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Links from Protein

Items: 13

1.

SurA N-terminal domain-containing protein

This domain is found at the N-terminus of the chaperone SurA and related proteins such as PpiD and foldase PrsA [1,2]. It is a helical domain that together with the C-terminal, forms a domain containing substrate-binding sites [2,3]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that. facilitates folding of outer membrane porins.. Bitto E, McKay DB;. Structure. 2002;10:1489-1498.. [2]. 20970503. The crystal structure of the leptospiral hypothetical protein. LIC12922 reveals homology with the periplasmic chaperone SurA.. Giuseppe PO, Von Atzingen M, Nascimento AL, Zanchin NI,. Guimaraes BG;. J Struct Biol. 2011;173:312-322.. [3]. 32358557. Inter-domain dynamics in the chaperone SurA and multi-site. binding to its outer membrane protein clients.. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M,. Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R,. Ashcroft AE, Brockwell DJ, Radford SE;. Nat Commun. 2020;11:2155. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025010.5
Method:
HMM
2.

SurA N-terminal domain-containing protein

This domain is found at the N-terminal of the chaperone SurA and related proteins such as PpiD and foldase PrsA [1,2,3]. This is a helical domain that together with the C-terminal forms a domain containing substrate-binding sites [2,3]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that. facilitates folding of outer membrane porins.. Bitto E, McKay DB;. Structure. 2002;10:1489-1498.. [2]. 32358557. Inter-domain dynamics in the chaperone SurA and multi-site. binding to its outer membrane protein clients.. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M,. Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R,. Ashcroft AE, Brockwell DJ, Radford SE;. Nat Commun. 2020;11:2155.. [3]. 20970503. The crystal structure of the leptospiral hypothetical protein. LIC12922 reveals homology with the periplasmic chaperone SurA.. Giuseppe PO, Von Atzingen M, Nascimento AL, Zanchin NI,. Guimaraes BG;. J Struct Biol. 2011;173:312-322. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025009.5
Method:
HMM
3.

peptidyl-prolyl cis-trans isomerase

GO Terms:
Molecular Function:
peptidyl-prolyl cis-trans isomerase activity (GO:0003755)
Date:
2024-08-14
Family Accession:
NF024545.5
Method:
HMM
4.

peptidylprolyl isomerase

Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025002.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
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.

peptidylprolyl isomerase

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Date:
2023-09-19
Family Accession:
13837108
Method:
Sparcle
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