.44 E-value: 9.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 249 ACNSKELLEKhLKVTG---GKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIV 325
Cdd:PTZ00402 33 AANANEENDK-LQLTNaeeGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 326 GWMGwEPFKI--TYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMKKGMiDEG 403
Cdd:PTZ00402 112 ATLG-VSWDVgpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGS-AEG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 404 KAT-LRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDAL 482
Cdd:PTZ00402 190 QETcLRAKISVDNENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 483 GLYQPFVWEYSRLNVSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSMiQLSRL 562
Cdd:PTZ00402 270 GIRKPIVEDFSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFM-EWSKL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 563 EYHIREELNKTAARTLVVLNPLKVVITnIEAGLVMDLDAKKW-PEAPADDASSFYKvpfSRVVYIERTDFRL-KDSKDYY 640
Cdd:PTZ00402 349 WYFNTQILDPSVPRYTVVSNTLKVRCT-VEGQIHLEACEKLLhKKVPDMGEKTYYK---SDVIFLDAEDVALlKEGDEVT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 641 GLAPGKSVLLRYAYPikcTDVILADDKETVLEIraEYDPSKTikpKGVLHWVAEpSPgvDPLKVEVRLFDRLFCSENP-- 718
Cdd:PTZ00402 425 LMDWGNAYIKNIRRS---GEDALITDADIVLHL--EGDVKKT---KFKLTWVPE-SP--KAEVMELNEYDHLLTKKKPdp 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 565354490 719 -AELDDWLGDLSPESKVVIQNAyAVPSVSKatlGDKFQFERLGYFAVDKDSTSEKLV 774
Cdd:PTZ00402 494 eESIDDIIAPVTKYTQEVYGEE-ALSVLKK---GDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
265-765 |
7.47e-93 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 306.27 E-value: 7.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 265 GKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEPFKITYTSDYFQD 344
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 345 LYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNFNMYDLI 424
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 425 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLYQPFVWEYSRLNVSNTVMSK 504
Cdd:PLN02907 372 YYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 505 RKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSdssmiqLSRLEYHIREELNK-----TAARTLV 579
Cdd:PLN02907 452 RKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKN------LNLMEWDKLWTINKkiidpVCPRHTA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 580 VLNPLKVVITnIEAG-----LVMDLDAKKWPEApADDASSfykvpFSRVVYIERTDFRLkdskdyygLAPGKSV-LLRYA 653
Cdd:PLN02907 526 VLKEGRVLLT-LTDGpetpfVRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEA--------ISEGEEVtLMDWG 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 654 YPIkcTDVILADDKETVLEIRAEYDPS---KTIKPKgvLHWVAEPSPGVDPLKVEvrlFDRLFCSENPAELDDWLGDLSP 730
Cdd:PLN02907 591 NAI--IKEITKDEGGAVTALSGELHLEgsvKTTKLK--LTWLPDTNELVPLSLVE---FDYLITKKKLEEDDNFLDVLNP 663
|
490 500 510
....*....|....*....|....*....|....*
gi 565354490 731 ESKVVIQnAYAVPSVSKATLGDKFQFERLGYFAVD 765
Cdd:PLN02907 664 CTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
253-766 |
1.51e-87 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 287.49 E-value: 1.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 253 KELLEKHLK----VTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWM 328
Cdd:TIGR00463 76 KEKKRKGLRelpgAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 329 GWEPFKITYTSDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLR 408
Cdd:TIGR00463 156 GVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 409 MKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF--ETRRASYYWLLDALGLYQ 486
Cdd:TIGR00463 236 VKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 487 PFVWEYSRLNVSNTVMSKRKLNRLVTENWVdGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSMiQLSRLEYHI 566
Cdd:TIGR00463 316 FIHWGRLKIDDVRALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 567 REELNKTAARTLVVLNPLKVVITNIEAGLVMDLdakkwPEAPADDASSFYKVPFSRVVYIERTDFRLKdsKDYYGLapgk 646
Cdd:TIGR00463 394 RKIIDEEARRYFFIWNPVKIEIVGLPEPKRVER-----PLHPDHPEIGERVLILRGEIYVPKDDLEEG--VEPVRL---- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 647 svllryaypIKCTDVILADDKETVLEIRAEYDPSKTikpKGVLHWVAEPspgvDPLKVEVRLFDRLFcSENPAELDDwlg 726
Cdd:TIGR00463 463 ---------MDAVNVIYSKKELRYHSEGLEGARKLG---KSIIHWLPAK----DAVKVKVIMPDASI-VEGVIEADA--- 522
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 565354490 727 dlspeskvviqnayavpsvSKATLGDKFQFERLGYFAVDK 766
Cdd:TIGR00463 523 -------------------SELEVGDVVQFERFGFARLDS 543
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
265-766 |
1.82e-87 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 286.14 E-value: 1.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 265 GKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMGWEPFKITYTSDYFQD 344
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 345 LYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNFNMYDLI 424
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 425 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLYQPFVWEYSRLNVSNTVMSK 504
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 505 RKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSMiQLSRLEYHIREELNKTAARTLVV--LN 582
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNL-DWAKFWAENKKEIDKRAKRFMAIdkAD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 583 PLKVVITNIEAGlvMDLDAKKWPEAPADDASSFYKVPFSRVVYIERTDFRlkdskdyyGLAPGKS-VLLRYAYpIKCTDV 661
Cdd:PLN03233 329 HTALTVTNADEE--ADFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTE--------DIQLGEDiVLLRWGV-IEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 662 ilADDKEtvleirAEYDPSKTIK-PKGVLHWVAEPSpgvDPLKVEVRLFDRLFCSENPAELDDWLGDLSPESKV---VIQ 737
Cdd:PLN03233 398 --DGDLE------GHFIPDGDFKaAKKKISWIADVS---DNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAetdVIG 466
|
490 500
....*....|....*....|....*....
gi 565354490 738 NAyavpSVSKATLGDKFQFERLGYFAVDK 766
Cdd:PLN03233 467 DA----GLKTLKEHDIIQLERRGFYRVDR 491
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
263-763 |
1.01e-84 |
|
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: 277.06 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 263 TGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--W--EPFkitYT 338
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 339 SDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKM--------NSPWRDRPIEEslrlfdemKKGMIDEG-KATLRM 409
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 410 K--------QDM-----QNDNFNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLENITHSLCTLEFETRRASYY 476
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 477 WLLDALGLYQPfvwEYSRLNV----SNTVMSKRKlnrlvtenwvdgwddpRLMTLAGLRRRGVTSTAINAFVRGIGITRS 552
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 553 DSSMIQ-LSRLEYHIR-EELNKTAArtlvVLNPLKVVITNIEAGLVMDLDAKK---WPEAPADDASSFYK--VPFSR--- 622
Cdd:COG0008 279 DDQEIFsLEELIEAFDlDRVSRSPA----VFDPVKLVWLNGPYIRALDDEELAellAPELPEAGIREDLErlVPLVRera 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 623 -----------VVYIERTDfrLKDSKDYygLAPGKSVLLryaypIKCTdviladdkETVLEIRAEYDPsKTIkpKGVLHW 691
Cdd:COG0008 355 ktlselaelarFFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP-ETV--KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 692 VAEpspgvdplKVEVRlfdrlfcsenpaelddwLGDLSPESKVVIQNAYAVPSVSK--ATLGDKFQFERLGYFA 763
Cdd:COG0008 415 VSA--------EAGVK-----------------DGLLFMPLRVALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
261-775 |
2.30e-81 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 271.34 E-value: 2.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 261 KVTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEK--KEYIDHIKEIVGWMGWEPFKITYT 338
Cdd:PRK04156 96 NAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 339 SDYFQDLYELAVELIRRGHAYVDHQTPDEVKEYREKKMNSPWRDRPIEESLRLFDEMKKGMIDEGKATLRMKQDMQNDNF 418
Cdd:PRK04156 176 SDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 419 NMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFE--TRRASYywLLDALGLYQPFVWEYSRLN 496
Cdd:PRK04156 256 SVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYDYFGWEYPETIHYGRLK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 497 VSNTVMSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSmIQLSRLEYHIREELNKTAAR 576
Cdd:PRK04156 334 IEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 577 TLVVLNPLKVVITNIEaglvmDLDAKKwPEAPADDASSFYKVPFSRVVYIERTDFRlkdskdyyglAPGKSVLLRYAYPI 656
Cdd:PRK04156 413 YFFVRDPVELEIEGAE-----PLEAKI-PLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFNV 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 657 KctdvILADDKETVLEIRAEYDPSKTIKPKgVLHWVAEPSpgvdplKVEVRLfdrlfcsenpaelddwlgdLSPESKVVi 736
Cdd:PRK04156 477 E----ITGVSVDKARYHSDDLEEARKNKAP-IIQWVPEDE------SVPVRV-------------------LKPDGGDI- 525
|
490 500 510
....*....|....*....|....*....|....*....
gi 565354490 737 qNAYAVPSVSKATLGDKFQFERLGYFAVDKdSTSEKLVF 775
Cdd:PRK04156 526 -EGLAEPDVADLEVDDIVQFERFGFVRIDS-VEDDEVVA 562
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
8-164 |
6.57e-71 |
|
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: 229.37 E-value: 6.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 8 VLDLFLKIGLDEKTAKNTLANNKVTTNLTAVIHEAAVIDGCDRAVGNLLYTVATKFPANALNHRPTLLQYIVSTKIKTPA 87
Cdd:pfam04558 3 LIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTTL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565354490 88 QLEAAFAFLASTASENLKAHDFEEACGVGVEVSKEDIERAVSEVFEEKKTNILEQRYRINVGELFGHVRK--KLPWADP 164
Cdd:pfam04558 83 QVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
574-765 |
2.38e-49 |
|
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: 171.30 E-value: 2.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 574 AARTLVVLNPLKVVITNIEAGLVMDLDAKKWPEAPADDassFYKVPFSRVVYIERTDFRlkdskdyyGLAPGKSVLLRYA 653
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELG---TRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 654 YPIKCTDVIlADDKETVLEIRAEYDP---SKTIKPKG-VLHWVAEPspgvDPLKVEVRLFDRLFCSENPaelDDWLgdLS 729
Cdd:pfam03950 70 YNIKVTEVV-KDEDGNVTELHCTYDGddlGGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 565354490 730 PESKVVIQNAYAVPSVSKATLGDKFQFERLGYFAVD 765
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
266-576 |
5.18e-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: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKK--EYIDHIKEIVGWMGWEPFKITYTSDYFQ 343
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 344 DLYELAVELIRRGHAYVdhqtpdevkeyrekkmnspwrdrpieeslrlfdemkkgmidegkatlrmkqdmqndnfnmydl 423
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 424 iayrikftpHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFE--TRRASYywLLDALGLYQPFVWEYSRLNVSNTV 501
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565354490 502 MSKRKLNRLVTENWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDSSmIQLSRLEYHIREELNKTAAR 576
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
266-553 |
4.33e-39 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 144.54 E-value: 4.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--WEPfKITYTSDYFQ 343
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDE-GPYRQSDRFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 344 DLYELAVELIRRGhayvdhqtpdevkeyrekkmnspwrdrpieeslrlfdemkkgmidegkatlrmkqdmqndnfnmydl 423
Cdd:cd00418 80 LYRAYAEELIKKG------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 424 iayrikftphphagdkwcIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDALGLYQPFVWEYSRLNVS-NTVM 502
Cdd:cd00418 93 ------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEdGTKL 154
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 565354490 503 SKRKLNRlvtenwvdgwddprlmTLAGLRRRGVTSTAINAFVRGIGITRSD 553
Cdd:cd00418 155 SKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPD 189
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
266-356 |
7.78e-11 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 62.99 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 266 KVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--WE--PFKITYTSDY 341
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWDegPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 565354490 342 FQ----DLY-ELAVELIRRG 356
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
269-359 |
1.12e-10 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 63.33 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 269 TRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--WEPfKITYTSDYFqDLY 346
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DAY 85
|
90
....*....|....
gi 565354490 347 ELAVE-LIRRGHAY 359
Cdd:PRK05710 86 RAALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
262-398 |
1.09e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.13 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 262 VTGGKVLTRFPPEPNGFLHIGHAKAMFVDFGLAKERGGGCYLRFDDTNPEAEKKEYIDHIKEIVGWMG--WE--PFKITY 337
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegPDVGGE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565354490 338 TSDYFQ----DLY-ELAVELIRRGHAYVDHQTPDEV---KEYREKKMNSP-----WRDRPIEEslrLFDEMKKG 398
Cdd:PLN02627 121 YGPYRQsernAIYkQYAEKLLESGHVYPCFCTDEELeamKEEAELKKLPPrytgkWATASDEE---VQAELAKG 191
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
269-376 |
7.54e-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: 49.40 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 269 TRFPPEPNGFLHIGHAKAMFVDFGLAKE-----RGGGCYLRFDDTN-------------PEAEKKEYIDHIKEIVGW--- 327
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYmfl 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 565354490 328 --MGWEPFKITY------TSDyFQDLYELAVELIRR--GHAYVDHQTPDEVKEYREKKM 376
Cdd:cd00802 82 qaADFLLLYETEcdihlgGSD-QLGHIELGLELLKKagGPARPFGLTFGRVMGADGTKM 139
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
269-361 |
2.09e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 44.07 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565354490 269 TRFPPEPnGFLHIGHAKAMfvdfGLAKERGGGCYLRFDDTNPE------AEKKEYIDHIKEIVGWMGwepfkitytsDYF 342
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG----------EDF 66
|
90
....*....|....*....
gi 565354490 343 QDLYELAVELIRRGHAYVD 361
Cdd:cd02156 67 QQNRELYRWVKDNITLPVD 85
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
167-239 |
2.09e-04 |
|
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: 40.75 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565354490 167 VKEVVDLKLYKLLGERTAADNEKPVKKKKEKPAKTEDKAKVEETSAPKQSEEELNP----YLIFPTPEENYKVHTEI 239
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFsegfLGKFHKPGENPKTDGYV 77
|
|
| |
