Protein Family Models

AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes [1]. AKAP7_NLS carries the nuclear localisation signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein [2]. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains Pfam:PF02834. Presumably this domain carried out some as yet unknown enzymatic function. [1]. 12804576. AKAP7gamma is a nuclear RI-binding AKAP. Brown RL, August SL, Williams CJ, Moss SB;. Biochem Biophys Res Commun. 2003;306:394-401. [2]. 16483255. High-affinity AKAP7delta-protein kinase A interaction yields novel protein kinase A-anchoring disruptor peptides. Hundsrucker C, Krause G, Beyermann M, Prinz A, Zimmermann B, Diekmann O, Lorenz D, Stefan E, Nedvetsky P, Dathe M, Christian F, McSorley T, Krause E, McConnachie G, Herberg FW, Scott JD, Rosenthal W, Klussmann E;. Biochem J. 2006;396:297-306. (from Pfam)

Date:

2024-10-16

This family contains proteins related to Pfam:PF02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity. (from Pfam)

Date:

2024-08-14

Members of this family are bacterial and archaeal RNA ligases that are able to ligate tRNA half molecules containing 2',3'-cyclic phosphate and 5' hydroxyl termini to products containing the 2',5' phosphodiester linkage. Each member of this family contains an internal duplication, each of which contains an HXTX motif that defines the family. The structure of a related protein is known [1]. They belong to the 2H phosphoesterase superfamily [2]. They share a common active site, characterised by two conserved histidines, with vertebrate myelin-associated 2',3' phosphodiesterases, plant Arabidopsis thaliana CPDases and several several bacteria and virus proteins. [1]. 11080166. Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction. Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A;. EMBO J 2000;19:6207-6217. [2]. 12466548. Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Mazumder R, Iyer LM, Vasudevan S, Aravind L;. Nucleic Acids Res 2002;30:5229-5243. (from Pfam)

Date:

2024-10-16

2'-5' RNA ligase family protein such as RNA 2',3'-cyclic phosphodiesterase hydrolyzes RNA 2',3'-cyclic phosphodiester to the RNA 2'-phosphomonoester

Date:

2018-01-17

ThpR (two-histidine 2',3'-cyclic phosphodiesterase acting on RNA) was formerly named LigT, and called a 2'-5' RNA ligase, based on its ability to perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The more recent characterization in PMID:25239919 clarifies the likely biological role.

Gene:

thpR

Date:

2022-03-28