Summary: Tim44-like domain
Tim44-like domain Provide feedback
Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane . Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region . This family includes the C-terminal region of Tim44 that has been shown to form a stable proteolytic fragment in yeast. This region is also found in a set of smaller bacterial proteins. The molecular function of the bacterial members of this family is unknown but transport seems likely. The crystal structure of the C terminal of Tim44 has revealed a large hydrophobic pocket which might play an important role in interacting with the acyl chains of lipid molecules in the mitochondrial membrane .
Weiss C, Oppliger W, Vergeres G, Demel R, Jeno P, Horst M, de Kruijff B, Schatz G, Azem A; , Proc Natl Acad Sci U S A 1999;96:8890-8894.: Domain structure and lipid interaction of recombinant yeast Tim44. PUBMED:10430866 EPMC:10430866
Josyula R, Jin Z, McCombs D, DeLucas L, Sha B; , Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006;62:172-174.: Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p. PUBMED:16511294 EPMC:16511294
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007379
Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane [PUBMED:10430866]. Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region [PUBMED:10430866].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||mitochondrial inner membrane presequence translocase complex (GO:0005744)|
|Molecular function||P-P-bond-hydrolysis-driven protein transmembrane transporter activity (GO:0015450)|
|Biological process||intracellular protein transport (GO:0006886)|
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This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.
The clan contains the following 24 members:CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF4440 DUF4467 LEH Lumazine_bd Lumazine_bd_2 MBA1 MecA_N Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 Tim44 VirB8 WI12
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Curation and family details
|Seed source:||TIGRFAMs (release 2.0);|
|Author:||TIGRFAMs, Finn RD, Bateman A|
|Number in seed:||140|
|Number in full:||1637|
|Average length of the domain:||139.80 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||44.40 %|
|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:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Tim44 domain has been found. There are 4 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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