Summary: Hemolysin-type calcium-binding repeat (2 copies)
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Hemolysin-type calcium-binding repeat (2 copies) Provide feedback
No Pfam abstract.
Economou A, Hamilton WD, Johnston AW, Downie JA; , EMBO J 1990;9:349-354.: The Rhizobium nodulation gene nodO encodes a Ca2(+)-binding protein that is exported without N-terminal cleavage and is homologous to haemolysin and related proteins. PUBMED:2303029 EPMC:2303029
Baumann U, Wu S, Flaherty KM, McKay DB; , EMBO J 1993;12:3357-3364.: Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. PUBMED:8253063 EPMC:8253063
Chung YJ, Steen MT, Hansen JN; , J Bacteriol 1992;174:1417-1422.: The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein. PUBMED:1735728 EPMC:1735728
Internal database links
|Similarity to PfamA using HHSearch:||Peptidase_M10_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001343Gram-negative bacteria produce a number of proteins that are secreted into the growth medium by a mechanism that does not require a cleaved N-terminal signal sequence. These proteins, while having different functions, seem to share two properties: they bind calcium and they contain a multiple tandem repeat of a nonapeptide [PUBMED:2303029]. The nonapeptide is found in a group of bacterial exported proteins that includes haemolysin, cyclolysin, leukotoxin and metallopeptidases belonging to MEROPS peptidase family M10 (clan MA(M)), subfamily 10B (serralysin).
It has been suggested that the internally repeated domain of haemolysin may be involved in Ca-mediated binding to erythrocytes. It has been shown that such a domain is involved in the binding of calcium ions in a parallel beta roll structure [PUBMED:8253063].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||calcium ion binding (GO:0005509)|
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||305|
|Number in full:||35811|
|Average length of the domain:||17.60 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||19.13 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
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There are 2 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HemolysinCabind domain has been found. There are 173 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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