home *** CD-ROM | disk | FTP | other *** search
- ************************
- * HIT family signature *
- ************************
-
- Recently a family of small proteins of about 12 to 16 Kd has been described
- [1]. This family currently consists of:
-
- - Bovine protein kinase C inhibitor 1 (PKCI-1). PKCI-1 seems to be, in vitro,
- a specific inhibitor of PKC. It has been shown to bind zinc.
- - Yeast protein HIT1.
- - Escherichia coli hypothetical protein ycfF.
- - A hypothetical 13.2 Kd protein in hisE 3'region in Azospirillum brasilense.
- - A hypothetical 13.1 Kd protein in p37 5'region in Mycoplasma hyorhinis.
- - A hypothetical 12.4 Kd protein in psbAII 5'region in Synechococcus strain
- PCC 7942.
-
- The zinc-binding site of PKCI-1 [2] consists of three histidines that are
- closely positioned. These histidines are perfectly conserved in all members
- of this family for which the name HIT, for HIstidine Triad, has been proposed
- [1]. Except for PKCI-1, the function of these proteins is not yet known. Their
- widespread evolutionary conservation suggests that they are important for some
- cellular process(es).
-
- As a signature pattern, we selected the region of the histidine triad.
-
- -Consensus pattern: N-x(4)-[GA]-x-Q-x-[LIVM]-x-H-x-H-[LIVMF]-H
- [The three H's are probaby zinc ligands]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Seraphin B.
- seraphin@embl-heidelberg.de
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Seraphin B.
- DNA Seq. 3:177-179(1992).
- [ 2] Mozier N.M., Walsh M.P., Pearson J.D.
- FEBS Lett. 279:14-18(1991).
-