|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-678 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 881.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 5 EIEAKLAPLRAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLEDTEIAL-APKEAS--------FDRLKLEDLLK 75
Cdd:PLN02734 4 SLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELqAAVGAGgdgaaskeAFRQAVVNTLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 76 RRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEEGMLEVDCTSLTPEPVLKASGHVDRFADWMVKDMKNG 155
Cdd:PLN02734 84 RRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 156 ECFRADHLIKNSIEKLLNDKKT-SAAVKQDGQDVLARLEGFDNKDMHEVITRFNFKSPITGNDLTEPIAFNLMFPTQIGP 234
Cdd:PLN02734 164 TCFRADHLLKDFCEEKLEKDLTiSAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 235 TGDFKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPEDKSLAKFAKV 314
Cdd:PLN02734 244 SGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 315 ADQKLVLFSACNQLDGAPAQEVAIGEAVAKKTVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEMAHYAQDCWDAE 394
Cdd:PLN02734 324 ADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 395 ILTSYGWIECVGNADRACYDLQQHYKATNVKLVAEKKLPEPVDVNFVEAQANMALLGKSFKKDAKKIQTSLQQLTSEQVS 474
Cdd:PLN02734 404 IECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 475 ALEEELLAKKLYNLSV--DGQNYALTPEHLNIKKYTKKIHVQEITPSVIEPSYGIGRIMYALLEHSFRQREGDEQRTFLA 552
Cdd:PLN02734 484 EMKAKLESKGEAEFYVctLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFR 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 553 FKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRFEMSYKVDDSSGTIGRRYARTDEIGIPFGITVDFDSlkttpfTVTI 632
Cdd:PLN02734 564 FPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTI 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1972263277 633 RHAETMSQIRLEVSELGRLISDLVAGRQQWSDAQAKYPKFEASATE 678
Cdd:PLN02734 638 RERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPAHSSAADD 683
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
65-655 |
0e+00 |
|
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273051 [Multi-domain] Cd Length: 551 Bit Score: 648.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 65 FDRLKLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEEGMLEVDCTSLTPEPVLKASGHVDRF 144
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 145 ADWMVKDMKNGECFRADHLIKNSIEKllndkktsaavkqdgqdvlaRLEGFDNKDMHEVITRFNFKSP-ITGNDLTEPIA 223
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGK--------------------RLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 224 FNLMFPTQIGPTGDFKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDP 303
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 304 EDKSLAKFAKVADQKLVLFSacnqldgAPAQEVAIGEAVAKKTVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEM 383
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLP-------RQMQESGIGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 384 AHYAQDCWDAEILTSYGWIECVGNADRACYDLQQHYKATNVKLVAEKKLPEPVDVNFVEAQANMALLGKSFKKDAKKIQT 463
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 464 SLQQLTSEQVsalEEELlakklynlsvDGQNYALTPEHLNIKKYTKKIHVQEITPSVIEPSYGIGRIMYALLEHSFRQRE 543
Cdd:TIGR00389 374 NLSEDDLEER---EEEL----------DKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 544 GD-EQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRFEMSYKVDDsSGTIGRRYARTDEIGIPFGITVDFDS 622
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 1972263277 623 LKTTpfTVTIRHAETMSQIRLEVSELGRLISDL 655
Cdd:TIGR00389 520 LEDE--TVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
60-659 |
0e+00 |
|
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: 526.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 60 PKEASFDrlKLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILE-EGMLEVDCTSLTPEPVLKAS 138
Cdd:COG0423 2 ASEDTME--KIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 139 GHVDRFADWMVKDMKNGECFRADHLIKNSIEKLLndkktsaavkqdgqdvlarLEGFDNKDMHEVITRFNFKSPITGN-D 217
Cdd:COG0423 80 GHVDGFTDPLVDCKECKKRYRADHLIEEYLAIED-------------------AEGLSLEELEELIKENNIKCPNCGGkE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 218 LTEPIAFNLMFPTQIGPTGDFK--AFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMC 295
Cdd:COG0423 141 LTEVRQFNLMFKTNIGPVEDESstGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 296 EIEHFVDPEDKslakfakvadqklvlfsacnqldgapaqevaigeavakktvaNETLGYYMARCHQFLMKVGIDGRRLRF 375
Cdd:COG0423 221 ELEFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 376 RQHLSNEMAHYAQDCWDAEILTSYGWIECVGNADRACYDLQQHYKATNVKLvaekklpepvdvnfveaqanmallgksfk 455
Cdd:COG0423 259 RDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------------------------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 456 kdakkiqtslqqltseqvsaleeellakklynlsvdgqnyaltpehlnikKYTKKIHVQEITPSVIEPSYGIGRIMYALL 535
Cdd:COG0423 310 --------------------------------------------------TYFDPETGEKYIPHVIEPSFGVDRLLLAFL 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 536 EHSFRQRE-GDEQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRfemSYKVD-DSSGTIGRRYARTDEIGIP 613
Cdd:COG0423 340 EHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRK---AFNVEyDDSGSIGRRYRRQDEIGTP 416
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1972263277 614 FGITVDFDSLKTTpfTVTIRHAETMSQIRLEVSELGRLISDLVAGR 659
Cdd:COG0423 417 FCVTVDFDTLEDN--TVTIRDRDTMEQERVPIDELKAYLAELLKGE 460
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
70-416 |
9.15e-123 |
|
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: 365.37 E-value: 9.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 70 LEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEE-GMLEVDCTSLTPEpvlkasghvdrfadwm 148
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 149 vkdmkngecfradhliknsiekllndkktsaavkqdgqdvlarlegfdnkdmhevitrfnfkspitgndltepiafnLMF 228
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 229 PTQIGPTGD--FKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPEdK 306
Cdd:cd00774 68 KTSIGPVESggNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE-K 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 307 SLAKFAKVADQKLVLFSACNQLD--GAPAQEVAIGEAVakktVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEMA 384
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQSPenLRLTDHEKEELAH----YANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESA 222
|
330 340 350
....*....|....*....|....*....|..
gi 1972263277 385 HYAQDCWDAEILTSYGWIECVGNADRACYDLQ 416
Cdd:cd00774 223 HYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-655 |
2.88e-17 |
|
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: 77.24 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 561 KCSVLPISANDT-LIPVMDAVKEELSRFEMSYKVDDSSGTIGRRYARTDEIGIPFGITVDFDSLKTTpfTVTIRHAETMS 639
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEG--TVTVRRRDTGE 78
|
90
....*....|....*.
gi 1972263277 640 QIRLEVSELGRLISDL 655
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
14-67 |
7.76e-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: 57.74 E-value: 7.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1972263277 14 RAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLL-EDTEIALAPKEASFDR 67
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDT 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-678 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 881.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 5 EIEAKLAPLRAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLEDTEIAL-APKEAS--------FDRLKLEDLLK 75
Cdd:PLN02734 4 SLRDALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKELqAAVGAGgdgaaskeAFRQAVVNTLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 76 RRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEEGMLEVDCTSLTPEPVLKASGHVDRFADWMVKDMKNG 155
Cdd:PLN02734 84 RRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 156 ECFRADHLIKNSIEKLLNDKKT-SAAVKQDGQDVLARLEGFDNKDMHEVITRFNFKSPITGNDLTEPIAFNLMFPTQIGP 234
Cdd:PLN02734 164 TCFRADHLLKDFCEEKLEKDLTiSAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 235 TGDFKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPEDKSLAKFAKV 314
Cdd:PLN02734 244 SGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 315 ADQKLVLFSACNQLDGAPAQEVAIGEAVAKKTVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEMAHYAQDCWDAE 394
Cdd:PLN02734 324 ADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 395 ILTSYGWIECVGNADRACYDLQQHYKATNVKLVAEKKLPEPVDVNFVEAQANMALLGKSFKKDAKKIQTSLQQLTSEQVS 474
Cdd:PLN02734 404 IECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 475 ALEEELLAKKLYNLSV--DGQNYALTPEHLNIKKYTKKIHVQEITPSVIEPSYGIGRIMYALLEHSFRQREGDEQRTFLA 552
Cdd:PLN02734 484 EMKAKLESKGEAEFYVctLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFR 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 553 FKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRFEMSYKVDDSSGTIGRRYARTDEIGIPFGITVDFDSlkttpfTVTI 632
Cdd:PLN02734 564 FPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG------SVTI 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1972263277 633 RHAETMSQIRLEVSELGRLISDLVAGRQQWSDAQAKYPKFEASATE 678
Cdd:PLN02734 638 RERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPAHSSAADD 683
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
65-655 |
0e+00 |
|
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273051 [Multi-domain] Cd Length: 551 Bit Score: 648.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 65 FDRLKLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEEGMLEVDCTSLTPEPVLKASGHVDRF 144
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 145 ADWMVKDMKNGECFRADHLIKNSIEKllndkktsaavkqdgqdvlaRLEGFDNKDMHEVITRFNFKSP-ITGNDLTEPIA 223
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGK--------------------RLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 224 FNLMFPTQIGPTGDFKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDP 303
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 304 EDKSLAKFAKVADQKLVLFSacnqldgAPAQEVAIGEAVAKKTVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEM 383
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLP-------RQMQESGIGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 384 AHYAQDCWDAEILTSYGWIECVGNADRACYDLQQHYKATNVKLVAEKKLPEPVDVNFVEAQANMALLGKSFKKDAKKIQT 463
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 464 SLQQLTSEQVsalEEELlakklynlsvDGQNYALTPEHLNIKKYTKKIHVQEITPSVIEPSYGIGRIMYALLEHSFRQRE 543
Cdd:TIGR00389 374 NLSEDDLEER---EEEL----------DKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 544 GD-EQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRFEMSYKVDDsSGTIGRRYARTDEIGIPFGITVDFDS 622
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 1972263277 623 LKTTpfTVTIRHAETMSQIRLEVSELGRLISDL 655
Cdd:TIGR00389 520 LEDE--TVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
60-659 |
0e+00 |
|
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: 526.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 60 PKEASFDrlKLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILE-EGMLEVDCTSLTPEPVLKAS 138
Cdd:COG0423 2 ASEDTME--KIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 139 GHVDRFADWMVKDMKNGECFRADHLIKNSIEKLLndkktsaavkqdgqdvlarLEGFDNKDMHEVITRFNFKSPITGN-D 217
Cdd:COG0423 80 GHVDGFTDPLVDCKECKKRYRADHLIEEYLAIED-------------------AEGLSLEELEELIKENNIKCPNCGGkE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 218 LTEPIAFNLMFPTQIGPTGDFK--AFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMC 295
Cdd:COG0423 141 LTEVRQFNLMFKTNIGPVEDESstGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 296 EIEHFVDPEDKslakfakvadqklvlfsacnqldgapaqevaigeavakktvaNETLGYYMARCHQFLMKVGIDGRRLRF 375
Cdd:COG0423 221 ELEFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 376 RQHLSNEMAHYAQDCWDAEILTSYGWIECVGNADRACYDLQQHYKATNVKLvaekklpepvdvnfveaqanmallgksfk 455
Cdd:COG0423 259 RDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------------------------- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 456 kdakkiqtslqqltseqvsaleeellakklynlsvdgqnyaltpehlnikKYTKKIHVQEITPSVIEPSYGIGRIMYALL 535
Cdd:COG0423 310 --------------------------------------------------TYFDPETGEKYIPHVIEPSFGVDRLLLAFL 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 536 EHSFRQRE-GDEQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRfemSYKVD-DSSGTIGRRYARTDEIGIP 613
Cdd:COG0423 340 EHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRK---AFNVEyDDSGSIGRRYRRQDEIGTP 416
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1972263277 614 FGITVDFDSLKTTpfTVTIRHAETMSQIRLEVSELGRLISDLVAGR 659
Cdd:COG0423 417 FCVTVDFDTLEDN--TVTIRDRDTMEQERVPIDELKAYLAELLKGE 460
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
69-656 |
2.86e-173 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 502.35 E-value: 2.86e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 69 KLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILE-EGMLEVDCTSLTPEPVLKASGHVDRFADW 147
Cdd:PRK04173 6 KIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQErEDVVGIDSPIIMPPEVWEASGHVDNFSDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 148 MVKDMKNGECFRADHLIKNSIEKLLNDKKTsaavkqdgqdvlarlegfdnkDMHEVITRFNFKSPITGN-DLTEPIAFNL 226
Cdd:PRK04173 86 LVECKKCKKRYRADHLIEELGIDAEGLSNE---------------------ELKELIRENDIKCPECGGeNWTEVRQFNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 227 MFPTQIGPTGDFK--AFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPE 304
Cdd:PRK04173 145 MFKTFIGPVEDSKslGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVKPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 305 DKslakfakvadqklvlfsacnqldgapaqevaigeavakktvaNETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEMA 384
Cdd:PRK04173 225 TD------------------------------------------NEWFAYWIELRKNWLLDLGIDPENLRFREHLPEELA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 385 HYAQDCWDAEILTSYG--WIECVGNADRACYDLQQHYKATNVKLvaekklpepvdvnfveaqanmallgksfkkdakkiq 462
Cdd:PRK04173 263 HYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDL------------------------------------ 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 463 tslqqltseqvSALEEEllakklynlsVDGQNYaltpehlnikkytkkihvqeiTPSVIEPSYGIGRIMYALLEHSFRQR 542
Cdd:PRK04173 307 -----------SYFDDE----------TTGEKY---------------------IPYVIEPSAGLDRLLLAFLEDAYTEE 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 543 E--GDEQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELS-RFEMSYkvdDSSGTIGRRYARTDEIGIPFGITVD 619
Cdd:PRK04173 345 ElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRkDFNVDY---DDSGSIGKRYRRQDEIGTPFCITVD 421
|
570 580 590
....*....|....*....|....*....|....*..
gi 1972263277 620 FDSLKTTpfTVTIRHAETMSQIRLEVSELGRLISDLV 656
Cdd:PRK04173 422 FDTLEDN--TVTIRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
70-416 |
9.15e-123 |
|
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: 365.37 E-value: 9.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 70 LEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEE-GMLEVDCTSLTPEpvlkasghvdrfadwm 148
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 149 vkdmkngecfradhliknsiekllndkktsaavkqdgqdvlarlegfdnkdmhevitrfnfkspitgndltepiafnLMF 228
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 229 PTQIGPTGD--FKAFLRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPEdK 306
Cdd:cd00774 68 KTSIGPVESggNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE-K 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 307 SLAKFAKVADQKLVLFSACNQLD--GAPAQEVAIGEAVakktVANETLGYYMARCHQFLMKVGIDGRRLRFRQHLSNEMA 384
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQSPenLRLTDHEKEELAH----YANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESA 222
|
330 340 350
....*....|....*....|....*....|..
gi 1972263277 385 HYAQDCWDAEILTSYGWIECVGNADRACYDLQ 416
Cdd:cd00774 223 HYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
69-654 |
3.53e-62 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 216.41 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 69 KLEDLLKRRFFYDQSFAIYGGVTGLYDFGPMGCSLKANMLQEWRKHFILEEGMLE-VDCTSLTPEPVLKASGHVDRFADW 147
Cdd:PRK14894 8 QIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 148 MVkDMKNGEC-FRADHLiknsiekllndkktsaavkqdgqdvlarlegfdnkdmhevitrfNFKSPITGN-DLTEPIAFN 225
Cdd:PRK14894 88 LV-DCRDCKMrWRADHI--------------------------------------------QGVCPNCGSrDLTEPRPFN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 226 LMFPTQIGPTGDFKAF--LRPETAQGIFVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDP 303
Cdd:PRK14894 123 MMFRTQIGPVADSDSFayLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 304 --EDKSLAKFakvADQKLVLFSacnqldgapaqevaigeavakktvanetlgyymarchqflmKVGIDGRRLRFRQHLSN 381
Cdd:PRK14894 203 gtDEEWHQRW---LEARLAWWE-----------------------------------------QIGIPRSRITIYDVPPD 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 382 EMAHYAQDCWDaeILTSY---GWIECVGNADRACYDLQQHYKAT-----------NVKLVAEKKLPEPVD----VNFV-E 442
Cdd:PRK14894 239 ELAHYSKRTFD--LMYDYpniGVQEIEGIANRTDYDLGSHSKDQeqlnltarvnpNEDSTARLTYFDQASgrhvVPYViE 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 443 AQAN-----MALLGKSFKKDAKKiqtslqQLTSEQVSALEEELLAkklYNLSVdGQNYALTPE---HLNIKKYTKKIHVQ 514
Cdd:PRK14894 317 PSAGvgrcmLAVMCEGYAEELTK------AIPGEKLAAVGDALEA---FLKSV-GRSEKLAGEardAILARGEALLQALP 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 515 EITPSVIEPSYGIGRIMYALLEHSFRQREG--DEQ-RTFLAFKPLVAPIKCSVLPISAN-DTLIPVMDAVKEEL---SRF 587
Cdd:PRK14894 387 ERLPEVEQLLAMPGADQIELGKKLRGQAQPliDEHyRTVLRLKPRLAPIKVAVFPLKRNhEGLVATAKAVRRQLqvgGRM 466
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972263277 588 EMSYkvdDSSGTIGRRYARTDEIGIPFGITVDFDSL-----KTTPFTVTIRHAETMSQIRLEVSELGRLISD 654
Cdd:PRK14894 467 RTVY---DDTGAIGKLYRRQDEIGTPFCITVDFDTIgqgkdPALAGTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
534-656 |
1.71e-56 |
|
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: 187.38 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 534 LLEHSFRQREGDEQRTFLAFKPLVAPIKCSVLPISANDTLIPVMDAVKEELSRFEMSYKVDDsSGTIGRRYARTDEIGIP 613
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1972263277 614 FGITVDFDSLKttPFTVTIRHAETMSQIRLEVSELGRLISDLV 656
Cdd:cd00858 80 FCVTVDFDTLE--DGTVTIRERDSMRQVRVKIEELPSYLRELI 120
|
|
| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
10-60 |
1.44e-22 |
|
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: 91.01 E-value: 1.44e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1972263277 10 LAPLRAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLEDTEIALAP 60
Cdd:cd00935 1 LAPLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDKELALQP 51
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-655 |
2.88e-17 |
|
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: 77.24 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 561 KCSVLPISANDT-LIPVMDAVKEELSRFEMSYKVDDSSGTIGRRYARTDEIGIPFGITVDFDSLKTTpfTVTIRHAETMS 639
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEG--TVTVRRRDTGE 78
|
90
....*....|....*.
gi 1972263277 640 QIRLEVSELGRLISDL 655
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
14-55 |
2.87e-11 |
|
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: 58.71 E-value: 2.87e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1972263277 14 RAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLEDTE 55
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
14-67 |
7.76e-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: 57.74 E-value: 7.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1972263277 14 RAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLL-EDTEIALAPKEASFDR 67
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLkEATGQDYKPGAPPGDT 55
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
13-64 |
8.46e-11 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 57.50 E-value: 8.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1972263277 13 LRAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLED-TEIALAPKEAS 64
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKAlTGKDYKPGAAP 53
|
|
| 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 ... |
179-305 |
7.97e-10 |
|
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: 59.71 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 179 AAVKQDGQDVLARlEGFDNKDMHEVITRFNFKSPITgndltEPIAFNLMFPTQIGPTG--DFKAFLRPETAQGIFVNF-K 255
Cdd:cd00670 6 RALERFLDDRMAE-YGYQEILFPFLAPTVLFFKGGH-----LDGYRKEMYTFEDKGRElrDTDLVLRPAACEPIYQIFsG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1972263277 256 RLLEFNqgKLPFAAAQIGLGFRNEISPRQGLIRVREFTMCEIEHFVDPED 305
Cdd:cd00670 80 EILSYR--ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFGEPEE 127
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
239-304 |
4.25e-08 |
|
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: 54.05 E-value: 4.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972263277 239 KAFLRPETAQGIFVNFKRLLEfnqgKLPFAAAQIGLGFRNEISPRqGLIRVREFTMCEIEHFVDPE 304
Cdd:cd00768 52 DLYLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDG 112
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| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
559-648 |
2.76e-06 |
|
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: 46.24 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 559 PIKCSVLPIS-ANDTLIPVMDAVKEELSRFEMSYKVDDSSGTIGRRYARTDEIGIPFGITVDFDSLKTTpfTVTIRHAET 637
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|.
gi 1972263277 638 MSQIRLEVSEL 648
Cdd:cd00738 79 GESETLHVDEL 89
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| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
265-294 |
5.81e-05 |
|
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: 45.26 E-value: 5.81e-05
10 20 30
....*....|....*....|....*....|
gi 1972263277 265 LPFAAAQIGLGFRNEISPRQGLIRVREFTM 294
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
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| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
242-316 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972263277 242 LRPETAQGIfVNFKRLLEFNQGKLPFAAAQIGLGFRNEISPRQ-GLIRVREFTMCEIEHFVDPED--KSLAKFAKVAD 316
Cdd:pfam00587 13 LKPTNEPGH-TLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPGQspDELEDYIKLID 89
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|
| PLN02221 |
PLN02221 |
asparaginyl-tRNA synthetase |
4-98 |
2.20e-04 |
|
asparaginyl-tRNA synthetase
Pssm-ID: 177867 [Multi-domain] Cd Length: 572 Bit Score: 44.21 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 4 PEIEAKLAPLRAAVKEYGDLIRDLKAKGAPKIDIDKAVVELKARKRLLEDTEialapkeasfDRLKLEDLLKRR------ 77
Cdd:PLN02221 231 PPTEADVEAARLIVKERGEVVAQLKAAKASKEEITAAVAELKIAKESLAHIE----------ERSKLKPGLPKKdgkidy 300
|
90 100 110
....*....|....*....|....*....|....
gi 1972263277 78 ---FFYDQSFAIYGG----------VTGLYDFGP 98
Cdd:PLN02221 301 skdFFGRQAFLTVSGqlqvetyacaLSSVYTFGP 334
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|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
271-294 |
6.62e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 42.76 E-value: 6.62e-04
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
514-658 |
2.16e-03 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 41.40 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 514 QEITPSVIE--PSYGIGRIMYALLEHSFRQREGDEQRTFlafkPL-VAPIKCSVLPISAN--DTLIPVMDAVKEELSRFE 588
Cdd:PRK03991 455 EEKYPIILHcsPTGSIERVIYALLEKAAKEEEEGKVPML----PTwLSPTQVRVIPVSERhlDYAEEVADKLEAAGIRVD 530
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263277 589 msykVDDSSGTIGRRYARTDEIGIPFGITVDFDSLKTTPFTVTIRhaETMSQIRLEVSELGRLISDLVAG 658
Cdd:PRK03991 531 ----VDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIR--EESEKVEMTLEELIERIKEETKG 594
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
17-48 |
2.27e-03 |
|
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: 36.44 E-value: 2.27e-03
10 20 30
....*....|....*....|....*....|..
gi 1972263277 17 VKEYGDLIRDLKAKGAPKIDIDKAVVELKARK 48
Cdd:cd00936 5 IAAQGDLVRELKAKKAPKEEIDAAVKKLLALK 36
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