|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-796 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1632.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 10 SSEKEKNLELFLKVGLDERTAKNTIANNKVTANLTAVIHEAAVADGCSRTVGNLLYTVATKHPANALVHRPKLAQYIVLS 89
Cdd:PLN02859 2 DANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 90 KIKTPAQLEAAFSFFATTGPENFDINKFEEACGVGVEVSEEEIKQTVNEVFEENKTAILEQRYRTNVGDLFAHVRKRHPW 169
Cdd:PLN02859 82 KIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 170 ADPKIVKQFIDAKLRELLGERTAADDEKVPKKKKEKPAKVEEKVVAVsTPEQPSEEVLNPYSIFPQPSDNYKVHTSVFFS 249
Cdd:PLN02859 162 ADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAV-AAAPPSEEELNPYSIFPQPEENFKVHTEVFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 250 DGSILRCSNTRELLEKHLSRTGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQ 329
Cdd:PLN02859 241 DGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 330 EIVKWMGWEPYKITYTSDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEE 409
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 410 GKATLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNAL 489
Cdd:PLN02859 401 GKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 490 GLYQPYVWEYSRLNVSNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMIHLSRL 569
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 570 EYHIREELNKTAPRTIAVLHPLKVVITNLEAGTIMDLEARKWPDAQADDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGL 649
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 650 APGKSALLRYAFPIKCTDVILADDKETVLEIRAEYDPTKKTKPKGVLHWVSEPSPGVDPLKVEIRLFDRLFLSENPAELE 729
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELE 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1632262149 730 DWLADLNPQSKVIIPNAYAVPSLGSAVVGDTFQFERLGYFVVDKDSTPEKLVFNRTVTLRDSYRKGG 796
Cdd:PLN02859 721 DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
274-792 |
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: 585.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 274 VLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEP-YKITYTSDYFQDL 352
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 353 YDLAVELIRRGHAYVDHQTADEIKEYR----EKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLRMKQDMQSDNYNMY 428
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLY-QPYVWEYSRLNVSNT 507
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 508 VMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDcSMIHLSRLEYHIREELNKTAPRTIAV 587
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQD-NNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 588 LHPLKVVITNLEAgtimDLEARKWPDAQADDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGLAPGKSALLRYAFPIKCTD 667
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 668 ViLADDKETVLEIRAEYD-------PTKKTKPKGVLHWVsepsPGVDPLKVEIRLFDRLFLSENPAELEDWLADLNPQSk 740
Cdd:TIGR00440 396 V-EKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPES- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1632262149 741 VIIPNAYAVPSLGSAVVGDTFQFERLGYFVVD-KDSTPEKLVFNRTVTLRDSY 792
Cdd:TIGR00440 470 LVIKQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
273-578 |
1.95e-151 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 444.84 E-value: 1.95e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEP-YKITYTSDYFQD 351
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 352 LYDLAVELIRRGHAYVDHQTADEIKEYREKKM--NSPWRDRPIAESLKLF-EDMRRGLIEEGKATLRMKQDMQSDnYNMY 428
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLY-QPYVWEYSRLNV 504
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632262149 505 SNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMIHLSRLEYHIREELN 578
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
273-583 |
1.03e-140 |
|
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: 414.34 E-value: 1.03e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEPYKITYTSDYFQDL 352
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 353 YDLAVELIRRGHAYVDHQTadeikeyrekkmnspwrdrpiaeslklfedmrrglieegkatlrmkqdmqsdnynmydlia 432
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 433 yrikftphphaGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVSNTVMSKR 512
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1632262149 513 KLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCsMIHLSRLEYHIREELNKTAPR 583
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
270-770 |
1.59e-81 |
|
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: 268.58 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 270 TGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--W--EPYkitYT 345
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 346 SDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYREKKM--------NSPWRDRPIAEslklfedmRRGLIEEG-KATLRM 416
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 417 K--------QDMQS-----DNYNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYY 483
Cdd:COG0008 150 KipeegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 484 WLLNALGLYQPyvwEYSRLNV----SNTVMSKRKlnrlvtqnwvdgwddpRLMTLAGLRRRGVTSTAINAFVRGIGITRS 559
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 560 DCSMIH-LSRLEYHIreELNKTaPRTIAVLHPLKVVITN------LEAGTIMDLEARKWPDAQADD----ASAFYK---- 624
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAGIREdlerLVPLVRerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 625 -----VPFSNTVYIDQSDfrLKDSKDYfgLAPGKSALLryafpIKCTdviladdkETVLEIRAEYDPtkkTKPKGVLHWV 699
Cdd:COG0008 356 tlselAELARFFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP---ETVKGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1632262149 700 SEpspgvdplKVEIRlfDRLFLsenpAELEdwladlnpqskVIIPNAYAVPSLGS--AVVGDTFQFERLGYFV 770
Cdd:COG0008 416 SA--------EAGVK--DGLLF----MPLR-----------VALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
10-796 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 1632.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 10 SSEKEKNLELFLKVGLDERTAKNTIANNKVTANLTAVIHEAAVADGCSRTVGNLLYTVATKHPANALVHRPKLAQYIVLS 89
Cdd:PLN02859 2 DANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGVTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 90 KIKTPAQLEAAFSFFATTGPENFDINKFEEACGVGVEVSEEEIKQTVNEVFEENKTAILEQRYRTNVGDLFAHVRKRHPW 169
Cdd:PLN02859 82 KIKTPAQLEAAFSFFSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLPW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 170 ADPKIVKQFIDAKLRELLGERTAADDEKVPKKKKEKPAKVEEKVVAVsTPEQPSEEVLNPYSIFPQPSDNYKVHTSVFFS 249
Cdd:PLN02859 162 ADPKIVKKLIDKKLYELLGEKTAADNEKPVKKKKEKPAKVEEKKVAV-AAAPPSEEELNPYSIFPQPEENFKVHTEVFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 250 DGSILRCSNTRELLEKHLSRTGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQ 329
Cdd:PLN02859 241 DGSVLRPSNTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 330 EIVKWMGWEPYKITYTSDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEE 409
Cdd:PLN02859 321 EIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEESLKLFEDMRRGLIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 410 GKATLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNAL 489
Cdd:PLN02859 401 GKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 490 GLYQPYVWEYSRLNVSNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMIHLSRL 569
Cdd:PLN02859 481 GLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNSLIRMDRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 570 EYHIREELNKTAPRTIAVLHPLKVVITNLEAGTIMDLEARKWPDAQADDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGL 649
Cdd:PLN02859 561 EHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 650 APGKSALLRYAFPIKCTDVILADDKETVLEIRAEYDPTKKTKPKGVLHWVSEPSPGVDPLKVEIRLFDRLFLSENPAELE 729
Cdd:PLN02859 641 APGKSVLLRYAFPIKCTDVVLADDNETVVEIRAEYDPEKKTKPKGVLHWVAEPSPGVEPLKVEVRLFDKLFLSENPAELE 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1632262149 730 DWLADLNPQSKVIIPNAYAVPSLGSAVVGDTFQFERLGYFVVDKDSTPEKLVFNRTVTLRDSYRKGG 796
Cdd:PLN02859 721 DWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKDSYGKGG 787
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
260-794 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 778.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 260 RELLEKHLsRTG--GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGW 337
Cdd:PRK05347 15 RQIIDEDL-ASGkhTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 338 EP-YKITYTSDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYR----EKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKA 412
Cdd:PRK05347 94 DWsGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRgtltEPGKNSPYRDRSVEENLDLFERMRAGEFPEGSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 413 TLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGL- 491
Cdd:PRK05347 174 VLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 492 YQPYVWEYSRLNVSNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDcSMIHLSRLEY 571
Cdd:PRK05347 254 PHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQD-SVIDMSMLES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 572 HIREELNKTAPRTIAVLHPLKVVITNLEAGTIMDLEARKWPDaqaDDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGLAP 651
Cdd:PRK05347 333 CIREDLNENAPRAMAVLDPLKLVITNYPEGQVEELEAPNHPE---DPEMGTREVPFSRELYIEREDFMEEPPKKYFRLVP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 652 GKSALLRYAFPIKCTDVIlADDKETVLEIRAEYDPTKKT-------KPKGVLHWVSEPspgvDPLKVEIRLFDRLFLSEN 724
Cdd:PRK05347 410 GKEVRLRNAYVIKCEEVV-KDADGNITEIHCTYDPDTLSgnpadgrKVKGTIHWVSAA----HAVPAEVRLYDRLFTVPN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 725 PAELEDWLADLNPQSKVIIpNAYAVPSLGSAVVGDTFQFERLGYFVVDKDSTPEKLVFNRTVTLRDSYRK 794
Cdd:PRK05347 485 PAAGKDFLDFLNPDSLVIK-QGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGLRDSWAK 553
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
256-797 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 621.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 256 CSNTRELLEKHLSRTGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWM 335
Cdd:PTZ00437 34 CRNTPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 336 GWEPYKITYTSDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLR 415
Cdd:PTZ00437 114 GWKPDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 416 MKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPY 495
Cdd:PTZ00437 194 VKADMKSDNPNMRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 496 VWEYSRLNVSNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSdCSMIHLSRLEYHIRE 575
Cdd:PTZ00437 274 VWEFSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRS-MNVIQISMLENTLRE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 576 ELNKTAPRTIAVLHPLKVVITNLEAGTIMDL--EARKwPDAQADdasafyKVPFSNTVYIDQSDFRLKDS-KDYFGLAPG 652
Cdd:PTZ00437 353 DLDERCERRLMVIDPIKVVVDNWKGEREFECpnHPRK-PELGSR------KVMFTDTFYVDRSDFRTEDNnSKFYGLAPG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 653 KSAL-LRYAFPIKCTDVILADDKETVLeIRAEYDPTKKTKPKGVLHWVSEpsPGVDPlkVEIRLFDRLFLSENPAELEDW 731
Cdd:PTZ00437 426 PRVVgLKYSGNVVCKGFEVDAAGQPSV-IHVDIDFERKDKPKTNISWVSA--TACTP--VEVRLYNALLKDDRAAIDPEF 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632262149 732 LADLNPQSKVIIpNAYAVPSLGSAVVGDTFQFERLGYFVVDKDSTPEKLVFNRTVTLRDSYRKGGI 797
Cdd:PTZ00437 501 LKFIDEDSEVVS-HGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKEKATV 565
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
260-796 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 599.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 260 RELLEKHLsRTG--GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGW 337
Cdd:PRK14703 17 TEIIEEDL-EAGryPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 338 E-PYKITYTSDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYR----EKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKA 412
Cdd:PRK14703 96 DwGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRgtvtEPGTPSPYRDRSVEENLDLFRRMRAGEFPDGAH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 413 TLRMKQDMQSDNYNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLY 492
Cdd:PRK14703 176 VLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 493 --QPYVWEYSRLNVSNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDcSMIHLSRLE 570
Cdd:PRK14703 256 ppRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTN-STVDIGVLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 571 YHIREELNKTAPRTIAVLHPLKVVITNLEAGTIMDLEARKWPDAQADDASAfyKVPFSNTVYIDQSDFRLKDSKDYFGLA 650
Cdd:PRK14703 335 FAIRDDLNRRAPRVMAVLDPLKVVIENLPAGKVEELDLPYWPHDVPKEGSR--KVPFTRELYIERDDFSEDPPKGFKRLT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 651 PGKSALLRYAFPIKCTDVIlADDKETVLEIRAEYDPTKKT------KPKGVLHWVSEPSpgvdPLKVEIRLFDRLFLSEN 724
Cdd:PRK14703 413 PGREVRLRGAYIIRCDEVV-RDADGAVTELRCTYDPESAKgedtgrKAAGVIHWVSAKH----ALPAEVRLYDRLFKVPQ 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632262149 725 P-AELEDWLADLNPQSKVIIPNaYAVPSLGSAVVGDTFQFERLGYFVVDK-DSTPEKLVFNRTVTLRDSYRKGG 796
Cdd:PRK14703 488 PeAADEDFLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITLKDTWGARA 560
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
274-792 |
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: 585.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 274 VLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEP-YKITYTSDYFQDL 352
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 353 YDLAVELIRRGHAYVDHQTADEIKEYR----EKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLRMKQDMQSDNYNMY 428
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRgtltDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLY-QPYVWEYSRLNVSNT 507
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 508 VMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDcSMIHLSRLEYHIREELNKTAPRTIAV 587
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQD-NNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 588 LHPLKVVITNLEAgtimDLEARKWPDAQADDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGLAPGKSALLRYAFPIKCTD 667
Cdd:TIGR00440 320 IDPVEVVIENLSD----EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAER 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 668 ViLADDKETVLEIRAEYD-------PTKKTKPKGVLHWVsepsPGVDPLKVEIRLFDRLFLSENPAELEDWLADLNPQSk 740
Cdd:TIGR00440 396 V-EKDAAGKITTIFCTYDnktlgkePADGRKVKGVIHWV----SASSKYPTETRLYDRLFKVPNPGAPDDFLSVINPES- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1632262149 741 VIIPNAYAVPSLGSAVVGDTFQFERLGYFVVD-KDSTPEKLVFNRTVTLRDSY 792
Cdd:TIGR00440 470 LVIKQGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKDAT 522
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
273-578 |
1.95e-151 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 444.84 E-value: 1.95e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEP-YKITYTSDYFQD 351
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 352 LYDLAVELIRRGHAYVDHQTADEIKEYREKKM--NSPWRDRPIAESLKLF-EDMRRGLIEEGKATLRMKQDMQSDnYNMY 428
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEalGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMESP-YVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 DLIAYRIKFTP---HPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLY-QPYVWEYSRLNV 504
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632262149 505 SNTVMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMIHLSRLEYHIREELN 578
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLD 313
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
273-583 |
1.03e-140 |
|
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: 414.34 E-value: 1.03e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEPYKITYTSDYFQDL 352
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 353 YDLAVELIRRGHAYVDHQTadeikeyrekkmnspwrdrpiaeslklfedmrrglieegkatlrmkqdmqsdnynmydlia 432
Cdd:cd00807 81 YEYAEQLIKKGKAYVHHRT------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 433 yrikftphphaGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVSNTVMSKR 512
Cdd:cd00807 100 -----------GDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1632262149 513 KLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCsMIHLSRLEYHIREELNKTAPR 583
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADS-TIDWDKLEACVRKDLNPTAPR 238
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
272-772 |
7.69e-100 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 325.14 E-value: 7.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 272 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEPYKITYTSDYFQD 351
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQ 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 352 LYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGlIEEGKA-TLRMKQDMQSDNYNMYDL 430
Cdd:PLN02907 292 LMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNNSVEENLRLWKEMIAG-SERGLQcCVRGKLDMQDPNKSLRDP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 431 IAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVSNTVMS 510
Cdd:PLN02907 371 VYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 511 KRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSdcsmihLSRLEYHIREELNK-----TAPRTI 585
Cdd:PLN02907 451 KRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKN------LNLMEWDKLWTINKkiidpVCPRHT 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 586 AVLHPLKVVITnLEAG-----TIMDLEARKWPDAqADDASAfykvpFSNTVYIDQSDFRLKDSKDYFGLAPGKSALLRya 660
Cdd:PLN02907 525 AVLKEGRVLLT-LTDGpetpfVRIIPRHKKYEGA-GKKATT-----FTNRIWLDYADAEAISEGEEVTLMDWGNAIIK-- 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 661 fpikctdVILADDKETVLEIRAEYDP---TKKTKPKgvLHWVSEPSPGVDPLKVEirlFDRLFLSENPAELEDWLADLNP 737
Cdd:PLN02907 596 -------EITKDEGGAVTALSGELHLegsVKTTKLK--LTWLPDTNELVPLSLVE---FDYLITKKKLEEDDNFLDVLNP 663
|
490 500 510
....*....|....*....|....*....|....*
gi 1632262149 738 QSKVIIPnAYAVPSLGSAVVGDTFQFERLGYFVVD 772
Cdd:PLN02907 664 CTKKETA-ALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
272-781 |
1.45e-96 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 313.05 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 272 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGwEPYKI--TYTSDYF 349
Cdd:PTZ00402 51 GKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWDVgpTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 350 QDLYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGlIEEGKAT-LRMKQDMQSDNYNMY 428
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKG-SAEGQETcLRAKISVDNENKAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 DLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVSNTV 508
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 509 MSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSdCSMIHLSRLEYHIREELNKTAPRTIAVL 588
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKT-VNFMEWSKLWYFNTQILDPSVPRYTVVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 589 HPLKVVIT-----NLEAGTimDLEARKWPDAqadDASAFYKvpfSNTVYIDQSDFRLKDSKDYFGLAPGKSALLRyafPI 663
Cdd:PTZ00402 368 NTLKVRCTvegqiHLEACE--KLLHKKVPDM---GEKTYYK---SDVIFLDAEDVALLKEGDEVTLMDWGNAYIK---NI 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 664 KCT-DVILADDKETVLEIRAEydpTKKTKPKgvLHWVSEpSPgvDPLKVEIRLFDRLFLSENPaELEDWLADLNPQSKVI 742
Cdd:PTZ00402 437 RRSgEDALITDADIVLHLEGD---VKKTKFK--LTWVPE-SP--KAEVMELNEYDHLLTKKKP-DPEESIDDIIAPVTKY 507
|
490 500 510
....*....|....*....|....*....|....*....
gi 1632262149 743 IPNAYAVPSLGSAVVGDTFQFERLGYFVVDKDsTPEKLV 781
Cdd:PTZ00402 508 TQEVYGEEALSVLKKGDIIQLERRGYYIVDDV-TPKKVL 545
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
272-779 |
2.39e-88 |
|
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: 289.80 E-value: 2.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 272 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEPYKITYTSDYFQD 351
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 352 LYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLRMKQDMQSDNYNMYDLI 431
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 432 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEF--ETRRASYYWLLNALGLYQPYVWEYSRLNVSNTVM 509
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 510 SKRKLNRLVTQNWVdGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMiHLSRLEYHIREELNKTAPRTIAVLH 589
Cdd:TIGR00463 332 TSSARKGILRGEYS-GWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTM-SWKNIYALNRKIIDEEARRYFFIWN 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 590 PLKVVITNLEAGTIMdlEARKWPDaqaDDASAFYKVPFSNTVYIDQSDFRLKDS----KDYFGLAPGKSALLRYAFPIKc 665
Cdd:TIGR00463 410 PVKIEIVGLPEPKRV--ERPLHPD---HPEIGERVLILRGEIYVPKDDLEEGVEpvrlMDAVNVIYSKKELRYHSEGLE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 666 tdviladdketvleiraeydpTKKTKPKGVLHWVsepsPGVDPLKVEIRLFDRL----FLSENPAELEdwladlnpqskv 741
Cdd:TIGR00463 484 ---------------------GARKLGKSIIHWL----PAKDAVKVKVIMPDASivegVIEADASELE------------ 526
|
490 500 510
....*....|....*....|....*....|....*...
gi 1632262149 742 iipnayavpslgsavVGDTFQFERLGYFVVDKDSTPEK 779
Cdd:TIGR00463 527 ---------------VGDVVQFERFGFARLDSADKDGM 549
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
272-773 |
6.65e-88 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 287.68 E-value: 6.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 272 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMGWEPYKITYTSDYFQD 351
Cdd:PLN03233 10 GQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 352 LYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLRMKQDMQSDNYNMYDLI 431
Cdd:PLN03233 90 IRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLRDPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 432 AYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVSNTVMSK 511
Cdd:PLN03233 170 LFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLSK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 512 RKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMiHLSRLEYHIREELNKTAPRTIAV--LH 589
Cdd:PLN03233 250 RKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNL-DWAKFWAENKKEIDKRAKRFMAIdkAD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 590 PLKVVITNLEAGTimdlearkwpDAQADDASAFYKVPFSNTVYIDQSDFRLKDSKDYFGLAPGKS-ALLRYAFpIKCTDV 668
Cdd:PLN03233 329 HTALTVTNADEEA----------DFAFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDiVLLRWGV-IEISKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 669 ilADDKETVLEIRAEYDPTKKTkpkgvLHWVSEPSpgvDPLKVEIRLFDRLFLSENPAELEDWLADLNPQSKV---IIPN 745
Cdd:PLN03233 398 --DGDLEGHFIPDGDFKAAKKK-----ISWIADVS---DNIPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAetdVIGD 467
|
490 500
....*....|....*....|....*...
gi 1632262149 746 AyavpSLGSAVVGDTFQFERLGYFVVDK 773
Cdd:PLN03233 468 A----GLKTLKEHDIIQLERRGFYRVDR 491
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
270-770 |
1.59e-81 |
|
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: 268.58 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 270 TGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--W--EPYkitYT 345
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGldWdeGPY---YQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 346 SDYFQDLYDLAVELIRRGHAYVDHQTADEIKEYREKKM--------NSPWRDRPIAEslklfedmRRGLIEEG-KATLRM 416
Cdd:COG0008 78 SDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTapgkppryDGRCRDLSPEE--------LERMLAAGePPVLRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 417 K--------QDMQS-----DNYNMYDLIAYRikftphpHAGdkwciYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYY 483
Cdd:COG0008 150 KipeegvvfDDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 484 WLLNALGLYQPyvwEYSRLNV----SNTVMSKRKlnrlvtqnwvdgwddpRLMTLAGLRRRGVTSTAINAFVRGIGITRS 559
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK----------------GAVTVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 560 DCSMIH-LSRLEYHIreELNKTaPRTIAVLHPLKVVITN------LEAGTIMDLEARKWPDAQADD----ASAFYK---- 624
Cdd:COG0008 279 DDQEIFsLEELIEAF--DLDRV-SRSPAVFDPVKLVWLNgpyiraLDDEELAELLAPELPEAGIREdlerLVPLVRerak 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 625 -----VPFSNTVYIDQSDfrLKDSKDYfgLAPGKSALLryafpIKCTdviladdkETVLEIRAEYDPtkkTKPKGVLHWV 699
Cdd:COG0008 356 tlselAELARFFFIERED--EKAAKKR--LAPEEVRKV-----LKAA--------LEVLEAVETWDP---ETVKGTIHWV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1632262149 700 SEpspgvdplKVEIRlfDRLFLsenpAELEdwladlnpqskVIIPNAYAVPSLGS--AVVGDTFQFERLGYFV 770
Cdd:COG0008 416 SA--------EAGVK--DGLLF----MPLR-----------VALTGRTVEPSLFDvlELLGKERVFERLGYAI 463
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
272-782 |
8.46e-80 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 267.10 E-value: 8.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 272 GKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEK--KEYIDHIQEIVKWMGWEPYKITYTSDYF 349
Cdd:PRK04156 100 GKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRpdPEAYDMILEDLKWLGVKWDEVVIQSDRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 350 QDLYDLAVELIRRGHAYVDHQTADEIKEYREKKMNSPWRDRPIAESLKLFEDMRRGLIEEGKATLRMKQDMQSDNYNMYD 429
Cdd:PRK04156 180 EIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKTDLEHPNPSVRD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 430 LIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFE--TRRASYywLLNALGLYQPYVWEYSRLNVSNT 507
Cdd:PRK04156 260 WVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYDYFGWEYPETIHYGRLKIEGF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 508 VMSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSmIHLSRLEYHIREELNKTAPRTIAV 587
Cdd:PRK04156 338 VLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDAT-ISWENLYAINRKLIDPIANRYFFV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 588 LHPLKVVITNLEAGTImdlEARKWPDaqaDDASAFYKVPFSNTVYIDQSD-------FRLKDskdyfglapgksallryA 660
Cdd:PRK04156 417 RDPVELEIEGAEPLEA---KIPLHPD---RPERGEREIPVGGKVYVSSDDleaegkmVRLMD-----------------L 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 661 FPIKctdvILADDKETVLEIRAEYDPTKKTKPKgVLHWVsepspgvdPLKVEIRLfdrlflsenpaeledwladlnpqsK 740
Cdd:PRK04156 474 FNVE----ITGVSVDKARYHSDDLEEARKNKAP-IIQWV--------PEDESVPV------------------------R 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1632262149 741 VIIPNA-----YAVPSLGSAVVGDTFQFERLGYFVVDKdSTPEKLVF 782
Cdd:PRK04156 517 VLKPDGgdiegLAEPDVADLEVDDIVQFERFGFVRIDS-VEDDEVVA 562
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
17-172 |
4.43e-71 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461353 Cd Length: 161 Bit Score: 230.14 E-value: 4.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 17 LELFLKVGLDERTAKNTIANNKVTANLTAVIHEAAVADGCSRTVGNLLYTVATKHPANALVHRPKLAQYIVLSKIKTPAQ 96
Cdd:pfam04558 4 IELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESGCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKTTLQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632262149 97 LEAAFSFFATTGPENFDINKFEEACGVGVEVSEEEIKQTVNEVFEENKTAILEQRYRTNVGDLFAHVRK--RHPWADP 172
Cdd:pfam04558 84 VDAALKYLLKKANEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRKlpELKWADP 161
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
581-772 |
1.23e-50 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 175.15 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 581 APRTIAVLHPLKVVITNLEAGTIMDLEARKWPDaqaDDASAFYKVPFSNTVYIDQSDFrlkdskdyFGLAPGKSALLRYA 660
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPK---NPELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 661 FPIKCTDVIlADDKETVLEIRAEYDPT---KKTKPKG-VLHWVSEPspgvDPLKVEIRLFDRLFLSENPaelEDWLadLN 736
Cdd:pfam03950 70 YNIKVTEVV-KDEDGNVTELHCTYDGDdlgGARKVKGkIIHWVSAS----DAVPAEVRLYDRLFKDEDD---ADFL--LN 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1632262149 737 PQSKVIIPNAYAVPSLGSAVVGDTFQFERLGYFVVD 772
Cdd:pfam03950 140 PDSLKVLTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
273-583 |
4.05e-42 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 153.66 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKK--EYIDHIQEIVKWMGWEPYKITYTSDYFQ 350
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPdpEAYDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 351 DLYDLAVELIRRGHAYVdhqtadeikeyrekkmnspwrdrpiaeslklfedmrrglieegkatlrmkqdmqsdnynmydl 430
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 431 iayrikftpHPHAGDKWCIYPSYDYAHCIVDSLEDITHSLCTLEFE--TRRASYywLLNALGLYQPYVWEYSRLNVSNTV 508
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIdnTEKQRY--IYEYFGWEYPETIHWGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1632262149 509 MSKRKLNRLVTQNWVDGWDDPRLMTLAGLRRRGVTSTAINAFVRGIGITRSDCSmIHLSRLEYHIREELNKTAPR 583
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDAT-ISWENLYAINRKLIDPRANR 240
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
273-585 |
7.07e-39 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 144.15 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--WE--PYkitYTSDY 348
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGldWDegPY---RQSDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 349 FQDLYDLAVELIRRGhayvdhqtadeikeyrekkmnspwrdrpiaeslklfedmrrglieegkatlrmkqdmqsdnynmy 428
Cdd:cd00418 78 FDLYRAYAEELIKKG----------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 429 dliayrikftphphagdkwcIYPSYDYAHCIVDSLEDITHSLCTLEFETRRASYYWLLNALGLYQPYVWEYSRLNVS-NT 507
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEdGT 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1632262149 508 VMSKRKLNrlvtqnwvdgwddprlMTLAGLRRRGVTSTAINAFVRGIGITRSDCSMI-HLSRLEYHIREELNKTAPRTI 585
Cdd:cd00418 153 KLSKRKLN----------------TTLRALRRRGYLPEALRNYLALIGWSKPDGHELfTLEEMIAAFSVERVNSADATF 215
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
273-363 |
2.66e-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: 67.23 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 273 KVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--WE--PYKITYTSDY 348
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldWDegPDVGGPYGPY 80
|
90 100
....*....|....*....|
gi 1632262149 349 FQ----DLYDLAVE-LIRRG 363
Cdd:cd00808 81 RQserlEIYRKYAEkLLEKG 100
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
276-366 |
5.85e-11 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 64.10 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 276 TRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--WEPyKITYTSDYFqDLY 353
Cdd:PRK05710 8 GRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGlhWDG-PVLYQSQRH-DAY 85
|
90
....*....|....
gi 1632262149 354 DLAVE-LIRRGHAY 366
Cdd:PRK05710 86 RAALDrLRAQGLVY 99
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
270-394 |
3.23e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 53.59 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 270 TGGKVLTRFPPEPNGYLHIGHAKAMFIDFGLAKERDGGCYLRFDDTNPEAEKKEYIDHIQEIVKWMG--WE--------- 338
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGldWDegpdvggey 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1632262149 339 -PYKITYTSDYFQdlyDLAVELIRRGHAYVDHQTADEI---KEYREKKMNSP-----WRDRPIAE 394
Cdd:PLN02627 122 gPYRQSERNAIYK---QYAEKLLESGHVYPCFCTDEELeamKEEAELKKLPPrytgkWATASDEE 183
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
276-353 |
8.55e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 49.02 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632262149 276 TRFPPEPNGYLHIGHAKAMFIDFGLAKE-RDGG----CYLRFDDTN-------------PEAEKKEYIDHIQEIVKWMGW 337
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAyRKLGykvrCIALIDDAGgligdpankkgenAKAFVERWIERIKEDVEYMFL 81
|
90
....*....|....*.
gi 1632262149 338 EPYKITYTSDYFQDLY 353
Cdd:cd00802 82 QAADFLLLYETECDIH 97
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
276-336 |
5.20e-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: 42.91 E-value: 5.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1632262149 276 TRFPPEPnGYLHIGHAKAMfidfGLAKERDGGCYLRFDDTNPE------AEKKEYIDHIQEIVKWMG 336
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLI----CRAKGIADQCVVRIDDNPPVkvwqdpHELEERKESIEEDISVCG 63
|
|
| |
