|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
12-795 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1633.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 12 SPPELASFLAIGLDQRTAENALANRKVTANLTAVIAEAGV-SGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVSSKIK 90
Cdd:PLN02859 5 SEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVtNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 91 TPAQLDAALSFLSTLGPDPLDTAKFEETCGVGVVVSTEEIQSMVTDILKENMEAIVEQRYHINVGSLCGQVRKWHPWGDA 170
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 171 KFIKEEIDKRLTEILGPKTEADNVKPVKKKKEKPAKVEEKKTAVAaPAPPSEEELNPYSIFPQPEENLKVHTEIFFSDGN 250
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVA-AAPPSEEELNPYSIFPQPEENFKVHTEVFFSDGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 251 IWRAHNRKDILEKHLKATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIV 330
Cdd:PLN02859 244 VLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 331 RWMGWEPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKA 410
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 411 TLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQY 490
Cdd:PLN02859 404 TLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 491 QPYVWEYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRLERLEYH 570
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRLEHH 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 571 IREELNKVAPRAMVVLHPLKVVINNLDYGTIIDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPG 650
Cdd:PLN02859 564 IREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 651 KTVLLRYAFPIKCTEVIYGDNSDNIIEIRAEYDPSKATKPKGVLHWVAEPSPGVNPLKVEIRLFEKLFLSENPVELEDWL 730
Cdd:PLN02859 644 KSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELEDWL 723
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002271251 731 GDLNPRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTAEELVFNRTVTLRDSYGKAGP 795
Cdd:PLN02859 724 EDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
272-790 |
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: 591.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 272 VMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEP-YKVTYTSDYFQEL 350
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 351 YELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMKQDMQNDNKNMA 426
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLD-QYQPYVWEYSRLNISNN 505
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHiFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 506 VMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRLERLEYHIREELNKVAPRAMVV 585
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 586 LHPLKVVINNLDYgtiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPGKTVLLRYAFPIKcTE 665
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 666 VIYGDNSDNIIEIRAEYD-------PSKATKPKGVLHWVaepsPGVNPLKVEIRLFEKLFLSENPVELEDWLGDLNPRSK 738
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1002271251 739 eVIKGAYAVPSLATAALGDKFQFERLGYFAVDS-DSTAEELVFNRTVTLRDSY 790
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
271-576 |
8.73e-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: 425.19 E-value: 8.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEP-YKVTYTSDYFQE 349
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 350 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--NSPWRDRPIEESLKLF-EDMRHGLVAEGKATLRMKQDMQNDnKNMA 426
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTP---HPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQY-QPYVWEYSRLNI 502
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002271251 503 SNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRLERLEYHIREELN 576
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
271-581 |
9.67e-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: 398.93 E-value: 9.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEPYKVTYTSDYFQEL 350
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 351 YELAVCLIKKGLAYVDHQTpeeikeyrekqmnspwrdrpieeslklfedmrhglvaegkatlrmkqdmqndnknmadlia 430
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 431 yrikftphphaGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNISNNVMSKR 510
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002271251 511 KLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRLERLEYHIREELNKVAPR 581
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
268-768 |
3.69e-86 |
|
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: 280.91 E-value: 3.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 268 TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--W--EPYkvtYT 343
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 344 SDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--------NSPWRDRPIEEslklfedmRHGLVAEG-KATLRM 414
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 415 K--------QDM-----QNDNKNMADLIAYRikftphpHAGdkwfiYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYY 481
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 482 WLLVSLDQYQPyvwEYSRLNISNN----VMSKRKlnklvtekwvdgwddpRLLTLAGLRRRGVSSTAINSFIRGMGITRS 557
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 558 DNSLIR-LERLEYHIreELNKVaPRAMVVLHPLKVVINN------LDYGTIIDLDAKKWPDApGDDASAYYKVPFSRT-- 628
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEA-GIREDLERLVPLVREra 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 629 ------------VYIEQSDfrVKDSKDYygLAPGKTvllryAFPIKCTEviygdnsdNIIEIRAEYDPSKAtkpKGVLHW 696
Cdd:COG0008 355 ktlselaelarfFFIERED--EKAAKKR--LAPEEV-----RKVLKAAL--------EVLEAVETWDPETV---KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002271251 697 VAEpspgvnplKVEIRLfeKLFLseNPVELedwlgdlnprskeVIKGAYAVPSLAT--AALGDKFQFERLGYFA 768
Cdd:COG0008 415 VSA--------EAGVKD--GLLF--MPLRV-------------ALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
12-795 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1633.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 12 SPPELASFLAIGLDQRTAENALANRKVTANLTAVIAEAGV-SGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVSSKIK 90
Cdd:PLN02859 5 SEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVtNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSSKIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 91 TPAQLDAALSFLSTLGPDPLDTAKFEETCGVGVVVSTEEIQSMVTDILKENMEAIVEQRYHINVGSLCGQVRKWHPWGDA 170
Cdd:PLN02859 85 TPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPWADP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 171 KFIKEEIDKRLTEILGPKTEADNVKPVKKKKEKPAKVEEKKTAVAaPAPPSEEELNPYSIFPQPEENLKVHTEIFFSDGN 250
Cdd:PLN02859 165 KIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVA-AAPPSEEELNPYSIFPQPEENFKVHTEVFFSDGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 251 IWRAHNRKDILEKHLKATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIV 330
Cdd:PLN02859 244 VLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 331 RWMGWEPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKA 410
Cdd:PLN02859 324 EWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 411 TLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQY 490
Cdd:PLN02859 404 TLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 491 QPYVWEYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRLERLEYH 570
Cdd:PLN02859 484 QPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRLEHH 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 571 IREELNKVAPRAMVVLHPLKVVINNLDYGTIIDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPG 650
Cdd:PLN02859 564 IREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 651 KTVLLRYAFPIKCTEVIYGDNSDNIIEIRAEYDPSKATKPKGVLHWVAEPSPGVNPLKVEIRLFEKLFLSENPVELEDWL 730
Cdd:PLN02859 644 KSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELEDWL 723
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002271251 731 GDLNPRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTAEELVFNRTVTLRDSYGKAGP 795
Cdd:PLN02859 724 EDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
258-793 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 763.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 258 KDILEKHLkATG--GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGW 335
Cdd:PRK05347 15 RQIIDEDL-ASGkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 336 EP-YKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKA 410
Cdd:PRK05347 94 DWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 411 TLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLD-Q 489
Cdd:PRK05347 174 VLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPiP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 490 YQPYVWEYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDnSLIRLERLEY 569
Cdd:PRK05347 254 PHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 570 HIREELNKVAPRAMVVLHPLKVVINNLDYGTIIDLDAkkwPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAP 649
Cdd:PRK05347 333 CIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEA---PNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 650 GKTVLLRYAFPIKCTEVIYgDNSDNIIEIRAEYDP-------SKATKPKGVLHWVAEPspgvNPLKVEIRLFEKLFLSEN 722
Cdd:PRK05347 410 GKEVRLRNAYVIKCEEVVK-DADGNITEIHCTYDPdtlsgnpADGRKVKGTIHWVSAA----HAVPAEVRLYDRLFTVPN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002271251 723 PVELEDWLGDLNPRSKeVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTAEELVFNRTVTLRDSYGKA 793
Cdd:PRK05347 485 PAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
259-792 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 605.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 259 DILEKHLKA-TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWE- 336
Cdd:PRK14703 18 EIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 337 PYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATL 412
Cdd:PRK14703 98 GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 413 RMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQY-- 490
Cdd:PRK14703 178 RAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWpp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 491 QPYVWEYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSdNSLIRLERLEYH 570
Cdd:PRK14703 258 RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKT-NSTVDIGVLEFA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 571 IREELNKVAPRAMVVLHPLKVVINNLDYGTIIDLDAKKWPDAPGDDASAyyKVPFSRTVYIEQSDFRVKDSKDYYGLAPG 650
Cdd:PRK14703 337 IRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 651 KTVLLRYAFPIKCTEVIYGDNSdNIIEIRAEYDPSKAT------KPKGVLHWVAEPSpgvnPLKVEIRLFEKLFLSENPV 724
Cdd:PRK14703 415 REVRLRGAYIIRCDEVVRDADG-AVTELRCTYDPESAKgedtgrKAAGVIHWVSAKH----ALPAEVRLYDRLFKVPQPE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 725 ELE-DWLGDLNPRSKEVIKGaYAVPSLATAALGDKFQFERLGYFAVDS-DSTAEELVFNRTVTLRDSYGK 792
Cdd:PRK14703 490 AADeDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
256-793 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 595.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 256 NRKDILEKHLKATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGW 335
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 336 EPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMK 415
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 416 QDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVW 495
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 496 EYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRLERLEYHIREEL 575
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMN-VIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 576 NKVAPRAMVVLHPLKVVINNLDYGTIIDLdakkwPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDS-KDYYGLAPG-KTV 653
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKGEREFEC-----PNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNnSKFYGLAPGpRVV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 654 LLRYAFPIKCTEVIYGDNSDNIIeIRAEYDPSKATKPKGVLHWVAEpsPGVNPlkVEIRLFEKLFLSENPVELEDWLGDL 733
Cdd:PTZ00437 430 GLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSA--TACTP--VEVRLYNALLKDDRAAIDPEFLKFI 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 734 NPRSKEVIKGaYAVPSLATAALGDKFQFERLGYFAVDSDSTAEELVFNRTVTLRDSYGKA 793
Cdd:PTZ00437 505 DEDSEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
272-790 |
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: 591.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 272 VMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEP-YKVTYTSDYFQEL 350
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 351 YELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMKQDMQNDNKNMA 426
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLD-QYQPYVWEYSRLNISNN 505
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHiFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 506 VMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRLERLEYHIREELNKVAPRAMVV 585
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 586 LHPLKVVINNLDYgtiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPGKTVLLRYAFPIKcTE 665
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 666 VIYGDNSDNIIEIRAEYD-------PSKATKPKGVLHWVaepsPGVNPLKVEIRLFEKLFLSENPVELEDWLGDLNPRSK 738
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1002271251 739 eVIKGAYAVPSLATAALGDKFQFERLGYFAVDS-DSTAEELVFNRTVTLRDSY 790
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
271-576 |
8.73e-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: 425.19 E-value: 8.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEP-YKVTYTSDYFQE 349
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 350 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--NSPWRDRPIEESLKLF-EDMRHGLVAEGKATLRMKQDMQNDnKNMA 426
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTP---HPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQY-QPYVWEYSRLNI 502
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002271251 503 SNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRLERLEYHIREELN 576
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
271-581 |
9.67e-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: 398.93 E-value: 9.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEPYKVTYTSDYFQEL 350
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 351 YELAVCLIKKGLAYVDHQTpeeikeyrekqmnspwrdrpieeslklfedmrhglvaegkatlrmkqdmqndnknmadlia 430
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 431 yrikftphphaGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNISNNVMSKR 510
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002271251 511 KLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRLERLEYHIREELNKVAPR 581
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
267-770 |
4.44e-97 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 317.82 E-value: 4.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 267 ATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEPYKVTYTSDY 346
Cdd:PLN02907 209 AEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDY 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 347 FQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMKQDMQNDNKNMA 426
Cdd:PLN02907 289 FPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNISNNV 506
Cdd:PLN02907 369 DPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 507 MSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRLERLEYHIREELNKVAPRAMVVL 586
Cdd:PLN02907 449 LSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLN-LMEWDKLWTINKKIIDPVCPRHTAVL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 587 HPLKVVINNLDyG-----TIIDLDAKKWPDApGDDASAyykvpFSRTVYIEQSDFRVkdskdyygLAPGKTVLLR---YA 658
Cdd:PLN02907 528 KEGRVLLTLTD-GpetpfVRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEA--------ISEGEEVTLMdwgNA 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 659 FpIKcteVIYGDNSDNIIEIRAEYDPS---KATKPKgvLHWVAEPSPGVNPLKVEirlFEKLFLSENPVELEDWLGDLNP 735
Cdd:PLN02907 593 I-IK---EITKDEGGAVTALSGELHLEgsvKTTKLK--LTWLPDTNELVPLSLVE---FDYLITKKKLEEDDNFLDVLNP 663
|
490 500 510
....*....|....*....|....*....|....*
gi 1002271251 736 RSKeVIKGAYAVPSLATAALGDKFQFERLGYFAVD 770
Cdd:PLN02907 664 CTK-KETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
267-779 |
1.52e-93 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 304.96 E-value: 1.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 267 ATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGwEPYKV--TYTS 344
Cdd:PTZ00402 48 AEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 345 DYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGlVAEGKAT-LRMKQDMQNDNK 423
Cdd:PTZ00402 127 DYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKG-SAEGQETcLRAKISVDNENK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 424 NMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNIS 503
Cdd:PTZ00402 206 AMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNME 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 504 NNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRLERLEYHIREELNKVAPRAM 583
Cdd:PTZ00402 286 YSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN-FMEWSKLWYFNTQILDPSVPRYT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 584 VVLHPLKVvinNLDYGTIIDLDAKKWP---DAPGDDASAYYKvpfsrtvyieqSDFRVKDSKDYYGLAPGKTVLLR---- 656
Cdd:PTZ00402 365 VVSNTLKV---RCTVEGQIHLEACEKLlhkKVPDMGEKTYYK-----------SDVIFLDAEDVALLKEGDEVTLMdwgn 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 657 -YAFPIKcTEVIYGDNSDNIIEIRAEYDpSKATKPKgvLHWVAEpSPgvNPLKVEIRLFEKLFLSENPvELEDWLGDLNP 735
Cdd:PTZ00402 431 aYIKNIR-RSGEDALITDADIVLHLEGD-VKKTKFK--LTWVPE-SP--KAEVMELNEYDHLLTKKKP-DPEESIDDIIA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1002271251 736 RSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTAEELV 779
Cdd:PTZ00402 503 PVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
267-777 |
1.87e-89 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 291.53 E-value: 1.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 267 ATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEPYKVTYTSDY 346
Cdd:PLN03233 7 AIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 347 FQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGlVAEGKA-TLRMKQDMQNDNKNM 425
Cdd:PLN03233 87 FEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSG-KEEGGAwCLRAKIDMQSDNGTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 426 ADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNISNN 505
Cdd:PLN03233 166 RDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 506 VMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRsdnsliRLERLEY-----HIREELNKVAP 580
Cdd:PLN03233 246 VLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASR------RVVNLDWakfwaENKKEIDKRAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 581 RAMVV--LHPLKVVINNLDYGTiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyGLAPGKT-VLLRY 657
Cdd:PLN03233 320 RFMAIdkADHTALTVTNADEEA--DFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTE--------DIQLGEDiVLLRW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 658 AFpIKCTEvIYGDnsdniieIRAEYDPS---KATKPKgvLHWVAEPSPGVnplKVEIRLFEKLFLSENPVELEDWLGDLN 734
Cdd:PLN03233 390 GV-IEISK-IDGD-------LEGHFIPDgdfKAAKKK--ISWIADVSDNI---PVVLSEFDNLIIKEKLEEDDKFEDFIN 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1002271251 735 PRSK---EVIKGAyavpSLATAALGDKFQFERLGYFAVDSDSTAEE 777
Cdd:PLN03233 456 PDTLaetDVIGDA----GLKTLKEHDIIQLERRGFYRVDRPYMGEE 497
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
268-768 |
3.69e-86 |
|
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: 280.91 E-value: 3.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 268 TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--W--EPYkvtYT 343
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 344 SDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--------NSPWRDRPIEEslklfedmRHGLVAEG-KATLRM 414
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 415 K--------QDM-----QNDNKNMADLIAYRikftphpHAGdkwfiYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYY 481
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 482 WLLVSLDQYQPyvwEYSRLNISNN----VMSKRKlnklvtekwvdgwddpRLLTLAGLRRRGVSSTAINSFIRGMGITRS 557
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 558 DNSLIR-LERLEYHIreELNKVaPRAMVVLHPLKVVINN------LDYGTIIDLDAKKWPDApGDDASAYYKVPFSRT-- 628
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEA-GIREDLERLVPLVREra 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 629 ------------VYIEQSDfrVKDSKDYygLAPGKTvllryAFPIKCTEviygdnsdNIIEIRAEYDPSKAtkpKGVLHW 696
Cdd:COG0008 355 ktlselaelarfFFIERED--EKAAKKR--LAPEEV-----RKVLKAAL--------EVLEAVETWDPETV---KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002271251 697 VAEpspgvnplKVEIRLfeKLFLseNPVELedwlgdlnprskeVIKGAYAVPSLAT--AALGDKFQFERLGYFA 768
Cdd:COG0008 415 VSA--------EAGVKD--GLLF--MPLRV-------------ALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
267-771 |
6.59e-85 |
|
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: 280.56 E-value: 6.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 267 ATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMGWEPYKVTYTSDY 346
Cdd:TIGR00463 89 AKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 347 FQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMKQDMQNDNKNMA 426
Cdd:TIGR00463 169 IETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEF--DIRRPSYYWLLVSLDQYQPYVWEYSRLNISN 504
Cdd:TIGR00463 249 DWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 505 NVMSKRKLNKLVTEKWVdGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLiRLERLEYHIREELNKVAPRAMV 584
Cdd:TIGR00463 329 ALSTSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALNRKIIDEEARRYFF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 585 VLHPLKVVINNLDYGTIIDLdaKKWPDAPgddASAYYKVPFSRTVYIEQSDFRVKDskdyyglapgKTVLLRYAFPIKCT 664
Cdd:TIGR00463 407 IWNPVKIEIVGLPEPKRVER--PLHPDHP---EIGERVLILRGEIYVPKDDLEEGV----------EPVRLMDAVNVIYS 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 665 EVIYGDNSDNIIEIRaeydpskaTKPKGVLHWVAEPSpgvnPLKVEIRLFEKL----FLSENPVELEdwlgdlnprskev 740
Cdd:TIGR00463 472 KKELRYHSEGLEGAR--------KLGKSIIHWLPAKD----AVKVKVIMPDASivegVIEADASELE------------- 526
|
490 500 510
....*....|....*....|....*....|.
gi 1002271251 741 ikgayavpslataaLGDKFQFERLGYFAVDS 771
Cdd:TIGR00463 527 --------------VGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
266-780 |
9.88e-79 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 264.41 E-value: 9.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 266 KATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEK--KEYIDHIQEIVRWMGWEPYKVTYT 343
Cdd:PRK04156 96 NAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 344 SDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVAEGKATLRMKQDMQNDNK 423
Cdd:PRK04156 176 SDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 424 NMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEfdirrpsyywLLVSLD--QY--------QPY 493
Cdd:PRK04156 256 SVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKD----------HIDNTEkqRYiydyfgweYPE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 494 VWEYSRLNISNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRLERLEYHIRE 573
Cdd:PRK04156 326 TIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 574 ELNKVAPRAMVVLHPLKVVINNLDygtiiDLDAKKwPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyglAPGKTV 653
Cdd:PRK04156 405 LIDPIANRYFFVRDPVELEIEGAE-----PLEAKI-PLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 654 LLRYAFPIKCTEViygdNSDNIIEIRAEYDPSKATKPKgVLHWVAEPSPgvNPLKVEIrlfeklflsenPVEledwlgdl 733
Cdd:PRK04156 469 RLMDLFNVEITGV----SVDKARYHSDDLEEARKNKAP-IIQWVPEDES--VPVRVLK-----------PDG-------- 522
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1002271251 734 nprskEVIKGaYAVPSLATAALGDKFQFERLGYFAVDSDSTaEELVF 780
Cdd:PRK04156 523 -----GDIEG-LAEPDVADLEVDDIVQFERFGFVRIDSVED-DEVVA 562
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
15-170 |
1.63e-63 |
|
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: 209.73 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 15 ELAS-FLAIGLDQRTAENALANRKVTANLTAVIAEAGV-SGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVSSKIKTP 92
Cdd:pfam04558 2 ELIElFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVeSGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 93 AQLDAALSFLSTLGPDPLDTAKFEETCGVGVVVSTEEIQSMVTDILKENMEAIVEQRYHINVGSLCGQVRKW--HPWGDA 170
Cdd:pfam04558 82 LQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKLpeLKWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
579-770 |
9.25e-55 |
|
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: 186.32 E-value: 9.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 579 APRAMVVLHPLKVVINNLDYGTIIDLDAkkwPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyGLAPGKTVLLRYA 658
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEV---PNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 659 FPIKCTEVIYgDNSDNIIEIRAEYDP---SKATKPKG-VLHWVAEPspgvNPLKVEIRLFEKLFLSENPvelEDWLgdLN 734
Cdd:pfam03950 70 YNIKVTEVVK-DEDGNVTELHCTYDGddlGGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002271251 735 PRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVD 770
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
271-581 |
3.34e-38 |
|
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: 142.49 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKK--EYIDHIQEIVRWMGWEPYKVTYTSDYFQ 348
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 349 ELYELAVCLIKKGLAYVdhqtpeeikeyrekqmnspwrdrpieeslklfedmrhglvaegkatlrmkqdmqndnknmadl 428
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 429 iayrikftpHPHAGDKWFIYPSYDYAHCLVDSLENITHSL--CTLEFDIRRPSYywllvsLDQY----QPYVWEYSRLNI 502
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLrgKDHIDNTEKQRY------IYEYfgweYPETIHWGRLKI 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271251 503 SNNVMSKRKLNKLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRLERLEYHIREELNKVAPR 581
Cdd:cd09287 163 EGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
271-581 |
1.48e-36 |
|
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: 137.60 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--WE--PYkvtYTSDY 346
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDegPY---RQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 347 FQELYELAVCLIKKGlayvdhqtpeeikeyrekqmnspwrdrpieeslklfedmrhglvaegkatlrmkqdmqndnknma 426
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 427 dliayrikftphphagdkwfIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVSLDQYQPYVWEYSRLNISNN- 505
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGt 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002271251 506 VMSKRKLNKlvtekwvdgwddprllTLAGLRRRGVSSTAINSFIRGMGITRSDN-SLIRLERLEYHIREELNKVAPR 581
Cdd:cd00418 153 KLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGhELFTLEEMIAAFSVERVNSADA 213
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
271-361 |
3.55e-12 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 66.84 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 271 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--WE--PYKVTYTSDY 346
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWDegPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 1002271251 347 FQ----ELY-ELAVCLIKKG 361
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
274-364 |
6.10e-12 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 67.18 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 274 TRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--WEPyKVTYTSDYFqELY 351
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DAY 85
|
90
....*....|....
gi 1002271251 352 ELAV-CLIKKGLAY 364
Cdd:PRK05710 86 RAALdRLRAQGLVY 99
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
173-254 |
4.35e-08 |
|
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: 51.15 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 173 IKEEIDKRLTEILGPKTEADnvkPVKKKKEKPAKVEEKKTAVAAPAPPSEEELNPYS--------IFPQPEENLKVHTEI 244
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEAD---LKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSmfsegflgKFHKPGENPKTDGYV 77
|
90
....*....|
gi 1002271251 245 FFSDGNIWRA 254
Cdd:pfam04557 78 VTEHTMRLLK 87
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
267-392 |
1.28e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.13 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271251 267 ATGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYLRFDDTNPEAEKKEYIDHIQEIVRWMG--WE-------- 336
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegpdvgge 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002271251 337 --PYKVTYTSDYFQELYELavcLIKKGLAYVDHQTPEEIKEYRE--KQMNSP------WRDRPIEE 392
Cdd:PLN02627 121 ygPYRQSERNAIYKQYAEK---LLESGHVYPCFCTDEELEAMKEeaELKKLPprytgkWATASDEE 183
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
273-333 |
1.43e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 48.63 E-value: 1.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271251 273 MTRFPPEPNGYLHIGHAKAMFIDFGLAKERN-----GHCYLRFDDTN-------------PEAEKKEYIDHIQEIVRWM 333
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
274-334 |
1.97e-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: 1.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002271251 274 TRFPPEPnGYLHIGHAKAMfidfGLAKERNGHCYLRFDDTNPE------AEKKEYIDHIQEIVRWMG 334
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG 63
|
|
| |
