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Links from Protein

Items: 1 to 20 of 54

1.

Helix-turn-helix domain

The TyrR protein of Haemophilus influenzae is a 36-kD transcription factor whose major function is to control the expression of genes important in the biosynthesis and transport of aromatic amino acids [1]. This entry represents the C-terminal helix-turn-helix DNA-binding domain of TyrR and related proteins. [1]. 11344327. Solution structure of the DNA-binding domain of the TyrR protein. of Haemophilus influenzae.. Wang Y, Zhao S, Somerville RL, Jardetzky O;. Protein Sci. 2001;10:592-598. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Date:
2024-08-14
Family Accession:
NF036547.5
Method:
HMM
2.

Sigma-54 interaction domain

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Molecular Function:
transcription factor binding (GO:0008134)
Date:
2024-08-14
Family Accession:
NF025885.5
Method:
HMM
3.

PAS domain-containing protein

PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [1]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognises oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 10357859. PAS domains: internal sensors of oxygen, redox potential, and. light.. Taylor BL, Zhulin IB;. Microbiol Mol Biol Rev. 1999;63:479-506. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024586.5
Method:
HMM
4.

PAS domain-containing protein

This domain is found in many signalling proteins in which it functions as a sensor domain. It recognises FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). (from Pfam)

Date:
2024-08-14
Family Accession:
NF024818.5
Method:
HMM
5.

AAA family ATPase

This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function.. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650.. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the. assembly, operation, and disassembly of protein complexes.. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
ATP hydrolysis activity (GO:0016887)
Date:
2024-08-14
Family Accession:
NF019348.5
Method:
HMM
6.

sigma 54-interacting transcriptional regulator

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Molecular Function:
transcription factor binding (GO:0008134)
Date:
2024-08-14
Family Accession:
NF012385.5
Method:
HMM
7.

HPr family phosphocarrier protein

Date:
2024-08-14
Family Accession:
NF012599.5
Method:
HMM
8.

PAS domain-containing protein

The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [4]. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 9301332. PAS domain S-boxes in archaea, bacteria and sensors for oxygen. and redox.. Zhulin IB, Taylor BL, Dixon R;. Trends Biochem Sci 1997;22:331-333.. [2]. 7756254. 1.4 A structure of photoactive yellow protein, a cytosolic. photoreceptor: unusual fold, active site, and chromophore.. Borgstahl GE, Williams DR, Getzoff ED;. Biochemistry 1995;34:6278-6287.. [3]. 9382818. PAS: a multifunctional domain family comes to light.. Ponting CP, Aravind L;. Curr Biol 1997;7:674-677.. [4]. 15009198. The PAS fold: a redefination of the PAS domain based upon. structural prediction.. Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J;. Eur J Biochem 2004;271:1198-1208. (from Pfam)

GO Terms:
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Date:
2024-08-14
Family Accession:
NF013179.5
Method:
HMM
9.
new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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20.
new record, indexing in progress
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