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Links from Protein

Items: 12

1.

M10 family metallopeptidase C-terminal domain-containing protein

Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain Pfam:PF00353. (from Pfam)

GO Terms:
Molecular Function:
calcium ion binding (GO:0005509)
Cellular Component:
extracellular space (GO:0005615)
Date:
2024-08-14
Family Accession:
NF020137.5
Method:
HMM
2.

calcium-binding protein

This family consists of a number of bacteria specific domains which are found in haemolysin-type calcium binding proteins. This family is found in conjunction with Pfam:PF00353 and is often found in multiple copies. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018319.5
Method:
HMM
3.

putative Ig domain-containing protein

This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (Pfam:PF02494) and (Pfam:PF00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (Pfam:PF02639) and (Pfam:PF02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei ([1]). [1]. 12606174. Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei. Bentley SD, Maiwald M, Murphy LD, Pallen MJ, Yeats CA, Dover LG, Norbertczak HT, Besra GS, Quail MA, Harris DE, von Herbay A, Goble A, Rutter S, Squares R, Squares S, Barrell BG, Parkhill J, Relman DA;. Lancet 2003;361:637-644. (from Pfam)

Date:
2024-10-16
Family Accession:
NF017183.5
Method:
HMM
4.

RTX calcium-binding repeat protein

GO Terms:
Molecular Function:
calcium ion binding (GO:0005509)
Date:
2024-08-14
Family Accession:
NF012573.5
Method:
HMM
5.

matrixin family metalloprotease

The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. [1]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. [2]. 7656014. The NMR structure of the inhibited catalytic domain of human stromelysin-1. Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Esser CK, Hagmann WK, Springer JP, et al;. Nat Struct Biol 1994;1:111-118. (from Pfam)

GO Terms:
Molecular Function:
metalloendopeptidase activity (GO:0004222)
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
zinc ion binding (GO:0008270)
Cellular Component:
extracellular matrix (GO:0031012)
Date:
2024-10-16
Family Accession:
NF012630.5
Method:
HMM
6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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