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Conserved domains on  [gi|654744015|ref|WP_028200200|]
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MULTISPECIES: phenylalanine--tRNA ligase subunit alpha [Paraburkholderia]

Protein Classification

phenylalanine--tRNA ligase subunit alpha( domain architecture ID 17564626)

phenylalanine--tRNA ligase subunit alpha is the catalytic subunit of the enzyme complex that catalyzes the attachment of phenylalanine to tRNA(Phe)

CATH:  3.30.930.10
EC:  6.1.1.20
Gene Ontology:  GO:0005524|GO:0006432|GO:0000287|GO:0004826|GO:0000049
PubMed:  14665676|8274143|11310981|1852601|2053131|10447505|10704480|12458790

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 2-336 0e+00

Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


:

Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 592.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   2 DLDQIVADAQKAFAEASDVTTLENEKARFLGKSGALTELLKGLGKLDPETRKTEGARINLVKQQVEAALTARRQALADAL 81
Cdd:COG0016    3 ELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  82 LNQRLAAEAIDVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDG 161
Cdd:COG0016   83 LEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 162 KdadgrqLLLRTHTSPMQVRYARTNTPPIKVIVPGRTYRVD-SDATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFF 240
Cdd:COG0016  163 G------LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 241 ERdDIQVRFRPSYFPFTEPSAEIDMLFETGKNAG-------KWLEISGSGQVHPTVIRNMGLDPERYIGFAFGSGLERLT 313
Cdd:COG0016  237 GE-DVKVRFRPSYFPFTEPSAEVDISCFICGGKGcrvckgtGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLA 315

                        330       340
                 ....*....|....*....|...
gi 654744015 314 MLRYGVQDLRLFFENDLRFLRQF 336
Cdd:COG0016  316 MLKYGIDDIRLFFENDLRFLRQF 338
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 2-336 0e+00

Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 592.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   2 DLDQIVADAQKAFAEASDVTTLENEKARFLGKSGALTELLKGLGKLDPETRKTEGARINLVKQQVEAALTARRQALADAL 81
Cdd:COG0016    3 ELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  82 LNQRLAAEAIDVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDG 161
Cdd:COG0016   83 LEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 162 KdadgrqLLLRTHTSPMQVRYARTNTPPIKVIVPGRTYRVD-SDATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFF 240
Cdd:COG0016  163 G------LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 241 ERdDIQVRFRPSYFPFTEPSAEIDMLFETGKNAG-------KWLEISGSGQVHPTVIRNMGLDPERYIGFAFGSGLERLT 313
Cdd:COG0016  237 GE-DVKVRFRPSYFPFTEPSAEVDISCFICGGKGcrvckgtGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLA 315

                        330       340
                 ....*....|....*....|...
gi 654744015 314 MLRYGVQDLRLFFENDLRFLRQF 336
Cdd:COG0016  316 MLKYGIDDIRLFFENDLRFLRQF 338
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 36-336 1.84e-126

phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273095 [Multi-domain]  Cd Length: 293  Bit Score: 363.94  E-value: 1.84e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   36 ALTELLKGLGKLDP-ETRKTEGARINLVKQQVEAALTARRQALADALLNQRLAAEAIDVTLPGRGTGAGSLHPVMRTWER 114
Cdd:TIGR00468   1 KLKDLLKQLGKLTKeETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  115 VEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDgkdadgRQLLLRTHTSPMQVRYARTNT-PPIKVI 193
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIK------DRLLLRTHTTAVQLRTMEEQEkPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  194 VPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFErdDIQVRFRPSYFPFTEPSAEIDMLFETGKN 272
Cdd:TIGR00468 155 SPGRVFRNDTvDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFG--ETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654744015  273 agkWLEISGSGQVHPTVIRNMGLDPErYIGFAFGSGLERLTMLRYGVQDLRLFFENDLRFLRQF 336
Cdd:TIGR00468 233 ---WLEVLGAGMFRPEVLEPMGIDPT-YPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-336 4.81e-126

tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.


Pssm-ID: 396130 [Multi-domain]  Cd Length: 245  Bit Score: 360.74  E-value: 4.81e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   91 IDVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDGK-DADGRQL 169
Cdd:pfam01409   2 YDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPlKPVARRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  170 LLRTHTSPMQVRY-ARTNTPPIKVIVPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFERDDiQV 247
Cdd:pfam01409  82 LLRTHTTPVQARTlAKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEV-KV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  248 RFRPSYFPFTEPSAEIDMLFETGknaGKWLEISGSGQVHPTVIRNMGLDpERYIGFAFGSGLERLTMLRYGVQDLRLFFE 327
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYVCKL---GGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYE 236


                  ....*....
gi 654744015  328 NDLRFLRQF 336
Cdd:pfam01409 237 NDLRFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 106-331 6.80e-114

Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.


Pssm-ID: 238277 [Multi-domain]  Cd Length: 218  Bit Score: 329.12  E-value: 6.80e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 106 HPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDgkdaDGRQLLLRTHTSPMQVRYART 185
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYIN----DPARLLLRTHTSAVQARALAK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 186 NTPPIKVIVPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFErDDIQVRFRPSYFPFTEPSAEID 264
Cdd:cd00496   77 LKPPIRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFG-PITKVRFRPSYFPFTEPSFEVD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654744015 265 MLFEtgkNAGKWLEISGSGQVHPTVIRNMGLDpERYIGFAFGSGLERLTMLRYGVQDLRLFFENDLR 331
Cdd:cd00496  156 VYCP---GCLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
92-334 3.14e-62

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 205.84  E-value: 3.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  92 DVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVD----------- 160
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLKypgigdlpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 161 ----------GKDADG------------RQLLLRTHTSPMQVRY-ARTNTPPIKVIVPGRTYRVDS-DATHSPMFNQVEG 216
Cdd:PRK04172 299 vervkevhehGGDTGSrgwgykwdediaKRLVLRTHTTALSARYlASRPEPPQKYFSIGRVFRPDTiDATHLPEFYQLEG 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 217 LWIDENISFADLKGVYSDFLKKF-FErddiQVRFRPSYFPFTEPSAEIDMLFETgknaGKWLEISGSGQVHPTVIRNMGL 295
Cdd:PRK04172 379 IVMGEDVSFRDLLGILKEFYKRLgFE----EVKFRPAYFPFTEPSVEVEVYHEG----LGWVELGGAGIFRPEVLEPLGI 450

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 654744015 296 DperYIGFAFGSGLERLTMLRYGVQDLRLFFENDLRFLR 334
Cdd:PRK04172 451 D---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWLR 486
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 2-336 0e+00

Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439787 [Multi-domain]  Cd Length: 339  Bit Score: 592.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   2 DLDQIVADAQKAFAEASDVTTLENEKARFLGKSGALTELLKGLGKLDPETRKTEGARINLVKQQVEAALTARRQALADAL 81
Cdd:COG0016    3 ELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  82 LNQRLAAEAIDVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDG 161
Cdd:COG0016   83 LEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 162 KdadgrqLLLRTHTSPMQVRYARTNTPPIKVIVPGRTYRVD-SDATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFF 240
Cdd:COG0016  163 G------LLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 241 ERdDIQVRFRPSYFPFTEPSAEIDMLFETGKNAG-------KWLEISGSGQVHPTVIRNMGLDPERYIGFAFGSGLERLT 313
Cdd:COG0016  237 GE-DVKVRFRPSYFPFTEPSAEVDISCFICGGKGcrvckgtGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLA 315

                        330       340
                 ....*....|....*....|...
gi 654744015 314 MLRYGVQDLRLFFENDLRFLRQF 336
Cdd:COG0016  316 MLKYGIDDIRLFFENDLRFLRQF 338
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 36-336 1.84e-126

phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273095 [Multi-domain]  Cd Length: 293  Bit Score: 363.94  E-value: 1.84e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   36 ALTELLKGLGKLDP-ETRKTEGARINLVKQQVEAALTARRQALADALLNQRLAAEAIDVTLPGRGTGAGSLHPVMRTWER 114
Cdd:TIGR00468   1 KLKDLLKQLGKLTKeETKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  115 VEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDgkdadgRQLLLRTHTSPMQVRYARTNT-PPIKVI 193
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIK------DRLLLRTHTTAVQLRTMEEQEkPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  194 VPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFErdDIQVRFRPSYFPFTEPSAEIDMLFETGKN 272
Cdd:TIGR00468 155 SPGRVFRNDTvDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFG--ETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654744015  273 agkWLEISGSGQVHPTVIRNMGLDPErYIGFAFGSGLERLTMLRYGVQDLRLFFENDLRFLRQF 336
Cdd:TIGR00468 233 ---WLEVLGAGMFRPEVLEPMGIDPT-YPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-336 4.81e-126

tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.


Pssm-ID: 396130 [Multi-domain]  Cd Length: 245  Bit Score: 360.74  E-value: 4.81e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   91 IDVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDGK-DADGRQL 169
Cdd:pfam01409   2 YDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPlKPVARRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  170 LLRTHTSPMQVRY-ARTNTPPIKVIVPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFERDDiQV 247
Cdd:pfam01409  82 LLRTHTTPVQARTlAKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEV-KV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  248 RFRPSYFPFTEPSAEIDMLFETGknaGKWLEISGSGQVHPTVIRNMGLDpERYIGFAFGSGLERLTMLRYGVQDLRLFFE 327
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYVCKL---GGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYE 236


                  ....*....
gi 654744015  328 NDLRFLRQF 336
Cdd:pfam01409 237 NDLRFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 106-331 6.80e-114

Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.


Pssm-ID: 238277 [Multi-domain]  Cd Length: 218  Bit Score: 329.12  E-value: 6.80e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 106 HPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVDgkdaDGRQLLLRTHTSPMQVRYART 185
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYIN----DPARLLLRTHTSAVQARALAK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 186 NTPPIKVIVPGRTYRVDS-DATHSPMFNQVEGLWIDENISFADLKGVYSDFLKKFFErDDIQVRFRPSYFPFTEPSAEID 264
Cdd:cd00496   77 LKPPIRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFG-PITKVRFRPSYFPFTEPSFEVD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654744015 265 MLFEtgkNAGKWLEISGSGQVHPTVIRNMGLDpERYIGFAFGSGLERLTMLRYGVQDLRLFFENDLR 331
Cdd:cd00496  156 VYCP---GCLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
92-334 3.14e-62

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 205.84  E-value: 3.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  92 DVTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGPEIETDWYNFTSLNSPENHPARSMQDTFYVD----------- 160
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLKypgigdlpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 161 ----------GKDADG------------RQLLLRTHTSPMQVRY-ARTNTPPIKVIVPGRTYRVDS-DATHSPMFNQVEG 216
Cdd:PRK04172 299 vervkevhehGGDTGSrgwgykwdediaKRLVLRTHTTALSARYlASRPEPPQKYFSIGRVFRPDTiDATHLPEFYQLEG 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 217 LWIDENISFADLKGVYSDFLKKF-FErddiQVRFRPSYFPFTEPSAEIDMLFETgknaGKWLEISGSGQVHPTVIRNMGL 295
Cdd:PRK04172 379 IVMGEDVSFRDLLGILKEFYKRLgFE----EVKFRPAYFPFTEPSVEVEVYHEG----LGWVELGGAGIFRPEVLEPLGI 450

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 654744015 296 DperYIGFAFGSGLERLTMLRYGVQDLRLFFENDLRFLR 334
Cdd:PRK04172 451 D---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWLR 486
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 138-337 2.07e-45

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 159.54  E-value: 2.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 138 NFTSLNSPENHPARSMQDTFYVDgkdadgRQLLLRTHTSPMQVRYARTNTPpiKVIVPGRTYRVDS-DATHSPMFNQVEG 216
Cdd:PLN02788 104 NFDDVLVPPDHVSRSYNDTYYVD------AQTVLRCHTSAHQAELLRAGHT--HFLVTGDVYRRDSiDATHYPVFHQMEG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 217 L-------WID---ENISFA--DLKGVYSDFLKKFFerDDIQVRFRPSYFPFTEPSAEIDMLFEtgknaGKWLEISGSGQ 284
Cdd:PLN02788 176 VrvfspeeWEAsglDGTDLAaeDLKKTLEGLARHLF--GDVEMRWVDAYFPFTNPSFELEIFFK-----GEWLEVLGCGV 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 654744015 285 VHPTVIRNMGLDPERyiGFAFGSGLERLTMLRYGVQDLRLFFENDLRFLRQFA 337
Cdd:PLN02788 249 TEQEILKNNGRSDNV--AWAFGLGLERLAMVLFDIPDIRLFWSDDERFTSQFK 299
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 97-325 2.52e-43

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 155.90  E-value: 2.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  97 GRGTGAGSLHPVMRTWERVEQIFRTIGFDvadgpEIETDWY------NFTSLNSPENHPARSMQDTFYVDG--------- 161
Cdd:PTZ00326 220 GKKIGGGNLHPLLKVRREFREILLEMGFE-----EMPTNRYvessfwNFDALFQPQQHPARDAQDTFFLSKpetskvndl 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 162 --------------------------KDADGRQLLLRTHTSPMQVR--------YARTNtppikVIVPGRTYRVDS---- 203
Cdd:PTZ00326 295 dddyvervkkvhevggygsigwrydwKLEEARKNILRTHTTAVSARmlyklaqeYKKTG-----PFKPKKYFSIDRvfrn 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 204 ---DATHSPMFNQVEGLWIDENISFADLKGVysdfLKKFFERDDI-QVRFRPSYFPFTEPSAEIdmlFETGKNAGKWLEI 279
Cdd:PTZ00326 370 etlDATHLAEFHQVEGFVIDRNLTLGDLIGT----IREFFRRIGItKLRFKPAFNPYTEPSMEI---FGYHPGLKKWVEV 442

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 654744015 280 SGSGQVHPTVIRNMGLdPERYIGFAFGSGLERLTMLRYGVQDLR-LF 325
Cdd:PTZ00326 443 GNSGIFRPEMLRPMGF-PEDVTVIAWGLSLERPTMIKYGIKNIRdLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 97-326 4.47e-40

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 147.13  E-value: 4.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  97 GRGTGAGSLHPVMRTWERVEQIFRTIGFdvADGPE---IETDWYNFTSLNSPENHPARSMQDTF--------------YV 159
Cdd:PLN02853 212 GAPPEGGHLHPLLKVRQQFRKIFLQMGF--EEMPTnnfVESSFWNFDALFQPQQHPARDSHDTFflkapattrqlpedYV 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 160 -------------------DGKDADGRQLLLRTHTSPMQVR--YARTNTPpikvIVPGRTYRVDS-------DATHSPMF 211
Cdd:PLN02853 290 ervktvhesggygsigygyDWKREEANKNLLRTHTTAVSSRmlYKLAQKG----FKPKRYFSIDRvfrneavDRTHLAEF 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 212 NQVEGLWIDENISFADLKGVysdfLKKFFERDDI-QVRFRPSYFPFTEPSAEIdmlFETGKNAGKWLEISGSGQVHPTVI 290
Cdd:PLN02853 366 HQVEGLVCDRGLTLGDLIGV----LEDFFSRLGMtKLRFKPAYNPYTEPSMEI---FSYHEGLKKWVEVGNSGMFRPEML 438

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 654744015 291 RNMGLdPERYIGFAFGSGLERLTMLRYGVQDLRLFF 326
Cdd:PLN02853 439 LPMGL-PEDVNVIAWGLSLERPTMILYGIDNIRDLF 473
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 93-337 2.89e-31

phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129561 [Multi-domain]  Cd Length: 460  Bit Score: 122.49  E-value: 2.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015   93 VTLPGRGTGAGSLHPVMRTWERVEQIFRTIGFDVADGP---------EIETDWYNFTSLNSPENHPARSMQDTFYVDgkd 163
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPlfkifdnfkPVVTTMENFDNLGFPADHPGRQKSDCYYIN--- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  164 adgRQLLLRTHTSPMQVRY---ARTNTPPIKV--IVPGRTYRVDS-DATHSPMFNQVEG--------------------- 216
Cdd:TIGR00469 106 ---EQHLLRAHTSAHELECfqgGLDDSDNIKSgfLISADVYRRDEiDKTHYPVFHQADGaairkrtkadlfekepgyiek 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  217 -------------------------LWIDEN-------------ISFADLKGVYSDFLKKFFER--------------DD 244
Cdd:TIGR00469 183 feedirgteadlnkenvkiildddsIPLKENnpkqeyasdlavdLCEHELKHSIEGITKDLFGKkissmiknkanntpKE 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015  245 IQVRFRPSYFPFTEPSAEIDMLFEtgknaGKWLEISGSGQVHPTVIRNMGLDPERYIGFAFGSGLERLTMLRYGVQDLRL 324
Cdd:TIGR00469 263 LKVRWIDAYFPFTAPSWEIEIWFK-----DEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRL 337

                         330
                  ....*....|...
gi 654744015  325 FFENDLRFLRQFA 337
Cdd:TIGR00469 338 FWSNDEGFLRQFS 350
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
18-86 9.09e-23

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 89.75  E-value: 9.09e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654744015   18 SDVTTLENEKARFLGKSGALTELLKGLGKLDPETRKTEGARINLVKQQVEAALTARRQALADALLNQRL 86
Cdd:pfam02912   1 SDLEELEELRVKYLGKKGELTALLKGLGKLPPEERPAAGKLINELKQAIEAALEERKEELEAAELEARL 69
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 111-312 1.43e-09

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: 57.13  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 111 TWERVEQIFRTI----GFDVADGPEIETDwynfTSLNSPENHPARSMQDTFYVDGkdadgrQLLLRTHTSPMQVRYARTN 186
Cdd:cd00768    1 IRSKIEQKLRRFmaelGFQEVETPIVERE----PLLEKAGHEPKDLLPVGAENEE------DLYLRPTLEPGLVRLFVSH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654744015 187 --TPPIKVIVPGRTYR---VDSDATHSPMFNQVEGLW----IDENISFADLKGVYSDFLKKFFERDDIqVRFRPSYFPFT 257
Cdd:cd00768   71 irKLPLRLAEIGPAFRnegGRRGLRRVREFTQLEGEVfgedGEEASEFEELIELTEELLRALGIKLDI-VFVEKTPGEFS 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654744015 258 EPSAEIDMLFETGKNAGKWLEISGSGQVHPTVIRNMGLD----PERYI---GFAFGSGLERL 312
Cdd:cd00768  150 PGGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARAADLYfldeALEYRyppTIGFGLGLERL 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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