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Conserved domains on  [gi|193209162|ref|NP_001123055|]
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FDX-ACB domain-containing protein [Caenorhabditis elegans]

Protein Classification

FDX-ACB domain-containing protein( domain architecture ID 10658126)

FDX-ACB domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 3-74 7.89e-18

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: 70.15  E-value: 7.89e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193209162    3 SDVYDTIRTVGGELVEQVKLTDE-FENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:smart00896 21 AELLDAIREAGGDLLEDVRLFDVyEGGIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDKIVAALEKKFGAELR 93
 
Name Accession Description Interval E-value
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 3-74 7.89e-18

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: 70.15  E-value: 7.89e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193209162    3 SDVYDTIRTVGGELVEQVKLTDE-FENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:smart00896 21 AELLDAIREAGGDLLEDVRLFDVyEGGIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDKIVAALEKKFGAELR 93
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 3-73 1.14e-16

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: 72.03  E-value: 1.14e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193209162    3 SDVYDTIRTVGGELVEQVKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTL 73
Cdd:TIGR00469 390 NDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVEI 460
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 4-74 1.39e-16

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 71.72  E-value: 1.39e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193209162   4 DVYDTIRTVGGELVEQVKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:PLN02788 332 NLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 3-74 2.70e-13

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: 58.65  E-value: 2.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209162   3 SDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:pfam03147 21 ADILKAIREAGGELLESVELFDvyRGEKIPEGKKSLAFRLTFQSPERTLTDEEVNAIIEKIVEALEKKFGAELR 94
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 3-74 2.66e-10

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: 54.02  E-value: 2.66e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209162   3 SDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:COG0072  719 ADVLDAIRKAAGKLLEDVRLFDvyEGKGVPEGKKSLAFSLTLQDPDRTLTDEEIDAAMDKIVAALEKKFGAELR 792
 
Name Accession Description Interval E-value
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 3-74 7.89e-18

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: 70.15  E-value: 7.89e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193209162    3 SDVYDTIRTVGGELVEQVKLTDE-FENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:smart00896 21 AELLDAIREAGGDLLEDVRLFDVyEGGIPEGKKSLAYRLTYQSPDRTLTDEEVNAIHDKIVAALEKKFGAELR 93
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 3-73 1.14e-16

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: 72.03  E-value: 1.14e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193209162    3 SDVYDTIRTVGGELVEQVKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTL 73
Cdd:TIGR00469 390 NDFMDIIRNIAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDMIASALVDEFNVEI 460
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 4-74 1.39e-16

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 71.72  E-value: 1.39e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193209162   4 DVYDTIRTVGGELVEQVKLTDEFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:PLN02788 332 NLCEVVRGIAGDLVEEVKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 3-74 2.70e-13

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: 58.65  E-value: 2.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209162   3 SDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:pfam03147 21 ADILKAIREAGGELLESVELFDvyRGEKIPEGKKSLAFRLTFQSPERTLTDEEVNAIIEKIVEALEKKFGAELR 94
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 3-74 4.97e-12

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 59.03  E-value: 4.97e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209162   3 SDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:PRK00629 717 ADILKAIKKAGGKLLESVELFDvyEGKGIGEGKKSLAFRLTFQDPDRTLTDEEINAAMDKIVAALEEKFGAELR 790
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 3-74 2.66e-10

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: 54.02  E-value: 2.66e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193209162   3 SDVYDTIRTVGGELVEQVKLTD--EFENKKKEKKSQTYRIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:COG0072  719 ADVLDAIRKAAGKLLEDVRLFDvyEGKGVPEGKKSLAFSLTLQDPDRTLTDEEIDAAMDKIVAALEKKFGAELR 792
syfB CHL00192
phenylalanyl-tRNA synthetase beta chain; Provisional
 39-74 6.16e-03

phenylalanyl-tRNA synthetase beta chain; Provisional


Pssm-ID: 214391 [Multi-domain]  Cd Length: 704  Bit Score: 33.14  E-value: 6.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 193209162  39 RIVYRSHERALTKEEVNVIHKQIEQSLASSFGVTLR 74
Cdd:CHL00192 668 RLTFQSENKTLTNEEIDRIQQNLQKVLEKKLNAEIR 703
 
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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