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Links from Protein

Items: 18

1.

Phenylalanyl tRNA synthetase beta chain CLM domain

This domain corresponds to the catalytic like domain (CLM) in the beta chain of phe tRNA synthetase [1]. [1]. 21082706. Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. Mermershtain I, Finarov I, Klipcan L, Kessler N, Rozenberg H, Safro MG;. Protein Sci. 2011;20:160-167. (from Pfam)

Date:
2024-10-16
Family Accession:
NF036799.5
Method:
HMM
2.

tRNA synthetase B5 domain

This domain is found in phenylalanine-tRNA synthetase beta subunits. [1]. 10447505. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Wolf YI, Aravind L, Grishin NV, Koonin EV;. Genome Res 1999;9:689-710. (from Pfam)

GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
RNA binding (GO:0003723)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
phenylalanyl-tRNA aminoacylation (GO:0006432)
Date:
2024-10-16
Family Accession:
NF015449.5
Method:
HMM
3.

phenylalanine--tRNA ligase beta subunit-related protein

This domain is found in tRNA synthetase beta subunits as well as in some non tRNA synthetase proteins. [1]. 10447505. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Wolf YI, Aravind L, Grishin NV, Koonin EV;. Genome Res 1999;9:689-710. (from Pfam)

GO Terms:
Molecular Function:
RNA binding (GO:0003723)
Molecular Function:
phenylalanine-tRNA ligase activity (GO:0004826)
Date:
2024-10-16
Family Accession:
NF015448.5
Method:
HMM
4.

Ferredoxin-fold anticodon binding domain

This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold [1,2]. [1]. 10447505. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Wolf YI, Aravind L, Grishin NV, Koonin EV;. Genome Res 1999;9:689-710. [2]. 9016717. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M;. Structure 1997;5:59-68. (from Pfam)

Date:
2024-10-16
Family Accession:
NF015129.5
Method:
HMM
5.

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. (from Pfam)

GO Terms:
Molecular Function:
tRNA binding (GO:0000049)
Molecular Function:
aminoacyl-tRNA ligase activity (GO:0004812)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
tRNA aminoacylation (GO:0043039)
Date:
2024-08-14
Family Accession:
NF013568.5
Method:
HMM
6.
new record, indexing in progress
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7.
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.

phenylalanine--tRNA ligase subunit beta

phenylalanine--tRNA ligase subunit beta is part of the enzyme complex that catalyzes the attachment of phenylalanine to tRNA(Phe)

Date:
2024-04-09
Family Accession:
11479069
Method:
Sparcle
18.

phenylalanine--tRNA ligase subunit beta

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 HMM 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, however, so this HMM was built in fragment mode

Gene:
pheT
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
phenylalanine-tRNA ligase activity (GO:0004826)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
phenylalanyl-tRNA aminoacylation (GO:0006432)
Date:
2024-05-15
Family Accession:
TIGR00472.1
Method:
HMM
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