|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
62-720 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 896.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 62 LAPLRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKELSL----------APAEDLFdRAKMEDLIKRRFF 131
Cdd:PLN02734 9 LAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELqaavgaggdgAASKEAF-RQAVVNTLERRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 132 YDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQEQMLEVECSILTPEPVLKASGHVERFADLMTKDIKTGECFR 211
Cdd:PLN02734 88 YIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCFR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 212 LDHLIKGHLEKIKSDKNT-KIELKAEIEDILIKLDGMNADEMSALMKRFEMKSPISGNDLTPPIEFNLMFNTQIGPSGLV 290
Cdd:PLN02734 168 ADHLLKDFCEEKLEKDLTiSAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSGLS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 291 KGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV--KEHPKFESVKNTQ 368
Cdd:PLN02734 248 VGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPedKSHPKFSEVADLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 369 MLLYSADNQEQGKPAELTTIGDAVSKGIVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEMAHYACDCWDAECLSS 448
Cdd:PLN02734 328 FLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIECS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 449 YGWIECVGCADRSAYDLTQHTKATGIRLAAEKKLPAPKQIEVVEAIANKAAIGKAFKKDSQAINDTLATLDNAALEEMQK 528
Cdd:PLN02734 408 YGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEMKA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 529 ELDSNGEYTL--ITARGEFKLTPSLVNVKKTQKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMREGDEQRTYFSLPPT 606
Cdd:PLN02734 488 KLESKGEAEFyvCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFPPL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 607 VAPMKCVVLPLSGNAEFQPFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTikephTVTLRERDS 686
Cdd:PLN02734 568 VAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG-----SVTIRERDS 642
|
650 660 670
....*....|....*....|....*....|....
gi 114053191 687 MRQVRLPMADVPTVVRDLSNSKILWSDVEQKYPK 720
Cdd:PLN02734 643 KDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPA 676
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
117-704 |
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: 635.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 117 FDRAKMEDLIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQEQMLEVECSILTPEPVLKASGHVERF 196
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 197 ADLMTKDIKTGECFRLDHLIKGHLEKiksdkntkielkaeiediliKLDGMNADEMSALMKRFEMKSPISGND-LTPPIE 275
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGK--------------------RLWGFSGPELNEVMEKYDINCPNCGGEnLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 276 FNLMFNTQIGPSGLVKGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV 355
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 356 --KEHPKFESVKNTQMLLYSADNQEQGkpaelttIGDAVSKGIVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEM 433
Cdd:TIGR00389 221 ldKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 434 AHYACDCWDAECLSSYGWIECVGCADRSAYDLTQHTKATGIRLAAEKKLPAPKQIEVVEAIANKAAIGKAFKKDSQAIND 513
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 514 TLATLDnaaLEEMQKELDSNgeytlitargEFKLTPSLVNVKKTQKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMRE 593
Cdd:TIGR00389 374 NLSEDD---LEEREEELDKN----------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 594 GD-EQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQELITVDVSHKVDDsSGSIGRRYARTDELGVPYAVTVDFDT 672
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|..
gi 114053191 673 IKEpHTVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:TIGR00389 520 LED-ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
121-704 |
1.23e-173 |
|
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: 505.41 E-value: 1.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 121 KMEDLI---KRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQ-EQMLEVECSILTPEPVLKASGHVERF 196
Cdd:COG0423 6 TMEKIVslaKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 197 ADLMTKDIKTGECFRLDHLIKGHLEKIKsdkntkielkaeiedilikLDGMNADEMSALMKRFEMKSPISGN-DLTPPIE 275
Cdd:COG0423 86 TDPLVDCKECKKRYRADHLIEEYLAIED-------------------AEGLSLEELEELIKENNIKCPNCGGkELTEVRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 276 FNLMFNTQIGPSGLVK--GFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFC 353
Cdd:COG0423 147 FNLMFKTNIGPVEDESstGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 354 DvkehpkfesvkntqmllysadnqeqgkPAElttigdavskgivNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEM 433
Cdd:COG0423 227 D---------------------------PGT-------------DNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEEL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 434 AHYACDCWDAECLSSYGWIECVGCADRSAYDLTQHTKATGirlaaeKKLpapkqievveaiankaaigkafkkdsqaind 513
Cdd:COG0423 267 AHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSG------KDL------------------------------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 514 tlatldnaaleemqkeldsngEYTlitargefkltpslvnvkktqKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMRE 593
Cdd:COG0423 310 ---------------------TYF---------------------DPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEE 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 594 -GDEQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQEL---ITVDVshkvdDSSGSIGRRYARTDELGVPYAVTVD 669
Cdd:COG0423 348 vDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELrkaFNVEY-----DDSGSIGRRYRRQDEIGTPFCVTVD 422
|
570 580 590
....*....|....*....|....*....|....*
gi 114053191 670 FDTIkEPHTVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:COG0423 423 FDTL-EDNTVTIRDRDTMEQERVPIDELKAYLAEL 456
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
122-466 |
5.33e-119 |
|
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: 357.29 E-value: 5.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 122 MEDLIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQE-QMLEVECSILTPEpvlkasghverfadlm 200
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 201 tkdiktgecfrldhlikghlekiksdkntkielkaeiedilikldgmnademsalmkrfemkspisgndltppiefnLMF 280
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 281 NTQIGP--SGLVKGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV-KE 357
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPeKS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 358 HPKFESVKNTQMLLYSADNQ--EQGKPAELTTIGDAVskgiVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEMAH 435
Cdd:cd00774 148 HPWFDYWADQRLKWLPKFAQspENLRLTDHEKEELAH----YANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAH 223
|
330 340 350
....*....|....*....|....*....|.
gi 114053191 436 YACDCWDAECLSSYGWIECVGCADRSAYDLT 466
Cdd:cd00774 224 YASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
611-704 |
3.22e-24 |
|
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: 97.27 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 611 KCVVLPLSGNA-EFQPFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTIKEpHTVTLRERDSMRQ 689
Cdd:pfam03129 1 QVVVIPLGEKAeELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE-GTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 114053191 690 VRLPMADVPTVVRDL 704
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
66-120 |
4.66e-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: 58.51 E-value: 4.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 114053191 66 RANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKIL-EDKELSLAPAEDLFDRA 120
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
62-720 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 896.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 62 LAPLRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKELSL----------APAEDLFdRAKMEDLIKRRFF 131
Cdd:PLN02734 9 LAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELqaavgaggdgAASKEAF-RQAVVNTLERRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 132 YDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQEQMLEVECSILTPEPVLKASGHVERFADLMTKDIKTGECFR 211
Cdd:PLN02734 88 YIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCFR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 212 LDHLIKGHLEKIKSDKNT-KIELKAEIEDILIKLDGMNADEMSALMKRFEMKSPISGNDLTPPIEFNLMFNTQIGPSGLV 290
Cdd:PLN02734 168 ADHLLKDFCEEKLEKDLTiSAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSGLS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 291 KGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV--KEHPKFESVKNTQ 368
Cdd:PLN02734 248 VGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPedKSHPKFSEVADLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 369 MLLYSADNQEQGKPAELTTIGDAVSKGIVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEMAHYACDCWDAECLSS 448
Cdd:PLN02734 328 FLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIECS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 449 YGWIECVGCADRSAYDLTQHTKATGIRLAAEKKLPAPKQIEVVEAIANKAAIGKAFKKDSQAINDTLATLDNAALEEMQK 528
Cdd:PLN02734 408 YGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEMKA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 529 ELDSNGEYTL--ITARGEFKLTPSLVNVKKTQKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMREGDEQRTYFSLPPT 606
Cdd:PLN02734 488 KLESKGEAEFyvCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFPPL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 607 VAPMKCVVLPLSGNAEFQPFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTikephTVTLRERDS 686
Cdd:PLN02734 568 VAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG-----SVTIRERDS 642
|
650 660 670
....*....|....*....|....*....|....
gi 114053191 687 MRQVRLPMADVPTVVRDLSNSKILWSDVEQKYPK 720
Cdd:PLN02734 643 KDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPA 676
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
117-704 |
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: 635.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 117 FDRAKMEDLIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQEQMLEVECSILTPEPVLKASGHVERF 196
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 197 ADLMTKDIKTGECFRLDHLIKGHLEKiksdkntkielkaeiediliKLDGMNADEMSALMKRFEMKSPISGND-LTPPIE 275
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGK--------------------RLWGFSGPELNEVMEKYDINCPNCGGEnLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 276 FNLMFNTQIGPSGLVKGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV 355
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 356 --KEHPKFESVKNTQMLLYSADNQEQGkpaelttIGDAVSKGIVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEM 433
Cdd:TIGR00389 221 ldKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 434 AHYACDCWDAECLSSYGWIECVGCADRSAYDLTQHTKATGIRLAAEKKLPAPKQIEVVEAIANKAAIGKAFKKDSQAIND 513
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 514 TLATLDnaaLEEMQKELDSNgeytlitargEFKLTPSLVNVKKTQKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMRE 593
Cdd:TIGR00389 374 NLSEDD---LEEREEELDKN----------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 594 GD-EQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQELITVDVSHKVDDsSGSIGRRYARTDELGVPYAVTVDFDT 672
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|..
gi 114053191 673 IKEpHTVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:TIGR00389 520 LED-ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
121-704 |
1.23e-173 |
|
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: 505.41 E-value: 1.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 121 KMEDLI---KRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQ-EQMLEVECSILTPEPVLKASGHVERF 196
Cdd:COG0423 6 TMEKIVslaKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 197 ADLMTKDIKTGECFRLDHLIKGHLEKIKsdkntkielkaeiedilikLDGMNADEMSALMKRFEMKSPISGN-DLTPPIE 275
Cdd:COG0423 86 TDPLVDCKECKKRYRADHLIEEYLAIED-------------------AEGLSLEELEELIKENNIKCPNCGGkELTEVRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 276 FNLMFNTQIGPSGLVK--GFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFC 353
Cdd:COG0423 147 FNLMFKTNIGPVEDESstGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 354 DvkehpkfesvkntqmllysadnqeqgkPAElttigdavskgivNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEM 433
Cdd:COG0423 227 D---------------------------PGT-------------DNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEEL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 434 AHYACDCWDAECLSSYGWIECVGCADRSAYDLTQHTKATGirlaaeKKLpapkqievveaiankaaigkafkkdsqaind 513
Cdd:COG0423 267 AHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSG------KDL------------------------------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 514 tlatldnaaleemqkeldsngEYTlitargefkltpslvnvkktqKTIHVEEIIPSVIEPSFGVGRILYCILEHNFRMRE 593
Cdd:COG0423 310 ---------------------TYF---------------------DPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEE 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 594 -GDEQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQEL---ITVDVshkvdDSSGSIGRRYARTDELGVPYAVTVD 669
Cdd:COG0423 348 vDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELrkaFNVEY-----DDSGSIGRRYRRQDEIGTPFCVTVD 422
|
570 580 590
....*....|....*....|....*....|....*
gi 114053191 670 FDTIkEPHTVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:COG0423 423 FDTL-EDNTVTIRDRDTMEQERVPIDELKAYLAEL 456
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
114-704 |
3.13e-165 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 483.48 E-value: 3.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 114 EDLFDraKMEDLIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFI-LQEQMLEVECSILTPEPVLKASGH 192
Cdd:PRK04173 1 MDKME--KIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVqEREDVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 193 VERFADLMTKDIKTGECFRLDHLIKGHLEKIksDKNTKIELKAEIEDILIKldgmnademsalmkrfemkSPISGN-DLT 271
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA--EGLSNEELKELIRENDIK-------------------CPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 272 PPIEFNLMFNTQIGPSGLVK--GFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEI 349
Cdd:PRK04173 138 EVRQFNLMFKTFIGPVEDSKslGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 350 EHFCDvkehpkfesvkntqmllysadnqeqgkPAElttigdavskgivNNETLGYFMARIHMYMLAVGIDPKRLRFRQHM 429
Cdd:PRK04173 218 EFFVK---------------------------PGT-------------DNEWFAYWIELRKNWLLDLGIDPENLRFREHL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 430 GNEMAHYACDCWDAECLSSYG--WIECVGCADRSAYDLTQHTKATGirlaaeKKLpapkqievveaiankaaigkafkkd 507
Cdd:PRK04173 258 PEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSG------EDL------------------------- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 508 sqaindtlatldnaaleemqkeldsngEYtlitargeFKltpslvnvkktqKTIHVEEIIPSVIEPSFGVGRILYCILEH 587
Cdd:PRK04173 307 ---------------------------SY--------FD------------DETTGEKYIPYVIEPSAGLDRLLLAFLED 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 588 NFRMRE--GDEQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQELITvdvSHKVD-DSSGSIGRRYARTDELGVPY 664
Cdd:PRK04173 340 AYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRK---DFNVDyDDSGSIGKRYRRQDEIGTPF 416
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 114053191 665 AVTVDFDTIkEPHTVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:PRK04173 417 CITVDFDTL-EDNTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
122-466 |
5.33e-119 |
|
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: 357.29 E-value: 5.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 122 MEDLIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQE-QMLEVECSILTPEpvlkasghverfadlm 200
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 201 tkdiktgecfrldhlikghlekiksdkntkielkaeiedilikldgmnademsalmkrfemkspisgndltppiefnLMF 280
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 281 NTQIGP--SGLVKGFLRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDV-KE 357
Cdd:cd00774 68 KTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPeKS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 358 HPKFESVKNTQMLLYSADNQ--EQGKPAELTTIGDAVskgiVNNETLGYFMARIHMYMLAVGIDPKRLRFRQHMGNEMAH 435
Cdd:cd00774 148 HPWFDYWADQRLKWLPKFAQspENLRLTDHEKEELAH----YANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAH 223
|
330 340 350
....*....|....*....|....*....|.
gi 114053191 436 YACDCWDAECLSSYGWIECVGCADRSAYDLT 466
Cdd:cd00774 224 YASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
584-706 |
1.11e-60 |
|
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: 199.71 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 584 ILEHNFRMREGDEQRTYFSLPPTVAPMKCVVLPLSGNAEFQPFVRDLSQELITVDVSHKVDDsSGSIGRRYARTDELGVP 663
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 114053191 664 YAVTVDFDTIkEPHTVTLRERDSMRQVRLPMADVPTVVRDLSN 706
Cdd:cd00858 80 FCVTVDFDTL-EDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
125-703 |
1.31e-60 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 213.32 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 125 LIKRRFFYDQSFAIYGGITGQFDFGPMGCALKSNMIHLWKKFFILQEQMLE-VECSILTPEPVLKASGHVERFADLMT-- 201
Cdd:PRK14894 12 LAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLVdc 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 202 KDIKTGecFRLDHlIKGhlekiksdkntkielkaeiedilikldgmnademsalmkrfemKSPISGN-DLTPPIEFNLMF 280
Cdd:PRK14894 92 RDCKMR--WRADH-IQG-------------------------------------------VCPNCGSrDLTEPRPFNMMF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 281 NTQIGPSGLVKGF--LRPETAQGILVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFcdvkeh 358
Cdd:PRK14894 126 RTQIGPVADSDSFayLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYF------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 359 pkfesvkntqmllysadnqeqgkpaelttigdaVSKGIVNNETLGYFMARIhMYMLAVGIDPKRLRFRQHMGNEMAHYAC 438
Cdd:PRK14894 200 ---------------------------------VMPGTDEEWHQRWLEARL-AWWEQIGIPRSRITIYDVPPDELAHYSK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 439 DCWDaeCLSSY---GWIECVGCADRSAYDLTQHTK-ATGIRLAAE--------KKL----PAPKQIEVVEAIANKAAIGK 502
Cdd:PRK14894 246 RTFD--LMYDYpniGVQEIEGIANRTDYDLGSHSKdQEQLNLTARvnpnedstARLtyfdQASGRHVVPYVIEPSAGVGR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 503 AF---------KKDSQAINDTLATLDNAALEEMQKELDSNGEYT-----LITARGEfKLTPSLvnvkkTQKTIHVEEII- 567
Cdd:PRK14894 324 CMlavmcegyaEELTKAIPGEKLAAVGDALEAFLKSVGRSEKLAgeardAILARGE-ALLQAL-----PERLPEVEQLLa 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 568 -PSVIEPSFGV---GRILYCILEHnfrmregdeQRTYFSLPPTVAPMKCVVLPLSGNAE-FQPFVRDLSQELITVDVSHK 642
Cdd:PRK14894 398 mPGADQIELGKklrGQAQPLIDEH---------YRTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRT 468
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114053191 643 VDDSSGSIGRRYARTDELGVPYAVTVDFDTIKEPH------TVTLRERDSMRQVRLPMADVPTVVRD 703
Cdd:PRK14894 469 VYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQGKdpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
611-704 |
3.22e-24 |
|
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: 97.27 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 611 KCVVLPLSGNA-EFQPFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTIKEpHTVTLRERDSMRQ 689
Cdd:pfam03129 1 QVVVIPLGEKAeELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE-GTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 114053191 690 VRLPMADVPTVVRDL 704
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
62-112 |
6.82e-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: 94.86 E-value: 6.82e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 114053191 62 LAPLRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKELSLAP 112
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP 51
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
65-107 |
6.02e-13 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 63.67 E-value: 6.02e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 114053191 65 LRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKE 107
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALT 43
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
66-107 |
8.75e-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: 62.94 E-value: 8.75e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 114053191 66 RANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKE 107
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 ... |
66-120 |
4.66e-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: 58.51 E-value: 4.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 114053191 66 RANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKIL-EDKELSLAPAEDLFDRA 120
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDTP 56
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
609-698 |
1.11e-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: 55.87 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 609 PMKCVVLPLSGNAEFQ-PFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTIkEPHTVTLRERDSM 687
Cdd:cd00738 1 PIDVAIVPLTDPRVEArEYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDEL-ENGKVTVKSRDTG 79
|
90
....*....|.
gi 114053191 688 RQVRLPMADVP 698
Cdd:cd00738 80 ESETLHVDELP 90
|
|
| 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 ... |
294-361 |
1.31e-09 |
|
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: 59.33 E-value: 1.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114053191 294 LRPETAQGILVNF-KRLLEFNQgrLPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDVKEHPKF 361
Cdd:cd00670 65 LRPAACEPIYQIFsGEILSYRA--LPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEEAEEE 131
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
293-372 |
1.33e-09 |
|
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: 58.67 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 293 FLRPETAQGILVNFKRLLEfnqgRLPFAAAQIGNSFRNEISPRsGLLRVREFTMCEIEHFCDvkEHPKFESVKNTQMLLY 372
Cdd:cd00768 54 YLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGE--DGEEASEFEELIELTE 126
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
317-346 |
9.71e-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: 9.71e-06
10 20 30
....*....|....*....|....*....|
gi 114053191 317 LPFAAAQIGNSFRNEISPRSGLLRVREFTM 346
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
323-346 |
3.23e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 47.39 E-value: 3.23e-05
10 20
....*....|....*....|....
gi 114053191 323 QIGNSFRNEISPRSGLLRVREFTM 346
Cdd:PRK09194 134 QIQTKFRDEIRPRFGLMRGREFIM 157
|
|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
49-157 |
7.68e-05 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 46.14 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 49 REIIMADPKIEEILAPLRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKiledkelSLAPAEdlfDRAKMEDLIKR 128
Cdd:PLN02221 224 QDLIDNPPPTEADVEAARLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKE-------SLAHIE---ERSKLKPGLPK 293
|
90 100 110
....*....|....*....|....*....|....*...
gi 114053191 129 R---------FFYDQSFAIyggITGQFDFGPMGCALKS 157
Cdd:PLN02221 294 KdgkidyskdFFGRQAFLT---VSGQLQVETYACALSS 328
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
65-96 |
8.29e-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: 40.68 E-value: 8.29e-05
10 20 30
....*....|....*....|....*....|..
gi 114053191 65 LRANVKEQGDLVRKLKEEKAPEIDIKKAVAEL 96
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKL 32
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
294-353 |
1.63e-04 |
|
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: 43.17 E-value: 1.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114053191 294 LRPETAQGIlVNFKRLLEFNQGRLPFAAAQIGNSFRNEISPRS-GLLRVREFTMCEIEHFC 353
Cdd:pfam00587 13 LKPTNEPGH-TLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFH 72
|
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
63-107 |
2.50e-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: 2.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 114053191 63 APLRANVKEQGDLVRKLKEEKAPEIDIKKAVAELKTRKKILEDKE 107
Cdd:cd00938 1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
317-368 |
2.14e-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: 40.81 E-value: 2.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 114053191 317 LPFAAAQIGNSFRNEISPRSGLLRVREFTMCEIEHFCDVKEHPKfESVKNTQ 368
Cdd:cd00772 118 LPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEAD-EEFLNML 168
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
604-684 |
7.48e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 39.46 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 604 PPTVAPMKCVVLPL-SGNAEFQPFVRDLSQELITVDVSHKVDDSSGSIGRRYARTDELGVPYAVTVDFDTIKEpHTVTLR 682
Cdd:PRK12325 340 PESVAPFKVGIINLkQGDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAE-GKVELK 418
|
..
gi 114053191 683 ER 684
Cdd:PRK12325 419 DR 420
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
603-704 |
7.78e-03 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS 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, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 38.43 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053191 603 LPPTVAPMKCVVLPL----SGNAEFQPFVRDLSQELITVDVSHKVDDSSG-SIGRRYARTDELGVPYAVTVDFDTIKEpH 677
Cdd:cd00862 4 LPPRVAPIQVVIVPIgikdEKREEVLEAADELAERLKAAGIRVHVDDRDNyTPGWKFNDWELKGVPLRIEIGPRDLEK-N 82
|
90 100
....*....|....*....|....*..
gi 114053191 678 TVTLRERDSMRQVRLPMADVPTVVRDL 704
Cdd:cd00862 83 TVVIVRRDTGEKKTVPLAELVEKVPEL 109
|
|
| |
