Protein Family Models

This entry represents the region found N-terminal to the neuraminidase domain in the pore forming ABC toxins [1]. Paper describing PDB structure 6ogd. [1]. 31028251. Cryo-EM structures of the pore-forming A subunit from the. Yersinia entomophaga ABC toxin.. Piper SJ, Brillault L, Rothnagel R, Croll TI, Box JK, Chassagnon. I, Scherer S, Goldie KN, Jones SA, Schepers F, Hartley-Tassell. L, Ve T, Busby JN, Dalziel JE, Lott JS, Hankamer B, Stahlberg H,. Hurst MRH, Landsberg MJ;. Nat Commun. 2019;10:1952. (from Pfam)

Date:

2024-08-14

Cysteine-rich motor neuron 1 protein (CRIM1) interacts with growth factors implicated in motor neuron differentiation and survival, playing a role in central nervous system development. It is upregulated in endothelial cells during tube formation. CRIM1 also modulates BMP activity, which affects its processing and delivery to the cell surface. This is CRIM1 C-terminal domain containing the transmembrane region [1,2]. [1]. 12805376. CRIM1 regulates the rate of processing and delivery of bone. morphogenetic proteins to the cell surface.. Wilkinson L, Kolle G, Wen D, Piper M, Scott J, Little M;. J Biol Chem. 2003;278:34181-34188.. [2]. 12464430. CRIM1 is involved in endothelial cell capillary formation in. vitro and is expressed in blood vessels in vivo.. Glienke J, Sturz A, Menrad A, Thierauch KH;. Mech Dev. 2002;119:165-175. (from Pfam)

Date:

2024-08-14

This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1. [1]. 20838651. A global census of fission yeast deubiquitinating enzyme. localization and interaction networks reveals distinct. compartmentalization profiles and overlapping functions in. endocytosis and polarity.. Kouranti I, McLean JR, Feoktistova A, Liang P, Johnson AE,. Roberts-Galbraith RH, Gould KL;. PLoS Biol. 2010; [Epub ahead of print]. [2]. 17079730. Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting. complex, associates with ubiquitin peptidases and a ligase to. control sorting efficiency into multivesicular bodies.. Ren J, Kee Y, Huibregtse JM, Piper RC;. Mol Biol Cell. 2007;18:324-335. (from Pfam)

Date:

2024-08-14

Nse4 is the kleisin component of the Smc5/6 DNA repair complex. It bridges the heads of Smc5 and Smc6 [1,2,3,4]. This is the C-terminal domain of Nse4 that interacts with the head domain of Smc5 [4]. [1]. 15752197. Qri2/Nse4, a component of the essential Smc5/6 DNA repair. complex.. Hu B, Liao C, Millson SH, Mollapour M, Prodromou C, Pearl LH,. Piper PW, Panaretou B;. Mol Microbiol. 2005;55:1735-1750.. [2]. 15331764. Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3,. play a crucial role in meiosis.. Pebernard S, McDonald WH, Pavlova Y, Yates JR 3rd, Boddy MN;. Mol Biol Cell. 2004;15:4866-4876.. [3]. 22536443. Analysis of the Nse3/MAGE-binding domain of the Nse4/EID family. proteins.. Guerineau M, Kriz Z, Kozakova L, Bednarova K, Janos P, Palecek. J;. PLoS One. 2012;7:e35813.. [4]. 17005570. The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6. heads by the KLEISIN, Nse4, and non-Kleisin subunits.. Palecek J, Vidot S, Feng M, Doherty AJ, Lehmann AR;. J Biol Chem. 2006;281:36952-36959. (from Pfam)

Date:

2024-08-14

This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38, Swiss:O95433). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity [1]. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress [2]. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport [3]. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family) [4]. [1]. 12604615. Aha1 binds to the middle domain of Hsp90, contributes to client. protein activation and stimulates the ATPase activity of the. molecular chaperone.. Lotz GP, Lin H, Harst A, Obermann WM;. J Biol Chem 2003;0:0-0.. [2]. 12504007. Activation of the ATPase activity of hsp90 by the. stress-regulated cochaperone aha1.. Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh. S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R,. Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C;. Mol Cell 2002;10:1307-1318.. [3]. 1155476. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity [1]. [1]. 15039704. Structural basis for recruitment of the ATPase activator Aha1 to. the Hsp90 chaperone machinery.. Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic. I, Panaretou B, Piper PW, Pearl LH;. EMBO J. 2004;23:1402-1410. (from Pfam)

Date:

2024-08-14

This family consists of several Tenuivirus and Phlebovirus nucleocapsid proteins [1,2]. These are ssRNA viruses. In crystal structures the nucleocapsid protein from the Rift Valley fever virus (RVFV) displays a ring-shaped oligomeric assembly [3,4]. Electron microscopy (EM) also demonstrates that, in complex with RNA, the RVFV nucleocapsid protein forms rings in solution [4]. [1]. 2024478. Nucleotide sequence and RNA hybridization analyses reveal an. ambisense coding strategy for maize stripe virus RNA3.. Huiet L, Klaassen V, Tsai JH, Falk BW;. Virology 1991;182:47-53.. [2]. 1846496. Sequences and coding strategies of the S RNAs of Toscana and. Rift Valley fever viruses compared to those of Punta Toro,. Sicilian Sandfly fever, and Uukuniemi viruses.. Giorgi C, Accardi L, Nicoletti L, Gro MC, Takehara K, Hilditch. C, Morikawa S, Bishop DH;. Virology 1991;180:738-753.. [3]. 20547879. Structure of the Rift Valley fever virus nucleocapsid protein. reveals another architecture for RNA encapsidation.. Raymond DD, Piper ME, Gerrard SR, Smith JL;. Proc Natl Acad Sci U S A. 2010;107:11769-11774.. [4]. 21589902. The hexamer structure of Rift Valley fever virus nucleoprotein. suggests a mechanism for its assembly into ribonucleoprotein. complexes.. Ferron F, Li Z, Danek EI, Luo D, Wong Y, Coutard B, Lantez V,. Charrel R, Canard B, Walz T, Lescar J;. PLoS Pathog. 2011;7:e1002030. (from Pfam)

Date:

2024-08-14

This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119. [1]. 1646964. Crystal structure of an N-terminal fragment of the DNA gyrase B. protein.. Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G;. Nature 1991;351:624-629.. [2]. 10734094. Dimerization of Escherichia coli DNA-gyrase B provides a. structural mechanism for activating the ATPase catalytic center.. Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, Oudet. P, Moras D. J Biol Chem 2000;275:9468-9475.. [3]. 10575351. Isoleucine 10 is essential for DNA gyrase B function in. Escherichia coli.. Brino L, Bronner C, Oudet P, Mousli M. Biochimie 1999;81:973-980.. [4]. 9817206. NMR structure of the histidine kinase domain of the E. coli. osmosensor EnvZ.. Tanaka T, Saha SK, Tomomori C, Ishima R, Liu D, Tong KI, Park H,. Dutta R, Qin L, Swindells MB, Yamazaki T, Ono AM, Kainosho M,. Inouye M, Ikura M. Nature 1998;396:88-92.. [5]. 9657678. Identification of a residue involved in transition-state. stabilization in the ATPase reaction of DNA gyrase.. Smith CV, Maxwell A. Biochemistry 1998;37:9658-9667.. [6]. 9230303. Identification and structural characterization of the. ATP/ADP-binding site in the Hsp90 molecular chaperone.. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Cell 1997;90:65-75. (from Pfam)

Date:

2024-08-14