c2pfam

AT3G06480.1 :

Domain Description Evalue Bits GA Start End
WW WW domain 2.5E-10 29 21.60 22 52
DEAD DEAD/DEAH box helicase 0 164 20.60 459 629
ResIII Type III restriction enzyme, res subunit 6.6E-10 28 20.90 472 622
Helicase_C Helicase conserved C-terminal domain 0.059 2 20.90 502 563
Helicase_C Helicase conserved C-terminal domain 3E-35 110 20.90 666 774
DEAD DEAD/DEAH box helicase 0.28 -1 20.60 674 705
ERCC3_RAD25_C ERCC3/RAD25/XPB C-terminal helicase 4.7E-07 18 27.00 676 773

1088

WW
DEAD
ResIII
Helicase_C
Helicase_C
DEAD
ERCC3_RAD25_C

References:

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.

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.

Helicase_C

ERCC3_RAD25_C

ResIII

Domain	Description	Evalue	Bits	GA	Start	End
WW	WW domain	2.5E-10	29	21.60	22	52
DEAD	DEAD/DEAH box helicase	0	164	20.60	459	629
ResIII	Type III restriction enzyme, res subunit	6.6E-10	28	20.90	472	622
Helicase_C	Helicase conserved C-terminal domain	0.059	2	20.90	502	563
Helicase_C	Helicase conserved C-terminal domain	3E-35	110	20.90	666	774
DEAD	DEAD/DEAH box helicase	0.28	-1	20.60	674	705
ERCC3_RAD25_C	ERCC3/RAD25/XPB C-terminal helicase	4.7E-07	18	27.00	676	773