AT1G45180.1 :

DomainDescriptionEvalueBitsGAStartEnd
zinc_ribbon_16Zinc-ribbon like family0.33127.00571596
zf-rbx1RING-H2 zinc finger domain1.9E-134131.00589633
Zn_ribbon_17Zinc-ribbon, C4HC2 type6.8E-051327.30589630
zf-C3HC4_3Zinc finger, C3HC4 type (RING finger)2.5E-072127.00590634
zf-C3HC4_2Zinc finger, C3HC4 type (RING finger)2E-113427.00592632
zf-C3HC4Zinc finger, C3HC4 type (RING finger)1.1E-092821.00592632
zf-RING_11RING-like zinc finger3.5E-092727.00592619
zf-RING_UBOXRING-type zinc-finger2.1E-082425.20592630
zf-RING_5zinc-RING finger domain5.4E-082327.90592634
RINGvRING-variant domain0.0065721.60592632
Prok-RING_4Prokaryotic RING finger family 40.0081627.00592633
PHDPHD-finger0.012627.90592633
zf-RING_2Ring finger domain1E-134227.30592633
zinc_ribbon_16Zinc-ribbon like family9.9E-051327.00608633
zf-C3HC4_4zinc finger of C3HC4-type, RING0.0022830.00608632
FANCL_CFANCL C-terminal domain0.000771020.70608626
zf-ANAPC11Anaphase-promoting complex subunit 11 RING-H2 finger9E-071921.40609634

 645

zinc_ribbon_16
zf-rbx1
Zn_ribbon_17
zf-C3HC4_3
zf-C3HC4_2
zf-C3HC4
zf-RING_11
zf-RING_UBOX
zf-RING_5
RINGv
Prok-RING_4
PHD
zf-RING_2
zinc_ribbon_16
zf-C3HC4_4
FANCL_C
zf-ANAPC11


References:

FANCL_C
16474167 The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly. J Biol Chem. 2006;281:10896-10905.

zf-C3HC4
8804826 The RING finger domain: a recent example of a sequence-structure family. Curr Opin Struct Biol 1996;6:395-401.
10500182 RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc Natl Acad Sci U S A 1999;96:11364-11369.

zf-C3HC4_2

RINGv

zf-ANAPC11

zinc_ribbon_16

zf-RING_UBOX

zf-RING_5

zf-RING_2

zf-rbx1

zf-RING_11

zf-C3HC4_4

zf-C3HC4_3

Prok-RING_4

Zn_ribbon_17

PHD
7701562 The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem Sci 1995;20:56-59.
11124022 Structure of the PHD zinc finger from human williams-beuren syndrome transcription factor J Mol Biol 2000;304:723-729.
17142463 Proteome-wide analysis in S. cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. J Biol Chem. 2006; [Epub ahead of print]