|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-677 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 1154.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 5 TNEQLQDELDALNAQITKQGSAVRELK-KAGDADAVAEAVAKLQALKINAAEMGKSLV---------SDEPEFNRKAFDE 74
Cdd:PLN02734 1 SEDSLRDALAEKQAAVTAQGNAVRALKaSKADKAEIDAAIEKLKALKLEKSALEKELQaavgaggdgAASKEAFRQAVVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 75 LVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAESMLEMECTCLTPEAVLKTSGHVDRFTDLMVKDP 154
Cdd:PLN02734 81 TLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 155 QTAECFRADKLLEDAIDSLLEANPTMPVEEREDHLRIQRQADAFSPTELDELLIKYDCKGP-SGEAYTPSFPFNLMFKTS 233
Cdd:PLN02734 161 KTGTCFRADHLLKDFCEEKLEKDLTISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPdTKNPLSDPYPFNLMFQTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 234 IGPEGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKDKSHPNF 313
Cdd:PLN02734 241 IGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 314 KSVTDKELVLFGRDDQLGSGKTKTIACGEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHYAADCW 393
Cdd:PLN02734 321 SEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 394 DLEIKSSYGWQECVGHADRACYDLEVHSRATKTSMVATQKVDPPQEMEVAKLKFDRKLLGQAFKGDQRVVSGMLESLAES 473
Cdd:PLN02734 401 DAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 474 wtDFEPIATKLENDGKTTV------EGFEITKEMMTWTKQKKTVHEIKFTPSVIEPSFGMGRILYSLLEHSFYQRESDEQ 547
Cdd:PLN02734 481 --EAMEMKAKLESKGEAEFyvctlgKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 548 RVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDKSTAAIGRRYSRSDELGIPFAVTVDFdtlnDGT 627
Cdd:PLN02734 559 LNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGS 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 219116973 628 VTLRERDSTVQVRLPKNDINYLLFQIVHSRMTWEDVMKKYPVVSTGDDTE 677
Cdd:PLN02734 635 VTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPAHSSAADDE 684
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
67-646 |
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: 593.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 67 FNRKAFDELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAESMLEMECTCLTPEAVLKTSGHVDRF 146
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 147 TDLMVKDPQTAECFRADKLLEDAIDslleanptmpveeredhlriqRQADAFSPTELDELLIKYDCKGPS--GEAYTPSF 224
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLG---------------------KRLWGFSGPELNEVMEKYDINCPNcgGENLTEVR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 225 PFNLMFKTSIGPEGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVN 304
Cdd:TIGR00389 140 SFNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 305 PKDKSHPNFKSVTDKELVLFGRDDQlgsgktkTIACGEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATE 384
Cdd:TIGR00389 220 PLDKSHPKFEEVKQDILPLLPRQMQ-------ESGIGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 385 MAHYAADCWDLEIKSSYGWQECVGHADRACYDLEVHSRATKTSMVATQKVDPPQEMEVAKLKFDRKLLGQAFKGDQRVVS 464
Cdd:TIGR00389 293 MAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 465 GMLeslaeSWTDFEPIATKLENdgkttvEGFEITKEMMTWTKQKKTVHEIKFTPSVIEPSFGMGRILYSLLEHSFYQRES 544
Cdd:TIGR00389 373 SNL-----SEDDLEEREEELDK------NEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 545 D-EQRVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDkSTAAIGRRYSRSDELGIPFAVTVDFDTL 623
Cdd:TIGR00389 442 DgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYD-DSGTIGKRYRRADEIGTPFCVTIDFETL 520
|
570 580
....*....|....*....|...
gi 219116973 624 NDGTVTLRERDSTVQVRLPKNDI 646
Cdd:TIGR00389 521 EDETVTIRERDSMKQVRVKIKEL 543
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
74-649 |
6.15e-160 |
|
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: 469.20 E-value: 6.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 74 ELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFV-LAESMLEMECTCLTPEAVLKTSGHVDRFTDLMVK 152
Cdd:COG0423 12 SLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVqRRDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 153 DPQTAECFRADKLLEDAIdslleanptmpveEREDhlriqrqADAFSPTELDELLIKYDCKGPS--GEAYTPSFPFNLMF 230
Cdd:COG0423 92 CKECKKRYRADHLIEEYL-------------AIED-------AEGLSLEELEELIKENNIKCPNcgGKELTEVRQFNLMF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 231 KTSIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKDK 308
Cdd:COG0423 152 KTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 309 shpnfksvtdkelvlfgrddqlgsgktktiacgeavesglinNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHY 388
Cdd:COG0423 232 ------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 389 AADCWDLEIKSSYGWQECVGHADRACYDLEVHSRATKtsmvatqkvdppQEMEVaklkFDrkllgqafkgdqrvvsgmle 468
Cdd:COG0423 270 AKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSG------------KDLTY----FD-------------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 469 slaeswtdfepiatklendgkttvegfEITKEmmtwtkqkktvheiKFTPSVIEPSFGMGRILYSLLEHSFYQRESD-EQ 547
Cdd:COG0423 314 ---------------------------PETGE--------------KYIPHVIEPSFGVDRLLLAFLEHAYTEEEVDgEE 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 548 RVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMdSDLATRVDkSTAAIGRRYSRSDELGIPFAVTVDFDTLNDGT 627
Cdd:COG0423 353 RTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELR-KAFNVEYD-DSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNT 430
|
570 580
....*....|....*....|...
gi 219116973 628 VTLRERDSTVQVRLPKNDI-NYL 649
Cdd:COG0423 431 VTIRDRDTMEQERVPIDELkAYL 453
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
74-417 |
2.91e-100 |
|
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: 307.98 E-value: 2.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 74 ELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAES-MLEMECTCLTPEavlktsghvdrftdlmvk 152
Cdd:cd00774 3 ELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEdMLEIDSPIITPE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 153 dpqtaecfradklledaidslleanptmpveeredhlriqrqadafspteldellikydckgpsgeaytpsfpfnLMFKT 232
Cdd:cd00774 65 ---------------------------------------------------------------------------LMFKT 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 233 SIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKdKSH 310
Cdd:cd00774 70 SIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE-KSH 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 311 PNFKSVTDKELVLFGRDDQLGSGKTKTIAcgEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHYAA 390
Cdd:cd00774 149 PWFDYWADQRLKWLPKFAQSPENLRLTDH--EKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYAS 226
|
330 340
....*....|....*....|....*..
gi 219116973 391 DCWDLEIKSSYGWQECVGHADRACYDL 417
Cdd:cd00774 227 DCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-646 |
7.94e-19 |
|
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: 81.86 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 561 KCAVLPISSN-PECNEIVDDIARDLMDSDLATRVDKSTAAIGRRYSRSDELGIPFAVTVDFDTLNDGTVTLRERDSTVQV 639
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*..
gi 219116973 640 RLPKNDI 646
Cdd:pfam03129 81 TVSLDEL 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
5-677 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 1154.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 5 TNEQLQDELDALNAQITKQGSAVRELK-KAGDADAVAEAVAKLQALKINAAEMGKSLV---------SDEPEFNRKAFDE 74
Cdd:PLN02734 1 SEDSLRDALAEKQAAVTAQGNAVRALKaSKADKAEIDAAIEKLKALKLEKSALEKELQaavgaggdgAASKEAFRQAVVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 75 LVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAESMLEMECTCLTPEAVLKTSGHVDRFTDLMVKDP 154
Cdd:PLN02734 81 TLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 155 QTAECFRADKLLEDAIDSLLEANPTMPVEEREDHLRIQRQADAFSPTELDELLIKYDCKGP-SGEAYTPSFPFNLMFKTS 233
Cdd:PLN02734 161 KTGTCFRADHLLKDFCEEKLEKDLTISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPdTKNPLSDPYPFNLMFQTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 234 IGPEGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKDKSHPNF 313
Cdd:PLN02734 241 IGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 314 KSVTDKELVLFGRDDQLGSGKTKTIACGEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHYAADCW 393
Cdd:PLN02734 321 SEVADLEFLLFPREEQLGGQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 394 DLEIKSSYGWQECVGHADRACYDLEVHSRATKTSMVATQKVDPPQEMEVAKLKFDRKLLGQAFKGDQRVVSGMLESLAES 473
Cdd:PLN02734 401 DAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 474 wtDFEPIATKLENDGKTTV------EGFEITKEMMTWTKQKKTVHEIKFTPSVIEPSFGMGRILYSLLEHSFYQRESDEQ 547
Cdd:PLN02734 481 --EAMEMKAKLESKGEAEFyvctlgKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 548 RVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDKSTAAIGRRYSRSDELGIPFAVTVDFdtlnDGT 627
Cdd:PLN02734 559 LNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGS 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 219116973 628 VTLRERDSTVQVRLPKNDINYLLFQIVHSRMTWEDVMKKYPVVSTGDDTE 677
Cdd:PLN02734 635 VTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAKYPAHSSAADDE 684
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
67-646 |
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: 593.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 67 FNRKAFDELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAESMLEMECTCLTPEAVLKTSGHVDRF 146
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 147 TDLMVKDPQTAECFRADKLLEDAIDslleanptmpveeredhlriqRQADAFSPTELDELLIKYDCKGPS--GEAYTPSF 224
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLG---------------------KRLWGFSGPELNEVMEKYDINCPNcgGENLTEVR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 225 PFNLMFKTSIGPEGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVN 304
Cdd:TIGR00389 140 SFNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 305 PKDKSHPNFKSVTDKELVLFGRDDQlgsgktkTIACGEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATE 384
Cdd:TIGR00389 220 PLDKSHPKFEEVKQDILPLLPRQMQ-------ESGIGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 385 MAHYAADCWDLEIKSSYGWQECVGHADRACYDLEVHSRATKTSMVATQKVDPPQEMEVAKLKFDRKLLGQAFKGDQRVVS 464
Cdd:TIGR00389 293 MAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 465 GMLeslaeSWTDFEPIATKLENdgkttvEGFEITKEMMTWTKQKKTVHEIKFTPSVIEPSFGMGRILYSLLEHSFYQRES 544
Cdd:TIGR00389 373 SNL-----SEDDLEEREEELDK------NEVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 545 D-EQRVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDkSTAAIGRRYSRSDELGIPFAVTVDFDTL 623
Cdd:TIGR00389 442 DgEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYD-DSGTIGKRYRRADEIGTPFCVTIDFETL 520
|
570 580
....*....|....*....|...
gi 219116973 624 NDGTVTLRERDSTVQVRLPKNDI 646
Cdd:TIGR00389 521 EDETVTIRERDSMKQVRVKIKEL 543
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
74-649 |
6.15e-160 |
|
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: 469.20 E-value: 6.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 74 ELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFV-LAESMLEMECTCLTPEAVLKTSGHVDRFTDLMVK 152
Cdd:COG0423 12 SLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVqRRDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 153 DPQTAECFRADKLLEDAIdslleanptmpveEREDhlriqrqADAFSPTELDELLIKYDCKGPS--GEAYTPSFPFNLMF 230
Cdd:COG0423 92 CKECKKRYRADHLIEEYL-------------AIED-------AEGLSLEELEELIKENNIKCPNcgGKELTEVRQFNLMF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 231 KTSIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKDK 308
Cdd:COG0423 152 KTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 309 shpnfksvtdkelvlfgrddqlgsgktktiacgeavesglinNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHY 388
Cdd:COG0423 232 ------------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 389 AADCWDLEIKSSYGWQECVGHADRACYDLEVHSRATKtsmvatqkvdppQEMEVaklkFDrkllgqafkgdqrvvsgmle 468
Cdd:COG0423 270 AKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSG------------KDLTY----FD-------------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 469 slaeswtdfepiatklendgkttvegfEITKEmmtwtkqkktvheiKFTPSVIEPSFGMGRILYSLLEHSFYQRESD-EQ 547
Cdd:COG0423 314 ---------------------------PETGE--------------KYIPHVIEPSFGVDRLLLAFLEHAYTEEEVDgEE 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 548 RVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMdSDLATRVDkSTAAIGRRYSRSDELGIPFAVTVDFDTLNDGT 627
Cdd:COG0423 353 RTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELR-KAFNVEYD-DSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNT 430
|
570 580
....*....|....*....|...
gi 219116973 628 VTLRERDSTVQVRLPKNDI-NYL 649
Cdd:COG0423 431 VTIRDRDTMEQERVPIDELkAYL 453
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
74-649 |
3.71e-153 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 451.51 E-value: 3.71e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 74 ELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFV-LAESMLEMECTCLTPEAVLKTSGHVDRFTDLMVK 152
Cdd:PRK04173 9 SLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVqEREDVVGIDSPIIMPPEVWEASGHVDNFSDPLVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 153 DPQTAECFRADKLLEDAIDSLLEAnptmpveeredhlriqrqadafSPTELDELLIKYDCKGPS--GEAYTPSFPFNLMF 230
Cdd:PRK04173 89 CKKCKKRYRADHLIEELGIDAEGL----------------------SNEELKELIRENDIKCPEcgGENWTEVRQFNLMF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 231 KTSIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKDK 308
Cdd:PRK04173 147 KTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVKPGTD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 309 shpnfksvtdkelvlfgrddqlgsgktktiacgeavesglinNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHY 388
Cdd:PRK04173 227 ------------------------------------------NEWFAYWIELRKNWLLDLGIDPENLRFREHLPEELAHY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 389 AADCWDLEIKSSYG--WQECVGHADRACYDLEVHSRATKtsmvatqkvdppQEMEVaklkFDRkllgqafkgdqrvvsgm 466
Cdd:PRK04173 265 SKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSG------------EDLSY----FDD----------------- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 467 leslaeswtdfepiatklendgkttvegfEITKEmmtwtkqkktvheiKFTPSVIEPSFGMGRILYSLLEHSFYQRE--S 544
Cdd:PRK04173 312 -----------------------------ETTGE--------------KYIPYVIEPSAGLDRLLLAFLEDAYTEEElgG 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 545 DEQRVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDksTAAIGRRYSRSDELGIPFAVTVDFDTLN 624
Cdd:PRK04173 349 GDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKDFNVDYDD--SGSIGKRYRRQDEIGTPFCITVDFDTLE 426
|
570 580
....*....|....*....|....*.
gi 219116973 625 DGTVTLRERDSTVQVRLPKNDI-NYL 649
Cdd:PRK04173 427 DNTVTIRDRDTMEQVRVKIDELkDYL 452
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
74-417 |
2.91e-100 |
|
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: 307.98 E-value: 2.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 74 ELVLRKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMIDLWRKHFVLAES-MLEMECTCLTPEavlktsghvdrftdlmvk 152
Cdd:cd00774 3 ELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEdMLEIDSPIITPE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 153 dpqtaecfradklledaidslleanptmpveeredhlriqrqadafspteldellikydckgpsgeaytpsfpfnLMFKT 232
Cdd:cd00774 65 ---------------------------------------------------------------------------LMFKT 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 233 SIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVNPKdKSH 310
Cdd:cd00774 70 SIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE-KSH 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 311 PNFKSVTDKELVLFGRDDQLGSGKTKTIAcgEAVESGLINNETLAYFMARTQLYMEKIGMDPQRLRFRQHLATEMAHYAA 390
Cdd:cd00774 149 PWFDYWADQRLKWLPKFAQSPENLRLTDH--EKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYAS 226
|
330 340
....*....|....*....|....*..
gi 219116973 391 DCWDLEIKSSYGWQECVGHADRACYDL 417
Cdd:cd00774 227 DCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
71-646 |
1.43e-62 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 217.95 E-value: 1.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 71 AFDELVL---RKMFVVPSFEIHGGVKGLFDLGPPACSLKAAMI-DLWRKHFVLAESMLEMECTCLTPEAVLKTSGHVDRF 146
Cdd:PRK14894 5 SLDQIVAlakRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIaDWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEETF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 147 TDLMVkdpqtaECfradklledaidslleanPTMPVEEREDHlriqrqadafspteldellIKYDCKGPSGEAYTPSFPF 226
Cdd:PRK14894 85 NDPLV------DC------------------RDCKMRWRADH-------------------IQGVCPNCGSRDLTEPRPF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 227 NLMFKTSIGP--EGTSVGYLRPETAQGLFVNYRRLLDLNAGKMPFAAAQIGLGFRNEIAPRSGLLRVREFCMGEIEHFVN 304
Cdd:PRK14894 122 NMMFRTQIGPvaDSDSFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 305 PKdkshpnfksvTDKELVLFGRDDQLGsgktktiacgeavesglinnetlayfmartqlYMEKIGMDPQRLRFRQHLATE 384
Cdd:PRK14894 202 PG----------TDEEWHQRWLEARLA--------------------------------WWEQIGIPRSRITIYDVPPDE 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 385 MAHYAADCWDLEIK-SSYGWQECVGHADRACYDLEVHSRATKTsMVATQKVDPPQEmEVAKLK-FD----RKLLGQAFKG 458
Cdd:PRK14894 240 LAHYSKRTFDLMYDyPNIGVQEIEGIANRTDYDLGSHSKDQEQ-LNLTARVNPNED-STARLTyFDqasgRHVVPYVIEP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 459 DQRVVSGMLESLAESWTD--FEPIATKLENDGKTTVEGFeitkemmtwtkQKKTVHEIKFTPSVIEPSFGMGRILYSLLE 536
Cdd:PRK14894 318 SAGVGRCMLAVMCEGYAEelTKAIPGEKLAAVGDALEAF-----------LKSVGRSEKLAGEARDAILARGEALLQALP 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 537 HSFYQRES------------------------DEQ-RVVMRFTPQVAPEKCAVLPISSNPEcnEIV---DDIARDLMDSD 588
Cdd:PRK14894 387 ERLPEVEQllampgadqielgkklrgqaqpliDEHyRTVLRLKPRLAPIKVAVFPLKRNHE--GLVataKAVRRQLQVGG 464
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219116973 589 LATRVDKSTAAIGRRYSRSDELGIPFAVTVDFDTLND-------GTVTLRERDSTVQVRLPKNDI 646
Cdd:PRK14894 465 RMRTVYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQgkdpalaGTVTVRDRDTMAQERVPISEL 529
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
534-646 |
3.04e-47 |
|
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: 162.73 E-value: 3.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 534 LLEHSFYQRESDEQRVVMRFTPQVAPEKCAVLPISSNPECNEIVDDIARDLMDSDLATRVDKSTAaIGRRYSRSDELGIP 613
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDDSGS-IGRRYARQDEIGTP 79
|
90 100 110
....*....|....*....|....*....|...
gi 219116973 614 FAVTVDFDTLNDGTVTLRERDSTVQVRLPKNDI 646
Cdd:cd00858 80 FCVTVDFDTLEDGTVTIRERDSMRQVRVKIEEL 112
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
561-646 |
7.94e-19 |
|
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: 81.86 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 561 KCAVLPISSN-PECNEIVDDIARDLMDSDLATRVDKSTAAIGRRYSRSDELGIPFAVTVDFDTLNDGTVTLRERDSTVQV 639
Cdd:pfam03129 1 QVVVIPLGEKaEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*..
gi 219116973 640 RLPKNDI 646
Cdd:pfam03129 81 TVSLDEL 87
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
559-646 |
6.46e-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: 53.56 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 559 PEKCAVLPIS-SNPECNEIVDDIARDLMDSDLATRVDKSTAAIGRRYSRSDELGIPFAVTVDFDTLNDGTVTLRERDSTV 637
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
....*....
gi 219116973 638 QVRLPKNDI 646
Cdd:cd00738 81 SETLHVDEL 89
|
|
| 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 ... |
217-305 |
2.34e-08 |
|
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: 55.47 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 217 GEAYTPSFPfNLMFKTSIGPE---GTSVgYLRPETAQGLFVNYRRLLDLnAGKMPFAAAQIGLGFRNEIAPRSGLLRVRE 293
Cdd:cd00670 37 KGGHLDGYR-KEMYTFEDKGRelrDTDL-VLRPAACEPIYQIFSGEILS-YRALPLRLDQIGPCFRHEPSGRRGLMRVRE 113
|
90
....*....|..
gi 219116973 294 FCMGEIEHFVNP 305
Cdd:cd00670 114 FRQVEYVVFGEP 125
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
542-656 |
9.16e-05 |
|
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.
Pssm-ID: 239106 [Multi-domain] Cd Length: 128 Bit Score: 42.79 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 542 RESDEQRVVMRFTPQVAPEKCAVlpissnpECNEI----VDDIARDLMDSDLATRV-------DKSTAAIGRRYSRSDEL 610
Cdd:cd02426 10 RKKGRQRQVLKLHPCLAPYKVAI-------DCGKGdtaeLRDLCQGLKNELREAGLsvwpgylETQHSSLEQLLDKYDEM 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 219116973 611 GIPFAVTVDFDTLNDGTVTLRERDSTVQVRLPKNDINYLLFQIVHS 656
Cdd:cd02426 83 GVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYIAA 128
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
267-296 |
2.26e-04 |
|
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: 43.33 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|
gi 219116973 267 MPFAAAQIGLGFRNEIAPRSGLLRVREFCM 296
Cdd:cd00779 112 LPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
243-305 |
2.55e-04 |
|
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: 42.88 E-value: 2.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219116973 243 YLRPETAQGLFVNYRRLLDlnagKMPFAAAQIGLGFRNEIaPRSGLLRVREFCMGEIEHFVNP 305
Cdd:cd00768 54 YLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEG-GRRGLRRVREFTQLEGEVFGED 111
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
273-296 |
4.74e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 43.53 E-value: 4.74e-04
10 20
....*....|....*....|....
gi 219116973 273 QIGLGFRNEIAPRSGLLRVREFCM 296
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 ... |
243-323 |
7.85e-03 |
|
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: 38.16 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219116973 243 YLRPETAQGlFVNYRRLLDLNAGKMPFAAAQIGLGFRNEiAPRS--GLLRVREFCMGEIEHFVNPKDKSHPNFKSVTDKE 320
Cdd:pfam00587 12 ALKPTNEPG-HTLLFREEGLRSKDLPLKLAQFGTCFRHE-ASGDtrGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLID 89
|
...
gi 219116973 321 LVL 323
Cdd:pfam00587 90 RVY 92
|
|
| |
