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Conserved domains on  [gi|1476597390|gb|AXZ12878|]
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phenylalanine--tRNA ligase subunit alpha [Klebsiella pneumoniae]

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]; ...
 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: 650.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390   1 MSHLAELVASAKAAINEASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELEG 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 161 DATRLLRTQTSGVQIRTMENQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDL 239
Cdd:COG0016   161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016   241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                         330
                  ....*....|....*....
gi 1476597390 309 VTDLRAFFENDLRFLKQFK 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: 650.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390   1 MSHLAELVASAKAAINEASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELEG 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 161 DATRLLRTQTSGVQIRTMENQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDL 239
Cdd:COG0016   161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016   241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                         330
                  ....*....|....*....
gi 1476597390 309 VTDLRAFFENDLRFLKQFK 327
Cdd:COG0016   321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 9.56e-169

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: 470.64  E-value: 9.56e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  37 HLTLQMTTLRELPPEE-RPAAGAVINEAKEQVQQALNARKAELEGAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDR 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 116 IESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDATRLLRTQTSGVQIRTM-ENQQPPIRIIAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMeEQEKPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 195 RND-YDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEdLQVRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476597390 273 GMVHPNVLRNVGIDPEvYSGFAFGMGMERLTMLRYGVTDLRAFFENDLRFLKQFK 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 2.65e-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: 411.97  E-value: 2.65e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  91 TIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF-------DAT 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 164 RLLRTQTSGVQIRTM-ENQQPPIRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDLQV 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 1476597390 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 2.67e-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: 365.33  E-value: 2.67e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 107 HPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFD--ATRLLRTQTSGVQIRTMENQQPP 184
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINdpARLLLRTHTSAVQARALAKLKPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 185 IRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDLQVRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496    81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1476597390 264 -GKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDLR 321
Cdd:cd00496   161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-327 2.41e-68

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 221.24  E-value: 2.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  93 DVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFW------------- 159
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdlpeel 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 160 ----------------------FD---ATRL-LRTQTSGVQIRTM-ENQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEG 211
Cdd:PRK04172  299 vervkevhehggdtgsrgwgykWDediAKRLvLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDtIDATHLPEFYQLEG 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 212 LIVDKNISFTNLKGTLHDFLNNF-FEEdlqVRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVy 290
Cdd:PRK04172  379 IVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVYHEGLGWVELGGAGIFRPEVLEPLGIDVPV- 454

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1476597390 291 sgFAFGMGMERLTMLRYGVTDLRAFFENDLRFLKQFK 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: 650.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390   1 MSHLAELVASAKAAINEASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELEG 80
Cdd:COG0016     1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  81 AALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF 160
Cdd:COG0016    81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 161 DATRLLRTQTSGVQIRTMENQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDL 239
Cdd:COG0016   161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYG 308
Cdd:COG0016   241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                         330
                  ....*....|....*....
gi 1476597390 309 VTDLRAFFENDLRFLKQFK 327
Cdd:COG0016   321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 9.56e-169

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: 470.64  E-value: 9.56e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  37 HLTLQMTTLRELPPEE-RPAAGAVINEAKEQVQQALNARKAELEGAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDR 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 116 IESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDATRLLRTQTSGVQIRTM-ENQQPPIRIIAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMeEQEKPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 195 RND-YDQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEdLQVRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476597390 273 GMVHPNVLRNVGIDPEvYSGFAFGMGMERLTMLRYGVTDLRAFFENDLRFLKQFK 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 2.65e-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: 411.97  E-value: 2.65e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  91 TIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWF-------DAT 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 164 RLLRTQTSGVQIRTM-ENQQPPIRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDLQV 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 1476597390 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 2.67e-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: 365.33  E-value: 2.67e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 107 HPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFD--ATRLLRTQTSGVQIRTMENQQPP 184
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINdpARLLLRTHTSAVQARALAKLKPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 185 IRIIAPGRVYRNDY-DQTHTPMFHQMEGLIVDKNISFTNLKGTLHDFLNNFFEEDLQVRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496    81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1476597390 264 -GKWLEVLGCGMVHPNVLRNVGIDpEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDLR 321
Cdd:cd00496   161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
93-327 2.41e-68

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 221.24  E-value: 2.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  93 DVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFW------------- 159
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdlpeel 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 160 ----------------------FD---ATRL-LRTQTSGVQIRTM-ENQQPPIRIIAPGRVYRND-YDQTHTPMFHQMEG 211
Cdd:PRK04172  299 vervkevhehggdtgsrgwgykWDediAKRLvLRTHTTALSARYLaSRPEPPQKYFSIGRVFRPDtIDATHLPEFYQLEG 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 212 LIVDKNISFTNLKGTLHDFLNNF-FEEdlqVRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVy 290
Cdd:PRK04172  379 IVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVYHEGLGWVELGGAGIFRPEVLEPLGIDVPV- 454

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1476597390 291 sgFAFGMGMERLTMLRYGVTDLRAFFENDLRFLKQFK 327
Cdd:PRK04172  455 --LAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 95-327 8.59e-50

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 170.71  E-value: 8.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  95 SLPGRRIENGGLHPVTRTIDRIESFFGEL---GFTV--ATGPeIEDDYHNFDALNIPGHHPARADHDTFWFDATRLLRTQ 169
Cdd:PLN02788   56 SKIGMQLHRRPDHPLGILKNAIYDYFDENysnKFKKfdDLSP-IVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 170 TSGVQIRTMENQQPpiRIIAPGRVYRND-YDQTHTPMFHQMEGLIVdknisFTN-----------------LKGTLHDFL 231
Cdd:PLN02788  135 TSAHQAELLRAGHT--HFLVTGDVYRRDsIDATHYPVFHQMEGVRV-----FSPeeweasgldgtdlaaedLKKTLEGLA 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 232 NNFFEeDLQVRFRPSYFPFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIDPEVysGFAFGMGMERLTMLRYGVTD 311
Cdd:PLN02788  208 RHLFG-DVEMRWVDAYFPFTNPSFELEIFFK-GEWLEVLGCGVTEQEILKNNGRSDNV--AWAFGLGLERLAMVLFDIPD 283

                         250
                  ....*....|....*.
gi 1476597390 312 LRAFFENDLRFLKQFK 327
Cdd:PLN02788  284 IRLFWSDDERFTSQFK 299
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 98-316 1.84e-41

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 150.50  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  98 GRRIENGGLHPVTRTIDRIESFFGELGFT-VATGPEIEDDYHNFDALNIPGHHPARADHDTFW------FDATRL----- 165
Cdd:PTZ00326  220 GKKIGGGNLHPLLKVRREFREILLEMGFEeMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFlskpetSKVNDLdddyv 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 166 ------------------------------LRTQTSGVQIRT---MENQQPPIRIIAPG------RVYRND-YDQTHTPM 205
Cdd:PTZ00326  300 ervkkvhevggygsigwrydwkleearkniLRTHTTAVSARMlykLAQEYKKTGPFKPKkyfsidRVFRNEtLDATHLAE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 206 FHQMEGLIVDKNISFTNLKGTLHdflnNFFE----EDLqvRFRPSYFPFTEPSAEvdVMG---KNGKWLEVLGCGMVHPN 278
Cdd:PTZ00326  380 FHQVEGFVIDRNLTLGDLIGTIR----EFFRrigiTKL--RFKPAFNPYTEPSME--IFGyhpGLKKWVEVGNSGIFRPE 451

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1476597390 279 VLRNVGIDPEVySGFAFGMGMERLTMLRYGVTDLRAFF 316
Cdd:PTZ00326  452 MLRPMGFPEDV-TVIAWGLSLERPTMIKYGIKNIRDLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 98-316 4.92e-39

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 143.66  E-value: 4.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  98 GRRIENGGLHPVTRTIDRIESFFGELGFT-VATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDA---TR--------- 164
Cdd:PLN02853  212 GAPPEGGHLHPLLKVRQQFRKIFLQMGFEeMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKApatTRqlpedyver 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 165 ---------------------------LLRTQTSGVQIRTMEN--QQP--PIRIIAPGRVYRND-YDQTHTPMFHQMEGL 212
Cdd:PLN02853  292 vktvhesggygsigygydwkreeanknLLRTHTTAVSSRMLYKlaQKGfkPKRYFSIDRVFRNEaVDRTHLAEFHQVEGL 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 213 IVDKNISFTNLKGTLHDFLNNFFEEDLqvRFRPSYFPFTEPSAEV-DVMGKNGKWLEVLGCGMVHPNVLRNVGIdPEVYS 291
Cdd:PLN02853  372 VCDRGLTLGDLIGVLEDFFSRLGMTKL--RFKPAYNPYTEPSMEIfSYHEGLKKWVEVGNSGMFRPEMLLPMGL-PEDVN 448

                         250       260
                  ....*....|....*....|....*
gi 1476597390 292 GFAFGMGMERLTMLRYGVTDLRAFF 316
Cdd:PLN02853  449 VIAWGLSLERPTMILYGIDNIRDLF 473
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 94-326 9.02e-37

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: 137.13  E-value: 9.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390  94 VSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGP--EIEDDY-------HNFDALNIPGHHPARADHDTFWFDATR 164
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPlfKIFDNFkpvvttmENFDNLGFPADHPGRQKSDCYYINEQH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 165 LLRTQTSGVQIRTME---NQQPPIR--IIAPGRVYRND-YDQTHTPMFHQMEG--------------------------- 211
Cdd:TIGR00469 109 LLRAHTSAHELECFQgglDDSDNIKsgFLISADVYRRDeIDKTHYPVFHQADGaairkrtkadlfekepgyiekfeedir 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 212 ------------LIVDKNISFTN------------------------LKGTLHDFLN-----------NFFEEDLQVRFR 244
Cdd:TIGR00469 189 gteadlnkenvkIILDDDSIPLKennpkqeyasdlavdlcehelkhsIEGITKDLFGkkissmiknkaNNTPKELKVRWI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 245 PSYFPFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRAFFENDLRFLK 324
Cdd:TIGR00469 269 DAYFPFTAPSWEIEIWFK-DEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLR 347


                  ..
gi 1476597390 325 QF 326
Cdd:TIGR00469 348 QF 349
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
19-87 6.29e-31

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 111.32  E-value: 6.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1476597390  19 SDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELEGAALNARL 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 6.88e-14

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: 69.45  E-value: 6.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 112 TIDRIES----FFGELGFTVATGPEIEDDYHNFDAlnipGHHPARADHDTFWFDATRLLRTQTSGVQIRTMEN--QQPPI 185
Cdd:cd00768     1 IRSKIEQklrrFMAELGFQEVETPIVEREPLLEKA----GHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVShiRKLPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476597390 186 RIIAPGRVYRND---YDQTHTPMFHQMEGLIV----DKNISFTNLKGTLHDFLNNFFEEDLQVRFRPSYFPFT----EPS 254
Cdd:cd00768    77 RLAEIGPAFRNEggrRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSpggaGPG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476597390 255 AEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSG-------FAFGMGMERL 302
Cdd:cd00768   157 FEIEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALeyrypptIGFGLGLERL 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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