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Links from Protein

Items: 17

1.

4Fe-4S dicluster-binding protein

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. (from Pfam)

GO Terms:
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2024-08-14
Family Accession:
NF026048.5
Method:
HMM
2.

4Fe-4S dicluster domain-containing protein

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024247.5
Method:
HMM
3.

Dihydroorotate dehydrogenase

GO Terms:
Cellular Component:
cytoplasm (GO:0005737)
Molecular Function:
oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627)
Date:
2024-08-14
Family Accession:
NF013355.5
Method:
HMM
4.

tRNA-dihydrouridine synthase

Members of this family catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 (Swiss:Q9HGN6) from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 (Swiss:P53720) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [1]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [1]. [1]. 12003496. A conserved family of Saccharomyces cerevisiae synthases effects. dihydrouridine modification of tRNA.. Xing F, Martzen MR, Phizicky EM;. RNA 2002;8:370-381. (from Pfam)

GO Terms:
Biological Process:
tRNA processing (GO:0008033)
Molecular Function:
tRNA dihydrouridine synthase activity (GO:0017150)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-08-14
Family Accession:
NF013380.5
Method:
HMM
5.

4Fe-4S binding protein

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012267.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
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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
Family Accession:
15.

dihydropyrimidine dehydrogenase subunit B

dihydropyrimidine dehydrogenase subunit B catalyzes the first step in pyrimidine degradation by conversion to their corresponding 5,6-dihydropyrimidines

Date:
2017-02-03
Family Accession:
11483255
Method:
Sparcle
16.

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA

NADH-dependent; catalyzes the conversion of pyrimidines to 5,6-dihydro compounds in pyrimidine degradation

Gene:
preA
GO Terms:
Biological Process:
thymine catabolic process (GO:0006210)
Biological Process:
uracil catabolic process (GO:0006212)
Molecular Function:
dihydropyrimidine dehydrogenase (NADP+) activity (GO:0017113)
Date:
2021-08-23
Family Accession:
NF006183.0
Method:
HMM
17.
new record, indexing in progress
Family Accession:
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