|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
11-799 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 11 APPPPSPELVSFLAIGLDQRTAENALANRKVTANLTAVITEAGVVSGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVS 90
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 91 SKIKSPAQLDAALSFLSTLGPDSLDTAKFEETCGVGVVVSTEEIQSTVTDVLKENMEAIVEQRYHINVGSLCGQVRKRHP 170
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 171 WGDAKFIKEEIDKRLTEILGPKTEADNIKPMKKKKEKPAKVEDKKTAAAAPAPpSEEELNPYSIFPQPEENLKVHTEIFF 250
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPP-SEEELNPYSIFPQPEENFKVHTEVFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 251 SDGNIWRAHNTKDILEKHLKTTGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHI 330
Cdd:PLN02859 240 SDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 331 QEIVQWMGWEPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVP 410
Cdd:PLN02859 320 EEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 411 EGKATLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVA 490
Cdd:PLN02859 400 EGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 491 LDQYQPYVWEYSRLNISNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRVER 570
Cdd:PLN02859 480 LGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 571 LEYHIREELNKVASRTMVVLHPLKVVITNLESGKIIDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYG 650
Cdd:PLN02859 560 LEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 651 LAPGKTVLLRYAFPIKCTEVIYGDNTDNIVEIRAEYDPSKATKPKGVLHWVAEPSPGVDPLKVEIRLFERLFLSENPVEL 730
Cdd:PLN02859 640 LAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAEL 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573945447 731 EDWLGDLNPRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTPEELVFNRTVTLRDSYGKAGP 799
Cdd:PLN02859 720 EDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
276-794 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 584.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 276 VMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-YKVTYTSDYFQEL 354
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 355 YELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATLRMKQDMQNDNKNMA 430
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALD-QYQPYVWEYSRLNISNN 509
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHiFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 510 VMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRVERLEYHIREELNKVASRTMVV 589
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 590 LHPLKVVITNLESgkiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPGKTVLLRYAFPIKcTE 669
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 670 VIYGDNTDNIVEIRAEYD-------PSKATKPKGVLHWVaepsPGVDPLKVEIRLFERLFLSENPVELEDWLGDLNPRSK 742
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 573945447 743 eVIKGAYAVPSLATAALGDKFQFERLGYFAVDS-DSTPEELVFNRTVTLRDSY 794
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
275-580 |
2.72e-145 |
|
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: 429.43 E-value: 2.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-YKVTYTSDYFQE 353
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 354 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--NSPWRDRPIEESLKLF-EDMRHGLVPEGKATLRMKQDMQNDnKNMA 430
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 DLIAYRIKFTP---HPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQY-QPYVWEYSRLNI 506
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573945447 507 SNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRVERLEYHIREELN 580
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
275-585 |
1.77e-133 |
|
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: 395.85 E-value: 1.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEPYKVTYTSDYFQEL 354
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 355 YELAVCLIKKGLAYVDHQTpeeikeyrekqmnspwrdrpieeslklfedmrhglvpegkatlrmkqdmqndnknmadlia 434
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 435 yrikftphphaGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNNVMSKR 514
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573945447 515 KLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRVERLEYHIREELNKVASR 585
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
272-772 |
2.22e-85 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 278.99 E-value: 2.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 272 TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--W--EPYkvtYT 347
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 348 SDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--------NSPWRDRPIEEslklfedmRHGLVPEG-KATLRM 418
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 419 K--------QDM-----QNDNKNMADLIAYRikftphpHAGdkwfiYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYY 485
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 486 WLLVALDQYQPyvwEYSRLNISNN----VMSKRKlnrlvtekwvdgwddpRLLTLAGLRRRGVSSTAINSFIRGMGITRS 561
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 562 DNSLIR-VERLEYHIreELNKVaSRTMVVLHPLKVVITN------LESGKIIDLDAKKWPDApGDDASAYYKVPFSRT-- 632
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEA-GIREDLERLVPLVREra 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 633 ------------VYIEQSDfrVKDSKDYygLAPGKTvllryAFPIKCTEviygdntdNIVEIRAEYDPSKAtkpKGVLHW 700
Cdd:COG0008 355 ktlselaelarfFFIERED--EKAAKKR--LAPEEV-----RKVLKAAL--------EVLEAVETWDPETV---KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573945447 701 VAEpspgvdplKVEIRLfeRLFLseNPVELedwlgdlnprskeVIKGAYAVPSLAT--AALGDKFQFERLGYFA 772
Cdd:COG0008 415 VSA--------EAGVKD--GLLF--MPLRV-------------ALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
11-799 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 11 APPPPSPELVSFLAIGLDQRTAENALANRKVTANLTAVITEAGVVSGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVS 90
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 91 SKIKSPAQLDAALSFLSTLGPDSLDTAKFEETCGVGVVVSTEEIQSTVTDVLKENMEAIVEQRYHINVGSLCGQVRKRHP 170
Cdd:PLN02859 81 SKIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 171 WGDAKFIKEEIDKRLTEILGPKTEADNIKPMKKKKEKPAKVEDKKTAAAAPAPpSEEELNPYSIFPQPEENLKVHTEIFF 250
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAVAAAPP-SEEELNPYSIFPQPEENFKVHTEVFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 251 SDGNIWRAHNTKDILEKHLKTTGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHI 330
Cdd:PLN02859 240 SDGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 331 QEIVQWMGWEPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVP 410
Cdd:PLN02859 320 EEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 411 EGKATLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVA 490
Cdd:PLN02859 400 EGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 491 LDQYQPYVWEYSRLNISNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRVER 570
Cdd:PLN02859 480 LGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 571 LEYHIREELNKVASRTMVVLHPLKVVITNLESGKIIDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYG 650
Cdd:PLN02859 560 LEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 651 LAPGKTVLLRYAFPIKCTEVIYGDNTDNIVEIRAEYDPSKATKPKGVLHWVAEPSPGVDPLKVEIRLFERLFLSENPVEL 730
Cdd:PLN02859 640 LAPGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAEL 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573945447 731 EDWLGDLNPRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTPEELVFNRTVTLRDSYGKAGP 799
Cdd:PLN02859 720 EDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
262-797 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 765.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 262 KDILEKHLKTtG--GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGW 339
Cdd:PRK05347 15 RQIIDEDLAS-GkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 340 EP-YKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKA 414
Cdd:PRK05347 94 DWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 415 TLRMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALD-Q 493
Cdd:PRK05347 174 VLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPiP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 494 YQPYVWEYSRLNISNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDnSLIRVERLEY 573
Cdd:PRK05347 254 PHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 574 HIREELNKVASRTMVVLHPLKVVITNLESGKIIDLDAkkwPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAP 653
Cdd:PRK05347 333 CIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEA---PNHPEDPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 654 GKTVLLRYAFPIKCTEVIYgDNTDNIVEIRAEYDP-------SKATKPKGVLHWVAEPspgvDPLKVEIRLFERLFLSEN 726
Cdd:PRK05347 410 GKEVRLRNAYVIKCEEVVK-DADGNITEIHCTYDPdtlsgnpADGRKVKGTIHWVSAA----HAVPAEVRLYDRLFTVPN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573945447 727 PVELEDWLGDLNPRSKeVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTPEELVFNRTVTLRDSYGKA 797
Cdd:PRK05347 485 PAAGKDFLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAKI 554
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
263-796 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 610.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 263 DILEKHLKT-TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWE- 340
Cdd:PRK14703 18 EIIEEDLEAgRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 341 PYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATL 416
Cdd:PRK14703 98 GEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 417 RMKQDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQY-- 494
Cdd:PRK14703 178 RAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWpp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 495 QPYVWEYSRLNISNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSdNSLIRVERLEYH 574
Cdd:PRK14703 258 RPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKT-NSTVDIGVLEFA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 575 IREELNKVASRTMVVLHPLKVVITNLESGKIIDLDAKKWPDAPGDDASAyyKVPFSRTVYIEQSDFRVKDSKDYYGLAPG 654
Cdd:PRK14703 337 IRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLTPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 655 KTVLLRYAFPIKCTEVIYGDNtDNIVEIRAEYDPSKAT------KPKGVLHWVAEPSpgvdPLKVEIRLFERLFLSENPV 728
Cdd:PRK14703 415 REVRLRGAYIIRCDEVVRDAD-GAVTELRCTYDPESAKgedtgrKAAGVIHWVSAKH----ALPAEVRLYDRLFKVPQPE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 729 ELE-DWLGDLNPRSKEVIKGaYAVPSLATAALGDKFQFERLGYFAVDS-DSTPEELVFNRTVTLRDSYGK 796
Cdd:PRK14703 490 AADeDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGA 558
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
260-797 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 593.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 260 NTKDILEKHLKTTGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGW 339
Cdd:PTZ00437 36 NTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 340 EPYKVTYTSDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATLRMK 419
Cdd:PTZ00437 116 KPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 420 QDMQNDNKNMADLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVW 499
Cdd:PTZ00437 196 ADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 500 EYSRLNISNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRVERLEYHIREEL 579
Cdd:PTZ00437 276 EFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMN-VIQISMLENTLREDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 580 NKVASRTMVVLHPLKVVITNLESGKIIDLdakkwPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDS-KDYYGLAPG-KTV 657
Cdd:PTZ00437 355 DERCERRLMVIDPIKVVVDNWKGEREFEC-----PNHPRKPELGSRKVMFTDTFYVDRSDFRTEDNnSKFYGLAPGpRVV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 658 LLRYAFPIKCTEVIYGDNTDNIVeIRAEYDPSKATKPKGVLHWVAEpsPGVDPlkVEIRLFERLFLSENPVELEDWLGDL 737
Cdd:PTZ00437 430 GLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSA--TACTP--VEVRLYNALLKDDRAAIDPEFLKFI 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 738 NPRSKEVIKGaYAVPSLATAALGDKFQFERLGYFAVDSDSTPEELVFNRTVTLRDSYGKA 797
Cdd:PTZ00437 505 DEDSEVVSHG-YAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKA 563
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
276-794 |
0e+00 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 584.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 276 VMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-YKVTYTSDYFQEL 354
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 355 YELAVCLIKKGLAYVDHQTPEEIKEYR----EKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATLRMKQDMQNDNKNMA 430
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALD-QYQPYVWEYSRLNISNN 509
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHiFPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 510 VMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRVERLEYHIREELNKVASRTMVV 589
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNN-IEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 590 LHPLKVVITNLESgkiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRVKDSKDYYGLAPGKTVLLRYAFPIKcTE 669
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIK-AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 670 VIYGDNTDNIVEIRAEYD-------PSKATKPKGVLHWVaepsPGVDPLKVEIRLFERLFLSENPVELEDWLGDLNPRSK 742
Cdd:TIGR00440 395 RVEKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPESL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 573945447 743 eVIKGAYAVPSLATAALGDKFQFERLGYFAVDS-DSTPEELVFNRTVTLRDSY 794
Cdd:TIGR00440 471 -VIKQGFMEHSLGDAVANKRFQFEREGYFCLDSkESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
275-580 |
2.72e-145 |
|
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: 429.43 E-value: 2.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEP-YKVTYTSDYFQE 353
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 354 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--NSPWRDRPIEESLKLF-EDMRHGLVPEGKATLRMKQDMQNDnKNMA 430
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 DLIAYRIKFTP---HPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQY-QPYVWEYSRLNI 506
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573945447 507 SNNVMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLIRVERLEYHIREELN 580
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
275-585 |
1.77e-133 |
|
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: 395.85 E-value: 1.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEPYKVTYTSDYFQEL 354
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 355 YELAVCLIKKGLAYVDHQTpeeikeyrekqmnspwrdrpieeslklfedmrhglvpegkatlrmkqdmqndnknmadlia 434
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 435 yrikftphphaGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNNVMSKR 514
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573945447 515 KLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRVERLEYHIREELNKVASR 585
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
274-774 |
1.77e-97 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 318.98 E-value: 1.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 274 GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEPYKVTYTSDYFQE 353
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 354 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGlVPEGKA-TLRMKQDMQNDNKNMADL 432
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAG-SERGLQcCVRGKLDMQDPNKSLRDP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 433 IAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNNVMS 512
Cdd:PLN02907 371 VYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 513 KRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRVERLEYHIREELNKVASRTMVVLHP 592
Cdd:PLN02907 451 KRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLN-LMEWDKLWTINKKIIDPVCPRHTAVLKE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 593 LKVVITnLESGK-----IIDLDAKKWPDApGDDASAyykvpFSRTVYIEQSDFRVkdskdyygLAPGKTVLLR---YAFp 664
Cdd:PLN02907 530 GRVLLT-LTDGPetpfvRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEA--------ISEGEEVTLMdwgNAI- 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 665 IKcteVIYGDNTDNIVEIRAEYDPS---KATKPKgvLHWVAEPSPGVDPLKVEirlFERLFLSENPVELEDWLGDLNPRS 741
Cdd:PLN02907 594 IK---EITKDEGGAVTALSGELHLEgsvKTTKLK--LTWLPDTNELVPLSLVE---FDYLITKKKLEEDDNFLDVLNPCT 665
|
490 500 510
....*....|....*....|....*....|...
gi 573945447 742 KeVIKGAYAVPSLATAALGDKFQFERLGYFAVD 774
Cdd:PLN02907 666 K-KETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
274-783 |
1.24e-91 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 299.96 E-value: 1.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 274 GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGwEPYKV--TYTSDYF 351
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 352 QELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGlVPEGKAT-LRMKQDMQNDNKNMA 430
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKG-SAEGQETcLRAKISVDNENKAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 DLIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNNV 510
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 511 MSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNsLIRVERLEYHIREELNKVASRTMVVL 590
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVN-FMEWSKLWYFNTQILDPSVPRYTVVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 591 HPLKVVIT-----NLESGKiiDLDAKKWPDApgdDASAYYKvpfsrtvyieqSDFRVKDSKDYYGLAPGKTVLLR----- 660
Cdd:PTZ00402 368 NTLKVRCTvegqiHLEACE--KLLHKKVPDM---GEKTYYK-----------SDVIFLDAEDVALLKEGDEVTLMdwgna 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 661 YAFPIKcTEVIYGDNTDNIVEIRAEYDpSKATKPKgvLHWVAEpSPgvDPLKVEIRLFERLFLSENPvELEDWLGDLNPR 740
Cdd:PTZ00402 432 YIKNIR-RSGEDALITDADIVLHLEGD-VKKTKFK--LTWVPE-SP--KAEVMELNEYDHLLTKKKP-DPEESIDDIIAP 503
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 573945447 741 SKEVIKGAYAVPSLATAALGDKFQFERLGYFAVDSDSTPEELV 783
Cdd:PTZ00402 504 VTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVDDVTPKKVLI 546
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
274-774 |
2.01e-90 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 294.22 E-value: 2.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 274 GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEPYKVTYTSDYFQE 353
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 354 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGlVPEGKA-TLRMKQDMQNDNKNMADL 432
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSG-KEEGGAwCLRAKIDMQSDNGTLRDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 433 IAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNNVMS 512
Cdd:PLN03233 169 VLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 513 KRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRsdnsliRVERLEY-----HIREELNKVASRTM 587
Cdd:PLN03233 249 KRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASR------RVVNLDWakfwaENKKEIDKRAKRFM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 588 VV--LHPLKVVITNLESGKiiDLDAKKWPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyGLAPGKT-VLLRYAFp 664
Cdd:PLN03233 323 AIdkADHTALTVTNADEEA--DFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTE--------DIQLGEDiVLLRWGV- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 665 IKCTEvIYGDntdniveIRAEYDPS---KATKPKgvLHWVAEPSpgvDPLKVEIRLFERLFLSENPVELEDWLGDLNPRS 741
Cdd:PLN03233 392 IEISK-IDGD-------LEGHFIPDgdfKAAKKK--ISWIADVS---DNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDT 458
|
490 500 510
....*....|....*....|....*....|....*.
gi 573945447 742 K---EVIKGAyavpSLATAALGDKFQFERLGYFAVD 774
Cdd:PLN03233 459 LaetDVIGDA----GLKTLKEHDIIQLERRGFYRVD 490
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
272-772 |
2.22e-85 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 278.99 E-value: 2.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 272 TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--W--EPYkvtYT 347
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 348 SDYFQELYELAVCLIKKGLAYVDHQTPEEIKEYREKQM--------NSPWRDRPIEEslklfedmRHGLVPEG-KATLRM 418
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 419 K--------QDM-----QNDNKNMADLIAYRikftphpHAGdkwfiYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYY 485
Cdd:COG0008 150 KipeegvvfDDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 486 WLLVALDQYQPyvwEYSRLNISNN----VMSKRKlnrlvtekwvdgwddpRLLTLAGLRRRGVSSTAINSFIRGMGITRS 561
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLILGpdgtKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 562 DNSLIR-VERLEYHIreELNKVaSRTMVVLHPLKVVITN------LESGKIIDLDAKKWPDApGDDASAYYKVPFSRT-- 632
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEA-GIREDLERLVPLVREra 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 633 ------------VYIEQSDfrVKDSKDYygLAPGKTvllryAFPIKCTEviygdntdNIVEIRAEYDPSKAtkpKGVLHW 700
Cdd:COG0008 355 ktlselaelarfFFIERED--EKAAKKR--LAPEEV-----RKVLKAAL--------EVLEAVETWDPETV---KGTIHW 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573945447 701 VAEpspgvdplKVEIRLfeRLFLseNPVELedwlgdlnprskeVIKGAYAVPSLAT--AALGDKFQFERLGYFA 772
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 ... |
274-775 |
3.56e-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: 281.33 E-value: 3.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 274 GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMGWEPYKVTYTSDYFQE 353
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 354 LYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATLRMKQDMQNDNKNMADLI 433
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 434 AYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSLCTLEF--DIRRPSYYWLLVALDQYQPYVWEYSRLNISNNVM 511
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 512 SKRKLNRLVTEKWVdGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSLiRVERLEYHIREELNKVASRTMVVLH 591
Cdd:TIGR00463 332 TSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALNRKIIDEEARRYFFIWN 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 592 PLKVVITNLESGKIIDLdaKKWPDAPgddASAYYKVPFSRTVYIEQSDFRVKDskdyyglapgKTVLLRYAFPIKCTEVI 671
Cdd:TIGR00463 410 PVKIEIVGLPEPKRVER--PLHPDHP---EIGERVLILRGEIYVPKDDLEEGV----------EPVRLMDAVNVIYSKKE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 672 YGDNTDNIVEIRaeydpskaTKPKGVLHWVAEPspgvDPLKVEIRLFERL----FLSENPVELEdwlgdlnprskevikg 747
Cdd:TIGR00463 475 LRYHSEGLEGAR--------KLGKSIIHWLPAK----DAVKVKVIMPDASivegVIEADASELE---------------- 526
|
490 500
....*....|....*....|....*...
gi 573945447 748 ayavpslataaLGDKFQFERLGYFAVDS 775
Cdd:TIGR00463 527 -----------VGDVVQFERFGFARLDS 543
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
274-784 |
1.11e-76 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 259.01 E-value: 1.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 274 GKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEK--KEYIDHIQEIVQWMGWEPYKVTYTSDYF 351
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 352 QELYELAVCLIKKGLAYVDHQTPEEIKEYREKQMNSPWRDRPIEESLKLFEDMRHGLVPEGKATLRMKQDMQNDNKNMAD 431
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 432 LIAYRIKFTPHPHAGDKWFIYPSYDYAHCLVDSLENITHSL--CTLEFDIRRPSYywLLVALDQYQPYVWEYSRLNISNN 509
Cdd:PRK04156 260 WVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLrgKDHIDNTEKQRY--IYDYFGWEYPETIHYGRLKIEGF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 510 VMSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRVERLEYHIREELNKVASRTMVV 589
Cdd:PRK04156 338 VLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANRYFFV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 590 LHPLKVVITNLESGKIidldakKWPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyglAPGKTVLLRYAFPIKCTE 669
Cdd:PRK04156 417 RDPVELEIEGAEPLEA------KIPLHPDRPERGEREIPVGGKVYVSSDDLE----------AEGKMVRLMDLFNVEITG 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 670 ViygdntdniVEIRAEY---DPSKATKPKG-VLHWVAEPspgvDPLKVEIRLFERlflsenpveledwlgdlnprskEVI 745
Cdd:PRK04156 481 V---------SVDKARYhsdDLEEARKNKApIIQWVPED----ESVPVRVLKPDG----------------------GDI 525
|
490 500 510
....*....|....*....|....*....|....*....
gi 573945447 746 KGaYAVPSLATAALGDKFQFERLGYFAVDSdSTPEELVF 784
Cdd:PRK04156 526 EG-LAEPDVADLEVDDIVQFERFGFVRIDS-VEDDEVVA 562
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
18-174 |
6.61e-66 |
|
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: 216.27 E-value: 6.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 18 ELVS-FLAIGLDQRTAENALANRKVTANLTAVITEAGVVSGCDKSVGNLLYTVATKYPANALVHRPVVIQYIVSSKIKSP 96
Cdd:pfam04558 2 ELIElFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 97 AQLDAALSFLSTLGPDSLDTAKFEETCGVGVVVSTEEIQSTVTDVLKENMEAIVEQRYHINVGSLCGQVRK--RHPWGDA 174
Cdd:pfam04558 82 LQVDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
583-774 |
2.52e-54 |
|
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: 185.17 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 583 ASRTMVVLHPLKVVITNLESGKIIDLDAkkwPDAPGDDASAYYKVPFSRTVYIEQSDFRvkdskdyyGLAPGKTVLLRYA 662
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEV---PNHPKNPELGTRKVPFSREIYIEREDFK--------RLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 663 FPIKCTEVIYGDNtDNIVEIRAEYDP---SKATKPKG-VLHWVAEPspgvDPLKVEIRLFERLFLSENPvelEDWLgdLN 738
Cdd:pfam03950 70 YNIKVTEVVKDED-GNVTELHCTYDGddlGGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 573945447 739 PRSKEVIKGAYAVPSLATAALGDKFQFERLGYFAVD 774
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
275-602 |
1.47e-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: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--WE--PYkvtYTSDY 350
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDegPY---RQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 351 FQELYELAVCLIKKGlayvdhqtpeeikeyrekqmnspwrdrpieeslklfedmrhglvpegkatlrmkqdmqndnknma 430
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 431 dliayrikftphphagdkwfIYPSYDYAHCLVDSLENITHSLCTLEFDIRRPSYYWLLVALDQYQPYVWEYSRLNISNN- 509
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGt 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 510 VMSKRKLNRlvtekwvdgwddprllTLAGLRRRGVSSTAINSFIRGMGITRSDNSlirverlEYHIREELNKVASRTMVV 589
Cdd:cd00418 153 KLSKRKLNT----------------TLRALRRRGYLPEALRNYLALIGWSKPDGH-------ELFTLEEMIAAFSVERVN 209
|
330
....*....|...
gi 573945447 590 LHPLKVVITNLES 602
Cdd:cd00418 210 SADATFDWAKLEW 222
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
275-585 |
4.96e-36 |
|
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: 136.33 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKK--EYIDHIQEIVQWMGWEPYKVTYTSDYFQ 352
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 353 ELYELAVCLIKKGLAYVdhqtpeeikeyrekqmnspwrdrpieeslklfedmrhglvpegkatlrmkqdmqndnknmadl 432
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 433 iayrikftpHPHAGDKWFIYPSYDYAHCLVDSLENITHSL--CTLEFDIRRPSYYWLLVALDQyqPYVWEYSRLNISNNV 510
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLrgKDHIDNTEKQRYIYEYFGWEY--PETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573945447 511 MSKRKLNRLVTEKWVDGWDDPRLLTLAGLRRRGVSSTAINSFIRGMGITRSDNSlIRVERLEYHIREELNKVASR 585
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
278-368 |
1.83e-11 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 65.64 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 278 TRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--WEPyKVTYTSDYFqELY 355
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DAY 85
|
90
....*....|....
gi 573945447 356 ELAV-CLIKKGLAY 368
Cdd:PRK05710 86 RAALdRLRAQGLVY 99
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
275-365 |
2.50e-11 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 64.53 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 275 KVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--WE--PYKVTYTSDY 350
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWDegPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 573945447 351 FQ----ELY-ELAVCLIKKG 365
Cdd:cd00808 81 RQserlEIYrKYAEKLLEKG 100
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
177-258 |
2.77e-07 |
|
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: 48.84 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 177 IKEEIDKRLTEILGPKTEADNIKPMKKKKEKPAKVEDKKTAAAAPAPPSEEELNPYS-----IFPQPEENLKVHTEIFFS 251
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKKKKAKKKKAAKKKKKKAPIEEEENKRSMFSegflgKFHKPGENPKTDGYVVTE 80
|
....*..
gi 573945447 252 DGNIWRA 258
Cdd:pfam04557 81 HTMRLLK 87
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
272-396 |
6.09e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 52.82 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573945447 272 TGGKVMTRFPPEPNGYLHIGHAKAMFIDFGLAKERNGHCYVRFDDTNPEAEKKEYIDHIQEIVQWMG--WE--------- 340
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegpdvggey 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573945447 341 -PYKVTYTSDYFQELYELavcLIKKGLAYVDHQTPEEIKEYRE--KQMNSP------WRDRPIEE 396
Cdd:PLN02627 122 gPYRQSERNAIYKQYAEK---LLESGHVYPCFCTDEELEAMKEeaELKKLPprytgkWATASDEE 183
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
277-337 |
2.22e-06 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 47.86 E-value: 2.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573945447 277 MTRFPPEPNGYLHIGHAKAMFIDFGLAKERN-----GHCYVRFDDTN-------------PEAEKKEYIDHIQEIVQWM 337
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYM 79
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
278-338 |
9.08e-06 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 45.22 E-value: 9.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 573945447 278 TRFPPEPnGYLHIGHAKAMfidfGLAKERNGHCYVRFDDTNPE------AEKKEYIDHIQEIVQWMG 338
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG 63
|
|
| |
