|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
14-655 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 776.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 14 RGNLENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFILHEDMLEISATCLTPYSALKASGHVDRFTD 93
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 94 FMITDTKTNDYYRADKVLEEYAANRLSKNsnnPPKSEAERSELELIIIQAGSYNSDEIRRCLDKYSILSP-SGAEWSNPC 172
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKD---LTISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPdTKNPLSDPY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 173 PFNLMFKTKIGPKQSeddgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAE 252
Cdd:PLN02734 232 PFNLMFQTSIGPSGL------SVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 253 IEHFVHPERKNHPKFFIVENLCLPLYPRSSQLNNTNViKNMTLKEAVhgPNKVIDNETLAYFLARSHLFFKSIGINIGGL 332
Cdd:PLN02734 306 IEHFVDPEDKSHPKFSEVADLEFLLFPREEQLGGQKA-KPMRLGEAV--SKGIVNNETLGYFIGRTYLFLTKLGIDKERL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 333 RFRQHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLLASERYDEPQIRPFVKLLLNRPLIGKT 412
Cdd:PLN02734 383 RFRQHLANEMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 413 FKQEAPKVIEVLQDIANKCDMSVEEALKREGSynLNYKYCSdhTKYKWEITREMVNFELTSKRVTEEHFIPAVIEPSFGI 492
Cdd:PLN02734 463 FKGDQKVVVEALEAMNEKEAMEMKAKLESKGE--AEFYVCT--LGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGI 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 493 GRIIYCVLEHSFRIRDdeslnqvngekinvnkdiqtsiGEMQRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDECI 572
Cdd:PLN02734 539 GRIIYCLFEHSFYTRP----------------------GDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELT 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 573 GMGISCKLDTSSASIGRRYARTDEIGIPFGITVDFqtikDNTVTLRERDTMKQVRLHSSEVVKIISELSYQKLIWSDVLK 652
Cdd:PLN02734 597 AAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTA 672
|
...
gi 209876788 653 MYP 655
Cdd:PLN02734 673 KYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
17-640 |
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: 596.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 17 LENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFILHEDMLEISATCLTPYSALKASGHVDRFTDFMI 96
Cdd:TIGR00389 6 IMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNFTDWMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 97 TDTKTNDYYRADKVLEEYAANRLSKNSNnppkseaerSELELIIiqagsynsdeirrclDKYSILSPS--GAEWSNPCPF 174
Cdd:TIGR00389 86 DCKSCKERFRADHLIEEKLGKRLWGFSG---------PELNEVM---------------EKYDINCPNcgGENLTEVRSF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 175 NLMFKTKIGPkqseddGKCNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIE 254
Cdd:TIGR00389 142 NLMFQTEIGV------VGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 255 HFVHPERKNHPKFFIVENLCLPLYPRSSQLNntnviknmTLKEAVHgpNKVIDNETLAYFLARSHLFFKSIGINIGGLRF 334
Cdd:TIGR00389 216 FFVHPLDKSHPKFEEVKQDILPLLPRQMQES--------GIGEAVE--SGMIENETLGYFIARVKQFLLEIGINPDKLRF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 335 RQHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLLASERYDEPQIRPFVKLLLNRPLIGKTFK 414
Cdd:TIGR00389 286 RQHDKNEMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 415 QEAPKVIEVLQDianKCDMSVEEALKREgsynlnykycsdhtkyKWEITREMVNFELTSKRVTEEHFIPAVIEPSFGIGR 494
Cdd:TIGR00389 366 KDAKKIESNLSE---DDLEEREEELDKN----------------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 495 IIYCVLEHSFRIRddeslnQVNGEKinvnkdiqtsigemqRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDECIGM 574
Cdd:TIGR00389 427 IIYALLEHSYQEE------VLDGEE---------------REVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKT 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209876788 575 GISCKLDtSSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:TIGR00389 486 GIRIKYD-DSGTIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
19-640 |
1.24e-174 |
|
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: 505.41 E-value: 1.24e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 19 NLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFI-LHEDMLEISATCLTPYSALKASGHVDRFTDFMIT 97
Cdd:COG0423 12 SLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVqRRDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 98 DTKTNDYYRADKVLEEYAAnrlsknsnnppkseaerseleliIIQAGSYNSDEIRRCLDKYSILSPS--GAEWSNPCPFN 175
Cdd:COG0423 92 CKECKKRYRADHLIEEYLA-----------------------IEDAEGLSLEELEELIKENNIKCPNcgGKELTEVRQFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 176 LMFKTKIGPkqSEDDGkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIEH 255
Cdd:COG0423 149 LMFKTNIGP--VEDES--STGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 256 FVHPERknhpkffivenlclplyprssqlnntnviknmtlkeavhgpnkviDNETLAYFLARSHLFFKSIGINIGGLRFR 335
Cdd:COG0423 225 FVDPGT---------------------------------------------DNEWFAYWLALRKKWLLSLGIDPENLRFR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 336 QHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLlaseRYdepqirpfvklllnrpligktFKQ 415
Cdd:COG0423 260 DHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----TY---------------------FDP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 416 EapkvievlqdiankcdmsveealkregsynlnykycsdhtkykweitremvnfeltskrvTEEHFIPAVIEPSFGIGRI 495
Cdd:COG0423 315 E------------------------------------------------------------TGEKYIPHVIEPSFGVDRL 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 496 IYCVLEHSFriRDDEslnqVNGEKinvnkdiqtsigemqRCYLSIPPIIAPIKCSILPISSniifndiiniiRDECIGMG 575
Cdd:COG0423 335 LLAFLEHAY--TEEE----VDGEE---------------RTVLKLPPRLAPIKVAVLPLVK-----------KDGLVEKA 382
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209876788 576 ----------ISCKLDTsSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:COG0423 383 reiydelrkaFNVEYDD-SGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAEL 456
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
17-374 |
6.30e-112 |
|
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: 336.87 E-value: 6.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 17 LENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFIL-HEDMLEISATCLTPYsalkasghvdrftdfm 95
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLeEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 96 itdtktndyyradkvleeyaanrlsknsnnppkseaerseleliiiqagsynsdeirrcldkysilspsgaewsnpcpfn 175
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 176 LMFKTKIGPKQSEDdgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIEH 255
Cdd:cd00774 65 LMFKTSIGPVESGG----NLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 256 FVHPErKNHPKFFIVENLCLPLYPRSSQLNNTnviKNMTLKEAVHGpnKVIDNETLAYFLARSHLFFKSIGINIGGLRFR 335
Cdd:cd00774 141 FVDPE-KSHPWFDYWADQRLKWLPKFAQSPEN---LRLTDHEKEEL--AHYANETLDYFYAFPHGFLELEGIANRGDRFL 214
|
330 340 350
....*....|....*....|....*....|....*....
gi 209876788 336 QHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDL 374
Cdd:cd00774 215 QHHPNESAHYASDCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
575-640 |
3.62e-20 |
|
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: 85.33 E-value: 3.62e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209876788 575 GISCKLDTSSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:pfam03129 29 GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQETVSLDELVEKLKEL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
14-655 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 776.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 14 RGNLENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFILHEDMLEISATCLTPYSALKASGHVDRFTD 93
Cdd:PLN02734 75 RQAVVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 94 FMITDTKTNDYYRADKVLEEYAANRLSKNsnnPPKSEAERSELELIIIQAGSYNSDEIRRCLDKYSILSP-SGAEWSNPC 172
Cdd:PLN02734 155 LMVKDEKTGTCFRADHLLKDFCEEKLEKD---LTISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPdTKNPLSDPY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 173 PFNLMFKTKIGPKQSeddgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAE 252
Cdd:PLN02734 232 PFNLMFQTSIGPSGL------SVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 253 IEHFVHPERKNHPKFFIVENLCLPLYPRSSQLNNTNViKNMTLKEAVhgPNKVIDNETLAYFLARSHLFFKSIGINIGGL 332
Cdd:PLN02734 306 IEHFVDPEDKSHPKFSEVADLEFLLFPREEQLGGQKA-KPMRLGEAV--SKGIVNNETLGYFIGRTYLFLTKLGIDKERL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 333 RFRQHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLLASERYDEPQIRPFVKLLLNRPLIGKT 412
Cdd:PLN02734 383 RFRQHLANEMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 413 FKQEAPKVIEVLQDIANKCDMSVEEALKREGSynLNYKYCSdhTKYKWEITREMVNFELTSKRVTEEHFIPAVIEPSFGI 492
Cdd:PLN02734 463 FKGDQKVVVEALEAMNEKEAMEMKAKLESKGE--AEFYVCT--LGKEVEIKKNMVSISKEKKKEHQRVFTPSVIEPSFGI 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 493 GRIIYCVLEHSFRIRDdeslnqvngekinvnkdiqtsiGEMQRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDECI 572
Cdd:PLN02734 539 GRIIYCLFEHSFYTRP----------------------GDEQLNVFRFPPLVAPIKCTVFPLVQNQQLNAVAKVISKELT 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 573 GMGISCKLDTSSASIGRRYARTDEIGIPFGITVDFqtikDNTVTLRERDTMKQVRLHSSEVVKIISELSYQKLIWSDVLK 652
Cdd:PLN02734 597 AAGISHKIDITGTSIGKRYARTDELGVPFAVTVDS----DGSVTIRERDSKDQVRVPVEEVASVVKDLTDGRMTWEDVTA 672
|
...
gi 209876788 653 MYP 655
Cdd:PLN02734 673 KYP 675
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
17-640 |
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: 596.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 17 LENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFILHEDMLEISATCLTPYSALKASGHVDRFTDFMI 96
Cdd:TIGR00389 6 IMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNFTDWMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 97 TDTKTNDYYRADKVLEEYAANRLSKNSNnppkseaerSELELIIiqagsynsdeirrclDKYSILSPS--GAEWSNPCPF 174
Cdd:TIGR00389 86 DCKSCKERFRADHLIEEKLGKRLWGFSG---------PELNEVM---------------EKYDINCPNcgGENLTEVRSF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 175 NLMFKTKIGPkqseddGKCNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIE 254
Cdd:TIGR00389 142 NLMFQTEIGV------VGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 255 HFVHPERKNHPKFFIVENLCLPLYPRSSQLNntnviknmTLKEAVHgpNKVIDNETLAYFLARSHLFFKSIGINIGGLRF 334
Cdd:TIGR00389 216 FFVHPLDKSHPKFEEVKQDILPLLPRQMQES--------GIGEAVE--SGMIENETLGYFIARVKQFLLEIGINPDKLRF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 335 RQHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLLASERYDEPQIRPFVKLLLNRPLIGKTFK 414
Cdd:TIGR00389 286 RQHDKNEMAHYAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 415 QEAPKVIEVLQDianKCDMSVEEALKREgsynlnykycsdhtkyKWEITREMVNFELTSKRVTEEHFIPAVIEPSFGIGR 494
Cdd:TIGR00389 366 KDAKKIESNLSE---DDLEEREEELDKN----------------EVELDKDLVEIEMVTEVVHGEKYIPHVIEPSFGIDR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 495 IIYCVLEHSFRIRddeslnQVNGEKinvnkdiqtsigemqRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDECIGM 574
Cdd:TIGR00389 427 IIYALLEHSYQEE------VLDGEE---------------REVLRLPPHLAPIKVAVLPLVNKEELKEIAKEIFQALRKT 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209876788 575 GISCKLDtSSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:TIGR00389 486 GIRIKYD-DSGTIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKKL 550
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
19-640 |
1.24e-174 |
|
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: 505.41 E-value: 1.24e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 19 NLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFI-LHEDMLEISATCLTPYSALKASGHVDRFTDFMIT 97
Cdd:COG0423 12 SLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVqRRDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 98 DTKTNDYYRADKVLEEYAAnrlsknsnnppkseaerseleliIIQAGSYNSDEIRRCLDKYSILSPS--GAEWSNPCPFN 175
Cdd:COG0423 92 CKECKKRYRADHLIEEYLA-----------------------IEDAEGLSLEELEELIKENNIKCPNcgGKELTEVRQFN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 176 LMFKTKIGPkqSEDDGkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIEH 255
Cdd:COG0423 149 LMFKTNIGP--VEDES--STGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 256 FVHPERknhpkffivenlclplyprssqlnntnviknmtlkeavhgpnkviDNETLAYFLARSHLFFKSIGINIGGLRFR 335
Cdd:COG0423 225 FVDPGT---------------------------------------------DNEWFAYWLALRKKWLLSLGIDPENLRFR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 336 QHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDLIQHSKSAKVDLlaseRYdepqirpfvklllnrpligktFKQ 415
Cdd:COG0423 260 DHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDL----TY---------------------FDP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 416 EapkvievlqdiankcdmsveealkregsynlnykycsdhtkykweitremvnfeltskrvTEEHFIPAVIEPSFGIGRI 495
Cdd:COG0423 315 E------------------------------------------------------------TGEKYIPHVIEPSFGVDRL 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 496 IYCVLEHSFriRDDEslnqVNGEKinvnkdiqtsigemqRCYLSIPPIIAPIKCSILPISSniifndiiniiRDECIGMG 575
Cdd:COG0423 335 LLAFLEHAY--TEEE----VDGEE---------------RTVLKLPPRLAPIKVAVLPLVK-----------KDGLVEKA 382
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209876788 576 ----------ISCKLDTsSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:COG0423 383 reiydelrkaFNVEYDD-SGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAEL 456
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
16-640 |
7.72e-166 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 482.71 E-value: 7.72e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 16 NLENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFI-LHEDMLEISATCLTPYSALKASGHVDRFTDF 94
Cdd:PRK04173 6 KIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVqEREDVVGIDSPIIMPPEVWEASGHVDNFSDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 95 MITDTKTNDYYRADKVLEEYAANrlsknsnnppKSEAERSELELIIIQAGsynsdeirrcldkysILSPS--GAEWSNPC 172
Cdd:PRK04173 86 LVECKKCKKRYRADHLIEELGID----------AEGLSNEELKELIREND---------------IKCPEcgGENWTEVR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 173 PFNLMFKTKIGPKQSEDdgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAE 252
Cdd:PRK04173 141 QFNLMFKTFIGPVEDSK----SLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQME 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 253 IEHFVHPERknhpkffivenlclplyprssqlnntnviknmtlkeavhgpnkviDNETLAYFLARSHLFFKSIGINIGGL 332
Cdd:PRK04173 217 LEFFVKPGT---------------------------------------------DNEWFAYWIELRKNWLLDLGIDPENL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 333 RFRQHLETEMAHYASDCWDAEILTSYG--WIECAGHADRSCYDLIQHSKSAKVDLlaseRYdepqirpfvklllnrplig 410
Cdd:PRK04173 252 RFREHLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDL----SY------------------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 411 ktFKQEapkvievlqdiankcdmsveealkregsynlnykycsdhtkykweitremvnfeltskrVTEEHFIPAVIEPSF 490
Cdd:PRK04173 309 --FDDE-----------------------------------------------------------TTGEKYIPYVIEPSA 327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 491 GIGRIIYCVLEHSFRIRDdeslnQVNGEKinvnkdiqtsigemqRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDE 570
Cdd:PRK04173 328 GLDRLLLAFLEDAYTEEE-----LGGGDK---------------RTVLRLPPALAPVKVAVLPLVKKEKLSEKAREIYAE 387
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 571 CIGMgISCKLDTsSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:PRK04173 388 LRKD-FNVDYDD-SGSIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEK 455
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
17-374 |
6.30e-112 |
|
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: 336.87 E-value: 6.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 17 LENLLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEIEGLWRKHFIL-HEDMLEISATCLTPYsalkasghvdrftdfm 95
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLeEEDMLEIDSPIITPE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 96 itdtktndyyradkvleeyaanrlsknsnnppkseaerseleliiiqagsynsdeirrcldkysilspsgaewsnpcpfn 175
Cdd:cd00774 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 176 LMFKTKIGPKQSEDdgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIEH 255
Cdd:cd00774 65 LMFKTSIGPVESGG----NLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 256 FVHPErKNHPKFFIVENLCLPLYPRSSQLNNTnviKNMTLKEAVHGpnKVIDNETLAYFLARSHLFFKSIGINIGGLRFR 335
Cdd:cd00774 141 FVDPE-KSHPWFDYWADQRLKWLPKFAQSPEN---LRLTDHEKEEL--AHYANETLDYFYAFPHGFLELEGIANRGDRFL 214
|
330 340 350
....*....|....*....|....*....|....*....
gi 209876788 336 QHLETEMAHYASDCWDAEILTSYGWIECAGHADRSCYDL 374
Cdd:cd00774 215 QHHPNESAHYASDCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
20-639 |
4.65e-62 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 215.64 E-value: 4.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 20 LLRRRFFVIPSFEIYGGVAGLFDYGPPGCALKAEI-EGLWRKHFILHEDMLEISATCLTPYSALKASGHVDRFTDFMITD 98
Cdd:PRK14894 12 LAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIiADWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEETFNDPLVDC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 99 TKTNDYYRADKVleeyaanrlsknsnnppkseaerselELIIIQAGSYNSDEirrcldkysilspsgaewsnPCPFNLMF 178
Cdd:PRK14894 92 RDCKMRWRADHI--------------------------QGVCPNCGSRDLTE--------------------PRPFNMMF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 179 KTKIGPKQSEDdgkcNTGFLRPETAQGIFVNFRRLLDYNGKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAEIEHFVH 258
Cdd:PRK14894 126 RTQIGPVADSD----SFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 259 PErknhpkffivenlclplyprssqlnntnviknmtlkeavhgpnkvIDNETLAYFLARSHLFFKSIGINIGGLRFRQHL 338
Cdd:PRK14894 202 PG---------------------------------------------TDEEWHQRWLEARLAWWEQIGIPRSRITIYDVP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 339 ETEMAHYASDCWDaeILTSY---GWIECAGHADRSCYDLIQHSK-SAKVDLLASERYDEPQIrpfVKLLLNRPLIGktfK 414
Cdd:PRK14894 237 PDELAHYSKRTFD--LMYDYpniGVQEIEGIANRTDYDLGSHSKdQEQLNLTARVNPNEDST---ARLTYFDQASG---R 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 415 QEAPKVIEVLQDIAnKCDMSVeealKREGsynlnykycsdhtkYKWEITREMVNFELTSKRVTEEHFIPAVIEPSFGIGR 494
Cdd:PRK14894 309 HVVPYVIEPSAGVG-RCMLAV----MCEG--------------YAEELTKAIPGEKLAAVGDALEAFLKSVGRSEKLAGE 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 495 IIYCVLEHSFRIRD--DESLNQVN-------GEKINVNKDI----QTSIGEMQRCYLSIPPIIAPIKCSILPISSNIIFN 561
Cdd:PRK14894 370 ARDAILARGEALLQalPERLPEVEqllampgADQIELGKKLrgqaQPLIDEHYRTVLRLKPRLAPIKVAVFPLKRNHEGL 449
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 562 DIINIIRDECIGMGISCK-LDTSSASIGRRYARTDEIGIPFGITVDFQTIKDN-------TVTLRERDTMKQVRLHSSEV 633
Cdd:PRK14894 450 VATAKAVRRQLQVGGRMRtVYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQGkdpalagTVTVRDRDTMAQERVPISEL 529
|
....*.
gi 209876788 634 VKIISE 639
Cdd:PRK14894 530 EAYLRD 535
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
499-642 |
1.22e-43 |
|
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: 152.33 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 499 VLEHSFRIRDDESlnqvngekinvnkdiqtsigemQRCYLSIPPIIAPIKCSILPISSNIIFNDIINIIRDECIGMGISC 578
Cdd:cd00858 1 LLEHSFRVREGDE----------------------GRIVLRLPPALAPIKVAVLPLVKRDELVEIAKEISEELRELGFSV 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209876788 579 KLDTSsASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISELSY 642
Cdd:cd00858 59 KYDDS-GSIGRRYARQDEIGTPFCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
575-640 |
3.62e-20 |
|
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: 85.33 E-value: 3.62e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209876788 575 GISCKLDTSSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:pfam03129 29 GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQETVSLDELVEKLKEL 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 ... |
174-261 |
1.27e-12 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 67.80 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 174 FNLMFKTKIGPKQSEDDGKCntgfLRPETAQGIFVNF-RRLLDYngKKLPFAAAQIGLGFRNEIAPRNGLLRVREFQMAE 252
Cdd:cd00670 45 RKEMYTFEDKGRELRDTDLV----LRPAACEPIYQIFsGEILSY--RALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVE 118
|
....*....
gi 209876788 253 IEHFVHPER 261
Cdd:cd00670 119 YVVFGEPEE 127
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
546-634 |
2.46e-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: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 546 PIKCSILPIssniifNDIINIIRDECIGM-------GISCKLDTSSASIGRRYARTDEIGIPFGITVDFQTIKDNTVTLR 618
Cdd:cd00738 1 PIDVAIVPL------TDPRVEAREYAQKLlnallanGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVK 74
|
90
....*....|....*.
gi 209876788 619 ERDTMKQVRLHSSEVV 634
Cdd:cd00738 75 SRDTGESETLHVDELP 90
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
534-638 |
6.51e-07 |
|
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: 48.95 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 534 QRCYLSIPPIIAPIKCSIlpissnIIFNDIINIIRDECIGM-------GISC---KLDTSSASIGRRYARTDEIGIPFGI 603
Cdd:cd02426 15 QRQVLKLHPCLAPYKVAI------DCGKGDTAELRDLCQGLknelreaGLSVwpgYLETQHSSLEQLLDKYDEMGVLFTL 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 209876788 604 TVDFQTIKDNTVTLRERDTMKQVRLHSSEV----VKIIS 638
Cdd:cd02426 89 LISEQTLENGLLQLRSRDTTLKETIHISDLpdylLRYIA 127
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
197-260 |
2.72e-06 |
|
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: 48.65 E-value: 2.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209876788 197 FLRPETAQGIFVNFRRLLdyngKKLPFAAAQIGLGFRNEIaPRNGLLRVREFQMAEIEHFVHPE 260
Cdd:cd00768 54 YLRPTLEPGLVRLFVSHI----RKLPLRLAEIGPAFRNEG-GRRGLRRVREFTQLEGEVFGEDG 112
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
219-250 |
6.17e-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: 45.26 E-value: 6.17e-05
10 20 30
....*....|....*....|....*....|..
gi 209876788 219 KKLPFAAAQIGLGFRNEIAPRNGLLRVREFQM 250
Cdd:cd00779 110 KQLPLNLYQIQTKFRDEIRPRFGLMRGREFLM 141
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
188-261 |
6.42e-05 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 44.33 E-value: 6.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209876788 188 EDDGKCNTGfLRPETAQGIFVNFRRLLDyNGKKLPFAAAQIGLGFRNEiAPRN--GLLRVREFQMAEIEHFVHPER 261
Cdd:pfam00587 4 EDENGDELA-LKPTNEPGHTLLFREEGL-RSKDLPLKLAQFGTCFRHE-ASGDtrGLIRVRQFHQDDAHIFHAPGQ 76
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
219-250 |
1.73e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 44.69 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|..
gi 209876788 219 KKLPFAAAQIGLGFRNEIAPRNGLLRVREFQM 250
Cdd:PRK09194 126 KQLPLNLYQIQTKFRDEIRPRFGLMRGREFIM 157
|
|
| PRK12325 |
PRK12325 |
prolyl-tRNA synthetase; Provisional |
219-250 |
2.80e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 40.61 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|..
gi 209876788 219 KKLPFAAAQIGLGFRNEIAPRNGLLRVREFQM 250
Cdd:PRK12325 126 KDLPLNLYHIQWKFRDEIRPRFGVMRGREFLM 157
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| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
538-640 |
5.81e-03 |
|
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: 38.43 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209876788 538 LSIPPIIAPIKCSILPIssnIIFNDIINIIRDECIGM-------GISCKLD-TSSASIGRRYARTDEIGIPFGITVDFQT 609
Cdd:cd00862 2 LVLPPRVAPIQVVIVPI---GIKDEKREEVLEAADELaerlkaaGIRVHVDdRDNYTPGWKFNDWELKGVPLRIEIGPRD 78
|
90 100 110
....*....|....*....|....*....|.
gi 209876788 610 IKDNTVTLRERDTMKQVRLHSSEVVKIISEL 640
Cdd:cd00862 79 LEKNTVVIVRRDTGEKKTVPLAELVEKVPEL 109
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