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Conserved domains on  [gi|445925711|ref|WP_000003566|]
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MULTISPECIES: phenylalanine--tRNA ligase subunit alpha [Staphylococcus]

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]; ...
 4-344 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: 665.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   4 QQTMSELKQQALVDINEANDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEEKPAFGQKVNELRQTIQNELDERQQMLVK 83
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  84 EKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI 163
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 164 TDEILLRTHTSPVQARTMESRhgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGA 243
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQ--KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 244 DREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLK 323
Cdd:COG0016  239 DVKVRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLK 318

                        330       340
                 ....*....|....*....|.
gi 445925711 324 YGIEDIRHFYTNDVRFLDQFK 344
Cdd:COG0016  319 YGIDDIRLFFENDLRFLRQFG 339
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 4-344 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: 665.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   4 QQTMSELKQQALVDINEANDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEEKPAFGQKVNELRQTIQNELDERQQMLVK 83
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  84 EKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI 163
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 164 TDEILLRTHTSPVQARTMESRhgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGA 243
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQ--KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 244 DREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLK 323
Cdd:COG0016  239 DVKVRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLK 318

                        330       340
                 ....*....|....*....|.
gi 445925711 324 YGIEDIRHFYTNDVRFLDQFK 344
Cdd:COG0016  319 YGIDDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 94-343 5.08e-149

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: 419.68  E-value: 5.08e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   94 TIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI-------TDE 166
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  167 ILLRTHTSPVQARTMESRHgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADRE 246
Cdd:pfam01409  81 LLLRTHTTPVQARTLAKKP-KPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  247 IRLRPSYFPFTEPSVEVDVScfkckgkgcnVCKHTGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGI 326
Cdd:pfam01409 160 VRFRPSYFPFTEPSAEVDVY----------VCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGI 228

                         250
                  ....*....|....*..
gi 445925711  327 EDIRHFYTNDVRFLDQF 343
Cdd:pfam01409 229 DDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 42-344 1.19e-148

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: 420.57  E-value: 1.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   42 SGLMKLMKDLPNEE-KPAFGQKVNELRQTIQNELDERQQMLVKEKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIE 120
Cdd:TIGR00468   3 KDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  121 DLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDEILLRTHTSPVQARTMEsRHGQGPVKIICPGKVYR 200
Cdd:TIGR00468  83 DIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTME-EQEKPPIRIFSPGRVFR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  201 RDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGAdREIRLRPSYFPFTEPSVEVDVSCFKCKgkgcnvckh 280
Cdd:TIGR00468 162 NDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGK--------- 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445925711  281 tGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFK 344
Cdd:TIGR00468 232 -GWLEVLGAGMFRPEVLEPMGID-PTYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 110-338 1.73e-128

Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.


Pssm-ID: 238277 [Multi-domain]  Cd Length: 218  Bit Score: 366.49  E-value: 1.73e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 110 HPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDE--ILLRTHTSPVQARTMESRhgQ 187
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKL--K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 188 GPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADREIRLRPSYFPFTEPSVEVDVSC 267
Cdd:cd00496   79 PPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYC 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445925711 268 FKCkgkgcnvckhTGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVR 338
Cdd:cd00496  159 PGC----------LGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
96-340 1.02e-72

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 233.57  E-value: 1.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  96 DVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI----TDEI---- 167
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgIGDLpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 168 -------------------------------LLRTHTSPVQARTMeSRHGQGPVKIICPGKVYRRDSDDATHSHQFTQIE 216
Cdd:PRK04172 299 vervkevhehggdtgsrgwgykwdediakrlVLRTHTTALSARYL-ASRPEPPQKYFSIGRVFRPDTIDATHLPEFYQLE 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 217 GLVVDKNVKMSDLKGTLELLAKKLfGADrEIRLRPSYFPFTEPSVEVDVscfkckgkgcnvcKHT--GWIEILGAGMVHP 294
Cdd:PRK04172 378 GIVMGEDVSFRDLLGILKEFYKRL-GFE-EVKFRPAYFPFTEPSVEVEV-------------YHEglGWVELGGAGIFRP 442

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 445925711 295 NVLEMAGFDsseYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFL 340
Cdd:PRK04172 443 EVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWL 485
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 4-344 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: 665.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   4 QQTMSELKQQALVDINEANDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEEKPAFGQKVNELRQTIQNELDERQQMLVK 83
Cdd:COG0016    1 MEELEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  84 EKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI 163
Cdd:COG0016   81 AELEARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 164 TDEILLRTHTSPVQARTMESRhgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGA 243
Cdd:COG0016  161 DDGLLLRTHTSPVQIRTMEKQ--KPPIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 244 DREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLK 323
Cdd:COG0016  239 DVKVRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLK 318

                        330       340
                 ....*....|....*....|.
gi 445925711 324 YGIEDIRHFYTNDVRFLDQFK 344
Cdd:COG0016  319 YGIDDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 94-343 5.08e-149

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: 419.68  E-value: 5.08e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   94 TIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI-------TDE 166
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  167 ILLRTHTSPVQARTMESRHgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADRE 246
Cdd:pfam01409  81 LLLRTHTTPVQARTLAKKP-KPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  247 IRLRPSYFPFTEPSVEVDVScfkckgkgcnVCKHTGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGI 326
Cdd:pfam01409 160 VRFRPSYFPFTEPSAEVDVY----------VCKLGGWLEVGGAGMVHPNVLEAVGID-EDYSGFAFGLGVERLAMLKYGI 228

                         250
                  ....*....|....*..
gi 445925711  327 EDIRHFYTNDVRFLDQF 343
Cdd:pfam01409 229 DDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 42-344 1.19e-148

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: 420.57  E-value: 1.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   42 SGLMKLMKDLPNEE-KPAFGQKVNELRQTIQNELDERQQMLVKEKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIE 120
Cdd:TIGR00468   3 KDLLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  121 DLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDEILLRTHTSPVQARTMEsRHGQGPVKIICPGKVYR 200
Cdd:TIGR00468  83 DIFLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTME-EQEKPPIRIFSPGRVFR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  201 RDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGAdREIRLRPSYFPFTEPSVEVDVSCFKCKgkgcnvckh 280
Cdd:TIGR00468 162 NDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGK--------- 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445925711  281 tGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFK 344
Cdd:TIGR00468 232 -GWLEVLGAGMFRPEVLEPMGID-PTYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 110-338 1.73e-128

Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer.


Pssm-ID: 238277 [Multi-domain]  Cd Length: 218  Bit Score: 366.49  E-value: 1.73e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 110 HPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDE--ILLRTHTSPVQARTMESRhgQ 187
Cdd:cd00496    1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKL--K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 188 GPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADREIRLRPSYFPFTEPSVEVDVSC 267
Cdd:cd00496   79 PPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYC 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445925711 268 FKCkgkgcnvckhTGWIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVR 338
Cdd:cd00496  159 PGC----------LGWLEILGCGMVRPEVLENAGID-EEYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
96-340 1.02e-72

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 233.57  E-value: 1.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  96 DVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYI----TDEI---- 167
Cdd:PRK04172 219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYLkypgIGDLpeel 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 168 -------------------------------LLRTHTSPVQARTMeSRHGQGPVKIICPGKVYRRDSDDATHSHQFTQIE 216
Cdd:PRK04172 299 vervkevhehggdtgsrgwgykwdediakrlVLRTHTTALSARYL-ASRPEPPQKYFSIGRVFRPDTIDATHLPEFYQLE 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 217 GLVVDKNVKMSDLKGTLELLAKKLfGADrEIRLRPSYFPFTEPSVEVDVscfkckgkgcnvcKHT--GWIEILGAGMVHP 294
Cdd:PRK04172 378 GIVMGEDVSFRDLLGILKEFYKRL-GFE-EVKFRPAYFPFTEPSVEVEV-------------YHEglGWVELGGAGIFRP 442

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 445925711 295 NVLEMAGFDsseYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFL 340
Cdd:PRK04172 443 EVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWL 485
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 98-345 8.78e-53

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 179.19  E-value: 8.78e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  98 SLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYE----VEQDHYNFEMLNLPKSHPARDMQDSFYITDEILLRTHT 173
Cdd:PLN02788  56 SKIGMQLHRRPDHPLGILKNAIYDYFDENYSNKFKKFDdlspIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHT 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 174 SPVQARTMESRHGQgpvkIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMS------------DLKGTLELLAKKLF 241
Cdd:PLN02788 136 SAHQAELLRAGHTH----FLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEWEasgldgtdlaaeDLKKTLEGLARHLF 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 242 GaDREIRLRPSYFPFTEPSVEVDVscfKCKGKgcnvckhtgWIEILGAGMVHPNVLEMAGfdSSEYSGFAFGMGPDRIAM 321
Cdd:PLN02788 212 G-DVEMRWVDAYFPFTNPSFELEI---FFKGE---------WLEVLGCGVTEQEILKNNG--RSDNVAWAFGLGLERLAM 276

                        250       260
                 ....*....|....*....|....
gi 445925711 322 LKYGIEDIRHFYTNDVRFLDQFKA 345
Cdd:PLN02788 277 VLFDIPDIRLFWSDDERFTSQFKE 300
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 101-330 5.09e-37

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 138.95  E-value: 5.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 101 GRHIEIGSKHPLTRTIEEIEDLFLGLGYEivngyEVEQDHY------NFEMLNLPKSHPARDMQDSFYITD--------- 165
Cdd:PTZ00326 220 GKKIGGGNLHPLLKVRREFREILLEMGFE-----EMPTNRYvessfwNFDALFQPQQHPARDAQDTFFLSKpetskvndl 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 166 ------------EI--------------------LLRTHTSPVQARtMESRHGQGPVK--IICPGK------VYRRDSDD 205
Cdd:PTZ00326 295 dddyvervkkvhEVggygsigwrydwkleearknILRTHTTAVSAR-MLYKLAQEYKKtgPFKPKKyfsidrVFRNETLD 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 206 ATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLfGADReIRLRPSYFPFTEPSVEVdvscFKckgkgcnvcKHTG--- 282
Cdd:PTZ00326 374 ATHLAEFHQVEGFVIDRNLTLGDLIGTIREFFRRI-GITK-LRFKPAFNPYTEPSMEI----FG---------YHPGlkk 438

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 445925711 283 WIEILGAGMVHPNVLEMAGFDsSEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:PTZ00326 439 WVEVGNSGIFRPEMLRPMGFP-EDVTVIAWGLSLERPTMIKYGIKNIR 485
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 97-343 6.51e-34

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: 130.19  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711   97 VSLPGRHIEIGSKHPLTRTIEEIEDLFLGLG--------YEIVNGYE-VEQDHYNFEMLNLPKSHPARDMQDSFYITDEI 167
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADnnqrgnplFKIFDNFKpVVTTMENFDNLGFPADHPGRQKSDCYYINEQH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  168 LLRTHTSPVQARTMES-RHGQGPVK--IICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVK------------------- 225
Cdd:TIGR00469 109 LLRAHTSAHELECFQGgLDDSDNIKsgFLISADVYRRDEIDKTHYPVFHQADGAAIRKRTKadlfekepgyiekfeedir 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  226 -------------------------------MSD---------LKGTLELLAKKLFG-------------ADREIRLR-- 250
Cdd:TIGR00469 189 gteadlnkenvkiildddsiplkennpkqeyASDlavdlceheLKHSIEGITKDLFGkkissmiknkannTPKELKVRwi 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711  251 PSYFPFTEPSVEVDVScFKckgkgcnvckhTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:TIGR00469 269 DAYFPFTAPSWEIEIW-FK-----------DEWLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIR 336

                         330
                  ....*....|...
gi 445925711  331 HFYTNDVRFLDQF 343
Cdd:TIGR00469 337 LFWSNDEGFLRQF 349
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 101-330 1.87e-33

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 129.41  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 101 GRHIEIGSKHPLTRTIEEIEDLFLGLGYEIV--NGYeVEQDHYNFEMLNLPKSHPARDMQDSFYIT-------------- 164
Cdd:PLN02853 212 GAPPEGGHLHPLLKVRQQFRKIFLQMGFEEMptNNF-VESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpedyve 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 165 -------------------------DEILLRTHTSPVQARtMESRHGQGPVKiicPGK------VYRRDSDDATHSHQFT 213
Cdd:PLN02853 291 rvktvhesggygsigygydwkreeaNKNLLRTHTTAVSSR-MLYKLAQKGFK---PKRyfsidrVFRNEAVDRTHLAEFH 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 214 QIEGLVVDKNVKMSDLKGTLELLAKKLfGADrEIRLRPSYFPFTEPSVEVdvscFKckgkgcnvcKHTG---WIEILGAG 290
Cdd:PLN02853 367 QVEGLVCDRGLTLGDLIGVLEDFFSRL-GMT-KLRFKPAYNPYTEPSMEI----FS---------YHEGlkkWVEVGNSG 431

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 445925711 291 MVHPNVLEMAGFdSSEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:PLN02853 432 MFRPEMLLPMGL-PEDVNVIAWGLSLERPTMILYGIDNIR 470
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
22-90 3.65e-26

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 98.99  E-value: 3.65e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445925711   22 NDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEEKPAFGQKVNELRQTIQNELDERQQMLVKEKLNKQL 90
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 ...
 111-319 8.09e-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: 55.20  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 111 PLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNlpksHPARDMQDSFYITDEILLRTHTSPVQARTMESRHGQGPV 190
Cdd:cd00768    1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGH----EPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445925711 191 KIICPGKVYR--RDSDDATHSHQFTQIEGLVV----DKNVKMSDLKGTLELLAKKLFGADREIRLRPSYFPFT----EPS 260
Cdd:cd00768   77 RLAEIGPAFRneGGRRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSpggaGPG 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445925711 261 VEVDVscfkckgkgcNVCKHTGWiEILGAGMVHPNVLEMAGFDSSEYSG-------FAFGMGPDRI 319
Cdd:cd00768  157 FEIEV----------DHPEGRGL-EIGSGGYRQDEQARAADLYFLDEALeyrypptIGFGLGLERL 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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