|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-619 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 674.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 1 MSQNEEQTIDAFMSLGLSKQKSIETLKNVTLTKNLNSILREVG-CFELSQGARTLLYHLGTKIKPQISHHLPLLVEYISS 79
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGvTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 80 NKLDSSIRVDKAIEF-ALSHIKEINIDELEKFCGVGVVVTPEEIEKAVEKQIVVNRGELLKNRYRFNTGPLMQKVRSELP 158
Cdd:PLN02859 81 SKIKTPAQLEAAFSFfSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 159 WADGKAIKSEVDLQVFDLLGPKIEADLVPvsksekksskPVRNEPKPKSFVQEKN-EIEDQGLTILDVMKKVNFHAPGEN 237
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEK----------PVKKKKEKPAKVEEKKvAVAAAPPSEEELNPYSIFPQPEEN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 238 YKtegyVVTEY------------THKLLKDHLKTTSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDT 305
Cdd:PLN02859 231 FK----VHTEVffsdgsvlrpsnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 306 NPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQLYQWAVQLIEKGLAYVCHQTADEMKGF--NPQPSPWRERPIEEN 383
Cdd:PLN02859 307 NPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 384 LQLFQDMKNGKIDEGAATLRMKITLEEGK---LDPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEF 460
Cdd:PLN02859 387 LKLFEDMRRGLIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 461 QSRRSSYYWLCNALNIYCPVQWEYGRLNINYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLG 540
Cdd:PLN02859 467 ETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 541 VTGAQ-STVDPSMLEAYVRDYLNNTAPRRMVVLEPLKISIENFPFAEPVSVDVPNYPNKPEL---GSHTVVFDRTIYIEK 616
Cdd:PLN02859 547 ITRSDnSLIRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDdpsAFYKVPFSRVVYIER 626
|
...
gi 1284995279 617 SDF 619
Cdd:PLN02859 627 SDF 629
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-621 |
3.24e-168 |
|
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: 490.20 E-value: 3.24e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEMK---GFNPQP---SPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITLEEGKL--- 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 414 DPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYC-PVQWEYGRLNINYT 492
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 493 VVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVVL 572
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1284995279 573 EPLKISIENFPfAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDFME 621
Cdd:TIGR00440 321 DPVEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFRE 368
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-567 |
7.11e-161 |
|
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: 460.18 E-value: 7.11e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQLY 343
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 344 QWAVQLIEKGLAYVchqtademkgfnpqpspwrerpieenlqlfqdmkngkidegaatlrmkitleegkldpvayrvrft 423
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 424 pHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWEYGRLNINYTVVSKRKIAKLI 503
Cdd:cd00807 96 -HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQLV 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284995279 504 EEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPR 567
Cdd:cd00807 175 DEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-562 |
3.54e-142 |
|
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: 415.56 E-value: 3.54e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEMKGFNPQ----PSPWRERPIEENLQLFQ-DMKNGKIDEGAATLRMKITLEE--GKLDP 415
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESpyVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 416 VAYRVRFTP---HHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPV-QWEYGRLNINY 491
Cdd:pfam00749 162 VRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLDG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1284995279 492 TVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQS-TVDPSMLEAYVRDYLN 562
Cdd:pfam00749 242 TKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
264-583 |
3.34e-83 |
|
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: 268.97 E-value: 3.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEM---------KGFNPQ-PSPWRERPIEEnlqlfqdmKNGKIDEG-AATLRMKITLEEG 411
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEE--------LERMLAAGePPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 412 KL----------------DPVAYRVrftphhrTGnkwciYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALN 475
Cdd:COG0008 157 VFddlvrgeitfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 476 IYCPvqwEYGRLNINY----TVVSKRKIAKlieekivndwddprlfTLTALRRRGFPPEAINNFCAQLGVT--GAQSTVD 549
Cdd:COG0008 225 WEPP---EFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSksDDQEIFS 285
|
330 340 350
....*....|....*....|....*....|....
gi 1284995279 550 PSMLEAYVRdyLNNTaPRRMVVLEPLKISIENFP 583
Cdd:COG0008 286 LEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGP 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
1-619 |
0e+00 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 674.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 1 MSQNEEQTIDAFMSLGLSKQKSIETLKNVTLTKNLNSILREVG-CFELSQGARTLLYHLGTKIKPQISHHLPLLVEYISS 79
Cdd:PLN02859 1 KDANSEKPLELFLKIGLDERTARNAIANNKVTSNLTAVIHEAGvTNGCDKTVGNLLYTVATKYPANALVHRPTLLSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 80 NKLDSSIRVDKAIEF-ALSHIKEINIDELEKFCGVGVVVTPEEIEKAVEKQIVVNRGELLKNRYRFNTGPLMQKVRSELP 158
Cdd:PLN02859 81 SKIKTPAQLEAAFSFfSSTGPESFDLNKFEEACGVGVVVSPEDIEAAVNEVFEENKEKILEQRYRTNVGDLLGQVRKRLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 159 WADGKAIKSEVDLQVFDLLGPKIEADLVPvsksekksskPVRNEPKPKSFVQEKN-EIEDQGLTILDVMKKVNFHAPGEN 237
Cdd:PLN02859 161 WADPKIVKKLIDKKLYELLGEKTAADNEK----------PVKKKKEKPAKVEEKKvAVAAAPPSEEELNPYSIFPQPEEN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 238 YKtegyVVTEY------------THKLLKDHLKTTSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDT 305
Cdd:PLN02859 231 FK----VHTEVffsdgsvlrpsnTKEILEKHLKATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 306 NPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQLYQWAVQLIEKGLAYVCHQTADEMKGF--NPQPSPWRERPIEEN 383
Cdd:PLN02859 307 NPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYreKKMNSPWRDRPIEES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 384 LQLFQDMKNGKIDEGAATLRMKITLEEGK---LDPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEF 460
Cdd:PLN02859 387 LKLFEDMRRGLIEEGKATLRMKQDMQNDNfnmYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 461 QSRRSSYYWLCNALNIYCPVQWEYGRLNINYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLG 540
Cdd:PLN02859 467 ETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 541 VTGAQ-STVDPSMLEAYVRDYLNNTAPRRMVVLEPLKISIENFPFAEPVSVDVPNYPNKPEL---GSHTVVFDRTIYIEK 616
Cdd:PLN02859 547 ITRSDnSLIRMDRLEHHIREELNKTAPRTMVVLHPLKVVITNLESGEVIELDAKRWPDAQNDdpsAFYKVPFSRVVYIER 626
|
...
gi 1284995279 617 SDF 619
Cdd:PLN02859 627 SDF 629
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
264-622 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 581.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTPF-KITHSSDYFDQL 342
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSgELRYASDYFDQL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEMK---------GfnpQPSPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITLEEGKL 413
Cdd:PRK05347 110 YEYAVELIKKGKAYVDDLSAEEIReyrgtltepG---KNSPYRDRSVEENLDLFERMRAGEFPEGSAVLRAKIDMASPNI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 414 ---DPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYC-PVQWEYGRLNI 489
Cdd:PRK05347 187 nmrDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHRPLYDWVLDNLPIPPhPRQYEFSRLNL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 490 NYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRM 569
Cdd:PRK05347 267 TYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKQDSVIDMSMLESCIREDLNENAPRAM 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1284995279 570 VVLEPLKISIENFPFAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDFMEV 622
Cdd:PRK05347 347 AVLDPLKLVITNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDFMEE 399
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
264-621 |
3.24e-168 |
|
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: 490.20 E-value: 3.24e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWeGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEMK---GFNPQP---SPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITLEEGKL--- 413
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIReyrGTLTDPgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPvmr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 414 DPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYC-PVQWEYGRLNINYT 492
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFPrPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 493 VVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVVL 572
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1284995279 573 EPLKISIENFPfAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDFME 621
Cdd:TIGR00440 321 DPVEVVIENLS-DEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFRE 368
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
264-567 |
7.11e-161 |
|
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: 460.18 E-value: 7.11e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQLY 343
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 344 QWAVQLIEKGLAYVchqtademkgfnpqpspwrerpieenlqlfqdmkngkidegaatlrmkitleegkldpvayrvrft 423
Cdd:cd00807 82 EYAEQLIKKGKAYV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 424 pHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWEYGRLNINYTVVSKRKIAKLI 503
Cdd:cd00807 96 -HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKRKLLQLV 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284995279 504 EEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPR 567
Cdd:cd00807 175 DEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
264-621 |
5.11e-158 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 472.67 E-value: 5.11e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYT-PFKITHSSDYFDQL 342
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFERM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEM---KGFNPQP---SPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITLEEGKL--- 413
Cdd:PRK14703 112 YAYAEQLIKMGLAYVDSVSEEEIrelRGTVTEPgtpSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSPNMklr 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 414 DPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYC--PVQWEYGRLNINY 491
Cdd:PRK14703 192 DPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWPprPRQYEFARLALGY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 492 TVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVV 571
Cdd:PRK14703 272 TVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAPRVMAV 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1284995279 572 LEPLKISIENFPFAEPVSVDVPNYPNK-PELGSHTVVFDRTIYIEKSDFME 621
Cdd:PRK14703 352 LDPLKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSE 402
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
249-619 |
9.28e-156 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 460.22 E-value: 9.28e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 249 THKLLKDHLKTTSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYT 328
Cdd:PTZ00437 37 TPELLEKHEAVTGGKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 329 PFKITHSSDYFDQLYQWAVQLIEKGLAYVCHQTADEMKGF--NPQPSPWRERPIEENLQLFQDMKNGKIDEGAATLRMKI 406
Cdd:PTZ00437 117 PDWVTFSSDYFDQLHEFAVQLIKDGKAYVDHSTPDELKQQreQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 407 TLEEGK---LDPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWE 483
Cdd:PTZ00437 197 DMKSDNpnmRDFIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 484 YGRLNINYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNN 563
Cdd:PTZ00437 277 FSRLNVTGSLLSKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1284995279 564 TAPRRMVVLEPLKISIENfpFAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDF 619
Cdd:PTZ00437 357 RCERRLMVIDPIKVVVDN--WKGEREFECPNHPRKPELGSRKVMFTDTFYVDRSDF 410
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
264-562 |
3.54e-142 |
|
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: 415.56 E-value: 3.54e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWdYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEMKGFNPQ----PSPWRERPIEENLQLFQ-DMKNGKIDEGAATLRMKITLEE--GKLDP 415
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEqealGSPSRDRYDEENLHLFEeEMKKGSAEGGPATVRAKIPMESpyVFRDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 416 VAYRVRFTP---HHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPV-QWEYGRLNINY 491
Cdd:pfam00749 162 VRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPfIHEYLRLNLDG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1284995279 492 TVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQS-TVDPSMLEAYVRDYLN 562
Cdd:pfam00749 242 TKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDvNRLSKSLEAFDRKKLD 313
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
262-621 |
9.15e-94 |
|
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: 299.43 E-value: 9.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 262 GLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQ 341
Cdd:TIGR00463 92 GEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 342 LYQWAVQLIEKGLAYVCHQTADEMKGF--NPQPSPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITLEEGK---LDPV 416
Cdd:TIGR00463 172 YYDYTRKLIEMGKAYVCDCRPEEFRELrnRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNpaiRDWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 417 AYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEF--QSRRSSYYWLCNALNIycPVQWEYGRLNIN-YTV 493
Cdd:TIGR00463 252 IFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidNRRKQEYIYRYFGWEP--PEFIHWGRLKIDdVRA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 494 VSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVVLE 573
Cdd:TIGR00463 330 LSTSSARKGILRGEYSGWDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWN 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1284995279 574 PLKISIENFPfaEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDFME 621
Cdd:TIGR00463 410 PVKIEIVGLP--EPKRVERPLHPDHPEIGERVLILRGEIYVPKDDLEE 455
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
255-577 |
6.77e-90 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 290.71 E-value: 6.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 255 DHLKTTS---GLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGyTPFK 331
Cdd:PTZ00402 41 DKLQLTNaeeGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLG-VSWD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 332 I--THSSDYFDQLYQWAVQLIEKGLAYVCHQTADEMKG--FNPQPSPWRERPIEENLQLFQDMKNGKiDEGAAT-LRMKI 406
Cdd:PTZ00402 120 VgpTYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKcrFDGVPTKYRDISVEETKRLWNEMKKGS-AEGQETcLRAKI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 407 TLE-EGKL--DPVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWE 483
Cdd:PTZ00402 199 SVDnENKAmrDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVED 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 484 YGRLNINYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNN 563
Cdd:PTZ00402 279 FSRLNMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDP 358
|
330
....*....|....
gi 1284995279 564 TAPRRMVVLEPLKI 577
Cdd:PTZ00402 359 SVPRYTVVSNTLKV 372
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
264-583 |
3.34e-83 |
|
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: 268.97 E-value: 3.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSDYFDQL 342
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWdEGPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 343 YQWAVQLIEKGLAYVCHQTADEM---------KGFNPQ-PSPWRERPIEEnlqlfqdmKNGKIDEG-AATLRMKITLEEG 411
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELealretqtaPGKPPRyDGRCRDLSPEE--------LERMLAAGePPVLRFKIPEEGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 412 KL----------------DPVAYRVrftphhrTGnkwciYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALN 475
Cdd:COG0008 157 VFddlvrgeitfpnpnlrDPVLYRA-------DG-----YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 476 IYCPvqwEYGRLNINY----TVVSKRKIAKlieekivndwddprlfTLTALRRRGFPPEAINNFCAQLGVT--GAQSTVD 549
Cdd:COG0008 225 WEPP---EFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSksDDQEIFS 285
|
330 340 350
....*....|....*....|....*....|....
gi 1284995279 550 PSMLEAYVRdyLNNTaPRRMVVLEPLKISIENFP 583
Cdd:COG0008 286 LEELIEAFD--LDRV-SRSPAVFDPVKLVWLNGP 316
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
251-619 |
1.28e-82 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 270.57 E-value: 1.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 251 KLLKDHLKTTSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPE--KEEEKFFIAIKDMVTWLGYT 328
Cdd:PRK04156 89 KGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 329 PFKITHSSDYFDQLYQWAVQLIEKGLAYVCHQTADEMKGF--NPQPSPWRERPIEENLQLFQDMKNGKIDEGAATLRMKI 406
Cdd:PRK04156 169 WDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELrdAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVKT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 407 TLEEGklDP-----VAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQS--RRSSYywlcnalnIYCP 479
Cdd:PRK04156 249 DLEHP--NPsvrdwVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--------IYDY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 480 VQWEY------GRLNINYTVVSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSML 553
Cdd:PRK04156 319 FGWEYpetihyGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENL 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284995279 554 EAYVRDYLNNTAPRRMVVLEPLKISIENfpfAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDF 619
Cdd:PRK04156 399 YAINRKLIDPIANRYFFVRDPVELEIEG---AEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDL 461
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
262-618 |
2.95e-77 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 260.04 E-value: 2.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 262 GLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAI-KDMVTwLGYTPFKITHSSDYFD 340
Cdd:PLN02907 212 GKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENIlKDIET-LGIKYDAVTYTSDYFP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 341 QLYQWAVQLIEKGLAYVCHQTADEMKG--FNPQPSPWRERPIEENLQLFQDMKNGKiDEGAA-TLRMKITLEE--GKL-D 414
Cdd:PLN02907 291 QLMEMAEKLIKEGKAYVDDTPREQMRKerMDGIESKCRNNSVEENLRLWKEMIAGS-ERGLQcCVRGKLDMQDpnKSLrD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 415 PVAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYcPVQ-WEYGRLNINYTV 493
Cdd:PLN02907 370 PVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLR-KVHiWEFSRLNFVYTL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 494 VSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVVLE 573
Cdd:PLN02907 449 LSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLK 528
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1284995279 574 PLKI--SIENFPfAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSD 618
Cdd:PLN02907 529 EGRVllTLTDGP-ETPFVRIIPRHKKYEGAGKKATTFTNRIWLDYAD 574
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
261-618 |
1.22e-74 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 248.39 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 261 SGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTPFKITHSSDYFD 340
Cdd:PLN03233 9 AGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFTSDYFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 341 QLYQWAVQLIEKGLAYVCHQTADEMKG--FNPQPSPWRERPIEENLQLFQDMKNGKIDEGAATLRMKITL--EEGKL-DP 415
Cdd:PLN03233 89 PIRCYAIILIEEGLAYMDDTPQEEMKKerADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMqsDNGTLrDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 416 VAYRVRFTPHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWEYGRLNINYTVVS 495
Cdd:PLN03233 169 VLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTVLS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 496 KRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPRRMVV--LE 573
Cdd:PLN03233 249 KRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIdkAD 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1284995279 574 PLKISIENFPFAEPVSVDVPNY-PNKPELGSHTVVFDRTIYIEKSD 618
Cdd:PLN03233 329 HTALTVTNADEEADFAFSETDChPKDPGFGKRAMRICDEVLLEKAD 374
|
|
| tRNA_synt_1c_R1 |
pfam04558 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1; This is a region found N ... |
6-162 |
6.21e-57 |
|
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: 189.31 E-value: 6.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 6 EQTIDAFMSLGLSKQKSIETLKNVTLTKNLNSILREVGCFE-LSQGARTLLYHLGTKIKPQISHHLPLLVEYISSNKLDS 84
Cdd:pfam04558 1 EELIELFKSIGLSEKKAKETLKNKKLSASLKAIINEAGVESgCDKKQGNLLYTLATKLKGNALPHRPYLVKYIVDGKLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 85 SIRVDKAIEFALSH-IKEINIDELEKFCGVGVVVTPEEIEKAVEKQIVVNRGELLKNRYRFNTGPLMQKVR--SELPWAD 161
Cdd:pfam04558 81 TLQVDAALKYLLKKaNEPIDVAEFEKACGVGVVVTPEQIEAAVEKYIEENKEEILEKRYRFNVGKLLGEVRklPELKWAD 160
|
.
gi 1284995279 162 G 162
Cdd:pfam04558 161 P 161
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
264-563 |
8.32e-48 |
|
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: 167.26 E-value: 8.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYT----PFKithSSDYF 339
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDwdegPYR---QSDRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 340 DQLYQWAVQLIEKGlayvchqtademkgfnpqpspwrerpieenlqlfqdmkngkidegaatlrmkitleegkldpvayr 419
Cdd:cd00418 79 DLYRAYAEELIKKG------------------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 420 vrftphhrtgnkwcIYPTYDYTHCLCDSIENITHSLCTKEFQSRRSSYYWLCNALNIYCPVQWEYGRLNINY-TVVSKRK 498
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDgTKLSKRK 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 499 IAKlieekivndwddprlfTLTALRRRGFPPEAINNFCAQLGVT-----------------------GAQSTVDPSMLEA 555
Cdd:cd00418 159 LNT----------------TLRALRRRGYLPEALRNYLALIGWSkpdghelftleemiaafsvervnSADATFDWAKLEW 222
|
....*...
gi 1284995279 556 YVRDYLNN 563
Cdd:cd00418 223 LNREYIRE 230
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
264-567 |
1.01e-43 |
|
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: 156.74 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPE--KEEEKFFIAIKDMVTWLGYTPFKITHSSDYFDQ 341
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRtkRPDPEAYDMIPEDLEWLGVKWDEVVIASDRIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 342 LYQWAVQLIEKGLAYVchqtademkgfnpqpspwrerpieenlqlfqdmkngkidegaatlrmkitleegkldpvayrvr 421
Cdd:cd09287 82 YYEYARKLIEMGGAYV---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 422 ftpHHRTGNKWCIYPTYDYTHCLCDSIENITHSLCTKEFQS--RRSSYywlcnalnIYCPVQWEY------GRLNINYTV 493
Cdd:cd09287 98 ---HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntEKQRY--------IYEYFGWEYpetihwGRLKIEGGK 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284995279 494 VSKRKIAKLIEEKIVNDWDDPRLFTLTALRRRGFPPEAINNFCAQLGVTGAQSTVDPSMLEAYVRDYLNNTAPR 567
Cdd:cd09287 167 LSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA_synt_1c_R2 |
pfam04557 |
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N ... |
165-254 |
5.41e-23 |
|
Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2; This is a region found N terminal to the catalytic domain of glutaminyl-tRNA synthetase (EC 6.1.1.18) in eukaryotes but not in Escherichia coli. This region is thought to bind RNA in a non-specific manner, enhancing interactions between the tRNA and enzyme, but is not essential for enzyme function.
Pssm-ID: 461352 [Multi-domain] Cd Length: 87 Bit Score: 93.14 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 165 IKSEVDLQVFDLLGPKIEADLVPVSKSEkksskPVRNEPKPKSFVQEKNEIEDQG--LTILDVMKKVNFHAPGENYKTEG 242
Cdd:pfam04557 1 IKNEVDEQILDLLGPKTEADLKKPPKKK-----KKAKKKKAAKKKKKKAPIEEEEnkRSMFSEGFLGKFHKPGENPKTDG 75
|
90
....*....|..
gi 1284995279 243 YVVTEYTHKLLK 254
Cdd:pfam04557 76 YVVTEHTMRLLK 87
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
565-619 |
2.08e-19 |
|
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: 85.79 E-value: 2.08e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1284995279 565 APRRMVVLEPLKISIENFPFAEPVSVDVPNYPNKPELGSHTVVFDRTIYIEKSDF 619
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDF 55
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
264-353 |
4.62e-11 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 63.37 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 264 VRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLG------------YTPFK 331
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGldwdegpdvggpYGPYR 81
|
90 100
....*....|....*....|..
gi 1284995279 332 ithSSDYFDQLYQWAVQLIEKG 353
Cdd:cd00808 82 ---QSERLEIYRKYAEKLLEKG 100
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
260-366 |
1.40e-08 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 57.83 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 260 TSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPE---KEEEKFFIAikDMvTWLG---------- 326
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLArstKESEEAVLR--DL-KWLGldwdegpdvg 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1284995279 327 --YTPFKITHSSDYFdqlYQWAVQLIEKGLAYVCHQTADE---MK 366
Cdd:PLN02627 119 geYGPYRQSERNAIY---KQYAEKLLESGHVYPCFCTDEEleaMK 160
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
259-372 |
3.65e-06 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 49.08 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 259 TTSGLVRTRFPPEPNGILHIGHAKAININFGYAAANNGVCFLRYDDTNPEKEEEKFFIAIKDMVTWLGYTP-FKITHSSD 337
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWdGPVLYQSQ 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1284995279 338 YFDqLYQWAV-QLIEKGLAYVCHQTADEMKGFNPQP 372
Cdd:PRK05710 81 RHD-AYRAALdRLRAQGLVYPCFCSRKEIAAAAPAP 115
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
266-342 |
7.33e-04 |
|
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: 40.16 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284995279 266 TRFPPEPNGILHIGHAKAININFGYAAANN-----GVCFLRYDDTNP------------EKEEEKFFIA-IKDMVTWLgy 327
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRklgykVRCIALIDDAGGligdpankkgenAKAFVERWIErIKEDVEYM-- 79
|
90
....*....|....*
gi 1284995279 328 tpfkITHSSDYFDQL 342
Cdd:cd00802 80 ----FLQAADFLLLY 90
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
266-315 |
3.03e-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: 3.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1284995279 266 TRFPPEPnGILHIGHAKAININFGYAaannGVCFLRYDDTNPEKEEEKFF 315
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGIA----DQCVVRIDDNPPVKVWQDPH 46
|
|
| |
