Protein Family Models

This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins. Paper describing PDB structure 3h94. This domain is unresolved. [1]. 19695261. Crystal structure of the membrane fusion protein CusB from Escherichia coli. Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK, Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW;. J Mol Biol. 2009;393:342-355. Paper describing PDB structure 3ne5. This domain is unresolved. [2]. 21350490. Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, Yu EW;. Nature. 2011;470:558-562. Paper describing PDB structure 3rfu. This domain is unresolved. [3]. 21716286. Crystal structure of a copper-transporting PIB-type ATPase. Gourdon P, Liu XY, Skjorringe T, Morth JP, Moller LB, Pedersen BP, Nissen P;. Nature. 2011;475:59-64. Paper describing PDB structure 4bbj. This domain is unresolved. [4]. 24317491. Copper-transporting P-type ATPases use a unique ion-release pathway. Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P;. Nat Struct Mol Biol. 2014;21:43-48. (from Pfam)

Date:

2024-10-16

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

Date:

2024-08-14

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:

2024-10-16

copper-transporting P-type ATPase couples the hydrolysis of ATP with the export of Cu(+) or Cu(2+); P-type ATPases are distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

Date:

2024-09-10

Members of this P-type ATPase family apparently include both Cu(+) (EC 3.6.3.54) and Cu(2+) (EC 3.6.3.4) copper efflux transporters.

Date:

2021-05-12

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 HMM encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.

Date:

2024-06-04