AT3G01540.1 :

DomainDescriptionEvalueBitsGAStartEnd
WWWW domain1.6E-103021.601949
DEADDEAD/DEAH box helicase016320.60182351
ResIIIType III restriction enzyme, res subunit9.2E-092420.90196345
Helicase_CHelicase conserved C-terminal domain0.054320.90223280
IKI3IKI3 family0.00011919.30273316
ERCC3_RAD25_CERCC3/RAD25/XPB C-terminal helicase8.8E-061427.00388496
Helicase_CHelicase conserved C-terminal domain4.5E-3611220.90389497
DEADDEAD/DEAH box helicase0.002720.60396459
ResIIIType III restriction enzyme, res subunit0.057220.90398441

 618

WW
DEAD
ResIII
Helicase_C
IKI3
ERCC3_RAD25_C
Helicase_C
DEAD
ResIII


References:

ResIII

DEAD
10322435 Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem Sci 1999;24:192-198.
9862990 The DEAD box RNA helicase family in Arabidopsis thaliana. Nucleic Acids Res 1999;27:628-636.

ERCC3_RAD25_C

IKI3
10024884 Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell 1999;3:109-118.

Helicase_C

WW
7846762 The WW domain: a signalling site in dystrophin? Trends Biochem Sci 1994;19:531-533.
8757138 Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 1996;382:646-649.
11870222 Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1. J Cell Sci 2002;115:1041-1048.
11323714 Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nat Struct Biol 2001;8:407-412.
10932238 Converging on proline: the mechanism of WW domain peptide recognition. Nat Struct Biol 2000;7:611-613.
10744724 A novel pro-Arg motif recognized by WW domains. J Biol Chem 2000;275:10359-10369.
10037602 Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 1999;283:1325-1328.
9407065 The WW domain of neural protein FE65 interacts with proline-rich motifs in Ermekova KS, Zambrano N, Linn H, Minopoli G, Gertler F, Russo T, Sudol M; J Biol Chem 1998;272:32869-32877.
8797792 Towards prediction of cognate complexes between the WW domain and proline-rich ligands. FEBS Lett 1996;384:1-8.
7644498 The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc Natl Acad Sci U S A 1995;92:7819-7823.
7641887 Characterization of a novel protein-binding module--the WW domain. FEBS Lett 1995;369:67-71.