|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
7-670 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 7 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 77
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 78 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 157
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 158 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 236
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 237 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 316
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 317 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 396
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 397 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 476
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 477 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 554
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 555 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 634
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 943350815 635 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 670
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
65-655 |
0e+00 |
|
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273051 [Multi-domain] Cd Length: 551 Bit Score: 647.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 65 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 144
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 145 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 223
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 224 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 303
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 304 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 383
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 384 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 463
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 464 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 543
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 544 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 622
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 943350815 623 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 655
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
62-658 |
7.40e-179 |
|
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; Glycyl-tRNA synthetase, class II is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440192 [Multi-domain] Cd Length: 461 Bit Score: 516.97 E-value: 7.40e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 62 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 140
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 141 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 219
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 220 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 297
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 298 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 377
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 378 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 457
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 458 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 537
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 538 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 615
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 943350815 616 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 658
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
70-416 |
1.57e-127 |
|
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues.
Pssm-ID: 238397 [Multi-domain] Cd Length: 254 Bit Score: 377.70 E-value: 1.57e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 70 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 148
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 149 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 228
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 229 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 306
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 307 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 386
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 943350815 387 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 416
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-655 |
4.04e-21 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 88.41 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 561 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 639
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 943350815 640 QIRAEISELPSIVQDL 655
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
14-68 |
5.06e-13 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 63.90 E-value: 5.06e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 943350815 14 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 68
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
7-670 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 7 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 77
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 78 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 157
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 158 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 236
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 237 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 316
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 317 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 396
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 397 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 476
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 477 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 554
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 555 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 634
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 943350815 635 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 670
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
65-655 |
0e+00 |
|
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273051 [Multi-domain] Cd Length: 551 Bit Score: 647.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 65 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 144
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 145 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 223
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 224 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 303
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 304 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 383
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 384 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 463
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 464 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 543
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 544 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 622
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 943350815 623 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 655
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
62-658 |
7.40e-179 |
|
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; Glycyl-tRNA synthetase, class II is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440192 [Multi-domain] Cd Length: 461 Bit Score: 516.97 E-value: 7.40e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 62 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 140
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 141 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 219
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 220 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 297
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 298 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 377
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 378 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 457
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 458 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 537
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 538 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 615
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 943350815 616 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 658
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
62-655 |
1.19e-172 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 500.81 E-value: 1.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 62 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQ-ILEIDCTMLTPEPVLKTSGH 140
Cdd:PRK04173 5 EKIVSLAK------RRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREdVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 141 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcsVEKKSEmesvlaqldnygqqELADLFVNYNVKSPITGN-DLS 219
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA-------EGLSNE--------------ELKELIRENDIKCPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 220 PPVSFNLMFKTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 297
Cdd:PRK04173 138 EVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 298 EHFVDPSEkDHPKFQnvadlhlylysakaqvsgqsarkmrlgdaveqgvinntvlgYFIGRIYLYLTKVGISPDKLRFRQ 377
Cdd:PRK04173 218 EFFVKPGT-DNEWFA-----------------------------------------YWIELRKNWLLDLGIDPENLRFRE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 378 HMENEMAHYACDCWDAESKTSYG--WIEIVGCADRSCYDLSCHAratkvplvaekplkepktvnvvqfepskgaigKAYK 455
Cdd:PRK04173 256 HLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHS--------------------------------KHSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 456 KDaklvMEYlaicdecyitememllnekgeFTIETEGktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVF 535
Cdd:PRK04173 304 ED----LSY---------------------FDDETTG---------------------EKYIPYVIEPSAGLDRLLLAFL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 536 EHTFHVRE--GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGV 612
Cdd:PRK04173 338 EDAYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKD---FNVDyDDSGSIGKRYRRQDEIGT 414
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 943350815 613 AFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 655
Cdd:PRK04173 415 PFCITVDFDTLED--NTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
70-416 |
1.57e-127 |
|
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues.
Pssm-ID: 238397 [Multi-domain] Cd Length: 254 Bit Score: 377.70 E-value: 1.57e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 70 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 148
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 149 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 228
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 229 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 306
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 307 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 386
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 943350815 387 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 416
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
75-654 |
2.94e-66 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 227.58 E-value: 2.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 75 KRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILE-IDCTMLTPEPVLKTSGHVDKFADFMVkDVK 153
Cdd:PRK14894 14 KRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLV-DCR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 154 NGEC-FRADHLlkahlqklmsDKKCSvekksemesvlaqldNYGQQeladlfvnynvkspitgnDLSPPVSFNLMFKTFI 232
Cdd:PRK14894 93 DCKMrWRADHI----------QGVCP---------------NCGSR------------------DLTEPRPFNMMFRTQI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 233 GPGGNMP--GYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDhpk 310
Cdd:PRK14894 130 GPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDE--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 311 fqnvaDLHlylysakaqvsgQSARKMRLGdaveqgvinntvlgyfigriylYLTKVGISPDKLRFRQHMENEMAHYACDC 390
Cdd:PRK14894 207 -----EWH------------QRWLEARLA----------------------WWEQIGIPRSRITIYDVPPDELAHYSKRT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 391 WD-AESKTSYGWIEIVGCADRSCYDLSCHAR-ATKVPLVAEKPLKEPKTVNVVQFEPSKG--AIGKAYKKDAKLVMEYLA 466
Cdd:PRK14894 248 FDlMYDYPNIGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDSTARLTYFDQASGrhVVPYVIEPSAGVGRCMLA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 467 ICDECYITEM------EML--LNEKGEFTIETEGKTFQL---TKDMINVKRFQKTLYVEEVVPNV-----------IEPS 524
Cdd:PRK14894 328 VMCEGYAEELtkaipgEKLaaVGDALEAFLKSVGRSEKLageARDAILARGEALLQALPERLPEVeqllampgadqIELG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 525 FGL-GRIMYTVFEHTfhvregdeqRTFFSFPAVVAPFKCSVLPLSQNQE-FMPFVKELSEALTRHGVSHKVDDSSGSIGR 602
Cdd:PRK14894 408 KKLrGQAQPLIDEHY---------RTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRTVYDDTGAIGK 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 943350815 603 RYARTDEIGVAFGVTIDFDTVNKTPH-----TATLRDRDSMRQIRAEISELPSIVQD 654
Cdd:PRK14894 479 LYRRQDEIGTPFCITVDFDTIGQGKDpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
534-657 |
1.39e-58 |
|
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238435 [Multi-domain] Cd Length: 121 Bit Score: 193.16 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 534 VFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVA 613
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 943350815 614 FGVTIDFDTVNktPHTATLRDRDSMRQIRAEISELPSIVQDLAN 657
Cdd:cd00858 80 FCVTVDFDTLE--DGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
10-60 |
1.77e-25 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 99.10 E-value: 1.77e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 943350815 10 LAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQP 60
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP 51
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-655 |
4.04e-21 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 88.41 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 561 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 639
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 943350815 640 QIRAEISELPSIVQDL 655
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
14-55 |
1.80e-13 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 64.87 E-value: 1.80e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 943350815 14 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 55
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
14-68 |
5.06e-13 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 63.90 E-value: 5.06e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 943350815 14 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 68
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
13-55 |
8.85e-12 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 60.20 E-value: 8.85e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 943350815 13 LRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 55
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALT 43
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
189-305 |
9.25e-12 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 65.49 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 189 LAQLDNYGQQELADLFVNY---NVKSPI-TGNDLS-----PPVSFNLMFkTFIGPGGNMPG---YLRPETAQGIFLNF-K 255
Cdd:cd00670 1 GTALWRALERFLDDRMAEYgyqEILFPFlAPTVLFfkgghLDGYRKEMY-TFEDKGRELRDtdlVLRPAACEPIYQIFsG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 943350815 256 RLLEFNqgKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 305
Cdd:cd00670 80 EILSYR--ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEE 127
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
182-305 |
3.32e-10 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 60.21 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 182 KSEMESVL-AQLDNYGQQEladlfvnynVKSPITGNDlSPPVSFNLMFKTFIGPGGNMPG--YLRPETAQGIFLNFKRLL 258
Cdd:cd00768 2 RSKIEQKLrRFMAELGFQE---------VETPIVERE-PLLEKAGHEPKDLLPVGAENEEdlYLRPTLEPGLVRLFVSHI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 943350815 259 EfnqgKLPFAAAQIGNSFRNEISPRsGLIRVREFTMAEIEHFVDPSE 305
Cdd:cd00768 72 R----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGE 113
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
559-649 |
1.62e-09 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 55.10 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 559 PFKCSVLPLS-QNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTphTATLRDRDS 637
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|..
gi 943350815 638 MRQIRAEISELP 649
Cdd:cd00738 79 GESETLHVDELP 90
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-294 |
9.70e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 47.57 E-value: 9.70e-06
10 20 30
....*....|....*....|....*....|
gi 943350815 265 LPFAAAQIGNSFRNEISPRSGLIRVREFTM 294
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
14-98 |
1.09e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943350815 14 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE--LALQP----KDDIVDRAKmedtlkrRFFYDQAFAIY 87
Cdd:PLN02221 241 RLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAHIEerSKLKPglpkKDGKIDYSK-------DFFGRQAFLTV 313
|
90 100
....*....|....*....|.
gi 943350815 88 GG----------VSGLYDFGP 98
Cdd:PLN02221 314 SGqlqvetyacaLSSVYTFGP 334
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
17-56 |
1.96e-05 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 42.22 E-value: 1.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 943350815 17 VRQQGDLVRKLKEDKAPQVDVDKAVAELKARKrvLEAKEL 56
Cdd:cd00936 5 IAAQGDLVRELKAKKAPKEEIDAAVKKLLALK--ADYKEA 42
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
11-55 |
2.77e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 41.69 E-value: 2.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 943350815 11 APLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 55
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
271-294 |
4.20e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 46.62 E-value: 4.20e-05
10 20
....*....|....*....|....
gi 943350815 271 QIGNSFRNEISPRSGLIRVREFTM 294
Cdd:PRK09194 134 QIQTKFRDEIRPRFGLMRGREFIM 157
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
241-304 |
4.95e-05 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 44.71 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 943350815 241 YLRPETAQGIFLNFkRLLEFNQGKLPFAAAQIGNSFRNEISPRS-GLIRVREFTMAEIEHFVDPS 304
Cdd:pfam00587 12 ALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG 75
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
554-618 |
4.36e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.31 E-value: 4.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 943350815 554 PAVVAPFKCSVLPLSQ-NQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTI 618
Cdd:PRK12325 340 PESVAPFKVGIINLKQgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIV 405
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
264-314 |
2.27e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 40.43 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 943350815 264 KLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNV 314
Cdd:cd00772 117 DLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNM 167
|
|
| |
