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Links from Protein

Items: 15

1.

winged helix-turn-helix transcriptional regulator

Date:
2024-08-14
Family Accession:
NF024804.5
Method:
HMM
2.

helix-turn-helix domain-containing protein

This family represents a crp-like helix-turn-helix domain that is likely to bind DNA. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Date:
2024-08-14
Family Accession:
NF024934.5
Method:
HMM
3.

MarR family transcriptional regulator

The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds [1]. The structure of MarR is known [2] and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif. [1]. 9068629. The Salmonella typhimurium mar locus: molecular and genetic analyses and assessment of its role in virulence. Sulavik MC, Dazer M, Miller PF;. J Bacteriol 1997;179:1857-1866. [2]. 11473263. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Alekshun MN, Levy SB, Mealy TR, Seaton BA, Head JF;. Nat Struct Biol 2001;8:710-714. (from Pfam)

GO Terms:
Molecular Function:
DNA-binding transcription factor activity (GO:0003700)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Date:
2024-10-16
Family Accession:
NF024212.5
Method:
HMM
4.

DUF120 domain-containing protein

This domain is a CTP-dependent riboflavin kinase (RFK), found in archaea, that catalyses the phosphorylation of riboflavin to form flavin mononucleotide in riboflavin biosynthesis EC:2.7.1.26. Its structure resembles a RIFT barrel, structurally similar to but topologically distinct from bacterial and eukaryotic examples. The N-terminal is a winged helix-turn-helix DNA-binding domain, and the C-terminal half is most similar in sequence to a group of cradle-loop barrels. Swiss:O28174 has this domain attached to Pfam:PF00325. [1]. 18073108. A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels. Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M;. Structure. 2007;15:1577-1590. (from Pfam)

GO Terms:
Molecular Function:
phosphotransferase activity, alcohol group as acceptor (GO:0016773)
Date:
2024-10-16
Family Accession:
NF014084.5
Method:
HMM
5.
new record, indexing in progress
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6.
new record, indexing in progress
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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
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15.

CTP-dependent riboflavin kinase

CTP-dependent riboflavin kinase catalyzes the phosphorylation of riboflavin to form flavin mononucleotide in riboflavin biosynthesis

Date:
2018-06-28
Family Accession:
11442523
Method:
Sparcle
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