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Conserved domains on  [gi|1907094471|ref|XP_036014055|]
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phenylalanine--tRNA ligase, mitochondrial isoform X3 [Mus musculus]

Protein Classification

phenylalanine--tRNA ligase( domain architecture ID 1006086)

phenylalanine--tRNA ligase catalyzes the synthesis of phenylalanyl-tRNA (Phe)

CATH:  3.30.70.380|3.30.930.10
EC:  6.1.1.20
Gene Ontology:  GO:0005524|GO:0004826|GO:0000049|GO:0006432

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 32-407 4.89e-164

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 466.16  E-value: 4.89e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  32 WSSKPAASQSAVQGAPG------SVLEILGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFY 98
Cdd:PLN02788    3 SSSALVTPATAKSSSRRyrapavSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  99 QQYmvrsrTPLFSVYDQLPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQWDLLHAGLNAFLVVGDVY 178
Cdd:PLN02788   83 ENY-----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 179 RRDQIDCQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeEGSrsahkqethTMEAVKLVEFDLKQVLTRLVTHLFGDg 258
Cdd:PLN02788  158 RRDSIDATHYPVFHQMEGVRVFSPEEW--------------EAS---------GLDGTDLAAEDLKKTLEGLARHLFGD- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 259 LEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDER 338
Cdd:PLN02788  214 VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDER 293

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094471 339 FLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKK 407
Cdd:PLN02788  294 FTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKK 359
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 32-407 4.89e-164

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 466.16  E-value: 4.89e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  32 WSSKPAASQSAVQGAPG------SVLEILGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFY 98
Cdd:PLN02788    3 SSSALVTPATAKSSSRRyrapavSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  99 QQYmvrsrTPLFSVYDQLPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQWDLLHAGLNAFLVVGDVY 178
Cdd:PLN02788   83 ENY-----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 179 RRDQIDCQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeEGSrsahkqethTMEAVKLVEFDLKQVLTRLVTHLFGDg 258
Cdd:PLN02788  158 RRDSIDATHYPVFHQMEGVRVFSPEEW--------------EAS---------GLDGTDLAAEDLKKTLEGLARHLFGD- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 259 LEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDER 338
Cdd:PLN02788  214 VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDER 293

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094471 339 FLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKK 407
Cdd:PLN02788  294 FTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKK 359
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-406 7.67e-143

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: 414.86  E-value: 7.67e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  51 LEILGKSYPQDDHT-NLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQQYMVRSRTPLFSVYDQLPPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 130 LIPADHPSRKKGDNYYLNRAHMLRAHTSAHQWDLLHAGLN-------AFLVVGDVYRRDQIDCQHYPVFHQLEG--VRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 201 SKHELFagVKDGESLQLFEEGSRSAH------------------------KQETHTMEAVKLVEFDLKQVLTRLVTHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 257 ---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 320 AMVLYDIPDIRLFWSEDERFLKQFLLSDINQSVKFQPLSKYPAVFNDISFWLPSE-----NYTENDFYDIVRTVGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405

                         410
                  ....*....|..
gi 1907094471 395 KVDLIDKFEHPK 406
Cdd:TIGR00469 406 QIKLVDKFKHPK 417
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 84-338 3.71e-94

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: 281.74  E-value: 3.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  84 HPLWLIKERVKEHFYQQymvrsrtpLFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNR--AHMLRAHTSAHQW 161
Cdd:cd00496     1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDpaRLLLRTHTSAVQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 162 DLLHA--GLNAFLVVGDVYRRDQIDCQHYPVFHQLEGVRLFSKhelfagvkdgeslqlfeegsrsahkqethtmeavkLV 239
Cdd:cd00496    72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 240 EFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496   117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                         250       260
                  ....*....|....*....|..
gi 1907094471 317 ERLAMVLYDIPDIRLFWSEDER 338
Cdd:cd00496   197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-343 7.60e-53

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: 179.48  E-value: 7.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  84 HPLWLIKERVKEHFYQqyMvrsrtpLFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQwdl 163
Cdd:COG0016   107 HPLTQVIEEIEDIFVG--M------GFEVAEG-PEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ--- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 164 LHAGLN-----AFLVVGDVYRRDQIDCQHYPVFHQLEGVrlfskhelfagvkdgeslqlfeegsrsahkqethtmeAV-K 237
Cdd:COG0016   175 IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGL-------------------------------------VVdK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 238 LVEF-DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCG-----VMEqqlv 299
Cdd:COG0016   218 GISFaDLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGmvhpnVLR---- 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907094471 300 nSAGaqdrI------GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:COG0016   294 -AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 75-343 1.17e-48

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: 165.45  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  75 GRNLHNQKFHPLWLIKERVKEHFYQqyMVrsrtplFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------N 147
Cdd:pfam01409   8 GRRIEPGGLHPLTRTLERIRDIFLG--MG------FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 148 RAHMLRAHTSAHQWDLLHAGLNA---FLVVGDVYRRDQIDCQHYPVFHQLEGVRlfskhelfagVKDGESLQlfeegsrs 224
Cdd:pfam01409  79 RRLLLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA-------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 225 ahkqethtmeavklvefDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNSA 302
Cdd:pfam01409 141 -----------------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907094471 303 G-AQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:pfam01409 204 GiDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-407 7.09e-14

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 66.68  E-value: 7.09e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907094471  358 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKK 407
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGGIP 49
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 32-407 4.89e-164

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 466.16  E-value: 4.89e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  32 WSSKPAASQSAVQGAPG------SVLEILGKSYPQDD-------HTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFY 98
Cdd:PLN02788    3 SSSALVTPATAKSSSRRyrapavSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  99 QQYmvrsrTPLFSVYDQLPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQWDLLHAGLNAFLVVGDVY 178
Cdd:PLN02788   83 ENY-----SNKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 179 RRDQIDCQHYPVFHQLEGVRLFSKHELfagvkdgeslqlfeEGSrsahkqethTMEAVKLVEFDLKQVLTRLVTHLFGDg 258
Cdd:PLN02788  158 RRDSIDATHYPVFHQMEGVRVFSPEEW--------------EAS---------GLDGTDLAAEDLKKTLEGLARHLFGD- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 259 LEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDER 338
Cdd:PLN02788  214 VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDER 293

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094471 339 FLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKK 407
Cdd:PLN02788  294 FTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPKK 359
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-406 7.67e-143

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: 414.86  E-value: 7.67e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  51 LEILGKSYPQDDHT-NLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQQYMVRSRTPLFSVYDQLPPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 130 LIPADHPSRKKGDNYYLNRAHMLRAHTSAHQWDLLHAGLN-------AFLVVGDVYRRDQIDCQHYPVFHQLEG--VRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADGaaIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 201 SKHELFagVKDGESLQLFEEGSRSAH------------------------KQETHTMEAVKLVEFDLKQVLTRLVTHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 257 ---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 320 AMVLYDIPDIRLFWSEDERFLKQFLLSDINQSVKFQPLSKYPAVFNDISFWLPSE-----NYTENDFYDIVRTVGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405

                         410
                  ....*....|..
gi 1907094471 395 KVDLIDKFEHPK 406
Cdd:TIGR00469 406 QIKLVDKFKHPK 417
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 84-338 3.71e-94

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: 281.74  E-value: 3.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  84 HPLWLIKERVKEHFYQQymvrsrtpLFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNR--AHMLRAHTSAHQW 161
Cdd:cd00496     1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDpaRLLLRTHTSAVQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 162 DLLHA--GLNAFLVVGDVYRRDQIDCQHYPVFHQLEGVRLFSKhelfagvkdgeslqlfeegsrsahkqethtmeavkLV 239
Cdd:cd00496    72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 240 EFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496   117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                         250       260
                  ....*....|....*....|..
gi 1907094471 317 ERLAMVLYDIPDIRLFWSEDER 338
Cdd:cd00496   197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-343 7.60e-53

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: 179.48  E-value: 7.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  84 HPLWLIKERVKEHFYQqyMvrsrtpLFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQwdl 163
Cdd:COG0016   107 HPLTQVIEEIEDIFVG--M------GFEVAEG-PEIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ--- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 164 LHAGLN-----AFLVVGDVYRRDQIDCQHYPVFHQLEGVrlfskhelfagvkdgeslqlfeegsrsahkqethtmeAV-K 237
Cdd:COG0016   175 IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEGL-------------------------------------VVdK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 238 LVEF-DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCG-----VMEqqlv 299
Cdd:COG0016   218 GISFaDLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGmvhpnVLR---- 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907094471 300 nSAGaqdrI------GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:COG0016   294 -AVG----IdpeeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 55-343 1.79e-49

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: 169.03  E-value: 1.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  55 GKSYPQDDHTNLTQKVL-SKVGRNLHNQKF--------------HPLWLIKERVKEHFYQQymvrsrtpLFSVYDQlPPV 119
Cdd:TIGR00468  28 VKIELQDELTKLKPELEsAGLWSKLKFETYdvslpgtkiypgslHPLTRVIDEIRDIFLGL--------GFTEETG-PEV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 120 VTTWQNFDSLLIPADHPSRKKGDNYYLNRAHMLRAHTSAHQwdlLHA-------GLNAFlVVGDVYRRDQIDCQHYPVFH 192
Cdd:TIGR00468  99 ETDFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQ---LRTmeeqekpPIRIF-SPGRVFRNDTVDATHLPEFH 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 193 QLEGVRlfskhelfagVKDGESLQlfeegsrsahkqethtmeavklvefDLKQVLTRLVTHLFGdGLEVRWVDCYFPFTH 272
Cdd:TIGR00468 175 QVEGLV----------IDKNISFT-------------------------NLKGFLEEFLKKMFG-ETEIRFRPSYFPFTE 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907094471 273 PSFEMEIN-FRGE-WLEVLGCGVMEQQLVNSAGAQDRI-GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:TIGR00468 219 PSAEIDVYcPEGKgWLEVLGAGMFRPEVLEPMGIDPTYpGFAWGIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 75-343 1.17e-48

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: 165.45  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  75 GRNLHNQKFHPLWLIKERVKEHFYQqyMVrsrtplFSVYDQlPPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------N 147
Cdd:pfam01409   8 GRRIEPGGLHPLTRTLERIRDIFLG--MG------FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 148 RAHMLRAHTSAHQWDLLHAGLNA---FLVVGDVYRRDQIDCQHYPVFHQLEGVRlfskhelfagVKDGESLQlfeegsrs 224
Cdd:pfam01409  79 RRLLLRTHTTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA-------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 225 ahkqethtmeavklvefDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNSA 302
Cdd:pfam01409 141 -----------------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEAV 203

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907094471 303 G-AQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 343
Cdd:pfam01409 204 GiDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
94-341 1.42e-25

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 108.00  E-value: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  94 KEHFYQQYMVRSRTPLFS-----VYDqlPPVVTTWQNFDSLLIPADHPSRKKGDNYYLN----------------RAH-- 150
Cdd:PRK04172  231 KKHPYREFIDEVRDILVEmgfeeMKG--PLVETEFWNFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkEVHeh 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 151 ---------------------MLRAHT---SAHQwdlLHAGLNA---FLVVGDVYRRDQIDCQHYPVFHQLEGVRLfskh 203
Cdd:PRK04172  309 ggdtgsrgwgykwdediakrlVLRTHTtalSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLEGIVM---- 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 204 elfagvkdgeslqlfEEGsrsahkqethtmeavklVEFD-----LKQVLTRLvthlfgdGL-EVRWVDCYFPFTHPSFEM 277
Cdd:PRK04172  382 ---------------GED-----------------VSFRdllgiLKEFYKRL-------GFeEVKFRPAYFPFTEPSVEV 422

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907094471 278 EINF-RGEWLEVLGCGVMEQQLVNSAGAQDRIGwAFGLGLERLAMVLYDIPDIRLFWSEDERFLK 341
Cdd:PRK04172  423 EVYHeGLGWVELGGAGIFRPEVLEPLGIDVPVL-AWGLGIERLAMLRLGLDDIRDLYSSDIEWLR 486
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-407 7.09e-14

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 66.68  E-value: 7.09e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907094471  358 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKK 407
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGGIP 49
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-406 3.75e-10

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 56.34  E-value: 3.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907094471 358 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK 406
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEK 48
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 241-403 8.61e-09

phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273097 [Multi-domain]  Cd Length: 797  Bit Score: 57.69  E-value: 8.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 241 FDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRGEwleVLGC-GVMEQQLVNSAGAQDRIgWAFGLGLERL 319
Cdd:TIGR00472 615 YDLKGDVESLLELLGLSDDVYFKNTAENEELHPGQSATIYLKGK---KIGFiGELHPEIAKKYDLKEPT-FVFELDLDRL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 320 amvlydipdirlfwsederflkqflLSDINQSVKFQPLSKYPAVFNDISFWLPSENyTENDFYDIVRTVGGDLVEKVDLI 399
Cdd:TIGR00472 691 -------------------------LESLKKVPKYRPISKFPAVTRDISFLVPKDV-PANEIIKLIKKSGLELLEEVELF 744


                  ....
gi 1907094471 400 DKFE 403
Cdd:TIGR00472 745 DVYQ 748
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 84-332 4.22e-08

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 55.06  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471  84 HPLWLIKERVKEHFYQQYMVRSRTPLFsvydqlppVVTTWQNFDSLLIPADHPSRKKGDNYYLN---------------- 147
Cdd:PLN02853  221 HPLLKVRQQFRKIFLQMGFEEMPTNNF--------VESSFWNFDALFQPQQHPARDSHDTFFLKapattrqlpedyverv 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 148 -RAH----------------------MLRAHTSAHQWDLLHAGLNA------FLVVGDVYRRDQIDCQHYPVFHQLEGVr 198
Cdd:PLN02853  293 kTVHesggygsigygydwkreeanknLLRTHTTAVSSRMLYKLAQKgfkpkrYFSIDRVFRNEAVDRTHLAEFHQVEGL- 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 199 lfskhelfagVKD-GESLQlfeegsrsahkqethtmeavklvefDLKQVLTRLVTHLfgdGL-EVRWVDCYFPFTHPSfe 276
Cdd:PLN02853  372 ----------VCDrGLTLG-------------------------DLIGVLEDFFSRL---GMtKLRFKPAYNPYTEPS-- 411

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907094471 277 MEInFR-----GEWLEVLGCGVMEQQLVNSAGAQDR---IGWafGLGLERLAMVLYDIPDIR-LF 332
Cdd:PLN02853  412 MEI-FSyheglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIAW--GLSLERPTMILYGIDNIRdLF 473
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 344-403 4.40e-08

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 55.18  E-value: 4.40e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 344 LLSDINQSVKFQPLSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFE 403
Cdd:PRK00629  683 LLEAARKLPKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVYE 741
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 344-403 2.26e-07

Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439842 [Multi-domain]  Cd Length: 793  Bit Score: 52.86  E-value: 2.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 344 LLSDINQSVKFQPLSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFE 403
Cdd:COG0072   685 LLELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYE 743
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 123-332 4.93e-05

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 45.34  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 123 WqNFDSLLIPADHPSR----------------KKGDNYYLNR---AH----------------------MLRAHTSAHQW 161
Cdd:PTZ00326  261 W-NFDALFQPQQHPARdaqdtfflskpetskvNDLDDDYVERvkkVHevggygsigwrydwkleearknILRTHTTAVSA 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 162 DLLH-------AGLN----AFLVVGDVYRRDQIDCQHYPVFHQLEGVrlfskhelfagVKD-GESL-QLFeegsrsahkq 228
Cdd:PTZ00326  340 RMLYklaqeykKTGPfkpkKYFSIDRVFRNETLDATHLAEFHQVEGF-----------VIDrNLTLgDLI---------- 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094471 229 etHTMEavklvEFDLKQVLTRLvthlfgdglevRWVDCYFPFTHPSfeMEInF-----RGEWLEVLGCGVMEQQLVNSAG 303
Cdd:PTZ00326  399 --GTIR-----EFFRRIGITKL-----------RFKPAFNPYTEPS--MEI-FgyhpgLKKWVEVGNSGIFRPEMLRPMG 457

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907094471 304 AQDR---IGWafGLGLERLAMVLYDIPDIR-LF 332
Cdd:PTZ00326  458 FPEDvtvIAW--GLSLERPTMIKYGIKNIRdLF 488
 
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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