|
Name |
Accession |
Description |
Interval |
E-value |
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
7-598 |
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: 868.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 7 SERDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIMEENMLQVDGPMLTPYDVLKTSGHVDKF 86
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 87 TDWMCRNPKTGEYYRADHLIEQTLKKRLldkdvnpqdmknmekilttiDGFSGPELNLVMQEYNINDP-VTNDVLDALTS 165
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGKRL--------------------WGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 166 FNLMFETKIGASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDP 245
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 246 LNKSHAKFNEVLNEEIPLLSRRLQESGevqlpvkmtIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKN 325
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG---------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 326 EMAHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVKQKLDTPKERTEWVVEVNKKFFGSKFKQKAKLI 405
Cdd:TIGR00389 292 EMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 406 EsvlSKFSQDELIRRHEELEKNgeftcqvngqIVKLDSSLVTIKMKTTLQHIREYIPNVIEPSFGLGRIIYCIFDHCFQV 485
Cdd:TIGR00389 372 E---SNLSEDDLEEREEELDKN----------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 486 RV-DSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSNTsIGKKYARNDELGTPFGITIDF 564
Cdd:TIGR00389 439 EVlDGEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDDSGT-IGKRYRRADEIGTPFCVTIDF 517
|
570 580 590
....*....|....*....|....*....|....
gi 6325338 565 ETIKDQTVTLRERNSMRQVRGTITDVISTIDKML 598
Cdd:TIGR00389 518 ETLEDETVTIRERDSMKQVRVKIKELPSYIKKLL 551
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
9-613 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 764.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 9 RDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIMEENMLQVDGPMLTPYDVLKTSGHVDKFTD 88
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 89 WMCRNPKTGEYYRADHLIEQTLKKRLLDKDVNPQDMK-NMEKILTTIDGFSGPELNLVMQEYNINDPVTNDVLDALTSFN 167
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKDLTISAEKAaELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 168 LMFETKIGASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDPLN 247
Cdd:PLN02734 235 LMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPED 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 248 KSHAKFNEVLNEEIPLLSRRLQESGevQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKNEM 327
Cdd:PLN02734 315 KSHPKFSEVADLEFLLFPREEQLGG--QKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEM 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 328 AHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVKQKLDTPKERTEWVVEVNKKFFGSKFKQKAKLIES 407
Cdd:PLN02734 393 AHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 408 VLSKFSQDELIRRHEELEKNGEFTCQV--NGQIVKLDSSLVTIKMKTTLQHIREYIPNVIEPSFGLGRIIYCIFDHCFQV 485
Cdd:PLN02734 473 ALEAMNEKEAMEMKAKLESKGEAEFYVctLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYT 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 486 RVDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFe 565
Cdd:PLN02734 553 RPGDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS- 631
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6325338 566 tikDQTVTLRERNSMRQVRGTITDVISTIDKMLHnpDESDWDKSTFGL 613
Cdd:PLN02734 632 ---DGSVTIRERDSKDQVRVPVEEVASVVKDLTD--GRMTWEDVTAKY 674
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
4-598 |
1.23e-165 |
|
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: 480.76 E-value: 1.23e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 4 MSNSER-DKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIME-ENMLQVDGPMLTPYDVLKTSG 81
Cdd:COG0423 1 MASEDTmEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 82 HVDKFTDWMCRNPKTGEYYRADHLIEQTLKKRLLDkdvnpqdmknmekilttidGFSGPELNLVMQEYNINDPVTNDVld 161
Cdd:COG0423 81 HVDGFTDPLVDCKECKKRYRADHLIEEYLAIEDAE-------------------GLSLEELEELIKENNIKCPNCGGK-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 162 ALT---SFNLMFETKIGA--SGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLM 236
Cdd:COG0423 140 ELTevrQFNLMFKTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 237 AEIEHFVDPlnkshakfnevlneeipllsrrlqesGEvqlpvkmtigeavnsgmvENETLGYFMARVHQFLLNIGINKDK 316
Cdd:COG0423 220 MELEFFVDP--------------------------GT------------------DNEWFAYWLALRKKWLLSLGIDPEN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 317 FRFRQHLKNEMAHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVkqkldtpkertewvvevnkkffgs 396
Cdd:COG0423 256 LRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTY------------------------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 397 kFKQkakliesvlskfsqdelirrheelEKNgeftcqvngqivkldsslvtikmkttlqhiREYIPNVIEPSFGLGRIIY 476
Cdd:COG0423 312 -FDP------------------------ETG------------------------------EKYIPHVIEPSFGVDRLLL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 477 CIFDHCFQVR-VDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKR-EIYFkiDDSNtSIGKKYARNDEL 554
Cdd:COG0423 337 AFLEHAYTEEeVDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKAfNVEY--DDSG-SIGRRYRRQDEI 413
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6325338 555 GTPFGITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKML 598
Cdd:COG0423 414 GTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAELL 457
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
12-360 |
7.82e-111 |
|
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: 332.63 E-value: 7.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 12 LESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFI-MEENMLQVDGPMLTPYdvlktsghvdkftdwm 90
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVlEEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 91 crnpktgeyyradhlieqtlkkrlldkdvnpqdmknmekilttidgfsgpelnlvmqeynindpvtndvldaltsfnLMF 170
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 171 ETKIG--ASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDPlNK 248
Cdd:cd00774 68 KTSIGpvESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 249 SHAKFNEVLNEEIPLLSRRLQEsgevQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKNEMA 328
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQS----PENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESA 222
|
330 340 350
....*....|....*....|....*....|..
gi 6325338 329 HYATDCWDGEILTSYGWIECVGCADRAAFDLT 360
Cdd:cd00774 223 HYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
505-597 |
5.68e-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: 90.72 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 505 KVFVTTISNNDG-FPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRERNSMRQV 583
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 6325338 584 RGTITDVISTIDKM 597
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
7-598 |
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: 868.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 7 SERDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIMEENMLQVDGPMLTPYDVLKTSGHVDKF 86
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 87 TDWMCRNPKTGEYYRADHLIEQTLKKRLldkdvnpqdmknmekilttiDGFSGPELNLVMQEYNINDP-VTNDVLDALTS 165
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGKRL--------------------WGFSGPELNEVMEKYDINCPnCGGENLTEVRS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 166 FNLMFETKIGASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDP 245
Cdd:TIGR00389 141 FNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 246 LNKSHAKFNEVLNEEIPLLSRRLQESGevqlpvkmtIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKN 325
Cdd:TIGR00389 221 LDKSHPKFEEVKQDILPLLPRQMQESG---------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 326 EMAHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVKQKLDTPKERTEWVVEVNKKFFGSKFKQKAKLI 405
Cdd:TIGR00389 292 EMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 406 EsvlSKFSQDELIRRHEELEKNgeftcqvngqIVKLDSSLVTIKMKTTLQHIREYIPNVIEPSFGLGRIIYCIFDHCFQV 485
Cdd:TIGR00389 372 E---SNLSEDDLEEREEELDKN----------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 486 RV-DSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSNTsIGKKYARNDELGTPFGITIDF 564
Cdd:TIGR00389 439 EVlDGEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKTGIRIKYDDSGT-IGKRYRRADEIGTPFCVTIDF 517
|
570 580 590
....*....|....*....|....*....|....
gi 6325338 565 ETIKDQTVTLRERNSMRQVRGTITDVISTIDKML 598
Cdd:TIGR00389 518 ETLEDETVTIRERDSMKQVRVKIKELPSYIKKLL 551
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
9-613 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 764.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 9 RDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIMEENMLQVDGPMLTPYDVLKTSGHVDKFTD 88
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 89 WMCRNPKTGEYYRADHLIEQTLKKRLLDKDVNPQDMK-NMEKILTTIDGFSGPELNLVMQEYNINDPVTNDVLDALTSFN 167
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKDLTISAEKAaELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 168 LMFETKIGASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDPLN 247
Cdd:PLN02734 235 LMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPED 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 248 KSHAKFNEVLNEEIPLLSRRLQESGevQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKNEM 327
Cdd:PLN02734 315 KSHPKFSEVADLEFLLFPREEQLGG--QKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEM 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 328 AHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVKQKLDTPKERTEWVVEVNKKFFGSKFKQKAKLIES 407
Cdd:PLN02734 393 AHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 408 VLSKFSQDELIRRHEELEKNGEFTCQV--NGQIVKLDSSLVTIKMKTTLQHIREYIPNVIEPSFGLGRIIYCIFDHCFQV 485
Cdd:PLN02734 473 ALEAMNEKEAMEMKAKLESKGEAEFYVctLGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYT 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 486 RVDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFe 565
Cdd:PLN02734 553 RPGDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS- 631
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6325338 566 tikDQTVTLRERNSMRQVRGTITDVISTIDKMLHnpDESDWDKSTFGL 613
Cdd:PLN02734 632 ---DGSVTIRERDSKDQVRVPVEEVASVVKDLTD--GRMTWEDVTAKY 674
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
4-598 |
1.23e-165 |
|
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: 480.76 E-value: 1.23e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 4 MSNSER-DKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFIME-ENMLQVDGPMLTPYDVLKTSG 81
Cdd:COG0423 1 MASEDTmEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 82 HVDKFTDWMCRNPKTGEYYRADHLIEQTLKKRLLDkdvnpqdmknmekilttidGFSGPELNLVMQEYNINDPVTNDVld 161
Cdd:COG0423 81 HVDGFTDPLVDCKECKKRYRADHLIEEYLAIEDAE-------------------GLSLEELEELIKENNIKCPNCGGK-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 162 ALT---SFNLMFETKIGA--SGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLM 236
Cdd:COG0423 140 ELTevrQFNLMFKTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 237 AEIEHFVDPlnkshakfnevlneeipllsrrlqesGEvqlpvkmtigeavnsgmvENETLGYFMARVHQFLLNIGINKDK 316
Cdd:COG0423 220 MELEFFVDP--------------------------GT------------------DNEWFAYWLALRKKWLLSLGIDPEN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 317 FRFRQHLKNEMAHYATDCWDGEILTSYGWIECVGCADRAAFDLTVHSKKTGRSLTVkqkldtpkertewvvevnkkffgs 396
Cdd:COG0423 256 LRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTY------------------------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 397 kFKQkakliesvlskfsqdelirrheelEKNgeftcqvngqivkldsslvtikmkttlqhiREYIPNVIEPSFGLGRIIY 476
Cdd:COG0423 312 -FDP------------------------ETG------------------------------EKYIPHVIEPSFGVDRLLL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 477 CIFDHCFQVR-VDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKR-EIYFkiDDSNtSIGKKYARNDEL 554
Cdd:COG0423 337 AFLEHAYTEEeVDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRKAfNVEY--DDSG-SIGRRYRRQDEI 413
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6325338 555 GTPFGITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKML 598
Cdd:COG0423 414 GTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAELL 457
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
10-598 |
1.21e-159 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 465.37 E-value: 1.21e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 10 DKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFI-MEENMLQVDGPMLTPYDVLKTSGHVDKFTD 88
Cdd:PRK04173 5 EKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVqEREDVVGIDSPIIMPPEVWEASGHVDNFSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 89 WMCRNPKTGEYYRADHLIEQTLKKRLLDKDvnpqdmknmekilttidgfsgPELNLVMQEYNINDPVTNDVLdaLT---S 165
Cdd:PRK04173 85 PLVECKKCKKRYRADHLIEELGIDAEGLSN---------------------EELKELIRENDIKCPECGGEN--WTevrQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 166 FNLMFETKIGA--SGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFV 243
Cdd:PRK04173 142 FNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 244 DPlnkshakfnevlneeipllsrrlqesGEvqlpvkmtigeavnsgmvENETLGYFMARVHQFLLNIGINKDKFRFRQHL 323
Cdd:PRK04173 222 KP--------------------------GT------------------DNEWFAYWIELRKNWLLDLGIDPENLRFREHL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 324 KNEMAHYATDCWDGEILTSYG--WIECVGCADRAAFDLTVHSKKTGRSLTVkqkldtpkertewvvevnkkffgskFKQk 401
Cdd:PRK04173 258 PEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDLSY-------------------------FDD- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 402 akliesvlskfsqdelirrheelEKNGEftcqvngqivkldsslvtikmkttlqhirEYIPNVIEPSFGLGRIIYCIFDH 481
Cdd:PRK04173 312 -----------------------ETTGE-----------------------------KYIPYVIEPSAGLDRLLLAFLED 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 482 CF--QVRVDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKreiYFKID-DSNTSIGKKYARNDELGTPF 558
Cdd:PRK04173 340 AYteEELGGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAELRK---DFNVDyDDSGSIGKRYRRQDEIGTPF 416
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 6325338 559 GITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKML 598
Cdd:PRK04173 417 CITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
12-360 |
7.82e-111 |
|
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: 332.63 E-value: 7.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 12 LESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLIRLWREHFI-MEENMLQVDGPMLTPYdvlktsghvdkftdwm 90
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVlEEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 91 crnpktgeyyradhlieqtlkkrlldkdvnpqdmknmekilttidgfsgpelnlvmqeynindpvtndvldaltsfnLMF 170
Cdd:cd00774 65 -----------------------------------------------------------------------------LMF 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 171 ETKIG--ASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHFVDPlNK 248
Cdd:cd00774 68 KTSIGpvESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDP-EK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 249 SHAKFNEVLNEEIPLLSRRLQEsgevQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNIGINKDKFRFRQHLKNEMA 328
Cdd:cd00774 147 SHPWFDYWADQRLKWLPKFAQS----PENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESA 222
|
330 340 350
....*....|....*....|....*....|..
gi 6325338 329 HYATDCWDGEILTSYGWIECVGCADRAAFDLT 360
Cdd:cd00774 223 HYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
478-599 |
1.14e-55 |
|
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: 184.30 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 478 IFDHCFQVRVDSESRGFFSFPLQIAPIKVFVTTISNNDGFPAILKRISQALRKREIYFKIDDSnTSIGKKYARNDELGTP 557
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDDS-GSIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6325338 558 FGITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKMLH 599
Cdd:cd00858 80 FCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
4-590 |
1.93e-54 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 194.06 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 4 MSNSERDKLESTLRRRFFYTPSFEIYGGVSGLFDLGPPGCQLQNNLI-RLWREHFIMEENMLQVDGPMLTPYDVLKTSGH 82
Cdd:PRK14894 1 MPATSLDQIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIaDWWRTNVYERDDMEGLDAAILMNRLVWKYSGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 83 VDKFTDWM--CRNPKTgeYYRADHLieqtlkkrlldKDVNPQdmknmekilttidgfsgpelnlvMQEYNINDPvtndvl 160
Cdd:PRK14894 81 EETFNDPLvdCRDCKM--RWRADHI-----------QGVCPN-----------------------CGSRDLTEP------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 161 dalTSFNLMFETKIG--ASGQLKAFLRPETAQGQFLNFNKLLEINQGKIPFASASIGKSFRNEISPRSGLLRVREFLMAE 238
Cdd:PRK14894 119 ---RPFNMMFRTQIGpvADSDSFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQME 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 239 IEHFVDPlnkshakfnevlneeipllsrrlqesgevqlpvkmtigeavnsGMVENETLGYFMARVhQFLLNIGINKDKFR 318
Cdd:PRK14894 196 IEYFVMP-------------------------------------------GTDEEWHQRWLEARL-AWWEQIGIPRSRIT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 319 FRQHLKNEMAHYATDCWDgeILTSY---GWIECVGCADRAAFDLTVHSKKTGR-SLT--VKQKLDTPKERTEWVVEVNKK 392
Cdd:PRK14894 232 IYDVPPDELAHYSKRTFD--LMYDYpniGVQEIEGIANRTDYDLGSHSKDQEQlNLTarVNPNEDSTARLTYFDQASGRH 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 393 FFGSKFKQKA---KLIESVLSKFSQDELIRR--HEELEKNGE----FTCQVnGQIVKLDSSL---VTIKMKTTLQHIREY 460
Cdd:PRK14894 310 VVPYVIEPSAgvgRCMLAVMCEGYAEELTKAipGEKLAAVGDaleaFLKSV-GRSEKLAGEArdaILARGEALLQALPER 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 461 IPNVIE-------PSFGLGRIIycifDHCFQVRVDSESRGFFSFPLQIAPIKVFVTTIS-NNDGFPAILKRISQALRKRE 532
Cdd:PRK14894 389 LPEVEQllampgaDQIELGKKL----RGQAQPLIDEHYRTVLRLKPRLAPIKVAVFPLKrNHEGLVATAKAVRRQLQVGG 464
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325338 533 IYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQ-------TVTLRERNSMRQVRGTITDV 590
Cdd:PRK14894 465 RMRTVYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQGkdpalagTVTVRDRDTMAQERVPISEL 529
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
505-597 |
5.68e-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: 90.72 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 505 KVFVTTISNNDG-FPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRERNSMRQV 583
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 6325338 584 RGTITDVISTIDKM 597
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
503-584 |
2.33e-11 |
|
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: 60.49 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 503 PIKVFVTTIS-NNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRERNSMR 581
Cdd:cd00738 1 PIDVAIVPLTdPRVEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
...
gi 6325338 582 QVR 584
Cdd:cd00738 81 SET 83
|
|
| 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 ... |
166-310 |
1.36e-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: 55.86 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 166 FNLMFETKIGASGQLK--AFLRPETAQGQFLNFNKllEINQG-KIPFASASIGKSFRNEISPRSGLLRVREFLMAEIEHF 242
Cdd:cd00670 45 RKEMYTFEDKGRELRDtdLVLRPAACEPIYQIFSG--EILSYrALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVF 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325338 243 VDPlnkshakfnevlnEEIPLLSRRLQESG-----EVQLPVKMTIGEAVNSGMVENETLGYFMARVHQFLLNI 310
Cdd:cd00670 123 GEP-------------EEAEEERREWLELAeeiarELGLPVRVVVADDPFFGRGGKRGLDAGRETVVEFELLL 182
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
180-245 |
1.01e-07 |
|
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: 52.89 E-value: 1.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325338 180 LKAFLRPETAQGQFLNFNKLLEinqgKIPFASASIGKSFRNEISPRsGLLRVREFLMAEIEHFVDP 245
Cdd:cd00768 51 EDLYLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGED 111
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
498-577 |
3.88e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 46.39 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 498 PLQIAPIKVFVTTI-SNNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRE 576
Cdd:PRK12325 340 PESVAPFKVGIINLkQGDEACDAACEKLYAALSAAGIDVLYDDTDERPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKD 419
|
.
gi 6325338 577 R 577
Cdd:PRK12325 420 R 420
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
214-236 |
3.06e-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: 42.95 E-value: 3.06e-04
10 20
....*....|....*....|...
gi 6325338 214 IGKSFRNEISPRSGLLRVREFLM 236
Cdd:cd00779 119 IQTKFRDEIRPRFGLMRGREFLM 141
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
218-236 |
4.08e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 43.15 E-value: 4.08e-04
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
524-599 |
9.10e-04 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 42.20 E-value: 9.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325338 524 ISQALRKREIYFKIDDSNTSIGKKYARNDELGTPFGITIDFETIKDQTVTLRERNSMRQVRGTITDVISTIDKMLH 599
Cdd:CHL00201 344 IIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISYLKK 419
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
503-588 |
2.61e-03 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS 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: 238437 [Multi-domain] Cd Length: 91 Bit Score: 37.48 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 503 PIKVFVTTIsnNDGFPAILKRISQALRKREIYFKIDDSNTSIGKKyARNDEL-GTPFGITIDFETIKDQTVTLRERNSmr 581
Cdd:cd00860 1 PVQVVVIPV--TDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKK-IREAQLqKIPYILVVGDKEVETGTVSVRTRDG-- 75
|
....*..
gi 6325338 582 QVRGTIT 588
Cdd:cd00860 76 GDLGSMS 82
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
497-594 |
6.07e-03 |
|
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: 39.63 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325338 497 FPLQIAPIKVFVTTISnnDGFPAILKRISQALRKREIYFKIDDSNTSIGKKyARNDELG-TPFGITI-DFEtIKDQTVTL 574
Cdd:COG0441 533 FPLWLAPVQVVVLPIS--DKHADYAKEVAKKLRAAGIRVEVDLRNEKIGYK-IREAQLQkVPYMLVVgDKE-VENGTVSV 608
|
90 100
....*....|....*....|..
gi 6325338 575 RERNSmrQVRGTIT--DVISTI 594
Cdd:COG0441 609 RRRGG--GDLGTMSldEFIARL 628
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
214-236 |
8.39e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 39.07 E-value: 8.39e-03
10 20
....*....|....*....|...
gi 6325338 214 IGKSFRNEISPRSGLLRVREFLM 236
Cdd:PRK12325 135 IQWKFRDEIRPRFGVMRGREFLM 157
|
|
| |
