|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
9-461 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 698.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 9 LREKSLAVEDQELAVGTLEDSHAAKPETNAAIELPNKSKPEKSAVEKD--------------REDFREAVVKTLDRLLFV 74
Cdd:PLN02734 9 LAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKElqaavgaggdgaasKEAFRQAVVNTLERRLFY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 75 HKSFDIYHGVAGLYDFGPHGRTVELNILSLWRKCFVDEEDMMEVACTALTPEAVFNASGHVKKFTDLMVKDEVDGAFHRA 154
Cdd:PLN02734 89 IPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCFRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 155 DHLVKSYCENR-KKDPTISAENAAELDKVIAHVEDLSAEELGG-VWNHCSTAPVTKNPLShPPRPFNLMFQTSFGASGSL 232
Cdd:PLN02734 169 DHLLKDFCEEKlEKDLTISAEKAAELKDVLAVLDDLSAEELGAkIKEYGIKAPDTKNPLS-DPYPFNLMFQTSIGPSGLS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 233 IGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHKSHSKFSDVAKLE 312
Cdd:PLN02734 248 VGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 313 LLMFPREEQEKpGQFAKRLCLGEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAHYATDCWDAEIEC 392
Cdd:PLN02734 328 FLLFPREEQLG-GQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIEC 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42562400 393 SYGWIECVGIADRSDYDLRAHSEKSGHALVAQEKLAEPIEVEKLAITPEMKELGPAFKGNQKNVVEALE 461
Cdd:PLN02734 407 SYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALE 475
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
61-463 |
6.01e-149 |
|
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: 435.81 E-value: 6.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 61 REAVVKTLDRLLFVHKSFDIYHGVAGLYDFGPHGRTVELNILSLWRKCFVDEEDMMEVACTALTPEAVFNASGHVKKFTD 140
Cdd:TIGR00389 3 MEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNFTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 141 LMVKDEVDGAFHRADHLVKSycenrKKDPTISAENAAELDKVIaHVEDLSAEELGGvwnhcstapvtkNPLSHPpRPFNL 220
Cdd:TIGR00389 83 WMVDCKSCKERFRADHLIEE-----KLGKRLWGFSGPELNEVM-EKYDINCPNCGG------------ENLTEV-RSFNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 221 MFQTSFGASGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHK 300
Cdd:TIGR00389 144 MFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLDK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 301 SHSKFSDVAKLELLMFPREEQEKPgqfakrlcLGEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAH 380
Cdd:TIGR00389 224 SHPKFEEVKQDILPLLPRQMQESG--------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEMAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 381 YATDCWDAEIECSYGWIECVGIADRSDYDLRAHSEKSGHALVAQEKLAEPIEVEKLAITPEMKELGPAFKGNQKNVVEAL 460
Cdd:TIGR00389 296 YAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIESNL 375
|
...
gi 42562400 461 EVD 463
Cdd:TIGR00389 376 SED 378
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
73-418 |
3.04e-115 |
|
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: 346.32 E-value: 3.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 73 FVHKSFDIYHGVAGLYDFGPHGrtVEL--NILSLWRKCFVDE-EDMMEVACTALTPEAVFNASGHVKKFTDLMVKDEVDG 149
Cdd:COG0423 19 FVFPSSEIYGGLAGFYDYGPLG--VELknNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVDCKECK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 150 AFHRADHLVKSYCENRKKDptisAENAAELDKVIahvedlsaEELGGVWNHCSTAPVTknplshPPRPFNLMFQTSFGA- 228
Cdd:COG0423 97 KRYRADHLIEEYLAIEDAE----GLSLEELEELI--------KENNIKCPNCGGKELT------EVRQFNLMFKTNIGPv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 229 -SGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHKshskfsd 307
Cdd:COG0423 159 eDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTD------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 308 vaklellmfpreeqekpgqfakrlclgeavakghvnSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAHYATDCWD 387
Cdd:COG0423 232 ------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWD 275
|
330 340 350
....*....|....*....|....*....|.
gi 42562400 388 AEIECSYGWIECVGIADRSDYDLRAHSEKSG 418
Cdd:COG0423 276 IEYEFPFGWGELEGIAYRTDYDLSRHQEYSG 306
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
64-410 |
5.17e-96 |
|
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: 289.49 E-value: 5.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 64 VVKTLDRLLFVHKSFDIYHGVAGLYDFGPHGrtVEL--NILSLWRKCFV-DEEDMMEVACTALTPEavfnasghvkkftd 140
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLG--VELknNIKSAWRKSFVlEEEDMLEIDSPIITPE-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 141 lmvkdevdgafhradhlvksycenrkkdptisaenaaeldkviahvedlsaeelggvwnhcstapvtknplshpprpfnL 220
Cdd:cd00774 65 -------------------------------------------------------------------------------L 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 221 MFQTSFG--ASGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPE 298
Cdd:cd00774 66 MFKTSIGpvESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 299 hKSHSKFSDVAKLELLMFPREEQeKPGQFAKRLClgEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEM 378
Cdd:cd00774 146 -KSHPWFDYWADQRLKWLPKFAQ-SPENLRLTDH--EKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNES 221
|
330 340 350
....*....|....*....|....*....|..
gi 42562400 379 AHYATDCWDAEIECSYGWIECVGIADRSDYDL 410
Cdd:cd00774 222 AHYASDCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
235-319 |
1.17e-06 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 48.56 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 235 YLRPETAQGsFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQ-GLLRTREFTLAEIEHFVHPEhKSHSKFSDVAKLEL 313
Cdd:pfam00587 12 ALKPTNEPG-HTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG-QSPDELEDYIKLID 89
|
....*.
gi 42562400 314 LMFPRE 319
Cdd:pfam00587 90 RVYSRL 95
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
9-461 |
0e+00 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 698.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 9 LREKSLAVEDQELAVGTLEDSHAAKPETNAAIELPNKSKPEKSAVEKD--------------REDFREAVVKTLDRLLFV 74
Cdd:PLN02734 9 LAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALEKElqaavgaggdgaasKEAFRQAVVNTLERRLFY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 75 HKSFDIYHGVAGLYDFGPHGRTVELNILSLWRKCFVDEEDMMEVACTALTPEAVFNASGHVKKFTDLMVKDEVDGAFHRA 154
Cdd:PLN02734 89 IPSFKIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCFRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 155 DHLVKSYCENR-KKDPTISAENAAELDKVIAHVEDLSAEELGG-VWNHCSTAPVTKNPLShPPRPFNLMFQTSFGASGSL 232
Cdd:PLN02734 169 DHLLKDFCEEKlEKDLTISAEKAAELKDVLAVLDDLSAEELGAkIKEYGIKAPDTKNPLS-DPYPFNLMFQTSIGPSGLS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 233 IGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHKSHSKFSDVAKLE 312
Cdd:PLN02734 248 VGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPEDKSHPKFSEVADLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 313 LLMFPREEQEKpGQFAKRLCLGEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAHYATDCWDAEIEC 392
Cdd:PLN02734 328 FLLFPREEQLG-GQKAKPMRLGEAVSKGIVNNETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIEC 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42562400 393 SYGWIECVGIADRSDYDLRAHSEKSGHALVAQEKLAEPIEVEKLAITPEMKELGPAFKGNQKNVVEALE 461
Cdd:PLN02734 407 SYGWIECVGIADRSAYDLKAHSDKSKVPLVAHEKFAEPREVEVLVIVPNKKELGLAFKGDQKVVVEALE 475
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
61-463 |
6.01e-149 |
|
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: 435.81 E-value: 6.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 61 REAVVKTLDRLLFVHKSFDIYHGVAGLYDFGPHGRTVELNILSLWRKCFVDEEDMMEVACTALTPEAVFNASGHVKKFTD 140
Cdd:TIGR00389 3 MEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKNERVLEIDTPIITPEEVLKASGHVDNFTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 141 LMVKDEVDGAFHRADHLVKSycenrKKDPTISAENAAELDKVIaHVEDLSAEELGGvwnhcstapvtkNPLSHPpRPFNL 220
Cdd:TIGR00389 83 WMVDCKSCKERFRADHLIEE-----KLGKRLWGFSGPELNEVM-EKYDINCPNCGG------------ENLTEV-RSFNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 221 MFQTSFGASGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHK 300
Cdd:TIGR00389 144 MFQTEIGVVGKRKGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLDK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 301 SHSKFSDVAKLELLMFPREEQEKPgqfakrlcLGEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAH 380
Cdd:TIGR00389 224 SHPKFEEVKQDILPLLPRQMQESG--------IGEAVESGMIENETLGYFIARVKQFLLEIGINPDKLRFRQHDKNEMAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 381 YATDCWDAEIECSYGWIECVGIADRSDYDLRAHSEKSGHALVAQEKLAEPIEVEKLAITPEMKELGPAFKGNQKNVVEAL 460
Cdd:TIGR00389 296 YAKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKFSGKSLSVFDKLDEPREVTKWEIEPNKKKFGPKFRKDAKKIESNL 375
|
...
gi 42562400 461 EVD 463
Cdd:TIGR00389 376 SED 378
|
|
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
73-418 |
3.04e-115 |
|
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: 346.32 E-value: 3.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 73 FVHKSFDIYHGVAGLYDFGPHGrtVEL--NILSLWRKCFVDE-EDMMEVACTALTPEAVFNASGHVKKFTDLMVKDEVDG 149
Cdd:COG0423 19 FVFPSSEIYGGLAGFYDYGPLG--VELknNIKEAWWKSFVQRrDDVVGIDSPIIMPPKVWEASGHVDGFTDPLVDCKECK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 150 AFHRADHLVKSYCENRKKDptisAENAAELDKVIahvedlsaEELGGVWNHCSTAPVTknplshPPRPFNLMFQTSFGA- 228
Cdd:COG0423 97 KRYRADHLIEEYLAIEDAE----GLSLEELEELI--------KENNIKCPNCGGKELT------EVRQFNLMFKTNIGPv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 229 -SGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPEHKshskfsd 307
Cdd:COG0423 159 eDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTD------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 308 vaklellmfpreeqekpgqfakrlclgeavakghvnSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEMAHYATDCWD 387
Cdd:COG0423 232 ------------------------------------NEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWD 275
|
330 340 350
....*....|....*....|....*....|.
gi 42562400 388 AEIECSYGWIECVGIADRSDYDLRAHSEKSG 418
Cdd:COG0423 276 IEYEFPFGWGELEGIAYRTDYDLSRHQEYSG 306
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
62-418 |
3.73e-110 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 332.86 E-value: 3.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 62 EAVVKTLDRLLFVHKSFDIYHGVAGLYDFGPHGrtVEL--NILSLWRKCFV-DEEDMMEVACTALTPEAVFNASGHVKKF 138
Cdd:PRK04173 5 EKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLG--VELknNIKRAWWKSFVqEREDVVGIDSPIIMPPEVWEASGHVDNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 139 TDLMVKDEVDGAFHRADHLVKSYCENrkkdptISAENAAELDKVIahvedlsaEELGGVwnhCstaPVTKNPLSHPPRPF 218
Cdd:PRK04173 83 SDPLVECKKCKKRYRADHLIEELGID------AEGLSNEELKELI--------RENDIK---C---PECGGENWTEVRQF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 219 NLMFQTSFGA--SGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVH 296
Cdd:PRK04173 143 NLMFKTFIGPveDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 297 PEHKshskfsdvaklellmfpreeqekpgqfakrlclgeavakghvnSETLGFFIGRVYLFLIRLGIDKERLRFRHHLAN 376
Cdd:PRK04173 223 PGTD-------------------------------------------NEWFAYWIELRKNWLLDLGIDPENLRFREHLPE 259
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 42562400 377 EMAHYATDCWDAEIECSYG--WIECVGIADRSDYDLRAHSEKSG 418
Cdd:PRK04173 260 ELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSG 303
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
64-410 |
5.17e-96 |
|
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: 289.49 E-value: 5.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 64 VVKTLDRLLFVHKSFDIYHGVAGLYDFGPHGrtVEL--NILSLWRKCFV-DEEDMMEVACTALTPEavfnasghvkkftd 140
Cdd:cd00774 1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLG--VELknNIKSAWRKSFVlEEEDMLEIDSPIITPE-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 141 lmvkdevdgafhradhlvksycenrkkdptisaenaaeldkviahvedlsaeelggvwnhcstapvtknplshpprpfnL 220
Cdd:cd00774 65 -------------------------------------------------------------------------------L 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 221 MFQTSFG--ASGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVHPE 298
Cdd:cd00774 66 MFKTSIGpvESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 299 hKSHSKFSDVAKLELLMFPREEQeKPGQFAKRLClgEAVAKGHVNSETLGFFIGRVYLFLIRLGIDKERLRFRHHLANEM 378
Cdd:cd00774 146 -KSHPWFDYWADQRLKWLPKFAQ-SPENLRLTDH--EKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNES 221
|
330 340 350
....*....|....*....|....*....|..
gi 42562400 379 AHYATDCWDAEIECSYGWIECVGIADRSDYDL 410
Cdd:cd00774 222 AHYASDCWDAEKLYVPGWIEVSGGADRTDYDL 253
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
67-415 |
1.16e-44 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 163.63 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 67 TLDRLL-------FVHKSFDIYHGVAGLYDFGPHGRTVELNILSLWRKCFVDEEDMME-VACTALTPEAVFNASGHVKKF 138
Cdd:PRK14894 5 SLDQIValakrrgFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEgLDAAILMNRLVWKYSGHEETF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 139 TDLMVKDEVDGAFHRADHlVKSYCENrkkdptisaenaaeldkviahvedlsaeelggvwnhCSTAPVTKnplshpPRPF 218
Cdd:PRK14894 85 NDPLVDCRDCKMRWRADH-IQGVCPN------------------------------------CGSRDLTE------PRPF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 219 NLMFQTSFG--ASGSLIGYLRPETAQGSFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIEHFVH 296
Cdd:PRK14894 122 NMMFRTQIGpvADSDSFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 297 P--EHKSHSKFsdvakLEllmfpreeqekpgqfaKRLCLGEAVakghvnsetlgffigrvylflirlGIDKERLRFRHHL 374
Cdd:PRK14894 202 PgtDEEWHQRW-----LE----------------ARLAWWEQI------------------------GIPRSRITIYDVP 236
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42562400 375 ANEMAHYATDCWDAEIEC-SYGWIECVGIADRSDYDLRAHSE 415
Cdd:PRK14894 237 PDELAHYSKRTFDLMYDYpNIGVQEIEGIANRTDYDLGSHSK 278
|
|
| 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 ... |
213-298 |
1.06e-09 |
|
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: 58.56 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 213 HPPRPFNLMFQTSFGASGSLIG--YLRPETAQGSFCNFKDYYnLNGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAE 290
Cdd:cd00670 40 HLDGYRKEMYTFEDKGRELRDTdlVLRPAACEPIYQIFSGEI-LSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVE 118
|
....*...
gi 42562400 291 IEHFVHPE 298
Cdd:cd00670 119 YVVFGEPE 126
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
235-298 |
4.28e-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: 50.58 E-value: 4.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42562400 235 YLRPETAQGSFCNFKDyynlNGRKLPFAVAQVGRVFRNEISPRqGLLRTREFTLAEIEHFVHPE 298
Cdd:cd00768 54 YLRPTLEPGLVRLFVS----HIRKLPLRLAEIGPAFRNEGGRR-GLRRVREFTQLEGEVFGEDG 112
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
235-319 |
1.17e-06 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 48.56 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562400 235 YLRPETAQGsFCNFKDYYNLNGRKLPFAVAQVGRVFRNEISPRQ-GLLRTREFTLAEIEHFVHPEhKSHSKFSDVAKLEL 313
Cdd:pfam00587 12 ALKPTNEPG-HTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHIFHAPG-QSPDELEDYIKLID 89
|
....*.
gi 42562400 314 LMFPRE 319
Cdd:pfam00587 90 RVYSRL 95
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
257-287 |
1.08e-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: 1.08e-05
10 20 30
....*....|....*....|....*....|.
gi 42562400 257 RKLPFAVAQVGRVFRNEISPRQGLLRTREFT 287
Cdd:cd00779 110 KQLPLNLYQIQTKFRDEIRPRFGLMRGREFL 140
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
257-290 |
1.05e-03 |
|
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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 40.81 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....
gi 42562400 257 RKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAE 290
Cdd:cd00772 116 KDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKD 149
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
235-296 |
3.70e-03 |
|
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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 39.12 E-value: 3.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42562400 235 YLRP--ETAqgsFCNfkdYYNL---NGRKLPFAVAQVGRVFRNEISPRQGLLRTREFTLAEIeHFVH 296
Cdd:cd00778 95 ALRPtsETA---IYP---MFSKwirSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEG-HTAH 154
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
257-287 |
6.00e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 38.91 E-value: 6.00e-03
10 20 30
....*....|....*....|....*....|.
gi 42562400 257 RKLPFAVAQVGRVFRNEISPRQGLLRTREFT 287
Cdd:PRK09194 126 KQLPLNLYQIQTKFRDEIRPRFGLMRGREFI 156
|
|
| |
