AT3G04130.1 :

DomainDescriptionEvalueBitsGAStartEnd
Sigma70_r4_2Sigma-70, region 40.00021121.807296
HTH_24Winged helix-turn-helix DNA-binding0.00041021.907397
PAX'Paired box' domain0.25121.007899
TPR_15Tetratricopeptide repeat0.019426.20117151
PPRPPR repeat0.014625.00128150
PPR_longPentacotripeptide-repeat region of PRORP0.0056627.00129235
PPR_3Pentatricopeptide repeat domain0.29125.00156200
PPR_2PPR repeat family 2.4E-051530.00161202
PPRPPR repeat0.0013925.00162185
TPR_14Tetratricopeptide repeat0.29223.50164181
TPR_19Tetratricopeptide repeat0.000561025.00167216
PPR_1PPR repeat0.62023.80168180
PPR_3Pentatricopeptide repeat domain0.0013925.00181231
PPR_2PPR repeat family 3.5E-113330.00188236
PPRPPR repeat0.0042825.00192218
PPR_1PPR repeat0.0013823.80194213
PPR_longPentacotripeptide-repeat region of PRORP2.4E-051427.00202282
ATP13Mitochondrial ATPase expression0.015526.70208249
PPR_1PPR repeat3E-113323.80220250
PPR_3Pentatricopeptide repeat domain7.6E-071925.00220269
PPR_2PPR repeat family 3.9E-144330.00222271
PPRPPR repeat3.4E-092725.00226255
PAX'Paired box' domain0.0014921.00229270
PPR_3Pentatricopeptide repeat domain1.9E-092825.00247302
PPR_1PPR repeat2.3E-051423.80254285
PPR_2PPR repeat family 3.9E-133930.00257304
PPRPPR repeat9.8E-082225.00260289
PPR_longPentacotripeptide-repeat region of PRORP4E-092627.00274351
PPR_3Pentatricopeptide repeat domain3.3E-123625.00281338
ATP13Mitochondrial ATPase expression0.0016826.70287321
PPR_1PPR repeat3.3E-051423.80289321
PPR_2PPR repeat family 2.3E-103130.00292329
PPRPPR repeat5E-061725.00295325
TPR_14Tetratricopeptide repeat0.43223.50302319
TPR_15Tetratricopeptide repeat0.012526.20305441
TPR_19Tetratricopeptide repeat0.1325.00306352
PPR_3Pentatricopeptide repeat domain7.9E-102925.00317375
PPR_1PPR repeat7.2E-123523.80324353
PPR_2PPR repeat family 8.9E-133830.00327376
PPRPPR repeat1.2E-061925.00332353
PPR_longPentacotripeptide-repeat region of PRORP5.3E-123527.00332444
TPR_14Tetratricopeptide repeat0.0036823.50334353
TPR_4Tetratricopeptide repeat0.000351122.00337353
PPR_3Pentatricopeptide repeat domain7E-082325.00355411
PPR_1PPR repeat7.8E-102823.80360392
PPR_2PPR repeat family 3.3E-144330.00364412
PPRPPR repeat5.3E-113225.00366395
ATP13Mitochondrial ATPase expression0.23126.70370412
PPR_3Pentatricopeptide repeat domain0.000161225.00387430
PPR_1PPR repeat2.9E-051423.80397428
PPR_2PPR repeat family 2E-113430.00399449
PPRPPR repeat5.7E-051325.00403430
PPR_3Pentatricopeptide repeat domain0.033425.00423470
PPR_longPentacotripeptide-repeat region of PRORP2E-051427.00424502
PPR_1PPR repeat5.4E-092623.80433463
PPR_2PPR repeat family 1.7E-072130.00436474
PPRPPR repeat1.4E-072225.00438467
PPR_3Pentatricopeptide repeat domain0.0069725.00459503
Fe_dep_repr_CIron dependent repressor, metal binding and dimerisation domain2.8E-051420.70466499

 508

Sigma70_r4_2
HTH_24
PAX
TPR_15
PPR
PPR_long
PPR_3
PPR_2
PPR
TPR_14
TPR_19
PPR_1
PPR_3
PPR_2
PPR
PPR_1
PPR_long
ATP13
PPR_1
PPR_3
PPR_2
PPR
PAX
PPR_3
PPR_1
PPR_2
PPR
PPR_long
PPR_3
ATP13
PPR_1
PPR_2
PPR
TPR_14
TPR_15
TPR_19
PPR_3
PPR_1
PPR_2
PPR
PPR_long
TPR_14
TPR_4
PPR_3
PPR_1
PPR_2
PPR
ATP13
PPR_3
PPR_1
PPR_2
PPR
PPR_3
PPR_long
PPR_1
PPR_2
PPR
PPR_3
Fe_dep_repr_C


References:

TPR_4

Sigma70_r4_2
11931761 Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol Cell 2002;9:527-539.

PPR_long

TPR_15

TPR_14

PPR_1

PPR_2

HTH_24

PAX
9297966 Pax genes and organogenesis. Bioessays 1997;19:755-765.

PPR_3

ATP13

PPR
7664742 The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron-containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae. EMBO J 1995;14:4031-4043.
8039510 A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms. EMBO J 1994;13:3170-3181.
10664580 The PPR motif - a TPR-related motif prevalent in plant organellar proteins. Trends Biochem Sci 2000;25:45-47.

Fe_dep_repr_C
7568230 Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae. Proc Natl Acad Sci USA 1995;92:9843-9850.
7743135 Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 1995;3:87-100.

TPR_19