Summary: Mitochondrial inner-membrane-bound regulator
Mitochondrial inner-membrane-bound regulator Provide feedback
SLS is a fungal domain found bound to the mitochondrial inner-membrane . It reacts physically with fungal Kar2p to promote translocation across the endoplasmic-reticulum membrane. This action appeared to be mediated via the promotion of the Sec63p-mediated activation of Kar2p's ATPase activity. This indicates that the Sls1p protein is a GrpE-like protein in the endoplasmic reticulum. In S.cerevisiae the SLS1 gene (ScSLS1) is not essential but is also involved in ERAD and folding [2,3].
Rouillard JM, Dufour ME, Theunissen B, Mandart E, Dujardin G, Lacroute F;, Mol Gen Genet. 1996;252:700-708.: SLS1, a new Saccharomyces cerevisiae gene involved in mitochondrial metabolism, isolated as a syntheticlethal in association with an SSM4 deletion. PUBMED:8917313 EPMC:8917313
Bryan AC, Rodeheffer MS, Wearn CM, Shadel GS;, Genetics. 2002;160:75-82.: Sls1p is a membrane-bound regulator of transcription-coupled processes involved in Saccharomyces cerevisiae mitochondrial gene expression. PUBMED:11805046 EPMC:11805046
Kabani M, Beckerich JM, Gaillardin C;, Mol Cell Biol. 2000;20:6923-6934.: Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. PUBMED:10958688 EPMC:10958688
Internal database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR032741
Sls1 is a fungal mitochondrial membrane protein involved in mitochondrial metabolism [PUBMED:8917313]. It interacts physically with Kar2 to promote translocation across the endoplasmic-reticulum [PUBMED:10958688]. It may be part of a mitochondrial membrane-associated RNA-shuttling system, delivering NAM1-associated transcripts to the translation machinery [PUBMED:11805046].
|Cellular component||mitochondrial inner membrane (GO:0005743)|
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The KH domain is thought to be the second most prevalent RNA binding motif in proteins. The motif is characterised by a conserved GXXXGXXG in the middle of the domain. Structures of KH reveal that the KH domain is arranged as either a beta-alpha-alpha-beta-beta (mini-KH domain) or beta-alpha-alpha-beta-beta-alpha (maxi-KH domain). The secondary elements are separated by at least four loop segments. The second loop is located between beta-1 and al The KH domain can be found either as single or multiple copies. The KH domain usually binds RNA as a multimer.
The clan contains the following 11 members:DUF2096 DUF370 KH_1 KH_2 KH_4 KH_5 KH_6 KH_7 MOEP19 MRP-S24 SLS
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1679 (release 26.00|
|Author:||Wood V, Coggill P|
|Number in seed:||93|
|Number in full:||282|
|Average length of the domain:||204.70 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||24.05 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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