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Conserved domains on  [gi|1464439820|gb|AXQ39661|]
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phenylalanyl-tRNA synthetase subunit alpha, partial [Leuconostoc mesenteroides]

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]; ...
 1-281 2.66e-166

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: 464.14  E-value: 2.66e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820   1 RVKLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPH 80
Cdd:COG0016    28 RVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  81 VLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdf 160
Cdd:COG0016   108 PLTQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 161 sKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDV 240
Cdd:COG0016   182 -KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDI 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1464439820 241 SWNEVTPDMNP--EDIEWIEVLGAGMTHPNVLKMDGIDPEKYS 281
Cdd:COG0016   261 SCFICGGKGCRvcKGTGWLEILGCGMVHPNVLRAVGIDPEEYS 303
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-281 2.66e-166

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: 464.14  E-value: 2.66e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820   1 RVKLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPH 80
Cdd:COG0016    28 RVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  81 VLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdf 160
Cdd:COG0016   108 PLTQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 161 sKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDV 240
Cdd:COG0016   182 -KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDI 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1464439820 241 SWNEVTPDMNP--EDIEWIEVLGAGMTHPNVLKMDGIDPEKYS 281
Cdd:COG0016   261 SCFICGGKGCRvcKGTGWLEILGCGMVHPNVLRAVGIDPEEYS 303
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 10-278 2.41e-107

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: 313.09  E-value: 2.41e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  10 ELTGLLKGMKDVAAENRKMV-GEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVLQQIIDE 88
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEETKPAlGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  89 IEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHDfsKGPLKMI 168
Cdd:TIGR00468  81 IRDIFLGLGFTEETG----PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE--KPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 169 APGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKhQIRMRPSYFPFTEPSVEVDVSWnevtpd 248
Cdd:TIGR00468 155 SPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGET-EIRFRPSYFPFTEPSAEIDVYC------ 227

                         250       260       270
                  ....*....|....*....|....*....|
gi 1464439820 249 mnPEDIEWIEVLGAGMTHPNVLKMDGIDPE 278
Cdd:TIGR00468 228 --PEGKGWLEVLGAGMFRPEVLEPMGIDPT 255
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 64-278 3.09e-102

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: 298.34  E-value: 3.09e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  64 KIDVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEI-- 141
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEG----PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 142 -----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELF 216
Cdd:pfam01409  77 varrlLLRTHTTPVQARTLAKK--PKPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1464439820 217 GEKHQIRMRPSYFPFTEPSVEVDVSWnevtpdmnPEDIEWIEVLGAGMTHPNVLKMDGIDPE 278
Cdd:pfam01409 155 GFEVKVRFRPSYFPFTEPSAEVDVYV--------CKLGGWLEVGGAGMVHPNVLEAVGIDED 208
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 80-281 1.12e-97

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: 285.59  E-value: 1.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  80 HVLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPE--ILLRTQTSPVQSRSLEK 157
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTE----VEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 158 HdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVE 237
Cdd:cd00496    77 L---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1464439820 238 VDVSWnevtpdmnPEDIEWIEVLGAGMTHPNVLKMDGIDpEKYS 281
Cdd:cd00496   154 VDVYC--------PGCLGWLEILGCGMVRPEVLENAGID-EEYS 188
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
66-276 3.40e-49

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 169.24  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  66 DVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEiiddTVDSPEVETDEYNFERENLPKDHPARDMQDTFYI-------- 137
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFE----EMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgigdl 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 138 ---------------------------TPEI----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQ 186
Cdd:PRK04172  295 peelvervkevhehggdtgsrgwgykwDEDIakrlVLRTHTTALSARYLASR--PEPPQKYFSIGRVFRPDTIDATHLPE 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 187 FHQVEGMVVGENITMADLKGTLLSIMQEL-FGEkhqIRMRPSYFPFTEPSVEVDVswnEVtpdmnpEDIEWIEVLGAGMT 265
Cdd:PRK04172  373 FYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEV---YH------EGLGWVELGGAGIF 440

                         250
                  ....*....|.
gi 1464439820 266 HPNVLKMDGID 276
Cdd:PRK04172  441 RPEVLEPLGID 451
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-281 2.66e-166

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: 464.14  E-value: 2.66e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820   1 RVKLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPH 80
Cdd:COG0016    28 RVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  81 VLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdf 160
Cdd:COG0016   108 PLTQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 161 sKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDV 240
Cdd:COG0016   182 -KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDI 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1464439820 241 SWNEVTPDMNP--EDIEWIEVLGAGMTHPNVLKMDGIDPEKYS 281
Cdd:COG0016   261 SCFICGGKGCRvcKGTGWLEILGCGMVHPNVLRAVGIDPEEYS 303
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 10-278 2.41e-107

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: 313.09  E-value: 2.41e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  10 ELTGLLKGMKDVAAENRKMV-GEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVLQQIIDE 88
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEETKPAlGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  89 IEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHDfsKGPLKMI 168
Cdd:TIGR00468  81 IRDIFLGLGFTEETG----PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE--KPPIRIF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 169 APGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKhQIRMRPSYFPFTEPSVEVDVSWnevtpd 248
Cdd:TIGR00468 155 SPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGET-EIRFRPSYFPFTEPSAEIDVYC------ 227

                         250       260       270
                  ....*....|....*....|....*....|
gi 1464439820 249 mnPEDIEWIEVLGAGMTHPNVLKMDGIDPE 278
Cdd:TIGR00468 228 --PEGKGWLEVLGAGMFRPEVLEPMGIDPT 255
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 64-278 3.09e-102

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: 298.34  E-value: 3.09e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  64 KIDVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEI-- 141
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEG----PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 142 -----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELF 216
Cdd:pfam01409  77 varrlLLRTHTTPVQARTLAKK--PKPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1464439820 217 GEKHQIRMRPSYFPFTEPSVEVDVSWnevtpdmnPEDIEWIEVLGAGMTHPNVLKMDGIDPE 278
Cdd:pfam01409 155 GFEVKVRFRPSYFPFTEPSAEVDVYV--------CKLGGWLEVGGAGMVHPNVLEAVGIDED 208
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 80-281 1.12e-97

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: 285.59  E-value: 1.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  80 HVLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPE--ILLRTQTSPVQSRSLEK 157
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTE----VEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 158 HdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVE 237
Cdd:cd00496    77 L---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1464439820 238 VDVSWnevtpdmnPEDIEWIEVLGAGMTHPNVLKMDGIDpEKYS 281
Cdd:cd00496   154 VDVYC--------PGCLGWLEILGCGMVRPEVLENAGID-EEYS 188
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
66-276 3.40e-49

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 169.24  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  66 DVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEiiddTVDSPEVETDEYNFERENLPKDHPARDMQDTFYI-------- 137
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFE----EMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgigdl 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 138 ---------------------------TPEI----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQ 186
Cdd:PRK04172  295 peelvervkevhehggdtgsrgwgykwDEDIakrlVLRTHTTALSARYLASR--PEPPQKYFSIGRVFRPDTIDATHLPE 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 187 FHQVEGMVVGENITMADLKGTLLSIMQEL-FGEkhqIRMRPSYFPFTEPSVEVDVswnEVtpdmnpEDIEWIEVLGAGMT 265
Cdd:PRK04172  373 FYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEV---YH------EGLGWVELGGAGIF 440

                         250
                  ....*....|.
gi 1464439820 266 HPNVLKMDGID 276
Cdd:PRK04172  441 RPEVLEPLGID 451
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 74-274 2.51e-36

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 133.35  E-value: 2.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  74 HQVGqphVLQQIIDEIEQHFLGLGFEIIDDTvdSPEVETDEyNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSR 153
Cdd:PLN02788   68 HPLG---ILKNAIYDYFDENYSNKFKKFDDL--SPIVSTKQ-NFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 154 SLEkhdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVV------------GENITMADLKGTLLSIMQELFGEKhQ 221
Cdd:PLN02788  142 LLR-----AGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVfspeeweasgldGTDLAAEDLKKTLEGLARHLFGDV-E 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1464439820 222 IRMRPSYFPFTEPSVEVDVSWNEvtpdmnpediEWIEVLGAGMTHPNVLKMDG 274
Cdd:PLN02788  216 MRWVDAYFPFTNPSFELEIFFKG----------EWLEVLGCGVTEQEILKNNG 258
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 77-278 6.38e-29

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 114.68  E-value: 6.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  77 GQPHVLQQIIDEIEQHFLGLGFEiiddtvdspEVETDEY------NFERENLPKDHPARDMQDTFYIT-PEI-------- 141
Cdd:PTZ00326  226 GNLHPLLKVRREFREILLEMGFE---------EMPTNRYvessfwNFDALFQPQQHPARDAQDTFFLSkPETskvndldd 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 142 --------------------------------LLRTQTSPVQSRSLEK--HDFSKG----PLKMIAPGKVYRRDTDDATH 183
Cdd:PTZ00326  297 dyvervkkvhevggygsigwrydwkleearknILRTHTTAVSARMLYKlaQEYKKTgpfkPKKYFSIDRVFRNETLDATH 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 184 SHQFHQVEGMVVGENITMADLKGTLlsimqELFGEK---HQIRMRPSYFPFTEPSVEVdVSWnevtpdmNPEDIEWIEVL 260
Cdd:PTZ00326  377 LAEFHQVEGFVIDRNLTLGDLIGTI-----REFFRRigiTKLRFKPAFNPYTEPSMEI-FGY-------HPGLKKWVEVG 443

                         250
                  ....*....|....*...
gi 1464439820 261 GAGMTHPNVLKMDGIDPE 278
Cdd:PTZ00326  444 NSGIFRPEMLRPMGFPED 461
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 77-278 4.16e-23

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 98.21  E-value: 4.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  77 GQPHVLQQIIDEIEQHFLGLGFEiiddtvDSPE---VETDEYNFERENLPKDHPARDMQDTFYIT--------PEI---- 141
Cdd:PLN02853  218 GHLHPLLKVRQQFRKIFLQMGFE------EMPTnnfVESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlPEDyver 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 142 ---------------------------LLRTQTSPVQSRSLekHDFSKG---PLKMIAPGKVYRRDTDDATHSHQFHQVE 191
Cdd:PLN02853  292 vktvhesggygsigygydwkreeanknLLRTHTTAVSSRML--YKLAQKgfkPKRYFSIDRVFRNEAVDRTHLAEFHQVE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 192 GMVVGENITMADLKGTLLSIMQELfGEKhQIRMRPSYFPFTEPSVEVdVSWNEvtpDMNpediEWIEVLGAGMTHPNVLK 271
Cdd:PLN02853  370 GLVCDRGLTLGDLIGVLEDFFSRL-GMT-KLRFKPAYNPYTEPSMEI-FSYHE---GLK----KWVEVGNSGMFRPEMLL 439


                  ....*..
gi 1464439820 272 MDGIdPE 278
Cdd:PLN02853  440 PMGL-PE 445
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
1-60 1.07e-18

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 77.81  E-value: 1.07e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820   1 RVKLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQL 60
Cdd:pfam02912  10 RVKYLGKKGELTALLKGLGKLPPEERPAAGKLINELKQAIEAALEERKEELEAAELEARL 69
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 67-277 1.74e-18

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: 84.74  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  67 VTLPGSAHQVGQPHVLQQIIDEIEQHFLGLG--------FEIIDDTvdSPEVETDEyNFERENLPKDHPARDMQDTFYIT 138
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADnnqrgnplFKIFDNF--KPVVTTME-NFDNLGFPADHPGRQKSDCYYIN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 139 PEILLRTQTSPVQSRSLEK--HDFSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVV--------------------- 195
Cdd:TIGR00469 106 EQHLLRAHTSAHELECFQGglDDSDNIKSGFLISADVYRRDEIDKTHYPVFHQADGAAIrkrtkadlfekepgyiekfee 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 196 ------------GENITMAD--------------------------LKGTLLSIMQELFGEK---------------HQI 222
Cdd:TIGR00469 186 dirgteadlnkeNVKIILDDdsiplkennpkqeyasdlavdlceheLKHSIEGITKDLFGKKissmiknkanntpkeLKV 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1464439820 223 RMRPSYFPFTEPSVEVDVSWNEvtpdmnpediEWIEVLGAGMTHPNVLKMDGIDP 277
Cdd:TIGR00469 266 RWIDAYFPFTAPSWEIEIWFKD----------EWLELCGCGIIRHDILLRAGVHP 310
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 85-269 3.71e-10

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: 58.28  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820  85 IIDEIEQ----HFLGLGFEiiddTVDSPEVETDEYNFERENLPKD-HPARDMQDTFYitpeiLLRTQTSPVQSRSLEKHD 159
Cdd:cd00768     1 IRSKIEQklrrFMAELGFQ----EVETPIVEREPLLEKAGHEPKDlLPVGAENEEDL-----YLRPTLEPGLVRLFVSHI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464439820 160 FsKGPLKMIAPGKVYR--RDTDDATHSHQFHQVEGMVVGENI----TMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTE 233
Cdd:cd00768    72 R-KLPLRLAEIGPAFRneGGRRGLRRVREFTQLEGEVFGEDGeeasEFEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1464439820 234 PSVEVDVSWnEVtpdmNPEDIEWIEVLGAGMTHPNV 269
Cdd:cd00768   151 GGAGPGFEI-EV----DHPEGRGLEIGSGGYRQDEQ 181
 
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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