|
Name |
Accession |
Description |
Interval |
E-value |
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
3-508 |
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: 856.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 3 QQEDIFKKLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPTIWKASGH 82
Cdd:COG0423 2 ASEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 83 VDAFNDPLIDNKDSKKRYRADVLIEDYLAKLDekinkevekaakrfgeafdeqqfrstnprvlenqarrdavhtrfADAM 162
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIED--------------------------------------------AEGL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 163 nanDLSELRQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGI 242
Cdd:COG0423 118 ---SLEELEELIKENNIKCPNCGGKELTEVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 243 AQIGKAFRNEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDH--DKLAHYANAAT 320
Cdd:COG0423 195 AQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHlpEELAHYAKATW 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 321 DVEFEMPFGFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAELNQSYTPYVIETSIGVDRLFLSIMAGAYQEETLEgGESR 400
Cdd:COG0423 275 DIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEVD-GEER 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 401 VVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFDFRCQYDEKDSIGKRYRRQDAIGTPYCITIDYNTMKDDTVTI 480
Cdd:COG0423 354 TVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKAFNVEYDDSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTI 433
|
490 500
....*....|....*....|....*...
gi 503990627 481 RFRDTMQQERMPIAKLHEIISDKVSMRS 508
Cdd:COG0423 434 RDRDTMEQERVPIDELKAYLAELLKGER 461
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
5-504 |
0e+00 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 813.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 5 EDIFKKLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPTIWKASGHVD 84
Cdd:PRK04173 1 MDKMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 85 AFNDPLIDNKDSKKRYRADVLIEDYLAKLDEKINKEVEkaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamna 164
Cdd:PRK04173 81 NFSDPLVECKKCKKRYRADHLIEELGIDAEGLSNEELK------------------------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 165 ndlselrQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQ 244
Cdd:PRK04173 119 -------ELIRENDIKCPECGGENWTEVRQFNLMFKTFIGPVEDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 245 IGKAFRNEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDH--DKLAHYANAATDV 322
Cdd:PRK04173 192 IGKSFRNEITPRNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRFREHlpEELAHYSKATWDI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 323 EFEMPFG--FKEVEGIHSRTDFDLSQHEKFSGKKIQYFD-AELNQSYTPYVIETSIGVDRLFLSIMAGAYQEETLEGGES 399
Cdd:PRK04173 272 EYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDLSYFDdETTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 400 RVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFDFRCQYDEKDSIGKRYRRQDAIGTPYCITIDYNTMKDDTVT 479
Cdd:PRK04173 352 RTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKDFNVDYDDSGSIGKRYRRQDEIGTPFCITVDFDTLEDNTVT 431
|
490 500
....*....|....*....|....*
gi 503990627 480 IRFRDTMQQERMPIAKLHEIISDKV 504
Cdd:PRK04173 432 IRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
10-502 |
7.97e-157 |
|
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: 457.77 E-value: 7.97e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 10 KLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLhENIVGIDSAIFMHPTIWKASGHVDAFNDP 89
Cdd:TIGR00389 5 VIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKN-ERVLEIDTPIITPEEVLKASGHVDNFTDW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 90 LIDNKDSKKRYRADVLIEDYLAKLDEkiNKEVEkaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamnandlsE 169
Cdd:TIGR00389 84 MVDCKSCKERFRADHLIEEKLGKRLW--GFSGP----------------------------------------------E 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 170 LRQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGstADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAF 249
Cdd:TIGR00389 116 LNEVMEKYDINCPNCGGENLTEVRSFNLMFQTEIG--VVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSF 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 250 RNEIVARQFIFRMREFEQMEMQFFVRPGE-ELKWFEQWKEMRMKWHR--------------------------------- 295
Cdd:TIGR00389 194 RNEISPRNGLFRVREFEQAEIEFFVHPLDkSHPKFEEVKQDILPLLPrqmqesgigeavesgmienetlgyfiarvkqfl 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 296 -NLGMGDHKYRFHDHDK--LAHYANAATDVEFEMPFGFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAELN--------- 363
Cdd:TIGR00389 274 lEIGINPDKLRFRQHDKneMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEprevtkwei 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 364 ---------------------------------------------------------QSYTPYVIETSIGVDRLFLSIMA 386
Cdd:TIGR00389 354 epnkkkfgpkfrkdakkiesnlseddleereeeldkneveldkdlveiemvtevvhgEKYIPHVIEPSFGIDRIIYALLE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 387 GAYQEETLEgGESRVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFD-FRCQYDEKDSIGKRYRRQDAIGTPYC 465
Cdd:TIGR00389 434 HSYQEEVLD-GEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTgIRIKYDDSGTIGKRYRRADEIGTPFC 512
|
570 580 590
....*....|....*....|....*....|....*..
gi 503990627 466 ITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISD 502
Cdd:TIGR00389 513 VTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKK 549
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
11-382 |
1.30e-107 |
|
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: 321.08 E-value: 1.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 11 LISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPtiwkasghvdafndpl 90
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 91 idnkdskkryradvliedylakldekinkevekaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamnandlsel 170
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 171 rqiildceivcpvsgtrnwtevrqfnLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAFR 250
Cdd:cd00774 65 --------------------------LMFKTSIGPVESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 251 NEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDHDK--LAHYANAATDVEFEMPF 328
Cdd:cd00774 119 NEISPRNGLFRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKeeLAHYANETLDYFYAFPH 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 503990627 329 GFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAElNQSYTPYVIETSIGVDRLFL 382
Cdd:cd00774 199 GFLELEGIANRGDRFLQHHPNESAHYASDCWDA-EKLYVPGWIEVSGGADRTDY 251
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
413-503 |
1.33e-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: 83.40 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 413 KLAVLPLVRKDG-LSEKAEEILHMLR-FDFRCQYDEKD-SIGKRYRRQDAIGTPYCITIDYNTMKDDTVTIRFRDTMQQE 489
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRaAGIRVELDDRNeSIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 503990627 490 RMPIAKLHEIISDK 503
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
3-508 |
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: 856.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 3 QQEDIFKKLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPTIWKASGH 82
Cdd:COG0423 2 ASEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 83 VDAFNDPLIDNKDSKKRYRADVLIEDYLAKLDekinkevekaakrfgeafdeqqfrstnprvlenqarrdavhtrfADAM 162
Cdd:COG0423 82 VDGFTDPLVDCKECKKRYRADHLIEEYLAIED--------------------------------------------AEGL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 163 nanDLSELRQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGI 242
Cdd:COG0423 118 ---SLEELEELIKENNIKCPNCGGKELTEVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 243 AQIGKAFRNEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDH--DKLAHYANAAT 320
Cdd:COG0423 195 AQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHlpEELAHYAKATW 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 321 DVEFEMPFGFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAELNQSYTPYVIETSIGVDRLFLSIMAGAYQEETLEgGESR 400
Cdd:COG0423 275 DIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEVD-GEER 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 401 VVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFDFRCQYDEKDSIGKRYRRQDAIGTPYCITIDYNTMKDDTVTI 480
Cdd:COG0423 354 TVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKAFNVEYDDSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTI 433
|
490 500
....*....|....*....|....*...
gi 503990627 481 RFRDTMQQERMPIAKLHEIISDKVSMRS 508
Cdd:COG0423 434 RDRDTMEQERVPIDELKAYLAELLKGER 461
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
5-504 |
0e+00 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 813.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 5 EDIFKKLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPTIWKASGHVD 84
Cdd:PRK04173 1 MDKMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 85 AFNDPLIDNKDSKKRYRADVLIEDYLAKLDEKINKEVEkaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamna 164
Cdd:PRK04173 81 NFSDPLVECKKCKKRYRADHLIEELGIDAEGLSNEELK------------------------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 165 ndlselrQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQ 244
Cdd:PRK04173 119 -------ELIRENDIKCPECGGENWTEVRQFNLMFKTFIGPVEDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 245 IGKAFRNEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDH--DKLAHYANAATDV 322
Cdd:PRK04173 192 IGKSFRNEITPRNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRFREHlpEELAHYSKATWDI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 323 EFEMPFG--FKEVEGIHSRTDFDLSQHEKFSGKKIQYFD-AELNQSYTPYVIETSIGVDRLFLSIMAGAYQEETLEGGES 399
Cdd:PRK04173 272 EYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDLSYFDdETTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 400 RVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFDFRCQYDEKDSIGKRYRRQDAIGTPYCITIDYNTMKDDTVT 479
Cdd:PRK04173 352 RTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRKDFNVDYDDSGSIGKRYRRQDEIGTPFCITVDFDTLEDNTVT 431
|
490 500
....*....|....*....|....*
gi 503990627 480 IRFRDTMQQERMPIAKLHEIISDKV 504
Cdd:PRK04173 432 IRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
10-502 |
7.97e-157 |
|
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: 457.77 E-value: 7.97e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 10 KLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLhENIVGIDSAIFMHPTIWKASGHVDAFNDP 89
Cdd:TIGR00389 5 VIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKN-ERVLEIDTPIITPEEVLKASGHVDNFTDW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 90 LIDNKDSKKRYRADVLIEDYLAKLDEkiNKEVEkaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamnandlsE 169
Cdd:TIGR00389 84 MVDCKSCKERFRADHLIEEKLGKRLW--GFSGP----------------------------------------------E 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 170 LRQIILDCEIVCPVSGTRNWTEVRQFNLMFATEMGstADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAF 249
Cdd:TIGR00389 116 LNEVMEKYDINCPNCGGENLTEVRSFNLMFQTEIG--VVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSF 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 250 RNEIVARQFIFRMREFEQMEMQFFVRPGE-ELKWFEQWKEMRMKWHR--------------------------------- 295
Cdd:TIGR00389 194 RNEISPRNGLFRVREFEQAEIEFFVHPLDkSHPKFEEVKQDILPLLPrqmqesgigeavesgmienetlgyfiarvkqfl 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 296 -NLGMGDHKYRFHDHDK--LAHYANAATDVEFEMPFGFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAELN--------- 363
Cdd:TIGR00389 274 lEIGINPDKLRFRQHDKneMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEprevtkwei 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 364 ---------------------------------------------------------QSYTPYVIETSIGVDRLFLSIMA 386
Cdd:TIGR00389 354 epnkkkfgpkfrkdakkiesnlseddleereeeldkneveldkdlveiemvtevvhgEKYIPHVIEPSFGIDRIIYALLE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 387 GAYQEETLEgGESRVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLRFD-FRCQYDEKDSIGKRYRRQDAIGTPYC 465
Cdd:TIGR00389 434 HSYQEEVLD-GEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTgIRIKYDDSGTIGKRYRRADEIGTPFC 512
|
570 580 590
....*....|....*....|....*....|....*..
gi 503990627 466 ITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISD 502
Cdd:TIGR00389 513 VTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKK 549
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
10-504 |
2.66e-136 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 404.77 E-value: 2.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 10 KLISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPTIWKASGHVDAFNDP 89
Cdd:PRK14894 8 QIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEETFNDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 90 LIDNKDSKKRYRADvliedylakldekinkevekaakrfgeafdeqqfrstnprvlenqarrdavHTRFadamnandlse 169
Cdd:PRK14894 88 LVDCRDCKMRWRAD---------------------------------------------------HIQG----------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 170 lrqiildceiVCPVSGTRNWTEVRQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAF 249
Cdd:PRK14894 106 ----------VCPNCGSRDLTEPRPFNMMFRTQIGPVADSDSFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 250 RNEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHD--HDKLAHYANAATDVEFEMP 327
Cdd:PRK14894 176 RNEINPRNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIYDvpPDELAHYSKRTFDLMYDYP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 328 -FGFKEVEGIHSRTDFDLSQHEK---------------FSGKKIQYFDAELNQSYTPYVIETSIGVDRLFLSIMAGAYQE 391
Cdd:PRK14894 256 nIGVQEIEGIANRTDYDLGSHSKdqeqlnltarvnpneDSTARLTYFDQASGRHVVPYVIEPSAGVGRCMLAVMCEGYAE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 392 ET-------------------------------------LEGGES----------------------------------- 399
Cdd:PRK14894 336 ELtkaipgeklaavgdaleaflksvgrseklageardaiLARGEAllqalperlpeveqllampgadqielgkklrgqaq 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 400 -------RVVLKLPPALAPVKLAVLPLVRK-DGLSEKAEEILHMLRF--DFRCQYDEKDSIGKRYRRQDAIGTPYCITID 469
Cdd:PRK14894 416 plidehyRTVLRLKPRLAPIKVAVFPLKRNhEGLVATAKAVRRQLQVggRMRTVYDDTGAIGKLYRRQDEIGTPFCITVD 495
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 503990627 470 YNTMKDD-------TVTIRFRDTMQQERMPIAKLHEIISDKV 504
Cdd:PRK14894 496 FDTIGQGkdpalagTVTVRDRDTMAQERVPISELEAYLRDRV 537
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
11-382 |
1.30e-107 |
|
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: 321.08 E-value: 1.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 11 LISHCKEYGFVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLLHENIVGIDSAIFMHPtiwkasghvdafndpl 90
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 91 idnkdskkryradvliedylakldekinkevekaakrfgeafdeqqfrstnprvlenqarrdavhtrfadamnandlsel 170
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 171 rqiildceivcpvsgtrnwtevrqfnLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAFR 250
Cdd:cd00774 65 --------------------------LMFKTSIGPVESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 251 NEIVARQFIFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDHDK--LAHYANAATDVEFEMPF 328
Cdd:cd00774 119 NEISPRNGLFRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKeeLAHYANETLDYFYAFPH 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 503990627 329 GFKEVEGIHSRTDFDLSQHEKFSGKKIQYFDAElNQSYTPYVIETSIGVDRLFL 382
Cdd:cd00774 199 GFLELEGIANRGDRFLQHHPNESAHYASDCWDA-EKLYVPGWIEVSGGADRTDY 251
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
20-508 |
9.90e-76 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 251.97 E-value: 9.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 20 FVFPSSDIYDGLGAVYDYGQYGVELKNNLKKYWWDSMVLlHENIVGIDSAIFMHPTIWKASGHVDAFNDPLIDNKDSKKR 99
Cdd:PLN02734 87 FYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVL-EENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 100 YRADVLIEDYL-AKLDEKINKEVEKAAkrfgeafdeqqfrstnpRVLENQARrdavhtrfADAMNANDLSELrqiILDCE 178
Cdd:PLN02734 166 FRADHLLKDFCeEKLEKDLTISAEKAA-----------------ELKDVLAV--------LDDLSAEELGAK---IKEYG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 179 IVCPVSGTrNWTEVRQFNLMFATEMGSTadGAMKVYLRPETAQGIFVNYLNVQKTGRMKLPFGIAQIGKAFRNEIVARQF 258
Cdd:PLN02734 218 IKAPDTKN-PLSDPYPFNLMFQTSIGPS--GLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 259 IFRMREFEQMEMQFFVRPGE------------ELKWFEQWKEMRMKWHR------------------------------N 296
Cdd:PLN02734 295 LLRVREFTLAEIEHFVDPEDkshpkfsevadlEFLLFPREEQLGGQKAKpmrlgeavskgivnnetlgyfigrtylfltK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 297 LGMGDHKYRFHDH--DKLAHYANAATDVEFEMPFGFKEVEGIHSRTDFDLSQH-----------EKF------------- 350
Cdd:PLN02734 375 LGIDKERLRFRQHlaNEMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHsdkskvplvahEKFaeprevevlvivp 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 351 ------------------------------------SGKKIQYFDAELNQS---------------------YTPYVIET 373
Cdd:PLN02734 455 nkkelglafkgdqkvvvealeamnekeamemkakleSKGEAEFYVCTLGKEveikknmvsiskekkkehqrvFTPSVIEP 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 374 SIGVDRLFLSIMAGAYQeeTLEGGESRVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHML-RFDFRCQYDEK-DSIG 451
Cdd:PLN02734 535 SFGIGRIIYCLFEHSFY--TRPGDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELtAAGISHKIDITgTSIG 612
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 503990627 452 KRYRRQDAIGTPYCITIDYntmkDDTVTIRFRDTMQQERMPIAKLHEIISDKVSMRS 508
Cdd:PLN02734 613 KRYARTDELGVPFAVTVDS----DGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRM 665
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
384-504 |
5.05e-52 |
|
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: 172.36 E-value: 5.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 384 IMAGAYQEEtlEGGESRVVLKLPPALAPVKLAVLPLVRKDGLSEKAEEILHMLR-FDFRCQYDEKDSIGKRYRRQDAIGT 462
Cdd:cd00858 1 LLEHSFRVR--EGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELReLGFSVKYDDSGSIGRRYARQDEIGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503990627 463 PYCITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISDKV 504
Cdd:cd00858 79 PFCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELI 120
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
193-380 |
8.90e-27 |
|
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: 107.59 E-value: 8.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 193 RQFNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNvqktGRMKLPFGIAQIGKAFRNEIvARQFIFRMREFEQMEMQF 272
Cdd:cd00768 33 EKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVS----HIRKLPLRLAEIGPAFRNEG-GRRGLRRVREFTQLEGEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 273 FVRPGEELKWFEQWKEMRMKWHRNLGMGDHKYRFHDH--DKLAHYANAATDVEFEMPFG-FKEVEGIHSRTDFDLSQHEk 349
Cdd:cd00768 108 FGEDGEEASEFEELIELTEELLRALGIKLDIVFVEKTpgEFSPGGAGPGFEIEVDHPEGrGLEIGSGGYRQDEQARAAD- 186
|
170 180 190
....*....|....*....|....*....|.
gi 503990627 350 fsgkkiQYFDAELNQSYTPYVIETSIGVDRL 380
Cdd:cd00768 187 ------LYFLDEALEYRYPPTIGFGLGLERL 211
|
|
| 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 ... |
195-384 |
1.53e-22 |
|
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: 96.31 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 195 FNLMFATEMGSTADGAMKVYLRPETAQGIFVNYLNVQKTGRmKLPFGIAQIGKAFRNEIVARQFIFRMREFEQMEMQFFV 274
Cdd:cd00670 45 RKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEILSYR-ALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 275 RPGEELKWFEQWKEMRMKWHRNLGM-------GDHKYRFHDHDKLAHYANAATDVEFEMPF--GFKEVEGIHSRTDFDLS 345
Cdd:cd00670 124 EPEEAEEERREWLELAEEIARELGLpvrvvvaDDPFFGRGGKRGLDAGRETVVEFELLLPLpgRAKETAVGSANVHLDHF 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 503990627 346 QHEKfsgkkiqYFDAELNQSYtPYVIETSIGVDRLFLSI 384
Cdd:cd00670 204 GASF-------KIDEDGGGRA-HTGCGGAGGEERLVLAL 234
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
413-503 |
1.33e-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: 83.40 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 413 KLAVLPLVRKDG-LSEKAEEILHMLR-FDFRCQYDEKD-SIGKRYRRQDAIGTPYCITIDYNTMKDDTVTIRFRDTMQQE 489
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRaAGIRVELDDRNeSIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 503990627 490 RMPIAKLHEIISDK 503
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
411-501 |
1.61e-13 |
|
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: 66.27 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 411 PVKLAVLPLVRK-DGLSEKAEEIL-HMLRFDFRCQYDEKD-SIGKRYRRQDAIGTPYCITIDYNTMKDDTVTIRFRDTMQ 487
Cdd:cd00738 1 PIDVAIVPLTDPrVEAREYAQKLLnALLANGIRVLYDDRErKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 503990627 488 QERMPIAKLHEIIS 501
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
355-505 |
4.54e-07 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 52.57 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 355 IQYFDAElNQSYTPYVIETSI--GVDRLFLSIMAGAYQEEtlEGGEsrvVLKLPPALAPVKLAVLPLvrKDGLSEKAEEI 432
Cdd:PRK03991 447 IKYVDEN-GEEKYPIILHCSPtgSIERVIYALLEKAAKEE--EEGK---VPMLPTWLSPTQVRVIPV--SERHLDYAEEV 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503990627 433 LHMLR-FDFRCQYDEKD-SIGKRYRrqDAiGT---PYCITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISDKVS 505
Cdd:PRK03991 519 ADKLEaAGIRVDVDDRDeSLGKKIR--DA-GKewiPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEETK 593
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
214-386 |
4.68e-06 |
|
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: 47.02 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 214 YLRPETAQGIfVNYLNVQKTGRMKLPFGIAQIGKAFRNEIVARQF-IFRMREFEQMEMQFFVRPGEELKWFEQWKEMRMK 292
Cdd:pfam00587 12 ALKPTNEPGH-TLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTRgLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLIDR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 293 WHRNLGMGDHKYRFHDHDKLAHYANaATDVEFEMP-FG-FKEVEGIHSRTDFdlsQHEKFSGKkiqyFDAELNQSYTPYV 370
Cdd:pfam00587 91 VYSRLGLEVRVVRLSNSDGSAFYGP-KLDFEVVFPsLGkQRQTGTIQNDGFR---LPRRLGIR----YKDEDNESKFPYM 162
|
170
....*....|....*..
gi 503990627 371 IE-TSIGVDRLFLSIMA 386
Cdd:pfam00587 163 IHrAGLGVERFLAAILE 179
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
403-503 |
6.20e-06 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 46.91 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 403 LKLPPALAPVKLAVLPLVRKDG----LSEKAEEILHMLR-FDFRCQYDEKD--SIGKRYRRQDAIGTPYCITIDYNTMKD 475
Cdd:cd00862 2 LVLPPRVAPIQVVIVPIGIKDEkreeVLEAADELAERLKaAGIRVHVDDRDnyTPGWKFNDWELKGVPLRIEIGPRDLEK 81
|
90 100
....*....|....*....|....*...
gi 503990627 476 DTVTIRFRDTMQQERMPIAKLHEIISDK 503
Cdd:cd00862 82 NTVVIVRRDTGEKKTVPLAELVEKVPEL 109
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
393-496 |
6.95e-06 |
|
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: 45.49 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 393 TLEGGESRVVLKLPPALAPVKLAvLPLVRKDG--LSEKAEEILHMLR---------FDFRCQydekDSIGKRYRRQDAIG 461
Cdd:cd02426 9 GRKKGRQRQVLKLHPCLAPYKVA-IDCGKGDTaeLRDLCQGLKNELReaglsvwpgYLETQH----SSLEQLLDKYDEMG 83
|
90 100 110
....*....|....*....|....*....|....*
gi 503990627 462 TPYCITIDYNTMKDDTVTIRFRDTMQQERMPIAKL 496
Cdd:cd02426 84 VLFTLLISEQTLENGLLQLRSRDTTLKETIHISDL 118
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
374-505 |
2.65e-05 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 46.65 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 374 SIGVDRLFLSIMAgayqeetlEGgesrvvlKLPPALAPVKLAVLPLvrKDGLSEKAEEILHMLR-FDFRCQYD-EKDSIG 451
Cdd:COG0124 305 AIGLERLLLLLEE--------LG-------LLPAAEPPPDVYVVPL--GEEARAEALKLAQELRaAGIRVELDlGGRKLK 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503990627 452 KRYRRQDAIGTPYCITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISDKVS 505
Cdd:COG0124 368 KQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
404-509 |
1.85e-04 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 44.25 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 404 KLPPALAPVKLAVLPLVrkDGLSEKAEEILHMLR-FDFRCQYDEKD-SIGKRYRrqDA----IgtPYCITIDYNTMKDDT 477
Cdd:COG0441 532 AFPLWLAPVQVVVLPIS--DKHADYAKEVAKKLRaAGIRVEVDLRNeKIGYKIR--EAqlqkV--PYMLVVGDKEVENGT 605
|
90 100 110
....*....|....*....|....*....|..
gi 503990627 478 VTIRFRDTMQQERMPIAKLHEIISDKVSMRSL 509
Cdd:COG0441 606 VSVRRRGGGDLGTMSLDEFIARLKEEIRSRSL 637
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
287-508 |
3.75e-04 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 43.20 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 287 KEMRMKWHRNLGMGDH---KYRFHDHDKLAHYANAAT-DVEFEMPfgfkevegihsrtdfdlsqhEKFSgkkIQYFDaEL 362
Cdd:PRK12444 448 QSLNYKYRLNEGDGAFygpKIDFHIKDALNRSHQCGTiQLDFQMP--------------------EKFD---LNYID-EK 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503990627 363 NQSYTPYVIETSI--GVDRlFLSIM----AGAYqeetleggesrvvlklPPALAPVKLAVLPlVRKDGLSEKAEEILHML 436
Cdd:PRK12444 504 NEKRRPVVIHRAVlgSLDR-FLAILiehfGGAF----------------PAWLAPVQVKVIP-VSNAVHVQYADEVADKL 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503990627 437 R-FDFRCQYDEKDS-IGKRYRRQDAIGTPYCITIDYNTMKDDTVTIRFRDTMQQERMPIAKLHEIISDKVSMRS 508
Cdd:PRK12444 566 AqAGIRVERDERDEkLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIKNRK 639
|
|
| |
