U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 19

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

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

Date:
2024-08-14
Family Accession:
NF024634.5
Method:
HMM
3.

4Fe-4S binding domain

This 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:
NF024246.5
Method:
HMM
4.

(Fe-S)-binding protein

This family includes a domain with four conserved cysteines that probably form an Fe-S redox cluster. (from Pfam)

GO Terms:
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2024-08-14
Family Accession:
NF015987.5
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
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.

electron transport complex subunit RsxB

electron transport complex subunit RsxB is required to maintain the reduced state of SoxR; probably transfers electron from NAD(P)H to SoxR

Date:
2023-03-08
Family Accession:
11480380
Method:
Sparcle
18.

electron transport complex subunit RsxB

Gene:
rsxB
GO Terms:
Molecular Function:
electron transfer activity (GO:0009055)
Biological Process:
electron transport chain (GO:0022900)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2021-08-24
Family Accession:
NF003475.0
Method:
HMM
19.

RnfABCDGE type electron transport complex subunit B

The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit.

GO Terms:
Molecular Function:
electron transfer activity (GO:0009055)
Biological Process:
electron transport chain (GO:0022900)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2021-09-20
Family Accession:
TIGR01944.1
Method:
HMM
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center