PROSITE documentation PDOC51881Obg C-terminal (OCT) domain profile
Obg subfamily proteins (also known as ObgE, YhbZ and CgtA) are conserved P-loop GTPases, that are involved in a wide range of cellular processes, including sporulation, cellular differentiation, ribosome assembly, DNA replication, chromosome segregation, and stringent response in eubacteria and plant chloroplasts. Obg subfamily proteins have three domains: the Obg fold, the G domain (see <PDOC51710>), and the Obg C-terminal (OCT) domain. A potential role of the OCT domain in the regulation of the nucleotide-binding state has been suggested [1,2,3].
The OCT domain structure contains a four-stranded β sheet and three α helices flanked by an additional β strand (see <PDB:1UDX>) [1].
The profile we developed covers the entire OCT domain.
Last update:December 2018 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kukimoto-Niino M. Murayama K. Inoue M. Terada T. Tame J.R.H. Kuramitsu S. Shirouzu M. Yokoyama S. |
| Title | Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8. | |
| Source | J. Mol. Biol. 337:761-770(2004). | |
| PubMed ID | 15019792 | |
| DOI | 10.1016/j.jmb.2004.01.047 |
| 2 | Authors | Bang W.Y. Chen J. Jeong I.S. Kim S.W. Kim C.W. Jung H.S. Lee K.H. Kweon H.-S. Yoko I. Shiina T. Bahk J.D. |
| Title | Functional characterization of ObgC in ribosome biogenesis during chloroplast development. | |
| Source | Plant. J. 71:122-134(2012). | |
| PubMed ID | 22380942 | |
| DOI | 10.1111/j.1365-313X.2012.04976.x |
| 3 | Authors | Bang W.Y. Hata A. Jeong I.S. Umeda T. Masuda T. Chen J. Yoko I. Suwastika I.N. Kim D.W. Im C.H. Lee B.H. Lee Y. Lee K.W. Shiina T. Bahk J.D. |
| Title | AtObgC, a plant ortholog of bacterial Obg, is a chloroplast-targeting GTPase essential for early embryogenesis. | |
| Source | Plant Mol. Biol. 71:379-390(2009). | |
| PubMed ID | 19636801 | |
| DOI | 10.1007/s11103-009-9529-3 |
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