|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
11-614 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 903.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 11 RAKMGDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFAD 90
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 91 FMVKDVKNGECFRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFN 169
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 170 LMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 249
Cdd:PLN02734 235 LMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPED 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 250 KDHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAH 329
Cdd:PLN02734 315 KSHPKFSEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAH 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 330 YACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYL 409
Cdd:PLN02734 395 YAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 410 AICDECYITEMEMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 487
Cdd:PLN02734 475 EAMNEKEAMEMKAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 488 GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTv 567
Cdd:PLN02734 555 GDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG- 633
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 636666298 568 nktphTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 614
Cdd:PLN02734 634 -----SVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
9-599 |
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: 646.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 9 VDRAKMGDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 88
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 89 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 167
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 168 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 247
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 248 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 327
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 328 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 407
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 408 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 487
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 488 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 566
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 636666298 567 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 599
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
1-602 |
3.16e-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: 518.51 E-value: 3.16e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 1 MASPK--DDIVDRAKmgdtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEP 77
Cdd:COG0423 1 MASEDtmEKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 78 VLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPI 157
Cdd:COG0423 75 VWEASGHVDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 158 TGN-DLSPPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVR 234
Cdd:COG0423 136 CGGkELTEVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 235 EFTMAEIEHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISP 314
Cdd:COG0423 216 EFEQMELEFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 315 DKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGai 394
Cdd:COG0423 254 ENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG-- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 395 gkaykkdaklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRI 474
Cdd:COG0423 318 ---------------------------------------------------------------EKYIPHVIEPSFGVDRL 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 475 MYTVFEHTFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTD 552
Cdd:COG0423 335 LLAFLEHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQD 411
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 636666298 553 EIGVAFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 602
Cdd:COG0423 412 EIGTPFCVTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
16-360 |
6.98e-127 |
|
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: 374.62 E-value: 6.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 16 DTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfmvk 94
Cdd:cd00774 3 ELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 95 dvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMFKT 174
Cdd:cd00774 65 ---------------------------------------------------------------------------LMFKT 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 175 FIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEKDH 252
Cdd:cd00774 70 SIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EKSH 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 253 PKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYAC 332
Cdd:cd00774 149 PWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYAS 226
|
330 340
....*....|....*....|....*...
gi 636666298 333 DCWDAESKTSYGWIEIVGCADRSCYDLS 360
Cdd:cd00774 227 DCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
505-599 |
8.52e-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: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 505 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 583
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 636666298 584 QIRAEISELPSIVQDL 599
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
11-614 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 903.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 11 RAKMGDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFAD 90
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 91 FMVKDVKNGECFRADHLLKAHLQKLMSDKK-CSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFN 169
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKDLtISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 170 LMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 249
Cdd:PLN02734 235 LMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPED 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 250 KDHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAH 329
Cdd:PLN02734 315 KSHPKFSEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAH 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 330 YACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYL 409
Cdd:PLN02734 395 YAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 410 AICDECYITEMEMLLNEKGE--FTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 487
Cdd:PLN02734 475 EAMNEKEAMEMKAKLESKGEaeFYVCTLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 488 GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTv 567
Cdd:PLN02734 555 GDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDSDG- 633
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 636666298 568 nktphTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVEARYP 614
Cdd:PLN02734 634 -----SVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
9-599 |
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: 646.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 9 VDRAKMGDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKF 88
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 89 ADFMVKDVKNGECFRADHLLKahlqklmsdkkcsvekksemESVLAQLDNYGQQELADLFVNYNVKSP-ITGNDLSPPVS 167
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIE--------------------EKLGKRLWGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 168 FNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDP 247
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 248 SEKDHPKFQNVADLHLYLYSAKAQVSGqsarkmrLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEM 327
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG-------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 328 AHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVme 407
Cdd:TIGR00389 294 AHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 408 ylaicdecyitEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVRE 487
Cdd:TIGR00389 372 -----------ESNLSEDDLEEREEELDKNEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 488 GD-EQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVAFGVTIDFDT 566
Cdd:TIGR00389 441 LDgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDD-SGTIGKRYRRADEIGTPFCVTIDFET 519
|
570 580 590
....*....|....*....|....*....|...
gi 636666298 567 VNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 599
Cdd:TIGR00389 520 LED--ETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
1-602 |
3.16e-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: 518.51 E-value: 3.16e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 1 MASPK--DDIVDRAKmgdtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQE-EQILEIDCTMLTPEP 77
Cdd:COG0423 1 MASEDtmEKIVSLAK------RRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 78 VLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcSVEKKSEmesvlaqldnygqQELADLFVNYNVKSPI 157
Cdd:COG0423 75 VWEASGHVDGFTDPLVDCKECKKRYRADHLIEEYLAIE------DAEGLSL-------------EELEELIKENNIKCPN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 158 TGN-DLSPPVSFNLMFKTFIGPGGN--MPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVR 234
Cdd:COG0423 136 CGGkELTEVRQFNLMFKTNIGPVEDesSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 235 EFTMAEIEHFVDPSEKdhpkfqnvadlhlylysakaqvsgqsarkmrlgdaveqgvinNTVLGYFIGRIYLYLTKVGISP 314
Cdd:COG0423 216 EFEQMELEFFVDPGTD------------------------------------------NEWFAYWLALRKKWLLSLGIDP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 315 DKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLvaekplkepkTVnvvqFEPSKGai 394
Cdd:COG0423 254 ENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----------TY----FDPETG-- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 395 gkaykkdaklvmeylaicdecyitememllnekgeftietegktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRI 474
Cdd:COG0423 318 ---------------------------------------------------------------EKYIPHVIEPSFGVDRL 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 475 MYTVFEHTFHVRE-GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTD 552
Cdd:COG0423 335 LLAFLEHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKA---FNVEyDDSGSIGRRYRRQD 411
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 636666298 553 EIGVAFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDLANG 602
Cdd:COG0423 412 EIGTPFCVTVDFDTLED--NTVTIRDRDTMEQERVPIDELKAYLAELLKG 459
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
6-599 |
2.03e-173 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 501.20 E-value: 2.03e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 6 DDIVDRAKmgdtlkRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQ-ILEIDCTMLTPEPVLKTSGH 84
Cdd:PRK04173 5 EKIVSLAK------RRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREdVVGIDSPIIMPPEVWEASGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 85 VDKFADFMVKDVKNGECFRADHLLKAHLQKLmsdkkcsVEKKSEmesvlaqldnygqqELADLFVNYNVKSPITGN-DLS 163
Cdd:PRK04173 79 VDNFSDPLVECKKCKKRYRADHLIEELGIDA-------EGLSNE--------------ELKELIRENDIKCPECGGeNWT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 164 PPVSFNLMFKTFIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEI 241
Cdd:PRK04173 138 EVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 242 EHFVDPSEkDHPKFQnvadlhlylysakaqvsgqsarkmrlgdaveqgvinntvlgYFIGRIYLYLTKVGISPDKLRFRQ 321
Cdd:PRK04173 218 EFFVKPGT-DNEWFA-----------------------------------------YWIELRKNWLLDLGIDPENLRFRE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 322 HMENEMAHYACDCWDAESKTSYG--WIEIVGCADRSCYDLSCHAratkvplvaekplkepktvnvvqfepskgaigKAYK 399
Cdd:PRK04173 256 HLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHS--------------------------------KHSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 400 KDaklvMEYlaicdecyitememllnekgeFTIETEGktfqltkdminvkrfqktlyvEEVVPNVIEPSFGLGRIMYTVF 479
Cdd:PRK04173 304 ED----LSY---------------------FDDETTG---------------------EKYIPYVIEPSAGLDRLLLAFL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 480 EHTFHVRE--GDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHgvsHKVD-DSSGSIGRRYARTDEIGV 556
Cdd:PRK04173 338 EDAYTEEElgGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKD---FNVDyDDSGSIGKRYRRQDEIGT 414
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 636666298 557 AFGVTIDFDTVNKtpHTATLRDRDSMRQIRAEISELPSIVQDL 599
Cdd:PRK04173 415 PFCITVDFDTLED--NTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
16-360 |
6.98e-127 |
|
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: 374.62 E-value: 6.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 16 DTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEE-QILEIDCTMLTPEpvlktsghvdkfadfmvk 94
Cdd:cd00774 3 ELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 95 dvkngecfradhllkahlqklmsdkkcsvekksemesvlaqldnygqqeladlfvnynvkspitgndlsppvsfnLMFKT 174
Cdd:cd00774 65 ---------------------------------------------------------------------------LMFKT 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 175 FIGP--GGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPsEKDH 252
Cdd:cd00774 70 SIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EKSH 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 253 PKFQNVADLHLYLYSAKAQvsGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYAC 332
Cdd:cd00774 149 PWFDYWADQRLKWLPKFAQ--SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYAS 226
|
330 340
....*....|....*....|....*...
gi 636666298 333 DCWDAESKTSYGWIEIVGCADRSCYDLS 360
Cdd:cd00774 227 DCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
19-598 |
1.15e-66 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 227.58 E-value: 1.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 19 KRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILE-IDCTMLTPEPVLKTSGHVDKFADFMVkDVK 97
Cdd:PRK14894 14 KRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETFNDPLV-DCR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 98 NGEC-FRADHLlkahlqklmsDKKCSvekksemesvlaqldNYGQQeladlfvnynvkspitgnDLSPPVSFNLMFKTFI 176
Cdd:PRK14894 93 DCKMrWRADHI----------QGVCP---------------NCGSR------------------DLTEPRPFNMMFRTQI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 177 GPGGNMP--GYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDhpk 254
Cdd:PRK14894 130 GPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDE--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 255 fqnvaDLHlylysakaqvsgQSARKMRLGdaveqgvinntvlgyfigriylYLTKVGISPDKLRFRQHMENEMAHYACDC 334
Cdd:PRK14894 207 -----EWH------------QRWLEARLA----------------------WWEQIGIPRSRITIYDVPPDELAHYSKRT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 335 WD-AESKTSYGWIEIVGCADRSCYDLSCHAR-ATKVPLVAEKPLKEPKTVNVVQFEPSKG--AIGKAYKKDAKLVMEYLA 410
Cdd:PRK14894 248 FDlMYDYPNIGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDSTARLTYFDQASGrhVVPYVIEPSAGVGRCMLA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 411 ICDECYITEM------EML--LNEKGEFTIETEGKTFQL---TKDMINVKRFQKTLYVEEVVPNV-----------IEPS 468
Cdd:PRK14894 328 VMCEGYAEELtkaipgEKLaaVGDALEAFLKSVGRSEKLageARDAILARGEALLQALPERLPEVeqllampgadqIELG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 469 FGL-GRIMYTVFEHTfhvregdeqRTFFSFPAVVAPFKCSVLPLSQNQE-FMPFVKELSEALTRHGVSHKVDDSSGSIGR 546
Cdd:PRK14894 408 KKLrGQAQPLIDEHY---------RTVLRLKPRLAPIKVAVFPLKRNHEgLVATAKAVRRQLQVGGRMRTVYDDTGAIGK 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 636666298 547 RYARTDEIGVAFGVTIDFDTVNKTPH-----TATLRDRDSMRQIRAEISELPSIVQD 598
Cdd:PRK14894 479 LYRRQDEIGTPFCITVDFDTIGQGKDpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
478-601 |
1.86e-59 |
|
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: 194.70 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 478 VFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDsSGSIGRRYARTDEIGVA 557
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDD-SGSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 636666298 558 FGVTIDFDTVNktPHTATLRDRDSMRQIRAEISELPSIVQDLAN 601
Cdd:cd00858 80 FCVTVDFDTLE--DGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
505-599 |
8.52e-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: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 505 KCSVLPLSQN-QEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKtpHTATLRDRDSMR 583
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEE--GTVTVRRRDTGE 78
|
90
....*....|....*.
gi 636666298 584 QIRAEISELPSIVQDL 599
Cdd:pfam03129 79 QETVSLDELVEKLKEL 94
|
|
| 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 ... |
133-249 |
6.91e-12 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 65.49 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 133 LAQLDNYGQQELADLFVNY---NVKSPI-TGNDLS-----PPVSFNLMFkTFIGPGGNMPG---YLRPETAQGIFLNF-K 199
Cdd:cd00670 1 GTALWRALERFLDDRMAEYgyqEILFPFlAPTVLFfkgghLDGYRKEMY-TFEDKGRELRDtdlVLRPAACEPIYQIFsG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 636666298 200 RLLEFNqgKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSE 249
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 ... |
126-256 |
2.59e-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: 60.59 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 126 KSEMESVL-AQLDNYGQQEladlfvnynVKSPITGNDlSPPVSFNLMFKTFIGPGGNMPG--YLRPETAQGIFLNFKRLL 202
Cdd:cd00768 2 RSKIEQKLrRFMAELGFQE---------VETPIVERE-PLLEKAGHEPKDLLPVGAENEEdlYLRPTLEPGLVRLFVSHI 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 636666298 203 EfnqgKLPFAAAQIGNSFRNEISPRsGLIRVREFTMAEIEHFVDPSEKDHPKFQ 256
Cdd:cd00768 72 R----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDGEEASEFEE 120
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
503-593 |
5.94e-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: 56.25 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636666298 503 PFKCSVLPLS-QNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTphTATLRDRDS 581
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENG--KVTVKSRDT 78
|
90
....*....|..
gi 636666298 582 MRQIRAEISELP 593
Cdd:cd00738 79 GESETLHVDELP 90
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
209-238 |
9.26e-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: 9.26e-06
10 20 30
....*....|....*....|....*....|
gi 636666298 209 LPFAAAQIGNSFRNEISPRSGLIRVREFTM 238
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
215-238 |
3.20e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 47.00 E-value: 3.20e-05
10 20
....*....|....*....|....
gi 636666298 215 QIGNSFRNEISPRSGLIRVREFTM 238
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 ... |
185-248 |
5.08e-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: 5.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636666298 185 YLRPETAQGIFLNFkRLLEFNQGKLPFAAAQIGNSFRNEISPRS-GLIRVREFTMAEIEHFVDPS 248
Cdd:pfam00587 12 ALKPTNEPGHTLLF-REEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG 75
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
498-562 |
3.76e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 43.31 E-value: 3.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636666298 498 PAVVAPFKCSVLPLSQ-NQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTI 562
Cdd:PRK12325 340 PESVAPFKVGIINLKQgDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIV 405
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
208-258 |
1.85e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 40.43 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 636666298 208 KLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNV 258
Cdd:cd00772 117 DLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEFLNM 167
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