Summary: ScpA/B protein
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ScpA/B protein Provide feedback
ScpA and ScpB participate in chromosomal partition during cell division. It may act via the formation of a condensin-like complex containing smc that pull DNA away from mid-cell into both cell halves. These proteins are part of the Kleisin superfamily.
Schleiffer A, Kaitna S, Maurer-Stroh S, Glotzer M, Nasmyth K, Eisenhaber F; , Mol Cell 2003;11:571-575.: Kleisins: a superfamily of bacterial and eukaryotic SMC protein partners. PUBMED:12667442 EPMC:12667442
Internal database links
|Similarity to PfamA using HHSearch:||Rad21_Rec8|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003768
This family represents ScpA, which along with ScpB (INTERPRO) interacts with SMC in vivo forming a complex that is required for chromosome condensation and segregation [PUBMED:12065423, PUBMED:12897137]. The SMC-Scp complex appears to be similar to the MukB-MukE-Muk-F complex in Escherichia coli [PUBMED:10545099], where MukB (INTERPRO) is the homologue of SMC. ScpA and ScpB have little sequence similarity to MukE (INTERPRO) or MukF (INTERPRO), they are predicted to be structurally similar, being predominantly alpha-helical with coiled coil regions.
In general scpA and scpB form an operon in most bacterial genomes. Flanking genes are highly variable suggesting that the operon has moved throughout evolution. Bacteria containing an smc gene also contain scpA or scpB but not necessarily both. An exception is found in Deinococcus radiodurans, which contains scpB but neither smc nor scpA. In the archaea the gene order SMC-ScpA is conserved in nearly all species, as is the very short distance between the two genes, indicating co-transcription of the both in different archaeal genera and arguing that interaction of the gene products is not confined to the homologues in Bacillus subtilis. It would seem probable that, in light of all the studies, SMC, ScpA and ScpB proteins or homologues act together in chromosome condensation and segregation in all prokaryotes [PUBMED:12100548].
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The kleisin superfamily includes ScpA, Scc1, Rec8, and Barren . Scc1 interacts with SMC proteins through N- and C-terminal domains to form a ring-like structure .
The clan contains the following 2 members:Rad21_Rec8 ScpA_ScpB
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Curation and family details
|Author:||Mian N, Bateman A|
|Number in seed:||11|
|Number in full:||3012|
|Average length of the domain:||209.20 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||81.05 %|
|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:||9|
|Download:||download the raw HMM for this family|
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