U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 16

1.

carbohydrate-binding domain-containing protein

The DUF5010 C-terminal domain is a putative carbohydrate-binding domain.

Date:
2024-10-16
Family Accession:
NF036710.5
Method:
HMM
2.

family 43 glycosylhydrolase

The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller [1]. [1]. 12198486. Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nurizzo D, Turkenburg JP, Charnock SJ, Roberts SM, Dodson EJ, McKie VA, Taylor EJ, Gilbert HJ, Davies GJ;. Nat Struct Biol 2002;9:665-668. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Biological Process:
carbohydrate metabolic process (GO:0005975)
Date:
2024-10-16
Family Accession:
NF016497.5
Method:
HMM
3.

carbohydrate-binding protein

GO Terms:
Molecular Function:
carbohydrate binding (GO:0030246)
Date:
2024-08-14
Family Accession:
NF015387.5
Method:
HMM
4.

Glycosyl hydrolases family 32 N-terminal domain

This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure [1]. [1]. 14973124. The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M;. J Biol Chem 2004;279:18903-18910. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012475.5
Method:
HMM
5.

dockerin type I domain-containing protein

The dockerin repeat is the binding partner of the cohesin domain Pfam:PF00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome [1]. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium [2]. This family contains two copies of the repeat. [1]. 10390637. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides [In Process Citation]. Shoham Y, Lamed R, Bayer EA;. Trends Microbiol 1999;7:275-281. [2]. 10898940. Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy. Lytle BL, Volkman BF, Westler WM, Wu JH;. Arch Biochem Biophys 2000;379:237-244. (from Pfam)

GO Terms:
Biological Process:
polysaccharide catabolic process (GO:0000272)
Molecular Function:
hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Date:
2024-10-16
Family Accession:
NF012622.5
Method:
HMM
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.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.

glycoside hydrolase family 43 protein

glycoside hydrolase family 43 protein containing a family 6 carbohydrate binding module (CBM6), similar to Talaromyces purpureogenus bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (ABF3)

Date:
2019-03-21
Family Accession:
13035779
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center