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Conserved domains on  [gi|1275020546|gb|ARH02233|]
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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]; ...
 1-240 4.44e-146

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: 411.75  E-value: 4.44e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546   1 KLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVL 80
Cdd:COG0016    30 KYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLHPL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  81 QQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdfsK 160
Cdd:COG0016   110 TQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ---K 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 161 GPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDVSW 240
Cdd:COG0016   183 PPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISC 262
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-240 4.44e-146

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: 411.75  E-value: 4.44e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546   1 KLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVL 80
Cdd:COG0016    30 KYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLHPL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  81 QQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdfsK 160
Cdd:COG0016   110 TQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ---K 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 161 GPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDVSW 240
Cdd:COG0016   183 PPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISC 262
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 8-243 3.18e-94

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: 278.81  E-value: 3.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546   8 ELTGLLKGMKDVAAENRKMV-GEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVLQQIIDE 86
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEETKPAlGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  87 IEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHDfsKGPLKMI 166
Cdd:TIGR00468  81 IRDIFLGLGFTEETG----PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE--KPPIRIF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275020546 167 APGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKhQIRMRPSYFPFTEPSVEVDVSWNEV 243
Cdd:TIGR00468 155 SPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGET-EIRFRPSYFPFTEPSAEIDVYCPEG 230
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 62-242 1.29e-88

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: 262.52  E-value: 1.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  62 KIDVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEI-- 139
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEG----PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 140 -----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELF 214
Cdd:pfam01409  77 varrlLLRTHTTPVQARTLAKK--PKPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFF 154

                         170       180
                  ....*....|....*....|....*...
gi 1275020546 215 GEKHQIRMRPSYFPFTEPSVEVDVSWNE 242
Cdd:pfam01409 155 GFEVKVRFRPSYFPFTEPSAEVDVYVCK 182
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 78-244 1.71e-84

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: 251.31  E-value: 1.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  78 HVLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPE--ILLRTQTSPVQSRSLEK 155
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTE----VEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 156 HdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVE 235
Cdd:cd00496    77 L---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFE 153


                  ....*....
gi 1275020546 236 VDVSWNEVT 244
Cdd:cd00496   154 VDVYCPGCL 162
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
64-243 1.54e-43

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 153.45  E-value: 1.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  64 DVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEiiddTVDSPEVETDEYNFERENLPKDHPARDMQDTFYI-------- 135
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFE----EMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgigdl 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 136 ---------------------------TPEI----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQ 184
Cdd:PRK04172  295 peelvervkevhehggdtgsrgwgykwDEDIakrlVLRTHTTALSARYLASR--PEPPQKYFSIGRVFRPDTIDATHLPE 372

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275020546 185 FHQVEGMVVGENITMADLKGTLLSIMQEL-FGEkhqIRMRPSYFPFTEPSVEVDV-----SWNEV 243
Cdd:PRK04172  373 FYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVyheglGWVEL 434
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 1-240 4.44e-146

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: 411.75  E-value: 4.44e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546   1 KLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVL 80
Cdd:COG0016    30 KYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAELEARLAAETIDVTLPGRPRPLGSLHPL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  81 QQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHdfsK 160
Cdd:COG0016   110 TQVIEEIEDIFVGMGFEV----AEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQIRTMEKQ---K 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 161 GPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVEVDVSW 240
Cdd:COG0016   183 PPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISC 262
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 8-243 3.18e-94

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: 278.81  E-value: 3.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546   8 ELTGLLKGMKDVAAENRKMV-GEVGNDVRQTITELLKQKKQAQEEYALNQQLLAEKIDVTLPGSAHQVGQPHVLQQIIDE 86
Cdd:TIGR00468   1 KLKDLLKQLGKLTKEETKPAlGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  87 IEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSRSLEKHDfsKGPLKMI 166
Cdd:TIGR00468  81 IRDIFLGLGFTEETG----PEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQE--KPPIRIF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275020546 167 APGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKhQIRMRPSYFPFTEPSVEVDVSWNEV 243
Cdd:TIGR00468 155 SPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGET-EIRFRPSYFPFTEPSAEIDVYCPEG 230
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 62-242 1.29e-88

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: 262.52  E-value: 1.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  62 KIDVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEIIDDtvdsPEVETDEYNFERENLPKDHPARDMQDTFYITPEI-- 139
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEG----PEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLkp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 140 -----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELF 214
Cdd:pfam01409  77 varrlLLRTHTTPVQARTLAKK--PKPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFF 154

                         170       180
                  ....*....|....*....|....*...
gi 1275020546 215 GEKHQIRMRPSYFPFTEPSVEVDVSWNE 242
Cdd:pfam01409 155 GFEVKVRFRPSYFPFTEPSAEVDVYVCK 182
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 78-244 1.71e-84

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: 251.31  E-value: 1.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  78 HVLQQIIDEIEQHFLGLGFEIiddtVDSPEVETDEYNFERENLPKDHPARDMQDTFYITPE--ILLRTQTSPVQSRSLEK 155
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTE----VEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 156 HdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVVGENITMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTEPSVE 235
Cdd:cd00496    77 L---KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFE 153


                  ....*....
gi 1275020546 236 VDVSWNEVT 244
Cdd:cd00496   154 VDVYCPGCL 162
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
64-243 1.54e-43

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 153.45  E-value: 1.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  64 DVTLPGSAHQVGQPHVLQQIIDEIEQHFLGLGFEiiddTVDSPEVETDEYNFERENLPKDHPARDMQDTFYI-------- 135
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFE----EMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgigdl 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 136 ---------------------------TPEI----LLRTQTSPVQSRSLEKHdfSKGPLKMIAPGKVYRRDTDDATHSHQ 184
Cdd:PRK04172  295 peelvervkevhehggdtgsrgwgykwDEDIakrlVLRTHTTALSARYLASR--PEPPQKYFSIGRVFRPDTIDATHLPE 372

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275020546 185 FHQVEGMVVGENITMADLKGTLLSIMQEL-FGEkhqIRMRPSYFPFTEPSVEVDV-----SWNEV 243
Cdd:PRK04172  373 FYQLEGIVMGEDVSFRDLLGILKEFYKRLgFEE---VKFRPAYFPFTEPSVEVEVyheglGWVEL 434
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 72-243 1.92e-28

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 111.39  E-value: 1.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  72 HQVGqphVLQQIIDEIEQHFLGLGFEIIDDTvdSPEVETDEyNFERENLPKDHPARDMQDTFYITPEILLRTQTSPVQSR 151
Cdd:PLN02788   68 HPLG---ILKNAIYDYFDENYSNKFKKFDDL--SPIVSTKQ-NFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 152 SLEkhdfsKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVV------------GENITMADLKGTLLSIMQELFGEKhQ 219
Cdd:PLN02788  142 LLR-----AGHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVfspeeweasgldGTDLAAEDLKKTLEGLARHLFGDV-E 215

                         170       180
                  ....*....|....*....|....*...
gi 1275020546 220 IRMRPSYFPFTEPSVEVDV----SWNEV 243
Cdd:PLN02788  216 MRWVDAYFPFTNPSFELEIffkgEWLEV 243
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 75-236 8.24e-28

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 110.83  E-value: 8.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  75 GQPHVLQQIIDEIEQHFLGLGFEiiddtvdspEVETDEY------NFERENLPKDHPARDMQDTFYIT-PEI-------- 139
Cdd:PTZ00326  226 GNLHPLLKVRREFREILLEMGFE---------EMPTNRYvessfwNFDALFQPQQHPARDAQDTFFLSkPETskvndldd 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 140 --------------------------------LLRTQTSPVQSRSLEK--HDFSKG----PLKMIAPGKVYRRDTDDATH 181
Cdd:PTZ00326  297 dyvervkkvhevggygsigwrydwkleearknILRTHTTAVSARMLYKlaQEYKKTgpfkPKKYFSIDRVFRNETLDATH 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1275020546 182 SHQFHQVEGMVVGENITMADLKGTLlsimqELFGEK---HQIRMRPSYFPFTEPSVEV 236
Cdd:PTZ00326  377 LAEFHQVEGFVIDRNLTLGDLIGTI-----REFFRRigiTKLRFKPAFNPYTEPSMEI 429
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 75-236 1.33e-21

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 93.20  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  75 GQPHVLQQIIDEIEQHFLGLGFEiiddtvDSPE---VETDEYNFERENLPKDHPARDMQDTFYIT--------PEI---- 139
Cdd:PLN02853  218 GHLHPLLKVRQQFRKIFLQMGFE------EMPTnnfVESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlPEDyver 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 140 ---------------------------LLRTQTSPVQSRSLekHDFSKG---PLKMIAPGKVYRRDTDDATHSHQFHQVE 189
Cdd:PLN02853  292 vktvhesggygsigygydwkreeanknLLRTHTTAVSSRML--YKLAQKgfkPKRYFSIDRVFRNEAVDRTHLAEFHQVE 369

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1275020546 190 GMVVGENITMADLKGTLLSIMQELfGEKhQIRMRPSYFPFTEPSVEV 236
Cdd:PLN02853  370 GLVCDRGLTLGDLIGVLEDFFSRL-GMT-KLRFKPAYNPYTEPSMEI 414
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
1-58 7.03e-17

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 72.80  E-value: 7.03e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1275020546   1 KLLGKKGELTGLLKGMKDVAAENRKMVGEVGNDVRQTITELLKQKKQAQEEYALNQQL 58
Cdd:pfam02912  12 KYLGKKGELTALLKGLGKLPPEERPAAGKLINELKQAIEAALEERKEELEAAELEARL 69
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 65-240 5.31e-14

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: 70.87  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  65 VTLPGSAHQVGQPHVLQQIIDEIEQHFLGLG--------FEIIDDTvdSPEVETDEyNFERENLPKDHPARDMQDTFYIT 136
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADnnqrgnplFKIFDNF--KPVVTTME-NFDNLGFPADHPGRQKSDCYYIN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 137 PEILLRTQTSPVQSRSLEK--HDFSKGPLKMIAPGKVYRRDTDDATHSHQFHQVEGMVV--------------------- 193
Cdd:TIGR00469 106 EQHLLRAHTSAHELECFQGglDDSDNIKSGFLISADVYRRDEIDKTHYPVFHQADGAAIrkrtkadlfekepgyiekfee 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 194 ------------GENITMAD--------------------------LKGTLLSIMQELFGEK---------------HQI 220
Cdd:TIGR00469 186 dirgteadlnkeNVKIILDDdsiplkennpkqeyasdlavdlceheLKHSIEGITKDLFGKKissmiknkanntpkeLKV 265

                         250       260
                  ....*....|....*....|
gi 1275020546 221 RMRPSYFPFTEPSVEVDVSW 240
Cdd:TIGR00469 266 RWIDAYFPFTAPSWEIEIWF 285
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 83-240 2.71e-09

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 55.59  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546  83 IIDEIEQ----HFLGLGFEiiddTVDSPEVETDEYNFERENLPKD-HPARDMQDTFYitpeiLLRTQTSPVQSRSLEKHD 157
Cdd:cd00768     1 IRSKIEQklrrFMAELGFQ----EVETPIVEREPLLEKAGHEPKDlLPVGAENEEDL-----YLRPTLEPGLVRLFVSHI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275020546 158 FsKGPLKMIAPGKVYR--RDTDDATHSHQFHQVEGMVVGENI----TMADLKGTLLSIMQELFGEKHQIRMRPSYFPFTE 231
Cdd:cd00768    72 R-KLPLRLAEIGPAFRneGGRRGLRRVREFTQLEGEVFGEDGeeasEFEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150


                  ....*....
gi 1275020546 232 PSVEVDVSW 240
Cdd:cd00768   151 GGAGPGFEI 159
 
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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