|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
46-714 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 946.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 46 SMDSAEELLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIVD---------RAKMED 116
Cdd:PLN02734 1 SEDSLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 117 TLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDV 196
Cdd:PLN02734 81 TLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 197 KNGECFRADHLLKAHLQKLMSDKK-CSAEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPTTGNDLSPPVPFNLMFQTF 275
Cdd:PLN02734 161 KTGTCFRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 276 IGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHPKF 355
Cdd:PLN02734 241 IGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 356 QSVADLCLYLYSAKAQVTGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCW 435
Cdd:PLN02734 321 SEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 436 DAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLEYLSACDEC 515
Cdd:PLN02734 401 DAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 516 YISEMELLLSEKGE--FTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVREGDEQRT 593
Cdd:PLN02734 481 EAMEMKAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 594 FFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTvnktphT 673
Cdd:PLN02734 561 VFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------S 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 93102417 674 ATLRDRDSMRQIRAEVSELPNVVRDLANGNITWADVEARYP 714
Cdd:PLN02734 635 VTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 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: 662.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 109 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 188
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 189 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsaekksemESVLAQLDNYGQQELADLFVNYNVKSPT-TGNDLSPPVP 267
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPNcGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 268 FNLMFQTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 347
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 348 TEKDHPKFQSVADLCLYLYSAKAQVTGqsarkmrLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 427
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 428 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLE 507
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 508 YLSACDecyisemelllseKGEFTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVRE 587
Cdd:TIGR00389 374 NLSEDD-------------LEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 588 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDsSGSIGRRYARTDEIGVAFGITIDFDT 666
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 93102417 667 VNKtpHTATLRDRDSMRQIRAEVSELPNVVRDL 699
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
106-702 |
4.43e-180 |
|
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: 521.59 E-value: 4.43e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 184
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSAEKKSEmesvlaqldnygqQELADLFVNYNVKSPTTGN-DLS 263
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 264 PPVPFNLMFQTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 342 EHFVDPtEKDHPKFQsvadlclylysakaqvtgqsarkmrlgdaveqgvinnsvlgYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:COG0423 223 EFFVDP-GTDNEWFA-----------------------------------------YWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 422 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPNKGavgkaykkd 501
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 502 aklvleylsacdecyisemelllsekgeftietegktfqltkdmvsvkrfqktlhvEEVVPSVIEPSFGLGRIMYTILEH 581
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 582 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNgvsHKVD-DSSGSIGRRYARTDEIGVAFG 659
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 93102417 660 ITIDFDTVNKtpHTATLRDRDSMRQIRAEVSELPNVVRDLANG 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 |
5.01e-129 |
|
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: 383.09 E-value: 5.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 114 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 192
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 193 vkdvkngecfradhllkahlqklmsdkkcsaekksemesvlaqldnygqqeladlfvnynvkspttgndlsppvpfnLMF 272
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 273 QTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPtEK 350
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 351 DHPKFQSVADLCLYLYSAKAQvtGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 430
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 93102417 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 |
9.57e-22 |
|
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: 89.95 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 605 KCSVLPLSQN-QEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKtpHTATLRDRDSMR 683
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 93102417 684 QIRAEVSELPNVVRDL 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 |
1.75e-11 |
|
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: 59.66 E-value: 1.75e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 93102417 58 RLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVL-EAKELALQPKDDIVDRA 112
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
46-714 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 946.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 46 SMDSAEELLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIVD---------RAKMED 116
Cdd:PLN02734 1 SEDSLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELQAAVGAGGdgaaskeafRQAVVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 117 TLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDV 196
Cdd:PLN02734 81 TLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 197 KNGECFRADHLLKAHLQKLMSDKK-CSAEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPTTGNDLSPPVPFNLMFQTF 275
Cdd:PLN02734 161 KTGTCFRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 276 IGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHPKF 355
Cdd:PLN02734 241 IGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 356 QSVADLCLYLYSAKAQVTGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCW 435
Cdd:PLN02734 321 SEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 436 DAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLEYLSACDEC 515
Cdd:PLN02734 401 DAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 516 YISEMELLLSEKGE--FTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVREGDEQRT 593
Cdd:PLN02734 481 EAMEMKAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 594 FFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTvnktphT 673
Cdd:PLN02734 561 VFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------S 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 93102417 674 ATLRDRDSMRQIRAEVSELPNVVRDLANGNITWADVEARYP 714
Cdd:PLN02734 635 VTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 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: 662.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 109 VDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 188
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 189 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsaekksemESVLAQLDNYGQQELADLFVNYNVKSPT-TGNDLSPPVP 267
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPNcGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 268 FNLMFQTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 347
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 348 TEKDHPKFQSVADLCLYLYSAKAQVTGqsarkmrLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 427
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 428 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLE 507
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 508 YLSACDecyisemelllseKGEFTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVRE 587
Cdd:TIGR00389 374 NLSEDD-------------LEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 588 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDsSGSIGRRYARTDEIGVAFGITIDFDT 666
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 93102417 667 VNKtpHTATLRDRDSMRQIRAEVSELPNVVRDL 699
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
106-702 |
4.43e-180 |
|
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: 521.59 E-value: 4.43e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQE-EQILEIDCTMLTPEPVLKTSGH 184
Cdd:COG0423 8 EKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSAEKKSEmesvlaqldnygqQELADLFVNYNVKSPTTGN-DLS 263
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPNCGGkELT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 264 PPVPFNLMFQTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 342 EHFVDPtEKDHPKFQsvadlclylysakaqvtgqsarkmrlgdaveqgvinnsvlgYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:COG0423 223 EFFVDP-GTDNEWFA-----------------------------------------YWLALRKKWLLSLGIDPENLRFRD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 422 HMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPNKGavgkaykkd 501
Cdd:COG0423 261 HLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG--------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 502 aklvleylsacdecyisemelllsekgeftietegktfqltkdmvsvkrfqktlhvEEVVPSVIEPSFGLGRIMYTILEH 581
Cdd:COG0423 318 --------------------------------------------------------EKYIPHVIEPSFGVDRLLLAFLEH 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 582 TFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNgvsHKVD-DSSGSIGRRYARTDEIGVAFG 659
Cdd:COG0423 342 AYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQDEIGTPFC 418
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 93102417 660 ITIDFDTVNKtpHTATLRDRDSMRQIRAEVSELPNVVRDLANG 702
Cdd:COG0423 419 VTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
106-699 |
1.34e-174 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 507.36 E-value: 1.34e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 106 DDIVDRAKmedtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQ-ILEIDCTMLTPEPVLKTSGH 184
Cdd:PRK04173 5 EKIVSLAK------RRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREdVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 185 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcsAEKKSEmesvlaqldnygqqELADLFVNYNVKSPTTGN-DLS 263
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA-------EGLSNE--------------ELKELIRENDIKCPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 264 PPVPFNLMFQTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 341
Cdd:PRK04173 138 EVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 342 EHFVDPtEKDHPKFQsvadlclylysakaqvtgqsarkmrlgdaveqgvinnsvlgYFIGRIYLYLTKVGISPDKLRFRQ 421
Cdd:PRK04173 218 EFFVKP-GTDNEWFA-----------------------------------------YWIELRKNWLLDLGIDPENLRFRE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 422 HMENEMAHYACDCWDAESKTSYG--WIEIVGCADRSCYDLSCHAratkvplvaekplkepktvnvvqfepnkgavgKAYK 499
Cdd:PRK04173 256 HLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHS--------------------------------KHSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 500 KDaklvLEYlsacdecyisemelllsekgeftietegktfqltkdmvsvkrFQKTLHVEEVVPSVIEPSFGLGRIMYTIL 579
Cdd:PRK04173 304 ED----LSY------------------------------------------FDDETTGEKYIPYVIEPSAGLDRLLLAFL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 580 EHTFHVRE--GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNgvsHKVD-DSSGSIGRRYARTDEIGV 656
Cdd:PRK04173 338 EDAYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKD---FNVDyDDSGSIGKRYRRQDEIGT 414
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 93102417 657 AFGITIDFDTVNKtpHTATLRDRDSMRQIRAEVSELPNVVRDL 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 |
5.01e-129 |
|
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: 383.09 E-value: 5.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 114 MEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfm 192
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 193 vkdvkngecfradhllkahlqklmsdkkcsaekksemesvlaqldnygqqeladlfvnynvkspttgndlsppvpfnLMF 272
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 273 QTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPtEK 350
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 351 DHPKFQSVADLCLYLYSAKAQvtGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHY 430
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHY 224
|
330 340 350
....*....|....*....|....*....|
gi 93102417 431 ACDCWDAESKTSYGWIEIVGCADRSCYDLS 460
Cdd:cd00774 225 ASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
119-698 |
2.93e-66 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 228.73 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 119 KRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILE-IDCTMLTPEPVLKTSGHVDKFADFMVkDVK 197
Cdd:PRK14894 14 KRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLV-DCR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 198 NGEC-FRADHLlkahlqklmsDKKCsaekksemesvlaqldnygqqeladlfvnynvksPTTGN-DLSPPVPFNLMFQTF 275
Cdd:PRK14894 93 DCKMrWRADHI----------QGVC----------------------------------PNCGSrDLTEPRPFNMMFRTQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 276 IGPGGNMP--GYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHP 353
Cdd:PRK14894 129 IGPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDEEW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 354 KfqsvadlclylysakaqvtgQSARKMRLGdaveqgvinnsvlgyfigriylYLTKVGISPDKLRFRQHMENEMAHYACD 433
Cdd:PRK14894 209 H--------------------QRWLEARLA----------------------WWEQIGIPRSRITIYDVPPDELAHYSKR 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 434 CWD-AESKTSYGWIEIVGCADRSCYDLSCHAR-ATKVPLVAEKPLKEPKTVNVVQFEPNKG--AVGKAYKKDAKLVLEYL 509
Cdd:PRK14894 247 TFDlMYDYPNIGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDSTARLTYFDQASGrhVVPYVIEPSAGVGRCML 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 510 SACDECYISEM------ELL--LSEKGEFTIETEGKTFQL---TKDMVSVKRFQKTLHVEEVVPSV-----------IEP 567
Cdd:PRK14894 327 AVMCEGYAEELtkaipgEKLaaVGDALEAFLKSVGRSEKLageARDAILARGEALLQALPERLPEVeqllampgadqIEL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 568 SFGL-GRIMYTILEHTfhvregdeqRTFFSFPAVVAPFKCSVLPLSQNQE-FMPFVKELSEALTRNGVSHKVDDSSGSIG 645
Cdd:PRK14894 407 GKKLrGQAQPLIDEHY---------RTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRTVYDDTGAIG 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 93102417 646 RRYARTDEIGVAFGITIDFDTVNKTPH-----TATLRDRDSMRQIRAEVSELPNVVRD 698
Cdd:PRK14894 478 KLYRRQDEIGTPFCITVDFDTIGQGKDpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
578-701 |
1.86e-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: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 578 ILEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDsSGSIGRRYARTDEIGVA 657
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 93102417 658 FGITIDFDTVNktPHTATLRDRDSMRQIRAEVSELPNVVRDLAN 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 |
2.86e-24 |
|
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: 96.02 E-value: 2.86e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 93102417 54 LAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQP 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 |
9.57e-22 |
|
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: 89.95 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 605 KCSVLPLSQN-QEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKtpHTATLRDRDSMR 683
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 93102417 684 QIRAEVSELPNVVRDL 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 |
3.01e-12 |
|
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: 61.40 E-value: 3.01e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 93102417 58 RLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKE 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 |
1.75e-11 |
|
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: 59.66 E-value: 1.75e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 93102417 58 RLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVL-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 ... |
263-349 |
3.02e-11 |
|
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: 63.95 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 263 SPPVPFNLMFqTFIGPGGNMPG---YLRPETAQGIFLNF-KRLLEFNqgKLPFAAAQIGNSFRNEISPRSGLIRVREFTM 338
Cdd:cd00670 40 HLDGYRKEMY-TFEDKGRELRDtdlVLRPAACEPIYQIFsGEILSYR--ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQ 116
|
90
....*....|.
gi 93102417 339 AEIEHFVDPTE 349
Cdd:cd00670 117 VEYVVFGEPEE 127
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
603-693 |
1.75e-10 |
|
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: 58.18 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 603 PFKCSVLPLS-QNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKTphTATLRDRDS 681
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|..
gi 93102417 682 MRQIRAEVSELP 693
Cdd:cd00738 79 GESETLHVDELP 90
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
285-358 |
4.13e-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: 4.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102417 285 YLRPETAQGIFLNFKRLLEfnqgKLPFAAAQIGNSFRNEISPRsGLIRVREFTMAEIEHFVDPTEKDHPKFQSV 358
Cdd:cd00768 54 YLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGEEASEFEELI 122
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
57-99 |
4.27e-10 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 55.58 E-value: 4.27e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 93102417 57 LRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKE 99
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALT 43
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
309-338 |
8.06e-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: 8.06e-06
10 20 30
....*....|....*....|....*....|
gi 93102417 309 LPFAAAQIGNSFRNEISPRSGLIRVREFTM 338
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
58-142 |
2.33e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 47.68 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 58 RLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKE--LALQP----KDDIVDRAKmedtlkrRFFYDQAFAIY 131
Cdd:PLN02221 241 RLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAHIEerSKLKPglpkKDGKIDYSK-------DFFGRQAFLTV 313
|
90 100
....*....|....*....|.
gi 93102417 132 GG----------VSGLYDFGP 142
Cdd:PLN02221 314 SGqlqvetyacaLSSVYTFGP 334
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
315-338 |
3.65e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 47.00 E-value: 3.65e-05
10 20
....*....|....*....|....
gi 93102417 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 ... |
285-347 |
5.79e-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: 44.33 E-value: 5.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93102417 285 YLRPETAQGIFLNFkRLLEFNQGKLPFAAAQIGNSFRNEISPRS-GLIRVREFTMAEIEHFVDP 347
Cdd:pfam00587 12 ALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAP 74
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
598-662 |
1.10e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 45.24 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93102417 598 PAVVAPFKCSVLPLSQ-NQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITI 662
Cdd:PRK12325 340 PESVAPFKVGIINLKQgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIV 405
|
|
| thrS |
TIGR00418 |
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ... |
285-654 |
1.64e-04 |
|
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273068 [Multi-domain] Cd Length: 563 Bit Score: 45.01 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 285 YLRPETAQGIFLNFK-RLLEFNqgKLPFAAAQIGNSFRNEISPR-SGLIRVREFTMAEIeHFVDPTEKDHPKFQSVADLC 362
Cdd:TIGR00418 258 MLKPMNCPGHFLIFKsSLRSYR--DLPLRIAELGYSHRYEQSGElHGLMRVRGFTQDDA-HIFCTEDQIKEEFKNQFRLI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 363 LYLYsakaQVTGQSARKMRLgdaveqgvinnsvlgyfIGRIylylTKVGISPDKLrfrqhmenemahyacdcWDAeskts 442
Cdd:TIGR00418 335 QKVY----SDFGFSFDKYEL-----------------STRD----PEDFIGEDEL-----------------WEK----- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 443 ygwieivgcadrscydlscharatkvplvAEKPLKEPKTVNVVQFEPNKGavGKAYkkdaklvleylsacdecYISEMEL 522
Cdd:TIGR00418 368 -----------------------------AEAALEEALKELGVPYEIDPG--RGAF-----------------YGPKIDF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93102417 523 LLseKGEFTIETEGKTFQLtkDMVSVKRFQKTLHVE---EVVPSVIEPS-FG-LGRIMYTILEHtfhvregdeqrTFFSF 597
Cdd:TIGR00418 400 AF--KDALGREWQCATVQL--DFELPERFDLTYVDEdneEKRPVMIHRAiLGsIERFIAILLEK-----------YAGNF 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 93102417 598 PAVVAPFKCSVLPLsqNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGR--RYARTDEI 654
Cdd:TIGR00418 465 PLWLAPVQVVVIPV--NERHLDYAKKVAQKLKKAGIRVDVDDRNERLGKkiREAQKQKI 521
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
61-100 |
2.53e-04 |
|
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: 39.14 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 93102417 61 VRQQGDFVRKLKEDKAPQVDVDRAVAELKARKrvLEAKEL 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 |
2.94e-04 |
|
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: 38.99 E-value: 2.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 93102417 55 APLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKE 99
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
308-340 |
4.74e-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: 39.66 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|...
gi 93102417 308 KLPFAAAQIGNSFRNEISPRSGLIRVREFTMAE 340
Cdd:cd00772 117 DLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKD 149
|
|
| |
