Protein Family Models

SpoIVA (Sporulation stage IV protein A) acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species [1,2]. This entry represents the C-terminal domain of SpoIVA, which plays a key role in targeting the protein to the outer forespore membrane, in particular the five hydrophobic residues at the extreme C-terminal are essential for this function [1,2]. Structure predictions suggest that it has three conserved alpha helices followed by a beta-hairpin [1]. [1]. 23267091. ATP hydrolysis by a domain related to translation factor GTPases. drives polymerization of a static bacterial morphogenetic. protein.. Castaing JP, Nagy A, Anantharaman V, Aravind L, Ramamurthi KS;. Proc Natl Acad Sci U S A. 2013;110:E151-E160.. [2]. 9922240. A four-dimensional view of assembly of a morphogenetic protein. during sporulation in Bacillus subtilis.. Price KD, Losick R;. J Bacteriol. 1999;181:781-790. (from Pfam)

Date:

2024-08-14

Cadherin_tail is the cytoplasmic domain at the C-terminus of cadherin proteins [1]. This domain binds p120 catenin, an action critical for the surface stability of cadherin-catenin cell-cell adhesion complexes [2]. [1]. 9865466. A common protocadherin tail: multiple protocadherins share the. same sequence in their cytoplasmic domains and are expressed in. different regions of brain.. Obata S, Sago H, Mori N, Davidson M, St John T, Suzuki ST;. Cell Adhes Commun. 1998;6:323-333.. [2]. 20371349. Dynamic and static interactions between p120 catenin and. E-cadherin regulate the stability of cell-cell adhesion.. Ishiyama N, Lee SH, Liu S, Li GY, Smith MJ, Reichardt LF, Ikura. M;. Cell. 2010;141:117-128. (from Pfam)

Date:

2024-08-14

This is the structural middle domain of Stage IV sporulation protein A (SpoIVA) which follows the ATPase domain and the predicted secondary structure suggests that it is composed of two symmetrical units containing alpha-helices and beta-strands [1]. SpoIVA acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species [1,2]. [1]. 23267091. ATP hydrolysis by a domain related to translation factor GTPases. drives polymerization of a static bacterial morphogenetic. protein.. Castaing JP, Nagy A, Anantharaman V, Aravind L, Ramamurthi KS;. Proc Natl Acad Sci U S A. 2013;110:E151-E160.. [2]. 9922240. A four-dimensional view of assembly of a morphogenetic protein. during sporulation in Bacillus subtilis.. Price KD, Losick R;. J Bacteriol. 1999;181:781-790. (from Pfam)

Date:

2024-08-14

This is the N-terminal domain found in archaeal actin homolog Ta0583 found in thermophilic archaeon Thermoplasma acidophilum. Structural analysis indicate that the fold of Ta0583 contains the core structure of actin indicating that it belongs to the actin/Hsp70 superfamily of ATPases. Furthermore,Ta0583 co-crystallised with ADP shows that the nucleotide binds at the interface between the subdomains of Ta0583 in a manner similar to that of actin. It has been suggested that Ta0583 might function in the cellular organisation of T. acidophilum [1]. Other family members include ParM another actin-like protein found in Staphylococcus aureus. Crystal structure co-ordinates revealed that this protein is most structurally related to the chromosomally encoded Actin-like proteins (Alp) Ta0583 from the archaea Thermoplasma acidophilum. Furthermore, biophysical analyses have suggested that ParM filaments undergo a treadmilling-like mechanism of motion in vitro similar to that of F-actin. The recruitment of ParM to the segrosome complex, was shown to be required for the conversion of static ParM filaments to a dynamic form proficient for active segregation and facilitated by the C-terminus of ParR [2] [1]. 16500678. Crystal structure of an archaeal actin homolog.. Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A;. J Mol Biol. 2006;358:145-156.. [2]. 27310470. Dynamic Filament Formation by a Divergent Bacterial Actin-Like. ParM Protein.. Brzoska AJ, Jensen SO, Barton DA, Davies DS, Overall RL, Skurray. RA, Firth N;. PLoS One. 2016;11:e0156944. (from Pfam)

Date:

2024-08-14

In the budding yeast, S. cerevisiae, Pil1 and another cytoplasmic protein, Lsp1, together form large immobile assemblies at the plasma membrane that mark sites for endocytosis, called eisosomes. Endocytosis functions to recycle plasma membrane components, to regulate cell-surface expression of signalling receptors and to internalise nutrients in all eukaryotic cells. [1]. 16496001. Eisosomes mark static sites of endocytosis.. Walther TC, Brickner JH, Aguilar PS, Bernales S, Pantoja C,. Walter P;. Nature. 2006;439:998-1003.. [2]. 21900489. The filament-forming protein Pil1 assembles linear eisosomes in. fission yeast.. Kabeche R, Baldissard S, Hammond J, Howard L, Moseley JB;. Mol Biol Cell. 2011;22:4059-4067. (from Pfam)

Date:

2024-08-14

Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops [1]. The function of the domain is to capture cholesterol and pass it to the associated START domain Pfam:PF01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localisation of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins [2]. [1]. 12393907. MENTHO, a MLN64 homologue devoid of the START domain.. Alpy F, Wendling C, Rio MC, Tomasetto C;. J Biol Chem. 2002;277:50780-50787.. [2]. 15718238. Functional characterization of the MENTAL domain.. Alpy F, Latchumanan VK, Kedinger V, Janoshazi A, Thiele C,. Wendling C, Rio MC, Tomasetto C;. J Biol Chem. 2005;280:17945-17952. (from Pfam)

Date:

2024-08-14

SpoIVA is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species [1,2,3]. This protein assembles into static polymers driven by ATP hydrolysis and is anchored to the outer forespore membrane through its C-terminal domain [3]. This entry represents the ATPase domain located at the N-terminal of SpoIVA [1,2]. It contains a conserved 'sensor' threonine residue that is involved in coordinating a Mg+2 ion [3]. [1]. 9922240. A four-dimensional view of assembly of a morphogenetic protein. during sporulation in Bacillus subtilis.. Price KD, Losick R;. J Bacteriol. 1999;181:781-790.. [2]. 17114257. Morphogenesis of the Bacillus anthracis spore.. Giorno R, Bozue J, Cote C, Wenzel T, Moody KS, Mallozzi M, Ryan. M, Wang R, Zielke R, Maddock JR, Friedlander A, Welkos S, Driks. A;. J Bacteriol. 2007;189:691-705.. [3]. 23267091. ATP hydrolysis by a domain related to translation factor GTPases. drives polymerization of a static bacterial morphogenetic. protein.. Castaing JP, Nagy A, Anantharaman V, Aravind L, Ramamurthi KS;. Proc Natl Acad Sci U S A. 2013;110:E151-E160. (from Pfam)

Date:

2024-08-14

This is a family of Gram-negative bacterial proteins that form part of the type VI pathogenicity secretion system (T6SS) , including TssF. TssF is homologues to phage tail proteins and is required for proper assembly of the Hcp tube (the T6SS inner tube) in bacteria [2]. T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex [3]. T6SSs contain 13 conserved components (TssA-TssM) which are thought to form the core apparatus and to enable effector proteins to be injected into target cells in a single cell-contact-dependent step. TssF one of the core components of T6SSs machinery, has been shown to be recruited by TssK into the membrane-associated T6SS complex, contributing to the dynamic mechanism of the system [4]. Furthermore, it has been reported to interact with TssG proteins stabilizing each other while making contact with TssE, TssK and VgrG as well as with tube and sheath components. Bioinformatic analysis suggest that TssF and TssG share similarities with the J and I proteins of the bacteriophage P2 baseplate respectively. Further experimental studies show that functional TssF and TssK proteins assemble into static foci near the cell envelope. Moreover, biochemical and cytological approaches provide support to the role of TssE, TssF, TssG, TssK and VgrG as T6SS baseplate components and to a sequential re. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

This family consists of several fungal-specific SUR7 proteins. Its activity regulates expression of RVS161, a homologue of human endophilin, suggesting a function for both in endocytosis [1,2]. The protein carries four transmembrane domains and is thus likely to act as an anchoring protein for the eisosome to the plasma membrane. Eisosomes are the immobile protein complexes, that include the proteins Pil1 and Lsp1, which co-localise with sites of protein and lipid endocytosis at the plasma membrane. SUR7 protein may play a role in sporulation [2]. This family also includes PalI which is part of a pH signal transduction cascade. Based on the similarity of PalI to the yeast Rim9 meiotic signal transduction component it has been suggested that PalI might be a membrane sensor for ambient pH [4]. [1]. 9219339. Cloning of the multicopy suppressor gene SUR7: evidence for a. functional relationship between the yeast actin-binding protein. Rvs167 and a putative membranous protein.. Sivadon P, Peypouquet MF, Doignon F, Aigle M, Crouzet M;. Yeast 1997;13:747-761.. [2]. 11784867. The Sur7p family defines novel cortical domains in Saccharomyces. cerevisiae, affects sphingolipid metabolism, and is involved in. sporulation.. Young ME, Karpova TS, Brugger B, Moschenross DM, Wang GK,. Schneiter R, Wieland FT, Cooper JA;. Mol Cell Biol 2002;22:927-934.. [3]. 16496001. Eisosomes mark static sites of endocytosis.. Walther TC, Brickner JH, Aguilar PS, Bernales S, Pantoja C,. Walter P;. Nature. 2006;439:998-1003.. [4]. 9791171. Putative membrane components of signal transduction pathways for. ambient pH regulation in Aspergillus and meiosis i. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14