|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
51-714 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 51 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 121
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 122 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 201
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 202 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 280
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 281 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 360
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 361 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 440
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 441 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 520
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 521 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 598
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 599 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 678
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 194380518 679 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 714
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
109-699 |
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 194380518 109 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 188
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 189 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 267
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 268 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 347
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 348 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 427
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 428 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 507
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 508 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 587
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 588 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 666
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 194380518 667 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 699
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
106-702 |
2.03e-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: 2.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 184
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 263
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 264 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 342 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 422 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 501
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 502 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 581
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 582 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 659
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 194380518 660 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 702
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
114-460 |
7.20e-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: 7.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 114 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 192
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 193 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 272
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 273 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 350
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 351 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 430
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 194380518 431 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 460
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
605-699 |
2.25e-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: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 605 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 683
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 194380518 684 QIRAEISELPSIVQDL 699
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 ... |
58-112 |
5.34e-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: 5.34e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380518 58 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 112
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
51-714 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 928.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 51 EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD---------RAKMEDTLKRR 121
Cdd:PLN02734 6 RDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVNTLERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 122 FFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGEC 201
Cdd:PLN02734 86 LFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 202 FRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGG 280
Cdd:PLN02734 166 FRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 281 NMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVAD 360
Cdd:PLN02734 246 LSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 361 LHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESK 440
Cdd:PLN02734 326 LEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 441 TSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEM 520
Cdd:PLN02734 406 CSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 521 EMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFP 598
Cdd:PLN02734 486 KAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFP 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 599 AVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTvnktphTATLRD 678
Cdd:PLN02734 566 PLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTIRE 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 194380518 679 RDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 714
Cdd:PLN02734 640 RDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
109-699 |
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 194380518 109 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 188
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 189 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 267
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 268 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 347
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 348 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 427
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 428 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 507
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 508 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 587
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 588 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 666
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 194380518 667 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 699
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
106-702 |
2.03e-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: 2.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 184
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPITGN-DLS 263
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 264 PPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 342 EHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:COG0423 223 EFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 422 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGaigkaykkd 501
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 502 aklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVFEH 581
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 582 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGVAFG 659
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 194380518 660 VTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 702
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
106-699 |
2.17e-173 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 504.28 E-value: 2.17e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQ-ILEIDCTMLTPEPVLKTSGH 184
Cdd:PRK04173 5 EKIVSLAK------RRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREdVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcsVEKKSEmesvlaqldnygqqELADLFVNYNVKSPITGN-DLS 263
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA-------EGLSNE--------------ELKELIRENDIKCPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 264 PPVSFNLMFKTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:PRK04173 138 EVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 342 EHFVDPSEkDHPKFQnvadlhlylysakaqvsgqsarkmrlgdaveqgvinntvlgYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:PRK04173 218 EFFVKPGT-DNEWFA-----------------------------------------YWIELRKNWLLDLGIDPENLRFRE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 422 HMENEMAHYACDCWDAESKTSYG--WIEIVGCADRSCYDLSCHAratkvplvaekplkepktvnvvqfepskgaigKAYK 499
Cdd:PRK04173 256 HLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHS--------------------------------KHSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 500 KDaklvMEYlaicdecyitememllnekgeFTIETEGktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVF 579
Cdd:PRK04173 304 ED----LSY---------------------FDDETTG---------------------EKYIPYVIEPSAGLDRLLLAFL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 580 EHTFHVRE--GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGV 656
Cdd:PRK04173 338 EDAYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKD---FNVDyDDSGSIGKRYRRQDEIGT 414
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 194380518 657 AFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 699
Cdd:PRK04173 415 PFCITVDFDTLED--NTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
114-460 |
7.20e-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: 7.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 114 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 192
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 193 vkdvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMF 272
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 273 KTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEK 350
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 351 DHPKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 430
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 194380518 431 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 460
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
119-698 |
6.43e-66 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 227.58 E-value: 6.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 119 KRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILE-IDCTMLTPEPVLKTSGHVDKFADFMVkDVK 197
Cdd:PRK14894 14 KRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLV-DCR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 198 NGEC-FRADHLlkahlqklmsDKKCSvekksemesvlaqldNYGQQeladlfvnynvkspitgnDLSPPVSFNLMFKTFI 276
Cdd:PRK14894 93 DCKMrWRADHI----------QGVCP---------------NCGSR------------------DLTEPRPFNMMFRTQI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 277 GPGGNMP--GYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDhpk 354
Cdd:PRK14894 130 GPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDE--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 355 fqnvaDLHlylysakaqvsgQSARKMRLGdaveqgvinntvlgyfigriylYLTKVGISPDKLRFRQHMENEMAHYACDC 434
Cdd:PRK14894 207 -----EWH------------QRWLEARLA----------------------WWEQIGIPRSRITIYDVPPDELAHYSKRT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 435 WD-AESKTSYGWIEIVGCADRSCYDLSCHAR-ATKVPLVAEKPLKEPKTVNVVQFEPSKG--AIGKAYKKDAKLVMEYLA 510
Cdd:PRK14894 248 FDlMYDYPNIGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDSTARLTYFDQASGrhVVPYVIEPSAGVGRCMLA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 511 ICDECYITEM------EML--LNEKGEFTIETEGKTFQL---TKDMINVKRFQKTLYVEEVVPNV-----------IEPS 568
Cdd:PRK14894 328 VMCEGYAEELtkaipgEKLaaVGDALEAFLKSVGRSEKLageARDAILARGEALLQALPERLPEVeqllampgadqIELG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 569 FGL-GRIMYTVFEHTfhvregdeqRTFFSFPAVVAPFKCSVLPLSQNQE-FMPFVKELSEALTRHGVSHKVDDSSGSIGR 646
Cdd:PRK14894 408 KKLrGQAQPLIDEHY---------RTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRTVYDDTGAIGK 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 194380518 647 RYARTDEIGVAFGVTIDFDTVNKTPH-----TATLRDRDSMRQIRAEISELPSIVQD 698
Cdd:PRK14894 479 LYRRQDEIGTPFCITVDFDTIGQGKDpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
578-701 |
1.32e-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: 193.93 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 578 VFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVA 657
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 194380518 658 FGVTIDFDTVNktPHTATLRDRDSMRQIRAEISELPSIVQDLAN 701
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 ... |
54-104 |
2.14e-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: 2.14e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 194380518 54 LAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQP 104
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP 51
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
605-699 |
2.25e-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: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 605 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 683
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 194380518 684 QIRAEISELPSIVQDL 699
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
58-99 |
1.47e-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: 1.47e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194380518 58 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 99
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 ... |
58-112 |
5.34e-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: 5.34e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380518 58 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVL-EAKELALQPKDDIVDRA 112
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 ... |
233-349 |
5.98e-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: 66.26 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 233 LAQLDNYGQQELADLFVNY---NVKSPI-TGNDLS-----PPVSFNLMFkTFIGPGGNMPG---YLRPETAQGIFLNF-K 299
Cdd:cd00670 1 GTALWRALERFLDDRMAEYgyqEILFPFlAPTVLFfkgghLDGYRKEMY-TFEDKGRELRDtdlVLRPAACEPIYQIFsG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 194380518 300 RLLEFNqgKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 349
Cdd:cd00670 80 EILSYR--ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEE 127
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
57-99 |
8.38e-12 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 60.59 E-value: 8.38e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 194380518 57 LRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 99
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 ... |
226-356 |
2.20e-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: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 226 KSEMESVL-AQLDNYGQQEladlfvnynVKSPITGNDlSPPVSFNLMFKTFIGPGGNMPG--YLRPETAQGIFLNFKRLL 302
Cdd:cd00768 2 RSKIEQKLrRFMAELGFQE---------VETPIVERE-PLLEKAGHEPKDLLPVGAENEEdlYLRPTLEPGLVRLFVSHI 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 194380518 303 EfnqgKLPFAAAQIGNSFRNEISPRsGLIRVREFTMAEIEHFVDPSEKDHPKFQ 356
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 ... |
603-693 |
1.36e-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: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 603 PFKCSVLPLS-QNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTphTATLRDRDS 681
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|..
gi 194380518 682 MRQIRAEISELP 693
Cdd:cd00738 79 GESETLHVDELP 90
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
309-338 |
9.49e-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: 9.49e-06
10 20 30
....*....|....*....|....*....|
gi 194380518 309 LPFAAAQIGNSFRNEISPRSGLIRVREFTM 338
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
58-142 |
1.18e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 48.45 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380518 58 RLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE--LALQP----KDDIVDRAKmedtlkrRFFYDQAFAIY 131
Cdd:PLN02221 241 RLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAHIEerSKLKPglpkKDGKIDYSK-------DFFGRQAFLTV 313
|
90 100
....*....|....*....|.
gi 194380518 132 GG----------VSGLYDFGP 142
Cdd:PLN02221 314 SGqlqvetyacaLSSVYTFGP 334
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
61-100 |
1.70e-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: 1.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 194380518 61 VRQQGDLVRKLKEDKAPQVDVDKAVAELKARKrvLEAKEL 100
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 ... |
55-99 |
2.44e-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: 2.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 194380518 55 APLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKE 99
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
315-338 |
4.12e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 47.00 E-value: 4.12e-05
10 20
....*....|....*....|....
gi 194380518 315 QIGNSFRNEISPRSGLIRVREFTM 338
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 ... |
285-348 |
4.67e-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: 4.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380518 285 YLRPETAQGIFLNFkRLLEFNQGKLPFAAAQIGNSFRNEISPRS-GLIRVREFTMAEIEHFVDPS 348
Cdd:pfam00587 12 ALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG 75
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
598-662 |
4.33e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.31 E-value: 4.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380518 598 PAVVAPFKCSVLPLSQ-NQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTI 662
Cdd:PRK12325 340 PESVAPFKVGIINLKQgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIV 405
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
308-358 |
2.18e-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: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 194380518 308 KLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNV 358
Cdd:cd00772 117 DLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNM 167
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