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Links from Protein

Items: 9

1.

RuBisCO accumulation factor 1

This is the C-terminal domain, also known as the beta domain, of Rubsico Assembly Chaperone protein (Raf1). Raf1 is necessary for rubisco to catalyze the rate-limiting step of carbon fixation through carboxylating the five-carbon sugar substrate ribulose-1,5-bisphosphate. The beta domains primary function is dimerization, which is critical for Raf1 to achieve the necessary avidity for complex formation with RbcL (the large complex sub-unbit of Rubsico) assembly intermediates. The beta domain is also involved, to a small extent, in binding to RbcL with use of the lustiness near the beta domain's conserved top surface [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)

Date:
2024-10-16
Family Accession:
NF037186.5
Method:
HMM
2.

Rubisco accumulation factor 1 helix turn helix domain

This is helix turn helix domain found in alpha helical region of Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)

Date:
2024-10-16
Family Accession:
NF037466.5
Method:
HMM
3.

RuBisCO accumulation factor 1

This is the N-terminal alpha helical domain found in Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)

Gene:
raf1
Date:
2024-10-16
Family Accession:
NF037465.5
Method:
HMM
4.
new record, indexing in progress
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5.
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7.
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8.
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9.
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