Protein Family Models

This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases [1-2]. [1]. 21653810. Physiological adaptation of an Antarctic Na+/K+-ATPase to the. cold.. Galarza-Munoz G, Soto-Morales SI, Holmgren M, Rosenthal JJ;. J Exp Biol. 2011;214:2164-2174.. [2]. 1384045. Higher plant Ca(2+)-ATPase: primary structure and regulation of. mRNA abundance by salt.. Wimmers LE, Ewing NN, Bennett AB;. Proc Natl Acad Sci U S A. 1992;89:9205-9209. (from Pfam)

Date:

2024-08-14

This family contains haloacid dehalogenase-like hydrolase enzymes. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. (from Pfam)

Date:

2024-08-14

Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices. (from Pfam)

Date:

2024-08-14

This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2]. [1]. 8702766. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas. sp. YL. An alpha/beta hydrolase structure that is different from. the alpha/beta hydrolase fold.. Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K;. J Biol Chem 1996;271:20322-20330.. [2]. 20485265. A mitochondrial phosphatase required for cardiolipin. biosynthesis: the PGP phosphatase Gep4.. Osman C, Haag M, Wieland FT, Brugger B, Langer T;. EMBO J. 2010;29:1976-1987 (from Pfam)

Date:

2024-08-14

The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. P-type ATPases typically consist of only a single subunit encompassing the ATPase and ion translocation pathway, but these functions are split in some systems. The catalytic core of a P-type ATPase is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.

Date:

2022-10-11

This model describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes [1], out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes [2]. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping but not redundant functions. Accordingly, there are no human diseases linked to PMCA defects, although alterations of PMCA function do elicit physiological effects [3]. The calcium P-type ATPases have been characterized as Type IIB based on a phylogenetic analysis which distinguishes this group from the Type IIA SERCA calcium pump [4]. A separate analysis divides Type IIA into sub-types (SERCA and PMR1) [5] which are modelled by two corresponding HMMs (TIGR01116 and TIGR01522). This HMM is well separated from those.

Date:

2024-05-30