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Conserved domains on  [gi|491999360|ref|WP_005714554|]
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phenylalanine--tRNA ligase subunit alpha [Glaesserella parasuis]

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: 617.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   1 MQNLENIVAEALQAVEKASDVASLEALRVEYFGKKGHFTLLMQGLRDVPADERPAVGAKINEAKQKAQDALNGKKEQLET 80
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  81 EELNAKLASESIDVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWF 160
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 161 DAERLLRTQTSGVQIRTMEKMQPPIRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDL 239
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPDEYTGFAVGMGVERLTMLRYN 308
Cdd:COG0016  241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                        330
                 ....*....|....*....
gi 491999360 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: 617.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   1 MQNLENIVAEALQAVEKASDVASLEALRVEYFGKKGHFTLLMQGLRDVPADERPAVGAKINEAKQKAQDALNGKKEQLET 80
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  81 EELNAKLASESIDVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWF 160
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 161 DAERLLRTQTSGVQIRTMEKMQPPIRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDL 239
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPDEYTGFAVGMGVERLTMLRYN 308
Cdd:COG0016  241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                        330
                 ....*....|....*....
gi 491999360 309 VTDLRSFFENDLRFLKQFK 327
Cdd:COG0016  321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 2.63e-158

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: 444.06  E-value: 2.63e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   37 HFTLLMQGLRDVPADE-RPAVGAKINEAKQKAQDALNGKKEQLETEELNAKLASESIDVSLPGCKTELGGLHPVSITIER 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  116 VVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWFDAERLLRTQTSGVQIRTMEKMQ-PPIRIMAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEkPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  195 RND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEdLQVRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491999360  273 GMVHPNVLRNVGIDPdEYTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK 327
Cdd:TIGR00468 240 GMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-326 6.57e-135

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: 383.08  E-value: 6.57e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   91 SIDVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWF-------DAE 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  164 RLLRTQTSGVQIRTM-EKMQPPIRIMAPGRVYRNDY-DQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDLQV 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpDEYTGFAVGMGVERLTMLRYNVTDLRSFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 491999360  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 1.46e-123

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: 353.00  E-value: 1.46e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 107 HPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWFD--AERLLRTQTSGVQIRTMEKMQPP 184
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINdpARLLLRTHTSAVQARALAKLKPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 185 IRIMAPGRVYRNDY-DQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDLQVRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496   81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360 264 -GKWLEVLGCGMVHPNVLRNVGIDpDEYTGFAVGMGVERLTMLRYNVTDLRSFFENDLR 321
Cdd:cd00496  161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
74-327 1.14e-61

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 203.91  E-value: 1.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  74 KKEQLETEELNAKLASESI-------------DVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNF 140
Cdd:PRK04172 187 LKEGIELKEEITQLTPELLksgewkekefrpyNVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 141 DALNIPAHHPARADHDTFW-----------------------------------FDAER----LLRTQTSGVQIRTM-EK 180
Cdd:PRK04172 267 DALFQPQDHPAREMQDTFYlkypgigdlpeelvervkevhehggdtgsrgwgykWDEDIakrlVLRTHTTALSARYLaSR 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 181 MQPPIRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAF-FEEdlqVRFRPSYFPFTEPSAEVD 258
Cdd:PRK04172 347 PEPPQKYFSIGRVFRPDtIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVE 423

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360 259 VMGKNGKWLEVLGCGMVHPNVLRNVGIDpdeYTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK 327
Cdd:PRK04172 424 VYHEGLGWVELGGAGIFRPEVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 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: 617.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   1 MQNLENIVAEALQAVEKASDVASLEALRVEYFGKKGHFTLLMQGLRDVPADERPAVGAKINEAKQKAQDALNGKKEQLET 80
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  81 EELNAKLASESIDVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWF 160
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 161 DAERLLRTQTSGVQIRTMEKMQPPIRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDL 239
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQKPPIRIIAPGRVYRRDeSDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 240 QVRFRPSYFPFTEPSAEVDV-----------MGKNGKWLEVLGCGMVHPNVLRNVGIDPDEYTGFAVGMGVERLTMLRYN 308
Cdd:COG0016  241 KVRFRPSYFPFTEPSAEVDIscficggkgcrVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYG 320

                        330
                 ....*....|....*....
gi 491999360 309 VTDLRSFFENDLRFLKQFK 327
Cdd:COG0016  321 IDDIRLFFENDLRFLRQFG 339
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 37-327 2.63e-158

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: 444.06  E-value: 2.63e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   37 HFTLLMQGLRDVPADE-RPAVGAKINEAKQKAQDALNGKKEQLETEELNAKLASESIDVSLPGCKTELGGLHPVSITIER 115
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  116 VVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWFDAERLLRTQTSGVQIRTMEKMQ-PPIRIMAPGRVY 194
Cdd:TIGR00468  81 IRDIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEkPPIRIFSPGRVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  195 RND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEdLQVRFRPSYFPFTEPSAEVDVMGKNGK-WLEVLGC 272
Cdd:TIGR00468 161 RNDtVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGKgWLEVLGA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491999360  273 GMVHPNVLRNVGIDPdEYTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK 327
Cdd:TIGR00468 240 GMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 91-326 6.57e-135

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: 383.08  E-value: 6.57e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   91 SIDVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWF-------DAE 163
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  164 RLLRTQTSGVQIRTM-EKMQPPIRIMAPGRVYRNDY-DQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDLQV 241
Cdd:pfam01409  81 LLLRTHTTPVQARTLaKKPKPPIKIFSIGRVFRRDQvDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  242 RFRPSYFPFTEPSAEVDVM-GKNGKWLEVLGCGMVHPNVLRNVGIDpDEYTGFAVGMGVERLTMLRYNVTDLRSFFENDL 320
Cdd:pfam01409 161 RFRPSYFPFTEPSAEVDVYvCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGIDDIRDLYENDL 239


                  ....*.
gi 491999360  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 1.46e-123

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: 353.00  E-value: 1.46e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 107 HPVSITIERVVKFFSELGFSVEKGPEIETDYYNFDALNIPAHHPARADHDTFWFD--AERLLRTQTSGVQIRTMEKMQPP 184
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINdpARLLLRTHTSAVQARALAKLKPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 185 IRIMAPGRVYRNDY-DQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDLQVRFRPSYFPFTEPSAEVDVMGKN 263
Cdd:cd00496   81 IRIFSIGRVYRNDEiDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360 264 -GKWLEVLGCGMVHPNVLRNVGIDpDEYTGFAVGMGVERLTMLRYNVTDLRSFFENDLR 321
Cdd:cd00496  161 cLGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
74-327 1.14e-61

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 203.91  E-value: 1.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  74 KKEQLETEELNAKLASESI-------------DVSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGPEIETDYYNF 140
Cdd:PRK04172 187 LKEGIELKEEITQLTPELLksgewkekefrpyNVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 141 DALNIPAHHPARADHDTFW-----------------------------------FDAER----LLRTQTSGVQIRTM-EK 180
Cdd:PRK04172 267 DALFQPQDHPAREMQDTFYlkypgigdlpeelvervkevhehggdtgsrgwgykWDEDIakrlVLRTHTTALSARYLaSR 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 181 MQPPIRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFTELKGLLHDFLRAF-FEEdlqVRFRPSYFPFTEPSAEVD 258
Cdd:PRK04172 347 PEPPQKYFSIGRVFRPDtIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVE 423

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360 259 VMGKNGKWLEVLGCGMVHPNVLRNVGIDpdeYTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK 327
Cdd:PRK04172 424 VYHEGLGWVELGGAGIFRPEVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWLRERP 489
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 107-327 4.73e-45

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 158.00  E-value: 4.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 107 HPVSITIERVVKFFSEL---GFSV--EKGPeIETDYYNFDALNIPAHHPARADHDTFWFDAERLLRTQTSGVQIRTMEKM 181
Cdd:PLN02788  68 HPLGILKNAIYDYFDENysnKFKKfdDLSP-IVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 182 QPpiRIMAPGRVYRND-YDQTHTPMFHQIELLYVDKKANFT------------ELKGLLHDFLRAFFEeDLQVRFRPSYF 248
Cdd:PLN02788 147 HT--HFLVTGDVYRRDsIDATHYPVFHQMEGVRVFSPEEWEasgldgtdlaaeDLKKTLEGLARHLFG-DVEMRWVDAYF 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360 249 PFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIdPDEyTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK 327
Cdd:PLN02788 224 PFTNPSFELEIFFK-GEWLEVLGCGVTEQEILKNNGR-SDN-VAWAFGLGLERLAMVLFDIPDIRLFWSDDERFTSQFK 299
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 94-326 9.79e-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: 9.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360   94 VSLPGCKTELGGLHPVSITIERVVKFFSELGFSVEKGP---------EIETDYYNFDALNIPAHHPARADHDTFWFDAER 164
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPlfkifdnfkPVVTTMENFDNLGFPADHPGRQKSDCYYINEQH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  165 LLRTQTSGVQIRTMEKM-----QPPIRIMAPGRVYRND-YDQTHTPMFHQIEL--------------------------- 211
Cdd:TIGR00469 109 LLRAHTSAHELECFQGGlddsdNIKSGFLISADVYRRDeIDKTHYPVFHQADGaairkrtkadlfekepgyiekfeedir 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  212 ------------LYVDKKANFT--------------------ELKGLLHDFLRAFF---------------EEDLQVRFR 244
Cdd:TIGR00469 189 gteadlnkenvkIILDDDSIPLkennpkqeyasdlavdlcehELKHSIEGITKDLFgkkissmiknkanntPKELKVRWI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  245 PSYFPFTEPSAEVDVMGKnGKWLEVLGCGMVHPNVLRNVGIDPDEYTGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLK 324
Cdd:TIGR00469 269 DAYFPFTAPSWEIEIWFK-DEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLR 347


                  ..
gi 491999360  325 QF 326
Cdd:TIGR00469 348 QF 349
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 98-316 8.91e-34

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 129.32  E-value: 8.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  98 GCKTELGGLHPVSITIERVVKFFSELGFSvekgpEIETDYY------NFDALNIPAHHPARADHDTFWFD---------- 161
Cdd:PTZ00326 220 GKKIGGGNLHPLLKVRREFREILLEMGFE-----EMPTNRYvessfwNFDALFQPQQHPARDAQDTFFLSkpetskvndl 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 162 ------------------------------AER-LLRTQTSGVQIRTMEKMQ---------PPIRIMAPGRVYRND-YDQ 200
Cdd:PTZ00326 295 dddyvervkkvhevggygsigwrydwkleeARKnILRTHTTAVSARMLYKLAqeykktgpfKPKKYFSIDRVFRNEtLDA 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 201 THTPMFHQIELLYVDKKANFTELKGLLHDFLRAFFEEDLqvRFRPSYFPFTEPSAEvdVMG---KNGKWLEVLGCGMVHP 277
Cdd:PTZ00326 375 THLAEFHQVEGFVIDRNLTLGDLIGTIREFFRRIGITKL--RFKPAFNPYTEPSME--IFGyhpGLKKWVEVGNSGIFRP 450

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491999360 278 NVLRNVGIdPDEYTGFAVGMGVERLTMLRYNVTDLRSFF 316
Cdd:PTZ00326 451 EMLRPMGF-PEDVTVIAWGLSLERPTMIKYGIKNIRDLF 488
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 98-316 1.62e-32

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 125.94  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360  98 GCKTELGGLHPVSITIERVVKFFSELGFsvEKGPE---IETDYYNFDALNIPAHHPARADHDTFWFDA------------ 162
Cdd:PLN02853 212 GAPPEGGHLHPLLKVRQQFRKIFLQMGF--EEMPTnnfVESSFWNFDALFQPQQHPARDSHDTFFLKApattrqlpedyv 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 163 ER---------------------------LLRTQTSGVQIRTMEKM--QP--PIRIMAPGRVYRND-YDQTHTPMFHQIE 210
Cdd:PLN02853 290 ERvktvhesggygsigygydwkreeanknLLRTHTTAVSSRMLYKLaqKGfkPKRYFSIDRVFRNEaVDRTHLAEFHQVE 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 211 LLYVDKKANFTELKGLLHDFLRAFFEEDLqvRFRPSYFPFTEPSAEV-DVMGKNGKWLEVLGCGMVHPNVLRNVGIdPDE 289
Cdd:PLN02853 370 GLVCDRGLTLGDLIGVLEDFFSRLGMTKL--RFKPAYNPYTEPSMEIfSYHEGLKKWVEVGNSGMFRPEMLLPMGL-PED 446

                        250       260
                 ....*....|....*....|....*..
gi 491999360 290 YTGFAVGMGVERLTMLRYNVTDLRSFF 316
Cdd:PLN02853 447 VNVIAWGLSLERPTMILYGIDNIRDLF 473
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
19-87 4.69e-28

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 103.62  E-value: 4.69e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491999360   19 SDVASLEALRVEYFGKKGHFTLLMQGLRDVPADERPAVGAKINEAKQKAQDALNGKKEQLETEELNAKL 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 ...
 110-302 6.65e-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: 72.54  E-value: 6.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 110 SITIERVVKFFSELGFSVEKGPEIETDYYNFDAlnipAHHPARADHDTFWFDAERLLRTQTSGVQIRTM--EKMQPPIRI 187
Cdd:cd00768    3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKA----GHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFvsHIRKLPLRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491999360 188 MAPGRVYRND---YDQTHTPMFHQIELLYV----DKKANFTELKGLLHDFLRAFFEEDLQVRFRPSYFPFT----EPSAE 256
Cdd:cd00768   79 AEIGPAFRNEggrRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSpggaGPGFE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491999360 257 VDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPDEYTG-------FAVGMGVERL 302
Cdd:cd00768  159 IEVDHPEGRGLEIGSGGYRQDEQARAADLYFLDEALeyrypptIGFGLGLERL 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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