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Conserved domains on  [gi|767939114|ref|XP_011512551|]
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phenylalanine--tRNA ligase, mitochondrial isoform X4 [Homo sapiens]

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
 29-406 1.10e-161

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 460.38  E-value: 1.10e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939114 340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK 406
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPK 358
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 29-406 1.10e-161

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 460.38  E-value: 1.10e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939114 340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK 406
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPK 358
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-406 2.61e-139

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: 406.00  E-value: 2.61e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114   51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405

                         410
                  ....*....|..
gi 767939114  395 KVDLIDKFVHPK 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 5.42e-95

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: 283.67  E-value: 5.42e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496    1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496   72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496  117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                        250       260
                 ....*....|....*....|..
gi 767939114 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496  197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-343 2.07e-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: 181.02  E-value: 2.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016  107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016  175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016  223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767939114 299 vnSAGaqdrI------GWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 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 ...
 83-343 3.41e-49

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: 166.99  E-value: 3.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114   83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409  16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409  87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 767939114  310 WAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:pfam01409 212 FAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-404 3.20e-12

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: 62.06  E-value: 3.20e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767939114   358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVH 404
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEG 46
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 29-406 1.10e-161

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 460.38  E-value: 1.10e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  29 HQAWGSRPPAAECATQ-RAPG-SVVELLGKSYPQDD-------HSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYK 99
Cdd:PLN02788   4 SSALVTPATAKSSSRRyRAPAvSAVEIGGVAIARDEvvreddpTNNVPDHIFSKIGMQLHRRPDHPLGILKNAIYDYFDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 100 QYVGrfgtpLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYR 179
Cdd:PLN02788  84 NYSN-----KFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTYYVDAQTVLRCHTSAHQAELLRAGHTHFLVTGDVYR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 180 RDQIDSQHYPIFHQLEAVRLFSKHELfagikdgeslqlfeqssrsahkqETHTMEAVKLVEFDLKQTLTRLMAHLFGDeL 259
Cdd:PLN02788 159 RDSIDATHYPVFHQMEGVRVFSPEEW-----------------------EASGLDGTDLAAEDLKKTLEGLARHLFGD-V 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 260 EIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERF 339
Cdd:PLN02788 215 EMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAFGLGLERLAMVLFDIPDIRLFWSDDERF 294

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767939114 340 LKQFCVSNInqKVKFQPLSKYPAVINDISFWLPSEnYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK 406
Cdd:PLN02788 295 TSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDLVEEVKLIDNFTNPK 358
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 51-406 2.61e-139

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: 406.00  E-value: 2.61e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114   51 VELLGKSYPQDDHS-NLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSL 129
Cdd:TIGR00469   8 LEINGIKYATDGQTtNVTDKIIKLTDANKHLKEDHPLGIIRDLIEKKFNGADNNQRGNPLFKIFDNFKPVVTTMENFDNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  130 LIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLD-------AFLVVGDVYRRDQIDSQHYPIFHQLE--AVRLF 200
Cdd:TIGR00469  88 GFPADHPGRQKSDCYYINEQHLLRAHTSAHELECFQGGLDdsdniksGFLISADVYRRDEIDKTHYPVFHQADgaAIRKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  201 SKHELFagIKDGESLQLFEQSSRSAH------------------------KQETHTMEAVKLVEFDLKQTLTRLMAHLFG 256
Cdd:TIGR00469 168 TKADLF--EKEPGYIEKFEEDIRGTEadlnkenvkiildddsiplkennpKQEYASDLAVDLCEHELKHSIEGITKDLFG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  257 ---------------DELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQ--DRIGWAFGLGLERL 319
Cdd:TIGR00469 246 kkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDILLRAGVHpsETIGWAFGLGLDRI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  320 AMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSE-----NYAENDFYDLVRTIGGDLVE 394
Cdd:TIGR00469 326 AMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDieddaGFHENDFMDIIRNIAGDLVE 405

                         410
                  ....*....|..
gi 767939114  395 KVDLIDKFVHPK 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 5.42e-95

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: 283.67  E-value: 5.42e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  84 HPLWLIKERVKEHFYKQyvgrfgtpLFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRT--HMLRAHTSAHQW 161
Cdd:cd00496    1 HPLNKVIEEIEDIFVSM--------GFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDParLLLRTHTSAVQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 162 DLLHA--GLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKhelfagikdgeslqlfeqssrsahkqethtmeavkLV 239
Cdd:cd00496   72 RALAKlkPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKG-----------------------------------LT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 240 EFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHG--EWLEVLGCGVMEQQLVNSAGAQ-DRIGWAFGLGL 316
Cdd:cd00496  117 FADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDeEYSGFAFGIGL 196

                        250       260
                 ....*....|....*....|..
gi 767939114 317 ERLAMILYDIPDIRLFWCEDER 338
Cdd:cd00496  197 ERLAMLKYGIPDIRLFYSNDLR 218
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 84-343 2.07e-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: 181.02  E-value: 2.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  84 HPLWLIKERVKEHFykqyvGRFGtplFSVYDnlSP-VVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:COG0016  107 HPLTQVIEEIEDIF-----VGMG---FEVAE--GPeIETDWYNFEALNIPPDHPARDMQDTFYIDDGLLLRTHTSPVQ-- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 163 lLHAGLD-----AFLVVGDVYRRDQIDSQHYPIFHQLE--AVrlfSKHELFAgikdgeslqlfeqssrsahkqethtmea 235
Cdd:COG0016  175 -IRTMEKqkppiRIIAPGRVYRRDESDATHSPMFHQVEglVV---DKGISFA---------------------------- 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 236 vklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF------------HGEWLEVLGCG-----VMEqql 298
Cdd:COG0016  223 ------DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficggkgcrvckGTGWLEILGCGmvhpnVLR--- 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767939114 299 vnSAGaqdrI------GWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 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 ...
 83-343 3.41e-49

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: 166.99  E-value: 3.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114   83 HHPLWLIKERVKEHFYkqyvgRFGtplFSVYDNlSPVVTTWQNFDSLLIPADHPSRKKGDNYYL-------NRTHMLRAH 155
Cdd:pfam01409  16 LHPLTRTLERIRDIFL-----GMG---FEEVEG-PEVESDFYNFDALNIPQDHPARDMQDTFYLkkplkpvARRLLLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  156 TSAHQWDLLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqetht 232
Cdd:pfam01409  87 TTPVQARTLAKKPKPpikIFSIGRVFRRDQVDATHLPEFHQVEGLV----------VDENVTFA---------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  233 meavklvefDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINF--HGEWLEVLGCGVMEQQLVNSAG-AQDRIG 309
Cdd:pfam01409 141 ---------DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVckLGGWLEVGGAGMVHPNVLEAVGiDEDYSG 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 767939114  310 WAFGLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:pfam01409 212 FAFGLGVERLAMLKYGIDDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 84-343 4.63e-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: 168.26  E-value: 4.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114   84 HPLWLIKERVKEHFYKqyvgrFGtplFSVydNLSPVVTT-WQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQwd 162
Cdd:TIGR00468  72 HPLTRVIDEIRDIFLG-----LG---FTE--ETGPEVETdFWNFDALNIPQDHPARDMQDTFYIKDRLLLRTHTTAVQ-- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  163 lLHAGLDA------FLVVGDVYRRDQIDSQHYPIFHQLEAVRlfskhelfagIKDGESLQlfeqssrsahkqethtmeav 236
Cdd:TIGR00468 140 -LRTMEEQekppirIFSPGRVFRNDTVDATHLPEFHQVEGLV----------IDKNISFT-------------------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  237 klvefDLKQTLtRLMAHLFGDELEIRWVDCYFPFTHPSFEMEInFHGE---WLEVLGCGVMEQQLVNSAGAQDRI-GWAF 312
Cdd:TIGR00468 189 -----NLKGFL-EEFLKKMFGETEIRFRPSYFPFTEPSAEIDV-YCPEgkgWLEVLGAGMFRPEVLEPMGIDPTYpGFAW 261

                         250       260       270
                  ....*....|....*....|....*....|.
gi 767939114  313 GLGLERLAMILYDIPDIRLFWCEDERFLKQF 343
Cdd:TIGR00468 262 GIGIERLAMLKYGITDIRDLYENDLRFLRQF 292
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
117-332 2.12e-24

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 104.91  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 117 SPVVTT--WqNFDSLLIPADHPSRKKGDNYYLN----------------RTH-----------------------MLRAH 155
Cdd:PRK04172 256 GPLVETefW-NFDALFQPQDHPAREMQDTFYLKypgigdlpeelvervkEVHehggdtgsrgwgykwdediakrlVLRTH 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 156 T---SAHQwdlLHAGLDA---FLVVGDVYRRDQIDSQHYPIFHQLEavrlfskhelfaGIKDGESLqlfeqssrsahkqe 229
Cdd:PRK04172 335 TtalSARY---LASRPEPpqkYFSIGRVFRPDTIDATHLPEFYQLE------------GIVMGEDV-------------- 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 230 thtmeAVKlvefDLKQTLTRlMAHLFGDElEIRWVDCYFPFTHPSFEMEInFH--GEWLEVLGCGVMEQQLVNSAGAQDR 307
Cdd:PRK04172 386 -----SFR----DLLGILKE-FYKRLGFE-EVKFRPAYFPFTEPSVEVEV-YHegLGWVELGGAGIFRPEVLEPLGIDVP 453

                        250       260
                 ....*....|....*....|....*.
gi 767939114 308 IGwAFGLGLERLAMILYDIPDIR-LF 332
Cdd:PRK04172 454 VL-AWGLGIERLAMLRLGLDDIRdLY 478
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-404 3.20e-12

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: 62.06  E-value: 3.20e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767939114   358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVH 404
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEG 46
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 123-332 1.03e-08

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 56.99  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 123 WqNFDSLLIPADHPSRKKGDNYYLN-----------------RTH----------------------MLRAHTSAHQWDL 163
Cdd:PLN02853 253 W-NFDALFQPQQHPARDSHDTFFLKapattrqlpedyvervkTVHesggygsigygydwkreeanknLLRTHTTAVSSRM 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 164 LHA-GLDAF-----LVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagIKD-GESLQlfeqssrsahkqethtmeav 236
Cdd:PLN02853 332 LYKlAQKGFkpkryFSIDRVFRNEAVDRTHLAEFHQVEGL-----------VCDrGLTLG-------------------- 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 237 klvefDLKQTLTRLMAHLFGDELeiRWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNSAGAQDR---IG 309
Cdd:PLN02853 381 -----DLIGVLEDFFSRLGMTKL--RFKPAYNPYTEPS--MEIfSYHeglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIA 451

                        250       260
                 ....*....|....*....|....
gi 767939114 310 WafGLGLERLAMILYDIPDIR-LF 332
Cdd:PLN02853 452 W--GLSLERPTMILYGIDNIRdLF 473
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 358-406 2.10e-08

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: 51.33  E-value: 2.10e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767939114  358 SKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPK 406
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEK 48
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 241-402 1.39e-07

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: 53.83  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  241 FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEwleVLGC-GVMEQQLVNSAGAQDRIgWAFGLGLERL 319
Cdd:TIGR00472 615 YDLKGDVESLLELLGLSDDVYFKNTAENEELHPGQSATIYLKGK---KIGFiGELHPEIAKKYDLKEPT-FVFELDLDRL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114  320 AMILYDIPdirlfwcederflkqfcvsninqkvKFQPLSKYPAVINDISFWLPSENYAeNDFYDLVRTIGGDLVEKVDLI 399
Cdd:TIGR00472 691 LESLKKVP-------------------------KYRPISKFPAVTRDISFLVPKDVPA-NEIIKLIKKSGLELLEEVELF 744


                  ...
gi 767939114  400 DKF 402
Cdd:TIGR00472 745 DVY 747
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 123-332 4.20e-07

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 51.89  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 123 WqNFDSLLIPADHPSR----------------KKGDNYYLNR---TH----------------------MLRAHTSAHQW 161
Cdd:PTZ00326 261 W-NFDALFQPQQHPARdaqdtfflskpetskvNDLDDDYVERvkkVHevggygsigwrydwkleearknILRTHTTAVSA 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 162 DLLH-------AGLD----AFLVVGDVYRRDQIDSQHYPIFHQLEAVrlfskhelfagikdgeslqlfeqssrsahkqet 230
Cdd:PTZ00326 340 RMLYklaqeykKTGPfkpkKYFSIDRVFRNETLDATHLAEFHQVEGF--------------------------------- 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939114 231 htmeavkLVEFDLkqTLTRLMA--HLFGDELEI---RWVDCYFPFTHPSfeMEI-NFH---GEWLEVLGCGVMEQQLVNS 301
Cdd:PTZ00326 387 -------VIDRNL--TLGDLIGtiREFFRRIGItklRFKPAFNPYTEPS--MEIfGYHpglKKWVEVGNSGIFRPEMLRP 455

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 767939114 302 AGAQDR---IGWafGLGLERLAMILYDIPDIR-LF 332
Cdd:PTZ00326 456 MGFPEDvtvIAW--GLSLERPTMIKYGIKNIRdLF 488
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 351-402 1.31e-06

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 50.55  E-value: 1.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767939114 351 KVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLIDKF 402
Cdd:PRK00629 690 LPKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVY 740
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 345-400 4.85e-06

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: 48.62  E-value: 4.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939114 345 VSNINQKVKFQPLSKYPAVINDISFWLPsENYAENDFYDLVRTIGGDLVEKVDLID 400
Cdd:COG0072  686 LELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFD 740
 
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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