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Conserved domains on  [gi|1480895473|ref|WP_119557380|]
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phenylalanine--tRNA ligase subunit alpha [Staphylococcus epidermidis]

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]; ...
 7-344 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: 667.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473   7 MSELKQQALVDINEANDAQALQEVKVKYLGKKGSVSALMKNMKDLPNEEKPAYGQKVNELRQTIQSELDERQKLIKEEKL 86
Cdd:COG0016     4 LEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  87 NQQLSEETIDVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEE 166
Cdd:COG0016    84 EARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 167 ILMRTHTSPVQARTMEKRKGqgPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADRE 246
Cdd:COG0016   164 LLLRTHTSPVQIRTMEKQKP--PIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 247 IRLRPSYFPFTEPSVEVDVSCFKCKGQGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSMEYSGFAFGMGPDRIAMLKYGI 326
Cdd:COG0016   242 VRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYGI 321

                         330
                  ....*....|....*...
gi 1480895473 327 EDIRHFYTNDVRFLDQFK 344
Cdd:COG0016   322 DDIRLFFENDLRFLRQFG 339
 
Name Accession Description Interval E-value
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 7-344 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: 667.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473   7 MSELKQQALVDINEANDAQALQEVKVKYLGKKGSVSALMKNMKDLPNEEKPAYGQKVNELRQTIQSELDERQKLIKEEKL 86
Cdd:COG0016     4 LEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  87 NQQLSEETIDVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEE 166
Cdd:COG0016    84 EARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 167 ILMRTHTSPVQARTMEKRKGqgPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADRE 246
Cdd:COG0016   164 LLLRTHTSPVQIRTMEKQKP--PIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 247 IRLRPSYFPFTEPSVEVDVSCFKCKGQGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSMEYSGFAFGMGPDRIAMLKYGI 326
Cdd:COG0016   242 VRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYGI 321

                         330
                  ....*....|....*...
gi 1480895473 327 EDIRHFYTNDVRFLDQFK 344
Cdd:COG0016   322 DDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 94-343 3.34e-148

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: 417.75  E-value: 3.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  94 TIDVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYI-------TEE 166
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 167 ILMRTHTSPVQARTMEKRKgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADRE 246
Cdd:pfam01409  81 LLLRTHTTPVQARTLAKKP-KPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 247 IRLRPSYFPFTEPSVEVDVScfkckgqgcnVCKHTGWIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGI 326
Cdd:pfam01409 160 VRFRPSYFPFTEPSAEVDVY----------VCKLGGWLEVGGAGMVHPNVLEAVGIDE-DYSGFAFGLGVERLAMLKYGI 228

                         250
                  ....*....|....*..
gi 1480895473 327 EDIRHFYTNDVRFLDQF 343
Cdd:pfam01409 229 DDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 44-344 5.86e-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: 419.02  E-value: 5.86e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  44 LMKNMKDLPNEE-KPAYGQKVNELRQTIQSELDERQKLIKEEKLNQQLSEETIDVTLPSRHIEIGSKHPLTRTVEEIEDL 122
Cdd:TIGR00468   5 LLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 123 FLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEEILMRTHTSPVQARTMEKRKGqGPVKIICPGKVYRRD 202
Cdd:TIGR00468  85 FLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEK-PPIRIFSPGRVFRND 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 203 SDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGAdREIRLRPSYFPFTEPSVEVDVSCFKCKgqgcnvckhtG 282
Cdd:TIGR00468 164 TVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGK----------G 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1480895473 283 WIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFK 344
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 110-338 2.16e-130

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: 371.49  E-value: 2.16e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 110 HPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEE--ILMRTHTSPVQARTMEKRKGq 187
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKLKP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 188 gPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADREIRLRPSYFPFTEPSVEVDVSC 267
Cdd:cd00496    80 -PIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1480895473 268 FKCkgqgcnvckhTGWIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVR 338
Cdd:cd00496   159 PGC----------LGWLEILGCGMVRPEVLENAGIDE-EYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
96-340 6.19e-71

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 228.95  E-value: 6.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  96 DVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFY--------ITEEI 167
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdLPEEL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 168 L-------------------------------MRTHTSPVQARTMEKRkGQGPVKIICPGKVYRRDSDDATHSHQFTQIE 216
Cdd:PRK04172  299 VervkevhehggdtgsrgwgykwdediakrlvLRTHTTALSARYLASR-PEPPQKYFSIGRVFRPDTIDATHLPEFYQLE 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 217 GLVVDKNIKMSDLKGTLELVAKKLfGADrEIRLRPSYFPFTEPSVEVDVscfkckgqgcnvcKHT--GWIEILGAGMVHP 294
Cdd:PRK04172  378 GIVMGEDVSFRDLLGILKEFYKRL-GFE-EVKFRPAYFPFTEPSVEVEV-------------YHEglGWVELGGAGIFRP 442

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1480895473 295 NVLEMAGFDsmeYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFL 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]; ...
 7-344 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: 667.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473   7 MSELKQQALVDINEANDAQALQEVKVKYLGKKGSVSALMKNMKDLPNEEKPAYGQKVNELRQTIQSELDERQKLIKEEKL 86
Cdd:COG0016     4 LEALKEEALAAIAAASDLEELEALRVKYLGKKGELTELLKGLGKLPPEERPAAGKLANELKQAIEAALEARKEELEAAEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  87 NQQLSEETIDVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEE 166
Cdd:COG0016    84 EARLAAETIDVTLPGRPRPLGSLHPLTQVIEEIEDIFVGMGFEVAEGPEIETDWYNFEALNIPPDHPARDMQDTFYIDDG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 167 ILMRTHTSPVQARTMEKRKGqgPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADRE 246
Cdd:COG0016   164 LLLRTHTSPVQIRTMEKQKP--PIRIIAPGRVYRRDESDATHSPMFHQVEGLVVDKGISFADLKGTLEEFAKAFFGEDVK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 247 IRLRPSYFPFTEPSVEVDVSCFKCKGQGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSMEYSGFAFGMGPDRIAMLKYGI 326
Cdd:COG0016   242 VRFRPSYFPFTEPSAEVDISCFICGGKGCRVCKGTGWLEILGCGMVHPNVLRAVGIDPEEYSGFAFGMGIERLAMLKYGI 321

                         330
                  ....*....|....*...
gi 1480895473 327 EDIRHFYTNDVRFLDQFK 344
Cdd:COG0016   322 DDIRLFFENDLRFLRQFG 339
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 94-343 3.34e-148

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: 417.75  E-value: 3.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  94 TIDVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYI-------TEE 166
Cdd:pfam01409   1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVEGPEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 167 ILMRTHTSPVQARTMEKRKgQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADRE 246
Cdd:pfam01409  81 LLLRTHTTPVQARTLAKKP-KPPIKIFSIGRVFRRDQVDATHLPEFHQVEGLVVDENVTFADLKGVLEEFLRKFFGFEVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 247 IRLRPSYFPFTEPSVEVDVScfkckgqgcnVCKHTGWIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGI 326
Cdd:pfam01409 160 VRFRPSYFPFTEPSAEVDVY----------VCKLGGWLEVGGAGMVHPNVLEAVGIDE-DYSGFAFGLGVERLAMLKYGI 228

                         250
                  ....*....|....*..
gi 1480895473 327 EDIRHFYTNDVRFLDQF 343
Cdd:pfam01409 229 DDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 44-344 5.86e-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: 419.02  E-value: 5.86e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  44 LMKNMKDLPNEE-KPAYGQKVNELRQTIQSELDERQKLIKEEKLNQQLSEETIDVTLPSRHIEIGSKHPLTRTVEEIEDL 122
Cdd:TIGR00468   5 LLKQLGKLTKEEtKPALGALINEVKIELQDELTKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 123 FLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEEILMRTHTSPVQARTMEKRKGqGPVKIICPGKVYRRD 202
Cdd:TIGR00468  85 FLGLGFTEETGPEVETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQLRTMEEQEK-PPIRIFSPGRVFRND 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 203 SDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGAdREIRLRPSYFPFTEPSVEVDVSCFKCKgqgcnvckhtG 282
Cdd:TIGR00468 164 TVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMFGE-TEIRFRPSYFPFTEPSAEIDVYCPEGK----------G 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1480895473 283 WIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFK 344
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDP-TYPGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQFK 293
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 110-338 2.16e-130

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: 371.49  E-value: 2.16e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 110 HPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFYITEE--ILMRTHTSPVQARTMEKRKGq 187
Cdd:cd00496     1 HPLNKVIEEIEDIFVSMGFTEVEGPEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQARALAKLKP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 188 gPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMSDLKGTLELVAKKLFGADREIRLRPSYFPFTEPSVEVDVSC 267
Cdd:cd00496    80 -PIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1480895473 268 FKCkgqgcnvckhTGWIEILGAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVR 338
Cdd:cd00496   159 PGC----------LGWLEILGCGMVRPEVLENAGIDE-EYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
96-340 6.19e-71

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 228.95  E-value: 6.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  96 DVTLPSRHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYEVEQDYYNFEALNLPKSHPARDMQDSFY--------ITEEI 167
Cdd:PRK04172  219 NVKAPPPKIYPGKKHPYREFIDEVRDILVEMGFEEMKGPLVETEFWNFDALFQPQDHPAREMQDTFYlkypgigdLPEEL 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 168 L-------------------------------MRTHTSPVQARTMEKRkGQGPVKIICPGKVYRRDSDDATHSHQFTQIE 216
Cdd:PRK04172  299 VervkevhehggdtgsrgwgykwdediakrlvLRTHTTALSARYLASR-PEPPQKYFSIGRVFRPDTIDATHLPEFYQLE 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 217 GLVVDKNIKMSDLKGTLELVAKKLfGADrEIRLRPSYFPFTEPSVEVDVscfkckgqgcnvcKHT--GWIEILGAGMVHP 294
Cdd:PRK04172  378 GIVMGEDVSFRDLLGILKEFYKRL-GFE-EVKFRPAYFPFTEPSVEVEV-------------YHEglGWVELGGAGIFRP 442

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1480895473 295 NVLEMAGFDsmeYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFL 340
Cdd:PRK04172  443 EVLEPLGID---VPVLAWGLGIERLAMLRLGLDDIRDLYSSDIEWL 485
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 108-345 9.06e-51

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 174.18  E-value: 9.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 108 SKHPLTRTVEEIEDLF---LGLGYEIVDG-YEVEQDYYNFEALNLPKSHPARDMQDSFYITEEILMRTHTSPVQARTMEK 183
Cdd:PLN02788   66 PDHPLGILKNAIYDYFdenYSNKFKKFDDlSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 184 rkgqGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIKMS------------DLKGTLELVAKKLFGaDREIRLRP 251
Cdd:PLN02788  146 ----GHTHFLVTGDVYRRDSIDATHYPVFHQMEGVRVFSPEEWEasgldgtdlaaeDLKKTLEGLARHLFG-DVEMRWVD 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 252 SYFPFTEPSVEVDVScFKCKgqgcnvckhtgWIEILGAGMVHPNVLEMAGFDsmEYSGFAFGMGPDRIAMLKYGIEDIRH 331
Cdd:PLN02788  221 AYFPFTNPSFELEIF-FKGE-----------WLEVLGCGVTEQEILKNNGRS--DNVAWAFGLGLERLAMVLFDIPDIRL 286

                         250
                  ....*....|....
gi 1480895473 332 FYTNDVRFLDQFKA 345
Cdd:PLN02788  287 FWSDDERFTSQFKE 300
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 102-330 1.17e-37

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 140.87  E-value: 1.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 102 RHIEIGSKHPLTRTVEEIEDLFLGLGYEIVDGYE-VEQDYYNFEALNLPKSHPARDMQDSFYIT---------------- 164
Cdd:PTZ00326  221 KKIGGGNLHPLLKVRREFREILLEMGFEEMPTNRyVESSFWNFDALFQPQQHPARDAQDTFFLSkpetskvndldddyve 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 165 ----------------------EE----ILmRTHTSPVQARtMEKRKGQGPVK--IICPGK------VYRRDSDDATHSH 210
Cdd:PTZ00326  301 rvkkvhevggygsigwrydwklEEarknIL-RTHTTAVSAR-MLYKLAQEYKKtgPFKPKKyfsidrVFRNETLDATHLA 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 211 QFTQIEGLVVDKNIKMSDLKGTLELVAKKLfGADReIRLRPSYFPFTEPSVEVdvscFKckgqgcnvcKHTG---WIEIL 287
Cdd:PTZ00326  379 EFHQVEGFVIDRNLTLGDLIGTIREFFRRI-GITK-LRFKPAFNPYTEPSMEI----FG---------YHPGlkkWVEVG 443

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1480895473 288 GAGMVHPNVLEMAGFDSmEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:PTZ00326  444 NSGIFRPEMLRPMGFPE-DVTVIAWGLSLERPTMIKYGIKNIR 485
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 104-330 1.16e-33

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 129.79  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 104 IEIGSKHPLTRTVEEIEDLFLGLGYEivdgyE------VEQDYYNFEALNLPKSHPARDMQDSFYIT------------- 164
Cdd:PLN02853  215 PEGGHLHPLLKVRQQFRKIFLQMGFE-----EmptnnfVESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpedyv 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 165 -----------------------EEI---LMRTHTSPVQARTMEK--RKGQGPVKIICPGKVYRRDSDDATHSHQFTQIE 216
Cdd:PLN02853  290 ervktvhesggygsigygydwkrEEAnknLLRTHTTAVSSRMLYKlaQKGFKPKRYFSIDRVFRNEAVDRTHLAEFHQVE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 217 GLVVDKNIKMSDLKGTLELVAKKLfGADrEIRLRPSYFPFTEPSVEVdvscFKckgqgcnvcKHTG---WIEILGAGMVH 293
Cdd:PLN02853  370 GLVCDRGLTLGDLIGVLEDFFSRL-GMT-KLRFKPAYNPYTEPSMEI----FS---------YHEGlkkWVEVGNSGMFR 434

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1480895473 294 PNVLEMAGFdSMEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:PLN02853  435 PEMLLPMGL-PEDVNVIAWGLSLERPTMILYGIDNIR 470
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 97-343 2.35e-32

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: 125.96  E-value: 2.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473  97 VTLPSRHIEIGSKHPLTRTVEEIEDLFLGLG--------YEIVDGYE-VEQDYYNFEALNLPKSHPARDMQDSFYITEEI 167
Cdd:TIGR00469  29 IKLTDANKHLKEDHPLGIIRDLIEKKFNGADnnqrgnplFKIFDNFKpVVTTMENFDNLGFPADHPGRQKSDCYYINEQH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 168 LMRTHTSPVQARTMEK-RKGQGPVK--IICPGKVYRRDSDDATHSHQFTQIEGLVVDKNIK------------------- 225
Cdd:TIGR00469 109 LLRAHTSAHELECFQGgLDDSDNIKsgFLISADVYRRDEIDKTHYPVFHQADGAAIRKRTKadlfekepgyiekfeedir 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 226 -------------------------------MSD---------LKGTLELVAKKLFG-------------ADREIRLR-- 250
Cdd:TIGR00469 189 gteadlnkenvkiildddsiplkennpkqeyASDlavdlceheLKHSIEGITKDLFGkkissmiknkannTPKELKVRwi 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 251 PSYFPFTEPSVEVDVSCfkcKGQgcnvckhtgWIEILGAGMVHPNVLEMAGFDSMEYSGFAFGMGPDRIAMLKYGIEDIR 330
Cdd:TIGR00469 269 DAYFPFTAPSWEIEIWF---KDE---------WLELCGCGIIRHDILLRAGVHPSETIGWAFGLGLDRIAMLLFDIPDIR 336

                         330
                  ....*....|...
gi 1480895473 331 HFYTNDVRFLDQF 343
Cdd:TIGR00469 337 LFWSNDEGFLRQF 349
Phe_tRNA-synt_N pfam02912
Aminoacyl tRNA synthetase class II, N-terminal domain;
22-90 1.50e-27

Aminoacyl tRNA synthetase class II, N-terminal domain;


Pssm-ID: 460745 [Multi-domain]  Cd Length: 69  Bit Score: 102.84  E-value: 1.50e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1480895473  22 NDAQALQEVKVKYLGKKGSVSALMKNMKDLPNEEKPAYGQKVNELRQTIQSELDERQKLIKEEKLNQQL 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 ...
 121-319 1.85e-08

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: 54.05  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 121 DLFLGLGYEIVDGYEVEQDYYNFEALNlpksHPARDMQDSFYITEEILMRTHTSPVQARTMEKRKGQGPVKIICPGKVYR 200
Cdd:cd00768    11 RFMAELGFQEVETPIVEREPLLEKAGH----EPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPLRLAEIGPAFR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480895473 201 --RDSDDATHSHQFTQIEGLVV----DKNIKMSDLKGTLELVAKKLFGADREIRLRPSYFPFT----EPSVEVDVscfkc 270
Cdd:cd00768    87 neGGRRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSpggaGPGFEIEV----- 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1480895473 271 kgqgcNVCKHTGWiEILGAGMVHPNVLEMAGFDSMEYSG-------FAFGMGPDRI 319
Cdd:cd00768   162 -----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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