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Links from Protein

Items: 9

1.

right-handed parallel beta-helix repeat-containing protein

This region contains a parallel beta helix region that shares some similarity with Pectate lyases. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024627.5
Method:
HMM
2.

NosD domain-containing protein

NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ) [1]. This region forms a parallel beta helix domain. [1]. 8626275. Identification and analysis of the dissimilatory nitrous oxide reduction genes, nosRZDFY, of Rhizobium meliloti. Holloway P, McCormick W, Watson RJ, Chan YK;. J Bacteriol 1996;178:1505-1514. (from Pfam)

Date:
2024-10-16
Family Accession:
NF016906.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

nitrous oxide reductase family maturation protein NosD

nitrous oxide reductase family maturation protein NosD is required for the assembly of the copper chromophores of nitrous oxide reductase

Date:
2020-03-09
Family Accession:
11499885
Method:
Sparcle
8.

nitrous oxide reductase family maturation protein NosD

Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.

Gene:
nosD
GO Terms:
Biological Process:
nitrogen cycle metabolic process (GO:0071941)
Date:
2021-05-12
Family Accession:
TIGR04247.1
Method:
HMM
9.

parallel beta-helix repeat protein

This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.

Date:
2020-10-23
Family Accession:
TIGR03804.1
Method:
HMM
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