NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16129670|ref|NP_416229|]
View 

phenylalanine--tRNA ligase subunit alpha [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-327 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: 651.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   1 MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELES 80
Cdd:COG0016   1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016  81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 161 DTTRLLRTQTSGVQIRTMKAQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDL 239
Cdd:COG0016 161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 240 QIRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016 241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                       330
                ....*....|....*....
gi 16129670 309 VTDLRSFFENDLRFLKQFK 327
Cdd:COG0016 321 IDDIRLFFENDLRFLRQFG 339
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-327 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: 651.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   1 MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELES 80
Cdd:COG0016   1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016  81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 161 DTTRLLRTQTSGVQIRTMKAQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDL 239
Cdd:COG0016 161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 240 QIRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016 241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                       330
                ....*....|....*....
gi 16129670 309 VTDLRSFFENDLRFLKQFK 327
Cdd:COG0016 321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 7.45e-170

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: 473.34  E-value: 7.45e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    37 HLTLQMTTLRELPPEE-RPAAGAVINEAKEQVQQALNARKAELESAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDR 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   116 IESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKAQQ-PPIRIIAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEkPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   195 RND-YDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEdLQIRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16129670   273 GMVHPNVLRNVGIDPEvYSGFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK 327
Cdd:TIGR00468 240 GMFRPEVLEPMGIDPT-YPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-326 3.92e-146

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: 411.20  E-value: 3.92e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    91 TIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF-------DTT 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   164 RLLRTQTSGVQIRTM-KAQQPPIRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQI 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 16129670   321 RFLKQF 326
Cdd:pfam01409 240 RFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 107-321 2.98e-128

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: 364.94  E-value: 2.98e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 107 HPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTT--RLLRTQTSGVQIRTMKAQQPP 184
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKLKPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 185 IRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQIRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496  81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129670 264 -GKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDLR 321
Cdd:cd00496 161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-327 8.24e-66

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 214.70  E-value: 8.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   93 DVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRL------- 165
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIgdlpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  166 --------------------------------LRTQTSGVQIRTM-KAQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEG 211
Cdd:PRK04172 299 vervkevhehggdtgsrgwgykwdediakrlvLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDtIDATHLPEFYQLEG 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  212 LIVDTNISFTNLKGTLHDFLRNF-FEEdlqIRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVy 290
Cdd:PRK04172 379 IVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVYHEGLGWVELGGAGIFRPEVLEPLGIDVPV- 454

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129670  291 sgFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK 327
Cdd:PRK04172 455 --LAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-327 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: 651.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   1 MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELES 80
Cdd:COG0016   1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016  81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 161 DTTRLLRTQTSGVQIRTMKAQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDL 239
Cdd:COG0016 161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 240 QIRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016 241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                       330
                ....*....|....*....
gi 16129670 309 VTDLRSFFENDLRFLKQFK 327
Cdd:COG0016 321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 7.45e-170

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: 473.34  E-value: 7.45e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    37 HLTLQMTTLRELPPEE-RPAAGAVINEAKEQVQQALNARKAELESAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDR 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   116 IESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKAQQ-PPIRIIAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEkPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   195 RND-YDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEdLQIRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16129670   273 GMVHPNVLRNVGIDPEvYSGFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK 327
Cdd:TIGR00468 240 GMFRPEVLEPMGIDPT-YPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-326 3.92e-146

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: 411.20  E-value: 3.92e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    91 TIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF-------DTT 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   164 RLLRTQTSGVQIRTM-KAQQPPIRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQI 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 16129670   321 RFLKQF 326
Cdd:pfam01409 240 RFLRQF 245
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 107-321 2.98e-128

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: 364.94  E-value: 2.98e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 107 HPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTT--RLLRTQTSGVQIRTMKAQQPP 184
Cdd:cd00496   1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKLKPP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 185 IRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQIRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496  81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129670 264 -GKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDLR 321
Cdd:cd00496 161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-327 8.24e-66

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 214.70  E-value: 8.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   93 DVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRL------- 165
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIgdlpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  166 --------------------------------LRTQTSGVQIRTM-KAQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEG 211
Cdd:PRK04172 299 vervkevhehggdtgsrgwgykwdediakrlvLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDtIDATHLPEFYQLEG 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  212 LIVDTNISFTNLKGTLHDFLRNF-FEEdlqIRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVy 290
Cdd:PRK04172 379 IVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVYHEGLGWVELGGAGIFRPEVLEPLGIDVPV- 454

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129670  291 sgFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK 327
Cdd:PRK04172 455 --LAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 95-327 2.36e-51

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 174.57  E-value: 2.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   95 SLPGRRIENGGLHPVTRTIDRIESFFGEL---GFTV--ATGPeIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQ 169
Cdd:PLN02788  56 SKIGMQLHRRPDHPLGILKNAIYDYFDENysnKFKKfdDLSP-IVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCH 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  170 TSGVQIRTMKAQQPpiRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDTNISFT------------NLKGTLHDFLRNFFE 236
Cdd:PLN02788 135 TSAHQAELLRAGHT--HFLVTGDVYRRDsIDATHYPVFHQMEGVRVFSPEEWEasgldgtdlaaeDLKKTLEGLARHLFG 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  237 eDLQIRFRPSYFPFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIDPEVysGFAFGMGMERLTMLRYGVTDLRSFF 316
Cdd:PLN02788 213 -DVEMRWVDAYFPFTNPSFELEIFFK-GEWLEVLGCGVTEQEILKNNGRSDNV--AWAFGLGLERLAMVLFDIPDIRLFW 288

                        250
                 ....*....|.
gi 16129670  317 ENDLRFLKQFK 327
Cdd:PLN02788 289 SDDERFTSQFK 299
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 98-316 5.46e-43

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 154.74  E-value: 5.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   98 GRRIENGGLHPVTRTIDRIESFFGELGFT-VATGPEIEDDYHNFDALNIPGHHPARADHDTFWFD---TTR--------- 164
Cdd:PTZ00326 220 GKKIGGGNLHPLLKVRREFREILLEMGFEeMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSkpeTSKvndldddyv 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  165 -----------------------------LLRTQTSGVQIRTMK--AQQ-------PPIRIIAPGRVYRND-YDQTHTPM 205
Cdd:PTZ00326 300 ervkkvhevggygsigwrydwkleearknILRTHTTAVSARMLYklAQEykktgpfKPKKYFSIDRVFRNEtLDATHLAE 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  206 FHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLqiRFRPSYFPFTEPSAEvdVMG---KNGKWLEVLGCGMVHPNVLRN 282
Cdd:PTZ00326 380 FHQVEGFVIDRNLTLGDLIGTIREFFRRIGITKL--RFKPAFNPYTEPSME--IFGyhpGLKKWVEVGNSGIFRPEMLRP 455

                        250       260       270
                 ....*....|....*....|....*....|....
gi 16129670  283 VGIDPEVySGFAFGMGMERLTMLRYGVTDLRSFF 316
Cdd:PTZ00326 456 MGFPEDV-TVIAWGLSLERPTMIKYGIKNIRDLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 98-316 6.24e-40

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 146.36  E-value: 6.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   98 GRRIENGGLHPVTRTIDRIESFFGELGFT-VATGPEIEDDYHNFDALNIPGHHPARADHDTFWFD---TTR--------- 164
Cdd:PLN02853 212 GAPPEGGHLHPLLKVRQQFRKIFLQMGFEeMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKapaTTRqlpedyver 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  165 ---------------------------LLRTQTSGVQIRTMK--AQQP--PIRIIAPGRVYRND-YDQTHTPMFHQMEGL 212
Cdd:PLN02853 292 vktvhesggygsigygydwkreeanknLLRTHTTAVSSRMLYklAQKGfkPKRYFSIDRVFRNEaVDRTHLAEFHQVEGL 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670  213 IVDTNISFTNLKGTLHDFLRNFFEEdlQIRFRPSYFPFTEPSAEV-DVMGKNGKWLEVLGCGMVHPNVLRNVGIdPEVYS 291
Cdd:PLN02853 372 VCDRGLTLGDLIGVLEDFFSRLGMT--KLRFKPAYNPYTEPSMEIfSYHEGLKKWVEVGNSGMFRPEMLLPMGL-PEDVN 448

                        250       260
                 ....*....|....*....|....*
gi 16129670  292 GFAFGMGMERLTMLRYGVTDLRSFF 316
Cdd:PLN02853 449 VIAWGLSLERPTMILYGIDNIRDLF 473
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 94-326 8.75e-36

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: 134.43  E-value: 8.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    94 VSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGP--EIEDDY-------HNFDALNIPGHHPARADHDTFWFDTTR 164
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPlfKIFDNFkpvvttmENFDNLGFPADHPGRQKSDCYYINEQH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   165 LLRTQTSGVQIRTMK-----AQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEG--------------------------- 211
Cdd:TIGR00469 109 LLRAHTSAHELECFQgglddSDNIKSGFLISADVYRRDeIDKTHYPVFHQADGaairkrtkadlfekepgyiekfeedir 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   212 ------------LIVDTNISFT--------------------NLKGTLHDFLRNFF---------------EEDLQIRFR 244
Cdd:TIGR00469 189 gteadlnkenvkIILDDDSIPLkennpkqeyasdlavdlcehELKHSIEGITKDLFgkkissmiknkanntPKELKVRWI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   245 PSYFPFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDLRFLK 324
Cdd:TIGR00469 269 DAYFPFTAPSWEIEIWFK-DEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLR 347


                  ..
gi 16129670   325 QF 326
Cdd:TIGR00469 348 QF 349
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
19-87 6.11e-32

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 114.02  E-value: 6.11e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129670    19 SDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELESAALNARL 87
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 ...
 112-302 3.44e-15

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: 73.31  E-value: 3.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 112 TIDRIES----FFGELGFTVATGPEIEDDYHNFDAlnipGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKA--QQPPI 185
Cdd:cd00768   1 IRSKIEQklrrFMAELGFQEVETPIVEREPLLEKA----GHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVShiRKLPL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 186 RIIAPGRVYRND---YDQTHTPMFHQMEGLIV----DTNISFTNLKGTLHDFLRNFFEEDLQIRFRPSYFPFT----EPS 254
Cdd:cd00768  77 RLAEIGPAFRNEggrRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSpggaGPG 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129670 255 AEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSG-------FAFGMGMERL 302
Cdd:cd00768 157 FEIEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALeyrypptIGFGLGLERL 211
tRNA_synthFbeta pfam17759
Phenylalanyl tRNA synthetase beta chain CLM domain; This domain corresponds to the catalytic ...
 92-290 5.19e-04

Phenylalanyl tRNA synthetase beta chain CLM domain; This domain corresponds to the catalytic like domain (CLM) in the beta chain of phe tRNA synthetase.


Pssm-ID: 465487 [Multi-domain]  Cd Length: 214  Bit Score: 40.61  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670    92 IDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVA-----TGPEIEDDYHNFD----ALNIPghHPARADHDTfwfdt 162
Cdd:pfam17759   1 IPSTLPKGPTTGGGLTPEQKLRRRVRDLLAAAGFTEVitysfTSPKDLDKLLEDDprrkAVKLA--NPLSEELSV----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   163 trlLRTQT--SGVQI--RTMKAQQPPIRIIAPGRVYRNDYDQT---------------HTPMFHQMEGLIVDtnisFTNL 223
Cdd:pfam17759  74 ---MRTSLlpGLLETlaYNLNRGNPDVRLFEIGRVFLPDELEElpreprrlaglltgkRLPESWQGKARPVD----FYDL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670   224 KGTLHDFLRNFFEEDLqiRFRPSYFPFTEP--SAEVDVMGKngkwleVLG-CGMVHPNVLRNVGIDPEVY 290
Cdd:pfam17759 147 KGIVEALLAALGIDDY--EFEAADHPALHPgrSAEILVGGK------VIGfIGELHPEVAKNFDLPQPVY 208
PheRS_beta_core cd00769
Phenylalanyl-tRNA synthetase (PheRS) beta chain core domain. PheRS belongs to class II ...
 176-290 2.64e-03

Phenylalanyl-tRNA synthetase (PheRS) beta chain core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure. 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. While the alpha chain contains a catalytic core domain, the beta chain has a non-catalytic core domain.


Pssm-ID: 238392 [Multi-domain]  Cd Length: 198  Bit Score: 38.39  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129670 176 RTMKAQQPPIRIIAPGRVYRNDYDQTHTP------MFHQMEGLIVDTN---ISFTNLKGTLHDFLRnFFEEDLQIRFRPS 246
Cdd:cd00769  70 RNLNRKNKPLRLFEIGRVFLKDEDGPEEEehlaalLSGNREPESWQGKgrpVDFYDAKGILEALLR-ALGIIVEFELEEL 148

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16129670 247 YFPFTEP--SAEVDVMGkngkwlEVLGC-GMVHPNVLRNVGIDPEVY 290
Cdd:cd00769 149 DADLFHPgrSAKIYVNG------EVIGFiGELHPEVLKEFDLKEPVY 189
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH