| Description | Probable mediator of RNA polymerase II transcription subunit 37e |
| Sequence | MSGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRFSDSSVQSDMKLWPFKIQAGPADKPMIYVEYKGEEKEFAAEEISSMVLIKMREIAEAYLGVTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKSKKDITGNPRALRRLRTSCERAKRTLSSTAQTTIEIDSLYEGIDFYSTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSTVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQGAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTTLIPRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIQDEKIGEKLPAADKKKIEDSIEQAIQWLEGNQLAEADEFEDKMKELESICNPIIAKMYQGAGGEAGGPGASGMDDDAPPASGGAGPKIEEVD |
| Length | 651 |
| Position | Unknown |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Kingdom | Viridiplantae |
| Lineage | Eukaryota> Viridiplantae> Streptophyta> Embryophyta> Tracheophyta> Spermatophyta> Magnoliopsida> eudicotyledons> Gunneridae> Pentapetalae> rosids> malvids> Brassicales> Brassicaceae> Camelineae> Arabidopsis. |
| Aromaticity | 0.06 |
| Grand average of hydropathy | -0.436 |
| Instability index | 35.37 |
| Isoelectric point | 5.03 |
| Molecular weight | 71356.92 |
| Publications | PubMed=8049382 PubMed=11130714 PubMed=27862469 PubMed=14593172 PubMed=16666375 PubMed=8075396 PubMed=11599561 PubMed=11402207 PubMed=11807141 PubMed=12805626 PubMed=15805473 PubMed=16003391 PubMed=16636050 PubMed=17272265 PubMed=18065690 PubMed=19617588 PubMed=20543027 PubMed=21612577 PubMed=21418353 PubMed=21586649 PubMed=22021418 PubMed=22092075 PubMed=22223895 PubMed=26408532 PubMed=28004282 |
| Annotated function |
In cooperation with other chaperones, Hsp70s are key
components that facilitate folding of de novo synthesized proteins,
assist translocation of precursor proteins into organelles, and are
responsible for degradation of damaged protein under stress conditions
(Probable). Probably involved in defense response. Chaperone involved
in protein targeting to chloroplasts. May cooperate with SGT1 and HSP90
in R gene-mediated resistance towards the oomycete Hyaloperonospora
parasitica (downy mildew). Plays a role with WPP-domain proteins in
facilitating WIT1 nuclear envelope targeting (PubMed:12805626,
PubMed:18065690, PubMed:19617588). Modulates stomatal aperture in
response to various environmental conditions and physiological
responses to the hormone abscisic acid (ABA) (PubMed:21586649).
|
| GO - Cellular Component | apoplast GO:0048046 IDA:TAIR cell wall GO:0005618 IDA:TAIR chloroplast GO:0009507 IDA:TAIR cytoplasm GO:0005737 IDA:UniProtKB cytosol GO:0005829 IDA:TAIR cytosolic ribosome GO:0022626 IDA:TAIR Golgi apparatus GO:0005794 IDA:TAIR nucleolus GO:0005730 IDA:TAIR nucleus GO:0005634 IDA:TAIR plasma membrane GO:0005886 IDA:TAIR plasmodesma GO:0009506 IDA:TAIR vacuolar membrane GO:0005774 IDA:TAIR |
| GO - Biological Function | ATP binding GO:0005524 IBA:GO_Central ATPase activity GO:0016887 IBA:GO_Central heat shock protein binding GO:0031072 IBA:GO_Central misfolded protein binding GO:0051787 IBA:GO_Central mRNA binding GO:0003729 IDA:TAIR protease binding GO:0002020 IPI:UniProtKB protein folding chaperone GO:0044183 IBA:GO_Central unfolded protein binding GO:0051082 IBA:GO_Central |
| GO - Biological Process | cellular response to unfolded protein GO:0034620 IBA:GO_Central chaperone cofactor-dependent protein refolding GO:0051085 IBA:GO_Central defense response to bacterium GO:0042742 IMUniProtKB defense response to fungus GO:0050832 IMUniProtKB defense response to other organism GO:0098542 IMTAIR heat acclimation GO:0010286 IMTAIR negative regulation of seed germination GO:0010187 IMTAIR protein refolding GO:0042026 IBA:GO_Central response to cadmium ion GO:0046686 IETAIR response to cold GO:0009409 IETAIR response to heat GO:0009408 IMUniProtKB response to virus GO:0009615 IETAIR stomatal closure GO:0090332 IMTAIR |
| Binary Interactions |
| Repeats |
>MDP31322
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No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level
3| 75.81| 18| 21| 38| 55| 1
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16- 33 (19.07/ 9.06) ....TTYSCVGVWQHDRveIIA
38- 55 (32.55/19.78) NR..TTPSYVAFTDSER..LIG
60- 78 (24.19/13.13) NQvaMNPVNTVF.DAKR..LIG
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No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level
2| 65.29| 23| 26| 535| 560| 2
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535- 560 (33.05/33.74) DEEHKKKVEA..KNALENyayNMRNTIQ
561- 585 (32.24/22.05) DEKIGEKLPAadKKKIED...SIEQAIQ
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No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level
2| 73.01| 23| 26| 458| 482| 4
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458- 482 (36.09/29.21) DNNllGKFELSGIPPAPRGVPQITV
487- 509 (36.91/23.36) DAN..GILNVSAEDKTTGQKNKITI
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No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level
2| 88.95| 29| 189| 170| 200| 5
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170- 200 (41.67/32.17) GLNVMRIINePTaAAIAYGLD.KKATSVGEKN
362- 391 (47.28/27.61) GKELCKSIN.PD.EAVAYGAAvQGAILSGEGN
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