|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-753 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 1340.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 4 SKDFLRTIVEEDLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQ 83
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 84 WLGFNWGENVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQRTVEENLDLLERMKNGEFK 163
Cdd:PRK14703 92 WLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 164 DGEHVLRAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDT 243
Cdd:PRK14703 172 DGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 244 LELKLPRPYQHEFARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVA 323
Cdd:PRK14703 252 LGPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 324 QLEFCIRDDLNQKVPRVLCVMDPLKVTIENYEG--SEEIDAPYYPHDVPKDGSRKLPFSKDIYIERDDFMENPPKGYFRL 401
Cdd:PRK14703 332 VLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAgkVEELDLPYWPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 402 TPEQPVRLRHGYIIACKEVIKNLDGKIIEIKAEYYPESKSGSDTsGIKVNSAIQWVSAKEAKTVELRVYDRLFKNEAPEG 481
Cdd:PRK14703 412 TPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 482 -----LEDLNPDSLKIIKNaLVEPAVITDKIDERFQFERQGYFYADPIDYTNEKPVFNKIVGLKDSWAK-----KTKIVE 551
Cdd:PRK14703 491 adedfLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGArareaAREKRA 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 552 PEVKNTQKVQMQKVQVVGSMEPMNEDQKAAFEKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNSPITLANIVVNEVA 631
Cdd:PRK14703 570 AAPKKTAKPRRSKAEARAEAAALNPEQRARFDRYLSELGLNEEDARTLARDPALAAFFEAALAAGKSPVQLANWVVNDLA 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 632 RELKQMELSQVKFTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVKDKGLVQISDPSEISPIIDEIIAKNPD 711
Cdd:PRK14703 650 GLLRDRELAALPFTPAALARLVALVDAGRISTRIAKDVLAELAASGGDPEAIVEAKGLEQVSDAGALEPIVEEVLAAHPD 729
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1845965866 712 NVAKFKAGNTKLLGFFVGQVLKSTGGKANPQVVNELVALKLK 753
Cdd:PRK14703 730 KVAAYRAGKTKLLGFFVGQVMRETGGKANPQQVRELLQKKLG 771
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
24-543 |
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: 656.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 24 VITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSKI 103
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 104 YDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQRTVEENLDLLERMKNGEFKDGEHVLRAKIDMSAANMKMR 183
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 184 DPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKlPRPYQHEFARLGINY 263
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIF-PRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 264 TVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPRVLCV 343
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 344 MDPLKVTIENYEGSEEI-DAPYYPhDVPKDGSRKLPFSKDIYIERDDFMENPPKGYFRLTPEQPVRLRHGYIIACKEVIK 422
Cdd:TIGR00440 320 IDPVEVVIENLSDEYELaTIPNHP-NTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 423 NLDGKIIEIKAEYYPESKSGSDTSGIKVNSAIQWVSAKEAKTVELRVYDRLFKNE---APEG-LEDLNPDSLkIIKNALV 498
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPnpgAPDDfLSVINPESL-VIKQGFM 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1845965866 499 EPAVITDKIDERFQFERQGYFYADPIDYTNEKPVFNKIVGLKDSW 543
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
23-339 |
1.36e-136 |
|
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: 402.40 E-value: 1.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGeNVYFTSDYFSK 102
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 103 IYDYAVKLIKMNKAYVdslteeeireyrgtvtqagkrsiyaqrtveenldllermkngefkdgehvlrakidmsaanmkm 182
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 183 rdpllyrirhahHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELklPRPYQHEFARLGIN 262
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL--YRPHQWEFSRLNLT 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845965866 263 YTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPR 339
Cdd:cd00807 162 YTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
22-519 |
7.88e-126 |
|
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: 383.37 E-value: 7.88e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 22 KEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFS 101
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 102 KIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQ----RTVEEnldlLERMK-NGEfkdgEHVLRAKI--- 173
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGrcrdLSPEE----LERMLaAGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 174 -----DM-----SAANMKMRDPLLYRirhahhfRTGddwciYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDT 243
Cdd:COG0008 155 gvvfdDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 244 LELKLPrpyqhEFARLGINY----TVMSKRKlldlvnGEYvsgwddprmpTIAGYKRRGYTKESILNFCDQIGIAKANSM 319
Cdd:COG0008 223 LGWEPP-----EFAHLPLILgpdgTKLSKRK------GAV----------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 320 V--DVAQLEFCIrdDLNqKVPRVLCVMDPLKVTIENYEGSEEID--------APYYP-HDVPKDGSRKLPFSKD------ 382
Cdd:COG0008 282 EifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRALDdeelaellAPELPeAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 383 --------IYIERDDfmENPPKGyfRLTPEQpVRlrhGYIIACKEVIKNLDgkiieikaEYYPESksgsdtsgikVNSAI 454
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAPEE-VR---KVLKAALEVLEAVE--------TWDPET----------VKGTI 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845965866 455 QWVSAkeaktvELRVYDRLFKNEapegledlnpdsLKI-IKNALVEPAVI-TDKI--DERFqFERQGYF 519
Cdd:COG0008 413 HWVSA------EAGVKDGLLFMP------------LRVaLTGRTVEPSLFdVLELlgKERV-FERLGYA 462
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
23-334 |
2.73e-125 |
|
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: 376.27 E-value: 2.73e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSK 102
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 103 IYDYAVKLIKMNKAYVDSLTEEEIREYRGtvTQAGKRSIYAQRTVEENLDL-LERMKNGEFKDGEHVLRAKIDMSaANMK 181
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLfEEEMKKGSAEGGPATVRAKIPME-SPYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 182 MRDPLLYRIR---HAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKLPrPYQHEFAR 258
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPP-PFIHEYLR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845965866 259 LGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKA--NSMVdVAQLEFCIRDDLN 334
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfdVNRL-SKSLEAFDRKKLD 313
|
|
| GatB_Yqey |
smart00845 |
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about ... |
608-752 |
6.81e-56 |
|
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB which transamidates Glu-tRNA to Gln-tRNA. The function of this domain is uncertain. It does however suggest that Yqey and its relatives have a role in tRNA metabolism.
Pssm-ID: 197913 [Multi-domain] Cd Length: 147 Bit Score: 188.10 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 608 FYEEAQILVNSPITLANIVVNEVARELK--QMELSQVKFTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVK 685
Cdd:smart00845 1 YFEEVVKAGADPKLAANWLLGELLGELNkeGLEIEESPITPEHLAELLKLIDDGTISGKIAKEVLEELLEGGKSPEEIVE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845965866 686 DKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKLLGFFVGQVLKSTGGKANPQVVNELVALKL 752
Cdd:smart00845 81 EKGLKQISDEGELEAIVDEVIAENPDAVEDYRAGKKKALGFLVGQVMKATRGKADPKLVNELLKEKL 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-753 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 1340.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 4 SKDFLRTIVEEDLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQ 83
Cdd:PRK14703 12 SPNFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 84 WLGFNWGENVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQRTVEENLDLLERMKNGEFK 163
Cdd:PRK14703 92 WLGFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 164 DGEHVLRAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDT 243
Cdd:PRK14703 172 DGAHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 244 LELKLPRPYQHEFARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVA 323
Cdd:PRK14703 252 LGPWPPRPRQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 324 QLEFCIRDDLNQKVPRVLCVMDPLKVTIENYEG--SEEIDAPYYPHDVPKDGSRKLPFSKDIYIERDDFMENPPKGYFRL 401
Cdd:PRK14703 332 VLEFAIRDDLNRRAPRVMAVLDPLKVVIENLPAgkVEELDLPYWPHDVPKEGSRKVPFTRELYIERDDFSEDPPKGFKRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 402 TPEQPVRLRHGYIIACKEVIKNLDGKIIEIKAEYYPESKSGSDTsGIKVNSAIQWVSAKEAKTVELRVYDRLFKNEAPEG 481
Cdd:PRK14703 412 TPGREVRLRGAYIIRCDEVVRDADGAVTELRCTYDPESAKGEDT-GRKAAGVIHWVSAKHALPAEVRLYDRLFKVPQPEA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 482 -----LEDLNPDSLKIIKNaLVEPAVITDKIDERFQFERQGYFYADPIDYTNEKPVFNKIVGLKDSWAK-----KTKIVE 551
Cdd:PRK14703 491 adedfLEFLNPDSLRVAQG-RVEPAVRDDPADTRYQFERQGYFWADPVDSRPDALVFNRIITLKDTWGArareaAREKRA 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 552 PEVKNTQKVQMQKVQVVGSMEPMNEDQKAAFEKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNSPITLANIVVNEVA 631
Cdd:PRK14703 570 AAPKKTAKPRRSKAEARAEAAALNPEQRARFDRYLSELGLNEEDARTLARDPALAAFFEAALAAGKSPVQLANWVVNDLA 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 632 RELKQMELSQVKFTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVKDKGLVQISDPSEISPIIDEIIAKNPD 711
Cdd:PRK14703 650 GLLRDRELAALPFTPAALARLVALVDAGRISTRIAKDVLAELAASGGDPEAIVEAKGLEQVSDAGALEPIVEEVLAAHPD 729
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1845965866 712 NVAKFKAGNTKLLGFFVGQVLKSTGGKANPQVVNELVALKLK 753
Cdd:PRK14703 730 KVAAYRAGKTKLLGFFVGQVMRETGGKANPQQVRELLQKKLG 771
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
2-546 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 1025.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 2 SESKDFLRTIVEEDLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDA 81
Cdd:PRK05347 8 ARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 82 VQWLGFNWGENVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQRTVEENLDLLERMKNGE 161
Cdd:PRK05347 88 VRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLFERMRAGE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 162 FKDGEHVLRAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLL 241
Cdd:PRK05347 168 FPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 242 DTLELKlPRPYQHEFARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVD 321
Cdd:PRK05347 248 DNLPIP-PHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 322 VAQLEFCIRDDLNQKVPRVLCVMDPLKVTIENY-EG-SEEIDAPYYPHDvPKDGSRKLPFSKDIYIERDDFMENPPKGYF 399
Cdd:PRK05347 327 MSMLESCIREDLNENAPRAMAVLDPLKLVITNYpEGqVEELEAPNHPED-PEMGTREVPFSRELYIEREDFMEEPPKKYF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 400 RLTPEQPVRLRHGYIIACKEVIKNLDGKIIEIKAEYYPESKSGSDTSGIKVNSAIQWVSAKEAKTVELRVYDRLFKNEAP 479
Cdd:PRK05347 406 RLVPGKEVRLRNAYVIKCEEVVKDADGNITEIHCTYDPDTLSGNPADGRKVKGTIHWVSAAHAVPAEVRLYDRLFTVPNP 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845965866 480 EG----LEDLNPDSLkIIKNALVEPAVITDKIDERFQFERQGYFYADPiDYTNEKPVFNKIVGLKDSWAKK 546
Cdd:PRK05347 486 AAgkdfLDFLNPDSL-VIKQGFVEPSLADAKPEDRFQFEREGYFCADK-DSTPGKLVFNRTVGLRDSWAKI 554
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
24-543 |
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: 656.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 24 VITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSKI 103
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 104 YDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQRTVEENLDLLERMKNGEFKDGEHVLRAKIDMSAANMKMR 183
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 184 DPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKlPRPYQHEFARLGINY 263
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIF-PRPAQYEFSRLNLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 264 TVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPRVLCV 343
Cdd:TIGR00440 240 TVLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 344 MDPLKVTIENYEGSEEI-DAPYYPhDVPKDGSRKLPFSKDIYIERDDFMENPPKGYFRLTPEQPVRLRHGYIIACKEVIK 422
Cdd:TIGR00440 320 IDPVEVVIENLSDEYELaTIPNHP-NTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 423 NLDGKIIEIKAEYYPESKSGSDTSGIKVNSAIQWVSAKEAKTVELRVYDRLFKNE---APEG-LEDLNPDSLkIIKNALV 498
Cdd:TIGR00440 399 DAAGKITTIFCTYDNKTLGKEPADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPnpgAPDDfLSVINPESL-VIKQGFM 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1845965866 499 EPAVITDKIDERFQFERQGYFYADPIDYTNEKPVFNKIVGLKDSW 543
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLDSKESTTEKVVFNRTVSLKDAT 522
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
9-548 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 538.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 9 RTIVEEDLKAGKYKeVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGfn 88
Cdd:PLN02859 251 KEILEKHLKATGGK-VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 89 WGE-NVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRgtvtQAGKRSIYAQRTVEENLDLLERMKNGEFKDGEH 167
Cdd:PLN02859 328 WEPfKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 168 VLRAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELK 247
Cdd:PLN02859 404 TLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLY 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 248 LprPYQHEFARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKA-NSMVDVAQLE 326
Cdd:PLN02859 484 Q--PYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSdNSLIRMDRLE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 327 FCIRDDLNQKVPRVLCVMDPLKVTIENYEGSE--EIDAPYYPHDVPKDGSR--KLPFSKDIYIERDDFMENPPKGYFRLT 402
Cdd:PLN02859 562 HHIREELNKTAPRTMVVLHPLKVVITNLESGEviELDAKRWPDAQNDDPSAfyKVPFSRVVYIERSDFRLKDSKDYYGLA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 403 PEQPVRLRHGYIIACKEVI-KNLDGKIIEIKAEYYPESKsgsdtsgIKVNSAIQWVSA----KEAKTVELRVYDRLFKNE 477
Cdd:PLN02859 642 PGKSVLLRYAFPIKCTDVVlADDNETVVEIRAEYDPEKK-------TKPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSE 714
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845965866 478 AP----EGLEDLNPDSLKIIKNALVEPAVITDKIDERFQFERQGYFYADPiDYTNEKPVFNKIVGLKDSWAKKTK 548
Cdd:PLN02859 715 NPaeleDWLEDLNPQSKEVISGAYAVPSLKDAKVGDRFQFERLGYFAVDK-DSTPEKLVFNRTVTLKDSYGKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
27-552 |
2.04e-149 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 448.28 E-value: 2.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 27 RFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGF--NWgenVYFTSDYFSKIY 104
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 105 DYAVKLIKMNKAYVDSLTEEEIREYRgtvtQAGKRSIYAQRTVEENLDLLERMKNGEFKDGEHVLRAKIDMSAANMKMRD 184
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQR----EQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 185 PLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDtlELKLPRPYQHEFARLGINYT 264
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLE--ELNLWRPHVWEFSRLNVTGS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 265 VMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPRVLCVM 344
Cdd:PTZ00437 286 LLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 345 DPLKVTIENYEGSEEIDAPYYPHDvPKDGSRKLPFSKDIYIERDDF-MENPPKGYFRLTP-EQPVRLRHGYIIACKEVIK 422
Cdd:PTZ00437 366 DPIKVVVDNWKGEREFECPNHPRK-PELGSRKVMFTDTFYVDRSDFrTEDNNSKFYGLAPgPRVVGLKYSGNVVCKGFEV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 423 NLDGKIIEIKAEYYPESKSGSDTSgikvnsaIQWVSAKEAKTVELRVYDRLFKNEA----PEGLEDLNPDSlKIIKNALV 498
Cdd:PTZ00437 445 DAAGQPSVIHVDIDFERKDKPKTN-------ISWVSATACTPVEVRLYNALLKDDRaaidPEFLKFIDEDS-EVVSHGYA 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1845965866 499 EPAVITDKIDERFQFERQGYFYADPiDYTNEKPVFNKIVGLKDSwAKKTKIVEP 552
Cdd:PTZ00437 517 EKGIENAKHFESVQAERFGYFVVDP-DTRPDHLVMNRVLGLRED-KEKATVAEP 568
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
23-339 |
1.36e-136 |
|
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: 402.40 E-value: 1.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGeNVYFTSDYFSK 102
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 103 IYDYAVKLIKMNKAYVdslteeeireyrgtvtqagkrsiyaqrtveenldllermkngefkdgehvlrakidmsaanmkm 182
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 183 rdpllyrirhahHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELklPRPYQHEFARLGIN 262
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRL--YRPHQWEFSRLNLT 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845965866 263 YTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPR 339
Cdd:cd00807 162 YTVMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
22-519 |
7.88e-126 |
|
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: 383.37 E-value: 7.88e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 22 KEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFS 101
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 102 KIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSIYAQ----RTVEEnldlLERMK-NGEfkdgEHVLRAKI--- 173
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGrcrdLSPEE----LERMLaAGE----PPVLRFKIpee 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 174 -----DM-----SAANMKMRDPLLYRirhahhfRTGddwciYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDT 243
Cdd:COG0008 155 gvvfdDLvrgeiTFPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 244 LELKLPrpyqhEFARLGINY----TVMSKRKlldlvnGEYvsgwddprmpTIAGYKRRGYTKESILNFCDQIGIAKANSM 319
Cdd:COG0008 223 LGWEPP-----EFAHLPLILgpdgTKLSKRK------GAV----------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 320 V--DVAQLEFCIrdDLNqKVPRVLCVMDPLKVTIENYEGSEEID--------APYYP-HDVPKDGSRKLPFSKD------ 382
Cdd:COG0008 282 EifSLEELIEAF--DLD-RVSRSPAVFDPVKLVWLNGPYIRALDdeelaellAPELPeAGIREDLERLVPLVREraktls 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 383 --------IYIERDDfmENPPKGyfRLTPEQpVRlrhGYIIACKEVIKNLDgkiieikaEYYPESksgsdtsgikVNSAI 454
Cdd:COG0008 359 elaelarfFFIERED--EKAAKK--RLAPEE-VR---KVLKAALEVLEAVE--------TWDPET----------VKGTI 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845965866 455 QWVSAkeaktvELRVYDRLFKNEapegledlnpdsLKI-IKNALVEPAVI-TDKI--DERFqFERQGYF 519
Cdd:COG0008 413 HWVSA------EAGVKDGLLFMP------------LRVaLTGRTVEPSLFdVLELlgKERV-FERLGYA 462
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
23-334 |
2.73e-125 |
|
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: 376.27 E-value: 2.73e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSK 102
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 103 IYDYAVKLIKMNKAYVDSLTEEEIREYRGtvTQAGKRSIYAQRTVEENLDL-LERMKNGEFKDGEHVLRAKIDMSaANMK 181
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEERE--EQEALGSPSRDRYDEENLHLfEEEMKKGSAEGGPATVRAKIPME-SPYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 182 MRDPLLYRIR---HAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKLPrPYQHEFAR 258
Cdd:pfam00749 158 FRDPVRGRIKftpQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPP-PFIHEYLR 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845965866 259 LGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKA--NSMVdVAQLEFCIRDDLN 334
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfdVNRL-SKSLEAFDRKKLD 313
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
1-525 |
1.42e-97 |
|
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: 312.91 E-value: 1.42e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 1 MSESKDFLRTIVEEDLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKD 80
Cdd:TIGR00463 71 LDIKKKEKKRKGLRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 81 AVQWLGFNWGENVYfTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSiyaqRTVEENLDLLERMKNG 160
Cdd:TIGR00463 151 DLEWLGVKWDEVVY-QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRD----RSVEENLERWEEMLEG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 161 EFKDGEHVLRAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRD--IYD 238
Cdd:TIGR00463 226 KEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRkqEYI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 239 WLLDTLELklprPYQHEFARLGINY--TVMSKRKLLDLVNGEYvSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKA 316
Cdd:TIGR00463 306 YRYFGWEP----PEFIHWGRLKIDDvrALSTSSARKGILRGEY-SGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKIN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 317 NSMVDVAQLEFCIRDDLNQKVPRVLCVMDPLKVTIENYEGSEEIDAPYYPHDvPKDGSRKLPFSKDIYIERDDFMENppk 396
Cdd:TIGR00463 381 DVTMSWKNIYALNRKIIDEEARRYFFIWNPVKIEIVGLPEPKRVERPLHPDH-PEIGERVLILRGEIYVPKDDLEEG--- 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 397 gyfrltpEQPVRLrhgyiiackeviKNLDGKIIEIKAEYYpeskSGSDTSGIKVNSA--IQWVSAKEAKTVELrvydrlf 474
Cdd:TIGR00463 457 -------VEPVRL------------MDAVNVIYSKKELRY----HSEGLEGARKLGKsiIHWLPAKDAVKVKV------- 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1845965866 475 kneapegledLNPDSLkiIKNALVEPAVITDKIDERFQFERQGYFYADPID 525
Cdd:TIGR00463 507 ----------IMPDAS--IVEGVIEADASELEVGDVVQFERFGFARLDSAD 545
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
15-518 |
8.79e-86 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 282.13 E-value: 8.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 15 DLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPtkeDTKYV-----EALKDAVQWLGFNW 89
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDP---RTKRPdpeayDMILEDLKWLGVKW 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 90 GEnVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRgtvtQAGKRSIYAQRTVEENLDLLERMKNGEFKDGEHVL 169
Cdd:PRK04156 170 DE-VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR----DAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 170 RAKIDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENN----RDIYD---Wlld 242
Cdd:PRK04156 245 RVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNtekqRYIYDyfgW--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 243 tlelklPRPYQHEFARLGINYTVMSKRKLLDLV-NGEYvSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVD 321
Cdd:PRK04156 322 ------EYPETIHYGRLKIEGFVLSTSKIRKGIeEGEY-SGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATIS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 322 VAQLEFCIRDDLNQKVPRVLCVMDPLKVTIENYEgSEEIDAPYYPhDVPKDGSRKLPFSKDIYIERDDFmenPPKGyfrl 401
Cdd:PRK04156 395 WENLYAINRKLIDPIANRYFFVRDPVELEIEGAE-PLEAKIPLHP-DRPERGEREIPVGGKVYVSSDDL---EAEG---- 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 402 tpeQPVRLRHgyiIACKEVIknldgKIIEIKAEYYPESKSGSDTSGIKVnsaIQWVSAKEAKTVELRVydrlfkneaPEG 481
Cdd:PRK04156 466 ---KMVRLMD---LFNVEIT-----GVSVDKARYHSDDLEEARKNKAPI---IQWVPEDESVPVRVLK---------PDG 522
|
490 500 510
....*....|....*....|....*....|....*..
gi 1845965866 482 ledlnpdslkIIKNALVEPAVITDKIDERFQFERQGY 518
Cdd:PRK04156 523 ----------GDIEGLAEPDVADLEVDDIVQFERFGF 549
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
13-522 |
1.51e-84 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 283.15 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 13 EEDLKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNwGEN 92
Cdd:PLN02907 203 EVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIK-YDA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 93 VYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSiyaqRTVEENLDLLERMKNGEFKDGEHVLRAK 172
Cdd:PLN02907 282 VTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRN----NSVEENLRLWKEMIAGSERGLQCCVRGK 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 173 IDMSAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDtlELKLPRPY 252
Cdd:PLN02907 358 LDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILE--DMGLRKVH 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 253 QHEFARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEfcirdD 332
Cdd:PLN02907 436 IWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLW-----T 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 333 LNQKV-----PRVLCVMDPLKVTIENYEGSEEIDAPYYP-H-DVPKDGSRKLPFSKDIYIERDDfMENPPKGyfrltpEQ 405
Cdd:PLN02907 511 INKKIidpvcPRHTAVLKEGRVLLTLTDGPETPFVRIIPrHkKYEGAGKKATTFTNRIWLDYAD-AEAISEG------EE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 406 PVRLRHGYIIAcKEVIKNLDGKIIEIKAEYYPEsksGS-DTSGIKvnsaIQWVSA-KEAKTVELRVYDRLFKNEAPEGLE 483
Cdd:PLN02907 584 VTLMDWGNAII-KEITKDEGGAVTALSGELHLE---GSvKTTKLK----LTWLPDtNELVPLSLVEFDYLITKKKLEEDD 655
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1845965866 484 D----LNPDSlKIIKNALVEPAVITDKIDERFQFERQGYFYAD 522
Cdd:PLN02907 656 NfldvLNPCT-KKETAALGDSNMRNLKRGEIIQLERKGYYRCD 697
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
23-522 |
3.19e-81 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 271.07 E-value: 3.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSK 102
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 103 IYDYAVKLIKMNKAYVDSLTEEEIREYR--GTVTQagkrsiYAQRTVEENLDLLERMKNGEFKDGEHVLRAKIDMSAANM 180
Cdd:PTZ00402 132 MYEKAEELIKKGLAYCDKTPREEMQKCRfdGVPTK------YRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 181 KMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKlpRPYQHEFARLG 260
Cdd:PTZ00402 206 AMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIR--KPIVEDFSRLN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 261 INYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPRV 340
Cdd:PTZ00402 284 MEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 341 LCVMDPLKV--TIENYEGSEEIDAPYYPHDvPKDGSRKLPFSKDIYIERDDFmenppkgyfrltpeqpVRLRHGYIIACK 418
Cdd:PTZ00402 364 TVVSNTLKVrcTVEGQIHLEACEKLLHKKV-PDMGEKTYYKSDVIFLDAEDV----------------ALLKEGDEVTLM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 419 E----VIKNL-----DGKIIEIKAEYYPEsksgSDTSgiKVNSAIQWV-SAKEAKTVELRVYDRLFKNEAP---EGLEDL 485
Cdd:PTZ00402 427 DwgnaYIKNIrrsgeDALITDADIVLHLE----GDVK--KTKFKLTWVpESPKAEVMELNEYDHLLTKKKPdpeESIDDI 500
|
490 500 510
....*....|....*....|....*....|....*..
gi 1845965866 486 NPDSLKIIKNALVEPAVITDKIDERFQFERQGYFYAD 522
Cdd:PTZ00402 501 IAPVTKYTQEVYGEEALSVLKKGDIIQLERRGYYIVD 537
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
16-532 |
1.41e-77 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 259.17 E-value: 1.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 16 LKAGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNwGENVYF 95
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 96 TSDYFSKIYDYAVKLIKMNKAYVDSLTEEEIREYRGTVTQAGKRSiyaqRTVEENLDLLERMKNGEFKDGEHVLRAKIDM 175
Cdd:PLN03233 83 TSDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRN----QSPEEALEMFKEMCSGKEEGGAWCLRAKIDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 176 SAANMKMRDPLLYRIRHAHHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKlpRPYQHE 255
Cdd:PLN03233 159 QSDNGTLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLR--RPRIHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 256 FARLGINYTVMSKRKLLDLVNGEYVSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQ 335
Cdd:PLN03233 237 FARMNFMNTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 336 KVPRVLCV--MDPLKVTIENyeGSEEID-----APYYPHDvPKDGSRKLPFSKDIYIERDDfMENPPKGyfrltpEQPVR 408
Cdd:PLN03233 317 RAKRFMAIdkADHTALTVTN--ADEEADfafseTDCHPKD-PGFGKRAMRICDEVLLEKAD-TEDIQLG------EDIVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 409 LRHGyIIACKEVIKNLDGKII---EIKAeyypesksgsdtsgikVNSAIQWVSAKEAKT-VELRVYDRLF---KNEAPEG 481
Cdd:PLN03233 387 LRWG-VIEISKIDGDLEGHFIpdgDFKA----------------AKKKISWIADVSDNIpVVLSEFDNLIikeKLEEDDK 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1845965866 482 LED-LNPDSLKiIKNALVEPAVITDKIDERFQFERQGYFYADPIDYTNEKPV 532
Cdd:PLN03233 450 FEDfINPDTLA-ETDVIGDAGLKTLKEHDIIQLERRGFYRVDRPYMGEEKPL 500
|
|
| GatB |
COG0064 |
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and ... |
577-753 |
8.11e-67 |
|
Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439834 [Multi-domain] Cd Length: 477 Bit Score: 228.75 E-value: 8.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 577 DQKaaFEKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNSPITLANIVVNEVARELK--QMELSQVKFTPSQIAELVK 654
Cdd:COG0064 300 DAK--RERFVEEYGLSEYDARVLTSDKELADYFEAAVKAGADPKLAANWIMGELLRRLNerGLEIEESPVTPEQLAELIK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 655 MIDDETISSKIAKDVFEEMVKSGINPTQIVKDKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKLLGFFVGQVLKS 734
Cdd:COG0064 378 LIDDGTISGKIAKEVFEEMLETGGDPEEIVEEKGLKQVSDEGALEAIVDEVLAANPDAVEDYKAGKEKALGFLVGQVMKA 457
|
170
....*....|....*....
gi 1845965866 735 TGGKANPQVVNELVALKLK 753
Cdd:COG0064 458 TKGKANPKLVNELLKEKLG 476
|
|
| gatB |
PRK05477 |
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB; |
577-752 |
1.06e-65 |
|
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB;
Pssm-ID: 235489 [Multi-domain] Cd Length: 474 Bit Score: 225.72 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 577 DQKAafEKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNSPITLANIVVNEVARELK--QMELSQVKFTPSQIAELVK 654
Cdd:PRK05477 299 DAKR--ARFVEEYGLSEYDARVLTSDKELADYFEAVVAAGADAKLAANWLMGELLGLLNeeGIEIEESPITPEQLAELIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 655 MIDDETISSKIAKDVFEEMVKSGINPTQIVKDKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKLLGFFVGQVLKS 734
Cdd:PRK05477 377 LIDDGTISGKIAKEVFEEMLETGGDPDEIVEEKGLKQISDEGALEAIVDEVLAANPKAVEDYKAGKEKALGFLVGQVMKA 456
|
170
....*....|....*...
gi 1845965866 735 TGGKANPQVVNELVALKL 752
Cdd:PRK05477 457 TKGKANPKLVNELLKEKL 474
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
338-522 |
6.48e-64 |
|
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: 210.59 E-value: 6.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 338 PRVLCVMDPLKVTIENYEG--SEEIDAPYYPHDvPKDGSRKLPFSKDIYIERDDFmenppkgyFRLTPEQPVRLRHGYII 415
Cdd:pfam03950 2 PRYMAVLDPVKVVIENYPEgqEETAEVPNHPKN-PELGTRKVPFSREIYIEREDF--------KRLAPGEEVRLMDAYNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 416 ACKEVIKNLDGKIIEIKAEYYPESKSGSDTSGIKVnsaIQWVSAKEAKTVELRVYDRLFKNEAPEGLEdLNPDSLKIIKN 495
Cdd:pfam03950 73 KVTEVVKDEDGNVTELHCTYDGDDLGGARKVKGKI---IHWVSASDAVPAEVRLYDRLFKDEDDADFL-LNPDSLKVLTE 148
|
170 180
....*....|....*....|....*..
gi 1845965866 496 ALVEPAVITDKIDERFQFERQGYFYAD 522
Cdd:pfam03950 149 GLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
24-335 |
1.76e-61 |
|
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: 206.17 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 24 VITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSKI 103
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 104 YDYAVKLIKMNkayvdslteeeireyrgtvtqagkrsiyaqrtveenldllermkngefkdgehvlrakidmsaanmkmr 183
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 184 dpllyrirhahhfrtgddwcIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLElkLPRPYQHEFARLGINY 263
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALG--WEPPRFYHFPRLLLED 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 264 -TVMSKRKLldlvngeyvsgwddprMPTIAGYKRRGYTKESILNFCDQIGIAK-----------------------ANSM 319
Cdd:cd00418 151 gTKLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKpdghelftleemiaafsvervnsADAT 214
|
330
....*....|....*.
gi 1845965866 320 VDVAQLEFCIRDDLNQ 335
Cdd:cd00418 215 FDWAKLEWLNREYIRE 230
|
|
| GatB_Yqey |
smart00845 |
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about ... |
608-752 |
6.81e-56 |
|
GatB domain; This domain is found in GatB and proteins related to bacterial Yqey. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB which transamidates Glu-tRNA to Gln-tRNA. The function of this domain is uncertain. It does however suggest that Yqey and its relatives have a role in tRNA metabolism.
Pssm-ID: 197913 [Multi-domain] Cd Length: 147 Bit Score: 188.10 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 608 FYEEAQILVNSPITLANIVVNEVARELK--QMELSQVKFTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVK 685
Cdd:smart00845 1 YFEEVVKAGADPKLAANWLLGELLGELNkeGLEIEESPITPEHLAELLKLIDDGTISGKIAKEVLEELLEGGKSPEEIVE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845965866 686 DKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKLLGFFVGQVLKSTGGKANPQVVNELVALKL 752
Cdd:smart00845 81 EKGLKQISDEGELEAIVDEVIAENPDAVEDYRAGKKKALGFLVGQVMKATRGKADPKLVNELLKEKL 147
|
|
| GatB_Yqey |
pfam02637 |
GatB domain; This domain is found in GatB. It is about 140 amino acid residues long. This ... |
608-752 |
5.31e-52 |
|
GatB domain; This domain is found in GatB. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB, which transamidates Glu-tRNA to Gln-tRNA.
Pssm-ID: 396969 [Multi-domain] Cd Length: 148 Bit Score: 177.37 E-value: 5.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 608 FYEEAQILVNSPITLANIVVNEVARELKQ--MELSQVKFTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVK 685
Cdd:pfam02637 2 FFEEAVKAGADPKLAANWLLGELLGYLNKegLDIDESPLTPEHLAELIKLIDEGTISGKIAKEVLEELLENGKSPEEIVE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845965866 686 DKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKLLGFFVGQVLKSTGGKANPQVVNELVALKL 752
Cdd:pfam02637 82 EKGLKQISDEEELEKIVDEVIAENPKAVEDYKSGKEKALGFLVGQVMKKTRGKADPKLVNELLKEKL 148
|
|
| PLN02751 |
PLN02751 |
glutamyl-tRNA(Gln) amidotransferase |
567-753 |
3.98e-38 |
|
glutamyl-tRNA(Gln) amidotransferase
Pssm-ID: 215400 [Multi-domain] Cd Length: 544 Bit Score: 149.60 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 567 VVGSMEPMNEDQKAAFEKytntLGLNSEVANILARDEHLSHFYEEAqILVNSPITL-ANIVVNEVARELKQMELS--QVK 643
Cdd:PLN02751 358 IRASMPELPEAKRRRYEN----MGLSMQDVLFLANDKNVAEFFDAT-LAKGADAKLaANWIMGDIAAYLKNEKVSisEIK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 644 FTPSQIAELVKMIDDETISSKIAKDVFEEMVKSGINPTQIVKDKGLVQISDPSEISPIIDEIIAKNPDNVAKFKAGNTKL 723
Cdd:PLN02751 433 LTPKELAELIASIKDGTISGKIGKEILPELLAKGGTVKGLVEEKGLVQISDPAEIEAMVDKVLEENPKQLEQYRGGKTKL 512
|
170 180 190
....*....|....*....|....*....|
gi 1845965866 724 LGFFVGQVLKSTGGKANPQVVNELVALKLK 753
Cdd:PLN02751 513 QGFFAGQVMKASKGKANPGLLNKILMEKLN 542
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
23-339 |
3.78e-37 |
|
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: 139.41 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPT--KEDTKYVEALKDAVQWLGFNWGEnVYFTSDYF 100
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDE-VVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 101 SKIYDYAVKLIKMNKAYVdslteeeireyrgtvtqagkrsiyaqrtveenldllermkngefkdgehvlrakidmsaanm 180
Cdd:cd09287 80 ELYYEYARKLIEMGGAYV-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 181 kmrdpllyrirhahHFRTGDDWCIYPMYDFAHCLSDYIEGVSHSICTLEFENNRDIYDWLLDTLELKLPRPYQheFARLG 260
Cdd:cd09287 98 --------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIH--WGRLK 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 261 INYTVMSKRKLL-DLVNGEYvSGWDDPRMPTIAGYKRRGYTKESILNFCDQIGIAKANSMVDVAQLEFCIRDDLNQKVPR 339
Cdd:cd09287 162 IEGGKLSTSKIRkGIESGEY-EGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| PRK04028 |
PRK04028 |
Glu-tRNA(Gln) amidotransferase subunit GatE; |
583-753 |
5.57e-14 |
|
Glu-tRNA(Gln) amidotransferase subunit GatE;
Pssm-ID: 235205 [Multi-domain] Cd Length: 630 Bit Score: 75.62 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 583 EKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNsPITLANIVVN---EVARELKQMElsqvKFTPSQIAELVKMIDDe 659
Cdd:PRK04028 460 ERLIKEYGLSEELAEQLAYSERLDLFEELVKKGVD-PTLIASTLENtlkELRREGVDVE----NITDEHIEEVFKLVSE- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 660 tisSKIAKDVFEEMVK-----SGINPTQIVKDKGLVQISDpSEISPIIDEIIAKNPDNVAKFKAGNTKLLgffVGQVLKS 734
Cdd:PRK04028 534 ---GKIAKEAIEEILKelaenPGKSAEEAAEELGLKGLSE-EEVEKIIDEIVEENIDFVKEKGMGAFGPL---MGEVMAE 606
|
170
....*....|....*....
gi 1845965866 735 TGGKANPQVVNELVALKLK 753
Cdd:PRK04028 607 LRGKADGKLVSEILREKLK 625
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
23-112 |
5.93e-14 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 72.23 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 23 EVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENV--------Y 94
Cdd:cd00808 1 KVRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpY 80
|
90
....*....|....*....
gi 1845965866 95 FTSDYFSkIYD-YAVKLIK 112
Cdd:cd00808 81 RQSERLE-IYRkYAEKLLE 98
|
|
| GatE |
COG2511 |
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal ... |
583-753 |
2.56e-13 |
|
Archaeal Glu-tRNAGln amidotransferase subunit E, contains GAD domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442001 [Multi-domain] Cd Length: 630 Bit Score: 73.29 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 583 EKYTNTLGLNSEVANILARDEHLSHFYEEAQILVNSPITLANIVVNEVaRELKQMELSQVKFTPSQIAELVKMIDDETIS 662
Cdd:COG2511 461 ERLVKEYGLNEELAEQIVDSERLDLFEELVEKKGVDPTLIASTLTSTL-TELRREGVDVENLTDEHIEEVFDLVAEGKIA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 663 SKIAKDVFEEMVKS-GINPTQIVKDKGLVQISDpSEISPIIDEIIAKNPDNVAKFKAGNTKLLgffVGQVLKSTGGKANP 741
Cdd:COG2511 540 KEAIEEILEALAENpDLSAEEAVEELGLGGLSE-EEVEEIIDEVVEENADQVKEKGMGAFGPL---MGEVMKELRGKADG 615
|
170
....*....|..
gi 1845965866 742 QVVNELVALKLK 753
Cdd:COG2511 616 KLVSEILREKIQ 627
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
25-106 |
3.37e-09 |
|
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: 55.95 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 25 ITRFPPEPNGFPHIGHAKSICINFGIAKD-----YNGHCNLRMDDTNPTKedtkyvealKDAVQWLGFNWGENVYFTSDY 99
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgYKVRCIALIDDAGGLI---------GDPANKKGENAKAFVERWIER 71
|
....*..
gi 1845965866 100 FSKIYDY 106
Cdd:cd00802 72 IKEDVEY 78
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
25-131 |
1.30e-08 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 57.17 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 25 ITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGENVYFTSDYFSkIY 104
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AY 85
|
90 100
....*....|....*....|....*...
gi 1845965866 105 DYAV-KLIKMNKAYVDSLTEEEIREYRG 131
Cdd:PRK05710 86 RAALdRLRAQGLVYPCFCSRKEIAAAAP 113
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
18-126 |
7.86e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 52.44 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 18 AGKYKEVITRFPPEPNGFPHIGHAKSICINFGIAKDYNGHCNLRMDDTNPTKEDTKYVEALKDAVQWLGFNWGE------ 91
Cdd:PLN02627 40 ESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvgg 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 1845965866 92 --NVYFTSDYFSKIYDYAVKLIKMNKAYVDSLTEEEI 126
Cdd:PLN02627 120 eyGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEEL 156
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
26-117 |
5.45e-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: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845965866 26 TRFPPEPnGFPHIGHAKSICINFGIAkdynGHCNLRMDDTNPTK------EDTKYVEALKDAVQWLGFNWGENVYFTSDY 99
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNRELYRWV 76
|
90 100
....*....|....*....|..
gi 1845965866 100 --FSKIYDY--AVKLIKMNKAY 117
Cdd:cd02156 77 kdNITLPVDpeQVELPRLNLET 98
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
223-270 |
3.49e-03 |
|
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: 37.52 E-value: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1845965866 223 HSICTLEFENNRDIYDWLLDTLELKLpRPYQHEFARLGINYTVMSKRK 270
Cdd:cd02156 59 ISVCGEDFQQNRELYRWVKDNITLPV-DPEQVELPRLNLETTVMSKRK 105
|
|
| |
