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Conserved domains on  [gi|85719322|ref|NP_001034278|]
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phenylalanine--tRNA ligase, mitochondrial isoform 2 [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
 1-218 3.50e-116

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 336.74  E-value: 3.50e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    1 MEAVKLVEFDLKQVLTRLVTHLFGDgLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAF 80
Cdd:PLN02788 189 LDGTDLAAEDLKKTLEGLARHLFGD-VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAF 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   81 GLGLERLAMVLYDIPDIRLFWSEDERFLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDL 160
Cdd:PLN02788 268 GLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDL 344

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 85719322  161 VEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR 218
Cdd:PLN02788 345 VEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 1-218 3.50e-116

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 336.74  E-value: 3.50e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    1 MEAVKLVEFDLKQVLTRLVTHLFGDgLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAF 80
Cdd:PLN02788 189 LDGTDLAAEDLKKTLEGLARHLFGD-VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAF 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   81 GLGLERLAMVLYDIPDIRLFWSEDERFLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDL 160
Cdd:PLN02788 268 GLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDL 344

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 85719322  161 VEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR 218
Cdd:PLN02788 345 VEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 3-216 2.57e-93

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: 280.42  E-value: 2.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322     3 AVKLVEFDLKQVLTRLVTHLFG---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLV 67
Cdd:TIGR00469 224 AVDLCEHELKHSIEGITKDLFGkkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDIL 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    68 NSAGAQ--DRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFLLSDINQSVKFQPLSKYPAVFNDISFWLPSE--- 142
Cdd:TIGR00469 304 LRAGVHpsETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDied 383

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85719322   143 --NYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVE 216
Cdd:TIGR00469 384 daGFHENDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 1-106 4.42e-47

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: 154.63  E-value: 4.42e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   1 MEAV----KLVEFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ- 73
Cdd:cd00496 106 IEGLvvdkGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDe 185

                        90       100       110
                ....*....|....*....|....*....|...
gi 85719322  74 DRIGWAFGLGLERLAMVLYDIPDIRLFWSEDER 106
Cdd:cd00496 186 EYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 126-218 5.63e-34

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: 116.76  E-value: 5.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    126 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEH-PKTHRTSHCYRITYRHMERTLSQREVGNVHQA 204
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 85719322    205 VQEAAVQLLGVEGR 218
Cdd:smart00896  80 IVAALEKKFGAELR 93
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 10-111 4.77e-33

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: 121.31  E-value: 4.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322  10 DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCGVMEQQLVNSAGaqdrI- 76
Cdd:COG0016 223 DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGMVHPNVLRAVG----Id 298

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 85719322  77 -----GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 111
Cdd:COG0016 299 peeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 10-111 9.80e-30

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: 110.36  E-value: 9.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    10 DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNSAG-AQDRIGWAFGLGLER 86
Cdd:pfam01409 141 DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEAVGiDEDYSGFAFGLGVER 220

                          90       100
                  ....*....|....*....|....*
gi 85719322    87 LAMVLYDIPDIRLFWSEDERFLKQF 111
Cdd:pfam01409 221 LAMLKYGIDDIRDLYENDLRFLRQF 245
 
Name Accession Description Interval E-value
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 1-218 3.50e-116

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 336.74  E-value: 3.50e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    1 MEAVKLVEFDLKQVLTRLVTHLFGDgLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAF 80
Cdd:PLN02788 189 LDGTDLAAEDLKKTLEGLARHLFGD-VEMRWVDAYFPFTNPSFELEIFFKGEWLEVLGCGVTEQEILKNNGRSDNVAWAF 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   81 GLGLERLAMVLYDIPDIRLFWSEDERFLKQFLLSDInqSVKFQPLSKYPAVFNDISFWLPSEnYTENDFYDIVRTVGGDL 160
Cdd:PLN02788 268 GLGLERLAMVLFDIPDIRLFWSDDERFTSQFKEGQL--GVKFKPYSKYPPCYKDISFWISDE-FTENNLCEVVRGIAGDL 344

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 85719322  161 VEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR 218
Cdd:PLN02788 345 VEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 3-216 2.57e-93

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: 280.42  E-value: 2.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322     3 AVKLVEFDLKQVLTRLVTHLFG---------------DGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLV 67
Cdd:TIGR00469 224 AVDLCEHELKHSIEGITKDLFGkkissmiknkanntpKELKVRWIDAYFPFTAPSWEIEIWFKDEWLELCGCGIIRHDIL 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    68 NSAGAQ--DRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFLLSDINQSVKFQPLSKYPAVFNDISFWLPSE--- 142
Cdd:TIGR00469 304 LRAGVHpsETIGWAFGLGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDLHLIPKFKPISHHPGCFNDLAFWLPEDied 383

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85719322   143 --NYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVE 216
Cdd:TIGR00469 384 daGFHENDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVE 459
PheRS_alpha_core cd00496
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ...
 1-106 4.42e-47

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: 154.63  E-value: 4.42e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   1 MEAV----KLVEFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRG--EWLEVLGCGVMEQQLVNSAGAQ- 73
Cdd:cd00496 106 IEGLvvdkGLTFADLKGTLEEFAKELFGPITKVRFRPSYFPFTEPSFEVDVYCPGclGWLEILGCGMVRPEVLENAGIDe 185

                        90       100       110
                ....*....|....*....|....*....|...
gi 85719322  74 DRIGWAFGLGLERLAMVLYDIPDIRLFWSEDER 106
Cdd:cd00496 186 EYSGFAFGIGLERLAMLKYGIPDIRLFYSNDLR 218
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 126-218 5.63e-34

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: 116.76  E-value: 5.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    126 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEH-PKTHRTSHCYRITYRHMERTLSQREVGNVHQA 204
Cdd:smart00896   1 SKFPAVRRDLAFVVD-EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDK 79

                           90
                   ....*....|....
gi 85719322    205 VQEAAVQLLGVEGR 218
Cdd:smart00896  80 IVAALEKKFGAELR 93
PheS COG0016
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ...
 10-111 4.77e-33

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: 121.31  E-value: 4.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322  10 DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINF---RGE---------WLEVLGCGVMEQQLVNSAGaqdrI- 76
Cdd:COG0016 223 DLKGTLEEFAKAFFGEDVKVRFRPSYFPFTEPSAEVDISCficGGKgcrvckgtgWLEILGCGMVHPNVLRAVG----Id 298

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 85719322  77 -----GWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQF 111
Cdd:COG0016 299 peeysGFAFGMGIERLAMLKYGIDDIRLFFENDLRFLRQF 338
tRNA-synt_2d pfam01409
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ...
 10-111 9.80e-30

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: 110.36  E-value: 9.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    10 DLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFR--GEWLEVLGCGVMEQQLVNSAG-AQDRIGWAFGLGLER 86
Cdd:pfam01409 141 DLKGVLEEFLRKFFGFEVKVRFRPSYFPFTEPSAEVDVYVCklGGWLEVGGAGMVHPNVLEAVGiDEDYSGFAFGLGVER 220

                          90       100
                  ....*....|....*....|....*
gi 85719322    87 LAMVLYDIPDIRLFWSEDERFLKQF 111
Cdd:pfam01409 221 LAMLKYGIDDIRDLYENDLRFLRQF 245
pheS TIGR00468
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ...
 10-111 1.50e-26

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: 103.16  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    10 DLKQVLTRLVTHLFGdGLEVRWVDCYFPFTHPSFEMEIN-FRGE-WLEVLGCGVMEQQLVNSAGAQDRI-GWAFGLGLER 86
Cdd:TIGR00468 189 NLKGFLEEFLKKMFG-ETEIRFRPSYFPFTEPSAEIDVYcPEGKgWLEVLGAGMFRPEVLEPMGIDPTYpGFAWGIGIER 267

                          90       100
                  ....*....|....*....|....*
gi 85719322    87 LAMVLYDIPDIRLFWSEDERFLKQF 111
Cdd:TIGR00468 268 LAMLKYGITDIRDLYENDLRFLRQF 292
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 126-218 2.70e-24

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: 92.16  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   126 SKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHMERTLSQREVGNVHQ 203
Cdd:pfam03147   1 SKYPAVRRDLAFVVD-EDVPAADILKAIREAGGELLESVELFDVYRGEKipEGKKSLAFRLTFQSPERTLTDEEVNAIIE 79

                          90
                  ....*....|....*
gi 85719322   204 AVQEAAVQLLGVEGR 218
Cdd:pfam03147  80 KIVEALEKKFGAELR 94
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 9-218 3.15e-18

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: 82.72  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322     9 FDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRGEwleVLGC-GVMEQQLVNSAGAQDRIgWAFGLGLERL 87
Cdd:TIGR00472 615 YDLKGDVESLLELLGLSDDVYFKNTAENEELHPGQSATIYLKGK---KIGFiGELHPEIAKKYDLKEPT-FVFELDLDRL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322    88 amvlydipdirlfwsederflkqflLSDINQSVKFQPLSKYPAVFNDISFWLPSENyTENDFYDIVRTVGGDLVEKVDLI 167
Cdd:TIGR00472 691 -------------------------LESLKKVPKYRPISKFPAVTRDISFLVPKDV-PANEIIKLIKKSGLELLEEVELF 744

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 85719322   168 DKF--EHPKTHRTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR 218
Cdd:TIGR00472 745 DVYqgKNIGEGKKSLALRLVLRDKERTLTDEEINKIVEKVLNALKEKLGAELR 797
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 112-216 8.74e-18

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 81.37  E-value: 8.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322  112 LLSDINQSVKFQPLSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHM 189
Cdd:PRK00629 683 LLEAARKLPKYKPISKFPAVRRDLALVVD-EDVPAADILKAIKKAGGKLLESVELFDVYEGKGigEGKKSLAFRLTFQDP 761

                         90       100
                 ....*....|....*....|....*..
gi 85719322  190 ERTLSQREVGNVHQAVQEAAVQLLGVE 216
Cdd:PRK00629 762 DRTLTDEEINAAMDKIVAALEEKFGAE 788
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 112-216 6.24e-17

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: 78.67  E-value: 6.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322 112 LLSDINQSVKFQPLSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPK--THRTSHCYRITYRHM 189
Cdd:COG0072 685 LLELARKVPKYKPISKFPAVRRDLALVVD-EDVPAADVLDAIRKAAGKLLEDVRLFDVYEGKGvpEGKKSLAFSLTLQDP 763

                        90       100
                ....*....|....*....|....*..
gi 85719322 190 ERTLSQREVGNVHQAVQEAAVQLLGVE 216
Cdd:COG0072 764 DRTLTDEEIDAAMDKIVAALEKKFGAE 790
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
28-109 3.66e-16

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 76.41  E-value: 3.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322   28 EVRWVDCYFPFTHPSFEMEINF-RGEWLEVLGCGVMEQQLVNSAGAQDRIGwAFGLGLERLAMVLYDIPDIRLFWSEDER 106
Cdd:PRK04172 405 EVKFRPAYFPFTEPSVEVEVYHeGLGWVELGGAGIFRPEVLEPLGIDVPVL-AWGLGIERLAMLRLGLDDIRDLYSSDIE 483


                 ...
gi 85719322  107 FLK 109
Cdd:PRK04172 484 WLR 486
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 105-218 3.07e-07

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 50.09  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85719322  105 ERFLKQFLLSDINQSVK------FQPLSKYPAVFNDISFWLPsENYTENDFYDIVRTVGGDLVEKVDLIDKF--EHPKTH 176
Cdd:CHL00192 583 EIYLFEINLDILQYSIQqnnlisYQPYSSYPKIIRDLSFIIK-KSISISKIKELIYQNGDNLLESITLFDYYkgKSIPNG 661

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 85719322  177 RTSHCYRITYRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR 218
Cdd:CHL00192 662 HTSLGLRLTFQSENKTLTNEEIDRIQQNLQKVLEKKLNAEIR 703
PLN02853 PLN02853
Probable phenylalanyl-tRNA synthetase alpha chain
 35-100 2.63e-04

Probable phenylalanyl-tRNA synthetase alpha chain


Pssm-ID: 215458 [Multi-domain]  Cd Length: 492  Bit Score: 41.20  E-value: 2.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85719322   35 YFPFTHPSfeMEInFR-----GEWLEVLGCGVMEQQLVNSAGAQDR---IGWafGLGLERLAMVLYDIPDIR-LF 100
Cdd:PLN02853 404 YNPYTEPS--MEI-FSyheglKKWVEVGNSGMFRPEMLLPMGLPEDvnvIAW--GLSLERPTMILYGIDNIRdLF 473
PTZ00326 PTZ00326
phenylalanyl-tRNA synthetase alpha chain; Provisional
 35-100 5.04e-04

phenylalanyl-tRNA synthetase alpha chain; Provisional


Pssm-ID: 240361 [Multi-domain]  Cd Length: 494  Bit Score: 40.34  E-value: 5.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85719322   35 YFPFTHPSfeMEInF-----RGEWLEVLGCGVMEQQLVNSAGAQDR---IGWafGLGLERLAMVLYDIPDIR-LF 100
Cdd:PTZ00326 419 FNPYTEPS--MEI-FgyhpgLKKWVEVGNSGIFRPEMLRPMGFPEDvtvIAW--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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