|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
61-724 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 61 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 131
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 132 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 211
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 212 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 290
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 291 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 370
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 371 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 450
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 451 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 530
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 531 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 608
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 609 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 688
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 116805340 689 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 724
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
119-709 |
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: 652.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 119 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 198
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 199 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 277
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 278 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 357
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 358 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 437
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 438 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 517
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 518 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 597
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 598 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 676
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 116805340 677 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 709
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
116-712 |
2.83e-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: 520.05 E-value: 2.83e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 116 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 194
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 195 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 273
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 274 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 351
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 352 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 431
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 432 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 511
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 512 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 591
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 592 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 669
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 116805340 670 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 712
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
124-470 |
9.72e-128 |
|
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: 380.01 E-value: 9.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 124 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 202
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 203 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 282
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 283 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 360
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 361 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 440
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 116805340 441 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 470
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
615-709 |
1.94e-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: 89.18 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 615 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 693
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 116805340 694 QIRAEISELPSIVQDL 709
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 ... |
68-122 |
4.77e-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: 64.29 E-value: 4.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 116805340 68 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 122
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
61-724 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 61 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 131
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 132 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 211
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 212 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 290
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 291 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 370
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 371 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 450
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 451 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 530
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 531 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 608
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 609 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 688
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 116805340 689 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 724
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
119-709 |
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: 652.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 119 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 198
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 199 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 277
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 278 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 357
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 358 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 437
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 438 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 517
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 518 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 597
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 598 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 676
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 116805340 677 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 709
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
116-712 |
2.83e-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: 520.05 E-value: 2.83e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 116 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 194
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 195 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 273
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 274 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 351
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 352 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 431
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 432 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 511
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 512 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 591
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 592 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 669
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 116805340 670 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 712
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
116-709 |
2.96e-173 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 504.28 E-value: 2.96e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 116 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQ-ILEIDCTMLTPEPVLKTSGH 194
Cdd:PRK04173 5 EKIVSLAK------RRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREdVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 195 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcsVEKKSEmesvlaqldnygqqELADLFVNYNVKSPITGN-DLS 273
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA-------EGLSNE--------------ELKELIRENDIKCPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 274 PPVSFNLMFKTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 351
Cdd:PRK04173 138 EVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 352 EHFVDPSEkDHPKFQnvadlhlylysakaqvsgqsarkmrlgdaveqgvinntvlgYFIGRIYLYLTKVGISPDKLRFRQ 431
Cdd:PRK04173 218 EFFVKPGT-DNEWFA-----------------------------------------YWIELRKNWLLDLGIDPENLRFRE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 432 HMENEMAHYACDCWDAESKTSYG--WIEIVGCADRSCYDLSCHAratkvplvaekplkepktvnvvqfepskgaigKAYK 509
Cdd:PRK04173 256 HLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHS--------------------------------KHSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 510 KDaklvMEYlaicdecyitememllnekgeFTIETEGktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVF 589
Cdd:PRK04173 304 ED----LSY---------------------FDDETTG---------------------EKYIPYVIEPSAGLDRLLLAFL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 590 EHTFHVRE--GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGV 666
Cdd:PRK04173 338 EDAYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKD---FNVDyDDSGSIGKRYRRQDEIGT 414
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 116805340 667 AFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 709
Cdd:PRK04173 415 PFCITVDFDTLED--NTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
124-470 |
9.72e-128 |
|
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: 380.01 E-value: 9.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 124 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 202
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 203 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 282
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 283 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 360
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 361 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 440
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 116805340 441 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 470
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
129-708 |
7.61e-66 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 227.58 E-value: 7.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 129 KRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILE-IDCTMLTPEPVLKTSGHVDKFADFMVkDVK 207
Cdd:PRK14894 14 KRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLV-DCR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 208 NGEC-FRADHLlkahlqklmsDKKCSvekksemesvlaqldNYGQQeladlfvnynvkspitgnDLSPPVSFNLMFKTFI 286
Cdd:PRK14894 93 DCKMrWRADHI----------QGVCP---------------NCGSR------------------DLTEPRPFNMMFRTQI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 287 GPGGNMP--GYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDhpk 364
Cdd:PRK14894 130 GPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDE--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 365 fqnvaDLHlylysakaqvsgQSARKMRLGdaveqgvinntvlgyfigriylYLTKVGISPDKLRFRQHMENEMAHYACDC 444
Cdd:PRK14894 207 -----EWH------------QRWLEARLA----------------------WWEQIGIPRSRITIYDVPPDELAHYSKRT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 445 WD-AESKTSYGWIEIVGCADRSCYDLSCHAR-ATKVPLVAEKPLKEPKTVNVVQFEPSKG--AIGKAYKKDAKLVMEYLA 520
Cdd:PRK14894 248 FDlMYDYPNIGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDSTARLTYFDQASGrhVVPYVIEPSAGVGRCMLA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 521 ICDECYITEM------EML--LNEKGEFTIETEGKTFQL---TKDMINVKRFQKTLYVEEVVPNV-----------IEPS 578
Cdd:PRK14894 328 VMCEGYAEELtkaipgEKLaaVGDALEAFLKSVGRSEKLageARDAILARGEALLQALPERLPEVeqllampgadqIELG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 579 FGL-GRIMYTVFEHTfhvregdeqRTFFSFPAVVAPFKCSVLPLSQNQE-FMPFVKELSEALTRHGVSHKVDDSSGSIGR 656
Cdd:PRK14894 408 KKLrGQAQPLIDEHY---------RTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRTVYDDTGAIGK 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 116805340 657 RYARTDEIGVAFGVTIDFDTVNKTPH-----TATLRDRDSMRQIRAEISELPSIVQD 708
Cdd:PRK14894 479 LYRRQDEIGTPFCITVDFDTIGQGKDpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
588-711 |
1.82e-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: 193.54 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 588 VFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVA 667
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 116805340 668 FGVTIDFDTVNktPHTATLRDRDSMRQIRAEISELPSIVQDLAN 711
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 ... |
64-114 |
2.20e-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: 2.20e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 116805340 64 LAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQP 114
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP 51
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
615-709 |
1.94e-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: 89.18 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 615 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 693
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 116805340 694 QIRAEISELPSIVQDL 709
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
68-109 |
1.18e-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: 65.25 E-value: 1.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 116805340 68 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 109
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 ... |
68-122 |
4.77e-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: 64.29 E-value: 4.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 116805340 68 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 122
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| 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 ... |
243-359 |
6.31e-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: 65.88 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 243 LAQLDNYGQQELADLFVNY---NVKSPI-TGNDLS-----PPVSFNLMFkTFIGPGGNMPG---YLRPETAQGIFLNF-K 309
Cdd:cd00670 1 GTALWRALERFLDDRMAEYgyqEILFPFlAPTVLFfkgghLDGYRKEMY-TFEDKGRELRDtdlVLRPAACEPIYQIFsG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 116805340 310 RLLEFNqgKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 359
Cdd:cd00670 80 EILSYR--ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEE 127
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
67-109 |
7.48e-12 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 60.59 E-value: 7.48e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 116805340 67 LRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 109
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALT 43
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
236-366 |
2.39e-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: 60.98 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 236 KSEMESVL-AQLDNYGQQEladlfvnynVKSPITGNDlSPPVSFNLMFKTFIGPGGNMPG--YLRPETAQGIFLNFKRLL 312
Cdd:cd00768 2 RSKIEQKLrRFMAELGFQE---------VETPIVERE-PLLEKAGHEPKDLLPVGAENEEdlYLRPTLEPGLVRLFVSHI 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 116805340 313 EfnqgKLPFAAAQIGNSFRNEISPRsGLIRVREFTMAEIEHFVDPSEKDHPKFQ 366
Cdd:cd00768 72 R----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGEEASEFEE 120
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
613-703 |
1.38e-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: 55.48 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 613 PFKCSVLPLS-QNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTphTATLRDRDS 691
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|..
gi 116805340 692 MRQIRAEISELP 703
Cdd:cd00738 79 GESETLHVDELP 90
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
319-348 |
9.48e-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: 47.96 E-value: 9.48e-06
10 20 30
....*....|....*....|....*....|
gi 116805340 319 LPFAAAQIGNSFRNEISPRSGLIRVREFTM 348
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
68-152 |
1.20e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116805340 68 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE--LALQP----KDDIVDRAKmedtlkrRFFYDQAFAIY 141
Cdd:PLN02221 241 RLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAHIEerSKLKPglpkKDGKIDYSK-------DFFGRQAFLTV 313
|
90 100
....*....|....*....|.
gi 116805340 142 GG----------VSGLYDFGP 152
Cdd:PLN02221 314 SGqlqvetyacaLSSVYTFGP 334
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
71-110 |
1.62e-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: 42.61 E-value: 1.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 116805340 71 VRQQGDLVRKLKEDKAPQVDVDKAVAELKARKrvLEAKEL 110
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 ... |
65-109 |
2.16e-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: 42.07 E-value: 2.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 116805340 65 APLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 109
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
325-348 |
4.16e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 47.00 E-value: 4.16e-05
10 20
....*....|....*....|....
gi 116805340 325 QIGNSFRNEISPRSGLIRVREFTM 348
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 ... |
295-358 |
4.70e-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: 4.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116805340 295 YLRPETAQGIFLNFkRLLEFNQGKLPFAAAQIGNSFRNEISPRS-GLIRVREFTMAEIEHFVDPS 358
Cdd:pfam00587 12 ALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG 75
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
608-672 |
4.37e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.31 E-value: 4.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116805340 608 PAVVAPFKCSVLPLSQ-NQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTI 672
Cdd:PRK12325 340 PESVAPFKVGIINLKQgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIV 405
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
318-368 |
2.20e-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: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 116805340 318 KLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNV 368
Cdd:cd00772 117 DLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNM 167
|
|
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