|
Name |
Accession |
Description |
Interval |
E-value |
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
15-640 |
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: 855.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 15 FNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKF 94
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 95 SDWMCRDLKTGEIFRADHLVEEVLEARLkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilak 174
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGKRL---------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 175 iDGYSGPELGELMEKYDIGNP-VTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASA 253
Cdd:TIGR00389 109 -WGFSGPELNEVMEKYDINCPnCGGENLTEVRSFNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 254 SIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAGstepivktVGEAVASRMVDN 333
Cdd:TIGR00389 188 QIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLDKSHPKFEEVKQDILPLLPRQMQESG--------IGEAVESGMIEN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:TIGR00389 260 ETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 QKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVEShllNMSQDDLASKAELLKANgkftikvdgvdgEVELDDKLVKIEQR 493
Cdd:TIGR00389 340 DKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES---NLSEDDLEEREEELDKN------------EVELDKDLVEIEMV 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 TKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRP-EDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRK 572
Cdd:TIGR00389 405 TEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVlDGEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRK 484
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443451 573 SQIPFKIDDSGvSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDIT 640
Cdd:TIGR00389 485 TGIRIKYDDSG-TIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKKLL 551
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
15-665 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 798.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 15 FNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKF 94
Cdd:PLN02734 73 AFRQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 95 SDWMCRDLKTGEIFRADHLVEEVLEARLKGDqearglvedanaaakddaekkkrkkkvkqikaVKLDDDVVKEYEEILAK 174
Cdd:PLN02734 153 TDLMVKDEKTGTCFRADHLLKDFCEEKLEKD--------------------------------LTISAEKAAELKDVLAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 175 IDGYSGPELGELMEKYDIGNPVTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASAS 254
Cdd:PLN02734 201 LDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 255 IGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAG-STEPIvkTVGEAVASRMVDN 333
Cdd:PLN02734 281 IGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLEFLLFPREEQLGGqKAKPM--RLGEAVSKGIVNN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:PLN02734 359 ETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAH 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 QKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVESHLLNMSQDDLASKAELLKANGKFTIKVDGVDGEVELDDKLVKIEQR 493
Cdd:PLN02734 439 EKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEMKAKLESKGEAEFYVCTLGKEVEIKKNMVSISKE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 TKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRKS 573
Cdd:PLN02734 519 KKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAA 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 574 QIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFesakDHSVTLRERDSTKQVRGSVENVIKAIRDITYNGASWEEGTKDl 653
Cdd:PLN02734 599 GISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAK- 673
|
650
....*....|..
gi 330443451 654 tpFIAQAEAEAE 665
Cdd:PLN02734 674 --YPAHSSAADD 683
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
18-638 |
7.82e-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: 480.37 E-value: 7.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 18 EQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILE-EDMLEVDCTMLTPYEVLKTSGHVDKFSD 96
Cdd:COG0423 8 EKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 97 WMCRDLKTGEIFRADHLVEEVLEArlkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilAKID 176
Cdd:COG0423 88 PLVDCKECKKRYRADHLIEEYLAI----------------------------------------------------EDAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 177 GYSGPELGELMEKYDIGNPVTGE-TLESPRAFNLMFETAIGP--SGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASA 253
Cdd:COG0423 116 GLSLEELEELIKENNIKCPNCGGkELTEVRQFNLMFKTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 254 SIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPldkshpkfneikdiklsflprdvqeagstepivktvGEavasrmvDN 333
Cdd:COG0423 196 QIGKSFRNEITPRNFIFRTREFEQMELEFFVDP------------------------------------GT-------DN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:COG0423 233 EWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYF 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 qkldnpievtkweidltkklfgpkfrkdapkveshllnmsqddlaskaellkangkftikvDGVDGEvelddklvkieqr 493
Cdd:COG0423 313 -------------------------------------------------------------DPETGE------------- 318
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 tkvehvrEYVPSVIEPSFGIGRIIYSVFEHSFWNRP-EDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRK 572
Cdd:COG0423 319 -------KYIPHVIEPSFGVDRLLLAFLEHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRK 391
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443451 573 SqipFKI--DDSGvSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRD 638
Cdd:COG0423 392 A---FNVeyDDSG-SIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAE 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
20-400 |
5.79e-114 |
|
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: 342.26 E-value: 5.79e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 20 LESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEE-DMLEVDCTMLTPYevlktsghvdkfsdwm 98
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 99 crdlktgeifradhlveevlearlkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilakidgy 178
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 179 sgpelgelmekydignpvtgetlesprafnLMFETAIGP--SGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASASIG 256
Cdd:cd00774 65 ------------------------------LMFKTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIG 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 257 KSFRNEISPRAGLLRVREFLMAEIEHFVDPlDKSHPKFNEIKDIKLSFLPRDVQeagSTEPIVKTVGEAVASRMVDNETL 336
Cdd:cd00774 115 KSFRNEISPRNGLFRVREFTQAEIEFFVDP-EKSHPWFDYWADQRLKWLPKFAQ---SPENLRLTDHEKEELAHYANETL 190
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443451 337 GYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLT 400
Cdd:cd00774 191 DYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
547-639 |
9.23e-22 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 89.95 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 547 KVLLVPLSNHKD-LVPVTTEVAKILRKSQIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQV 625
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 330443451 626 RGSVENVIKAIRDI 639
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 ... |
15-640 |
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: 855.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 15 FNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKF 94
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 95 SDWMCRDLKTGEIFRADHLVEEVLEARLkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilak 174
Cdd:TIGR00389 81 TDWMVDCKSCKERFRADHLIEEKLGKRL---------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 175 iDGYSGPELGELMEKYDIGNP-VTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASA 253
Cdd:TIGR00389 109 -WGFSGPELNEVMEKYDINCPnCGGENLTEVRSFNLMFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 254 SIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAGstepivktVGEAVASRMVDN 333
Cdd:TIGR00389 188 QIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLDKSHPKFEEVKQDILPLLPRQMQESG--------IGEAVESGMIEN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:TIGR00389 260 ETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 QKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVEShllNMSQDDLASKAELLKANgkftikvdgvdgEVELDDKLVKIEQR 493
Cdd:TIGR00389 340 DKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIES---NLSEDDLEEREEELDKN------------EVELDKDLVEIEMV 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 TKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRP-EDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRK 572
Cdd:TIGR00389 405 TEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVlDGEEREVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRK 484
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443451 573 SQIPFKIDDSGvSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDIT 640
Cdd:TIGR00389 485 TGIRIKYDDSG-TIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKKLL 551
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
15-665 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 798.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 15 FNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKF 94
Cdd:PLN02734 73 AFRQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 95 SDWMCRDLKTGEIFRADHLVEEVLEARLKGDqearglvedanaaakddaekkkrkkkvkqikaVKLDDDVVKEYEEILAK 174
Cdd:PLN02734 153 TDLMVKDEKTGTCFRADHLLKDFCEEKLEKD--------------------------------LTISAEKAAELKDVLAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 175 IDGYSGPELGELMEKYDIGNPVTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASAS 254
Cdd:PLN02734 201 LDDLSAEELGAKIKEYGIKAPDTKNPLSDPYPFNLMFQTSIGPSGLSVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 255 IGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAG-STEPIvkTVGEAVASRMVDN 333
Cdd:PLN02734 281 IGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLEFLLFPREEQLGGqKAKPM--RLGEAVSKGIVNN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:PLN02734 359 ETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAH 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 QKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVESHLLNMSQDDLASKAELLKANGKFTIKVDGVDGEVELDDKLVKIEQR 493
Cdd:PLN02734 439 EKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALEAMNEKEAMEMKAKLESKGEAEFYVCTLGKEVEIKKNMVSISKE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 TKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRKS 573
Cdd:PLN02734 519 KKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSFYTRPGDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELTAA 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 574 QIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFesakDHSVTLRERDSTKQVRGSVENVIKAIRDITYNGASWEEGTKDl 653
Cdd:PLN02734 599 GISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTAK- 673
|
650
....*....|..
gi 330443451 654 tpFIAQAEAEAE 665
Cdd:PLN02734 674 --YPAHSSAADD 683
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
18-638 |
7.82e-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: 480.37 E-value: 7.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 18 EQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILE-EDMLEVDCTMLTPYEVLKTSGHVDKFSD 96
Cdd:COG0423 8 EKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 97 WMCRDLKTGEIFRADHLVEEVLEArlkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilAKID 176
Cdd:COG0423 88 PLVDCKECKKRYRADHLIEEYLAI----------------------------------------------------EDAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 177 GYSGPELGELMEKYDIGNPVTGE-TLESPRAFNLMFETAIGP--SGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASA 253
Cdd:COG0423 116 GLSLEELEELIKENNIKCPNCGGkELTEVRQFNLMFKTNIGPveDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 254 SIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPldkshpkfneikdiklsflprdvqeagstepivktvGEavasrmvDN 333
Cdd:COG0423 196 QIGKSFRNEITPRNFIFRTREFEQMELEFFVDP------------------------------------GT-------DN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVR 413
Cdd:COG0423 233 EWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYF 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 414 qkldnpievtkweidltkklfgpkfrkdapkveshllnmsqddlaskaellkangkftikvDGVDGEvelddklvkieqr 493
Cdd:COG0423 313 -------------------------------------------------------------DPETGE------------- 318
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 494 tkvehvrEYVPSVIEPSFGIGRIIYSVFEHSFWNRP-EDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRK 572
Cdd:COG0423 319 -------KYIPHVIEPSFGVDRLLLAFLEHAYTEEEvDGEERTVLKLPPRLAPIKVAVLPLVKKDGLVEKAREIYDELRK 391
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330443451 573 SqipFKI--DDSGvSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRD 638
Cdd:COG0423 392 A---FNVeyDDSG-SIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAE 455
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
18-638 |
2.16e-159 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 466.53 E-value: 2.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 18 EQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILE-EDMLEVDCTMLTPYEVLKTSGHVDKFSD 96
Cdd:PRK04173 5 EKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQErEDVVGIDSPIIMPPEVWEASGHVDNFSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 97 WMCRDLKTGEIFRADHLVEEVLEarlkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilaKID 176
Cdd:PRK04173 85 PLVECKKCKKRYRADHLIEELGI------------------------------------------------------DAE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 177 GYSGPELGELMEKYDIGNPVTG-ETLESPRAFNLMFETAIGP--SGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASA 253
Cdd:PRK04173 111 GLSNEELKELIRENDIKCPECGgENWTEVRQFNLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 254 SIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPldkshpkfneikdiklsflprdvqeagstepivktvGEavasrmvDN 333
Cdd:PRK04173 191 QIGKSFRNEITPRNFIFRTREFEQMELEFFVKP------------------------------------GT-------DN 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 334 ETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYG--WIECVGCADRSAYDLTVHSKKTKEKLv 411
Cdd:PRK04173 228 EWFAYWIELRKNWLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDL- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 412 vrqkldnpievtkweidltkklfgpkfrkdapkveshllnmsqddlaskaellkangkfTIKVDGVDGEvelddklvkie 491
Cdd:PRK04173 307 -----------------------------------------------------------SYFDDETTGE----------- 316
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 492 qrtkvehvrEYVPSVIEPSFGIGRIIYSVFEHSF--WNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKI 569
Cdd:PRK04173 317 ---------KYIPYVIEPSAGLDRLLLAFLEDAYteEELGGGDKRTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAE 387
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443451 570 LRKSqipFKI--DDSGvSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRD 638
Cdd:PRK04173 388 LRKD---FNVdyDDSG-SIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAE 454
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
20-400 |
5.79e-114 |
|
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: 342.26 E-value: 5.79e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 20 LESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEE-DMLEVDCTMLTPYevlktsghvdkfsdwm 98
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEeDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 99 crdlktgeifradhlveevlearlkgdqearglvedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilakidgy 178
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 179 sgpelgelmekydignpvtgetlesprafnLMFETAIGP--SGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASASIG 256
Cdd:cd00774 65 ------------------------------LMFKTSIGPveSGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIG 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 257 KSFRNEISPRAGLLRVREFLMAEIEHFVDPlDKSHPKFNEIKDIKLSFLPRDVQeagSTEPIVKTVGEAVASRMVDNETL 336
Cdd:cd00774 115 KSFRNEISPRNGLFRVREFTQAEIEFFVDP-EKSHPWFDYWADQRLKWLPKFAQ---SPENLRLTDHEKEELAHYANETL 190
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443451 337 GYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLT 400
Cdd:cd00774 191 DYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
18-638 |
1.71e-55 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 197.92 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 18 EQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNII-DAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKFSD 96
Cdd:PRK14894 7 DQIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIaDWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEETFND 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 97 WM--CRDLKTGeiFRADHLveevlearlkgdqeaRGLVedanaaakddaekkkrkkkvkqikavkldddvvkeyeeilak 174
Cdd:PRK14894 87 PLvdCRDCKMR--WRADHI---------------QGVC------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 175 idgysgpelgelmekydignPVTGET-LESPRAFNLMFETAIGPSGQLK--GYLRPETAQGQFLNFNKLLEFNNSKTPFA 251
Cdd:PRK14894 108 --------------------PNCGSRdLTEPRPFNMMFRTQIGPVADSDsfAYLRPETAQGIFVNFANVLATSARKLPFG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 252 SASIGKSFRNEISPRAGLLRVREFLMAEIEHFVDP--LDKSHPKFNEikdiklsflprdvqeagstepivktvgeavaSR 329
Cdd:PRK14894 168 IAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPgtDEEWHQRWLE-------------------------------AR 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 330 MVDNEtlgyfiariyqflmKIGVDESKLRFRQHMANEMAHYAADCWDgeLKTSY---GWIECVGCADRSAYDLTVHSKKt 406
Cdd:PRK14894 217 LAWWE--------------QIGIPRSRITIYDVPPDELAHYSKRTFD--LMYDYpniGVQEIEGIANRTDYDLGSHSKD- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 407 KEKLVVRQKLdNPIEvtkweiDLTKKL--FGPKFRKD-----------------APKVESHLLNMSQ----DDLASKAEL 463
Cdd:PRK14894 280 QEQLNLTARV-NPNE------DSTARLtyFDQASGRHvvpyviepsagvgrcmlAVMCEGYAEELTKaipgEKLAAVGDA 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 464 LKANGKFTIKVDGVDGEVE-------------LDDKLVKIEQRTKvehvreyVPSVIEPSFGI---GRIIYSVFEHsfwn 527
Cdd:PRK14894 353 LEAFLKSVGRSEKLAGEARdailargeallqaLPERLPEVEQLLA-------MPGADQIELGKklrGQAQPLIDEH---- 421
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 528 rpednARSVLSFPPLVAPTKVLLVPLS-NHKDLVPVTTEVAKILRK-SQIPFKIDDSGvSIGKRYARNDELGTPFGVTID 605
Cdd:PRK14894 422 -----YRTVLRLKPRLAPIKVAVFPLKrNHEGLVATAKAVRRQLQVgGRMRTVYDDTG-AIGKLYRRQDEIGTPFCITVD 495
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 330443451 606 FESAKDH-------SVTLRERDSTKQVRGSVENVIKAIRD 638
Cdd:PRK14894 496 FDTIGQGkdpalagTVTVRDRDTMAQERVPISELEAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
520-641 |
5.31e-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: 183.14 E-value: 5.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 520 VFEHSFWNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRKSQIPFKIDDSGvSIGKRYARNDELGTP 599
Cdd:cd00858 1 LLEHSFRVREGDEGRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSVKYDDSG-SIGRRYARQDEIGTP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 330443451 600 FGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDITY 641
Cdd:cd00858 80 FCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
547-639 |
9.23e-22 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 89.95 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 547 KVLLVPLSNHKD-LVPVTTEVAKILRKSQIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQV 625
Cdd:pfam03129 1 QVVVIPLGEKAEeLEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 330443451 626 RGSVENVIKAIRDI 639
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
204-286 |
1.31e-07 |
|
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: 53.16 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 204 PRAFNLMFETAIGPSGQLKG--YLRPETAQGQFLNFNKLLEfNNSKTPFASASIGKSFRNEISPRAGLLRVREFLMAEIE 281
Cdd:cd00670 42 DGYRKEMYTFEDKGRELRDTdlVLRPAACEPIYQIFSGEIL-SYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYV 120
|
....*
gi 330443451 282 HFVDP 286
Cdd:cd00670 121 VFGEP 125
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
545-637 |
2.30e-07 |
|
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: 48.93 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 545 PTKVLLVPLSNHKD-LVPVTTEVAKILRKSQIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTK 623
Cdd:cd00738 1 PIDVAIVPLTDPRVeAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 330443451 624 QVRGSVENVIKAIR 637
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
224-286 |
3.05e-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: 51.73 E-value: 3.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443451 224 YLRPETAQGQFLNFNKLLEfnnsKTPFASASIGKSFRNEISPRaGLLRVREFLMAEIEHFVDP 286
Cdd:cd00768 54 YLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGED 111
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
509-640 |
1.73e-05 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 47.94 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 509 PSFGIGRIIYSVFEHSFWNRPEDNarsVLSFPPLVAPTKVLLVPLS-NHKDLvpvTTEVAKILRKSQIPFKIDDSGVSIG 587
Cdd:PRK03991 466 PTGSIERVIYALLEKAAKEEEEGK---VPMLPTWLSPTQVRVIPVSeRHLDY---AEEVADKLEAAGIRVDVDDRDESLG 539
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 330443451 588 KRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDIT 640
Cdd:PRK03991 540 KKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEET 592
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
255-306 |
2.01e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 46.80 E-value: 2.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 255 IGKSFRNEISPRAGLLRVREFLMAEIEHF-VDP--LDKSHPKFNEI-----KDIKLSFLP 306
Cdd:cd00779 119 IQTKFRDEIRPRFGLMRGREFLMKDAYSFdIDEesLEETYEKMYQAysrifKRLGLPFVK 178
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
259-277 |
2.74e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 43.92 E-value: 2.74e-04
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
545-637 |
5.59e-04 |
|
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: 39.41 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 545 PTKVLLVPLSNhkDLVPVTTEVAKILRKSQIPFKIDDSGVSIGKRyARNDEL-GTPFGVTIDFESAKDHSVTLRERDSTK 623
Cdd:cd00860 1 PVQVVVIPVTD--EHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKK-IREAQLqKIPYILVVGDKEVETGTVSVRTRDGGD 77
|
90
....*....|....
gi 330443451 624 QVRGSVENVIKAIR 637
Cdd:cd00860 78 LGSMSLDEFIEKLK 91
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
448-637 |
1.22e-03 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 41.75 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 448 HLLNMSQDDLASKAELLKANGKFTIKVDGVDGEVelddkLVKIEQRTKVEHVREyvpSVIEPSFgIGRIIYSVFEHSFWN 527
Cdd:PRK14938 169 YLKNILQPIFESENNENVSNGEMSILYRNVEGRI-----LPCINENPRIIAVYG---GVKELDF-PKEFIDSKNRIKIWW 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443451 528 RPEDNAR-------------SVLSFPPLV----APTKVLLVPLSnhKDLVPVTTEVAKILRKSQIPFKIDDSGVSIGKRY 590
Cdd:PRK14938 240 VNESRTYvdvgllvyyflleSIRKQPPTLpdwlNPIQVRILPVK--KDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKI 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 330443451 591 ARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIR 637
Cdd:PRK14938 318 RRAGTEWIPFVIIIGEREVKTSTLTVKIRANNEQKSMTVEELVKEIK 364
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|
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