Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9XH57

Entry ID Method Resolution Chain Position Source
AF-Q9XH57-F1 Predicted AlphaFoldDB

No variants for Q9XH57

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9XH57

No associated diseases with Q9XH57

8 regional properties for Q9XH57

Type Name Position InterPro Accession
domain Signal transduction response regulator, receiver domain 614 - 732 IPR001789
domain GAF domain 158 - 317 IPR003018
domain Histidine kinase/HSP90-like ATPase 455 - 589 IPR003594
domain Signal transduction histidine kinase, dimerisation/phosphoacceptor domain 341 - 408 IPR003661
domain Signal transduction histidine kinase-related protein, C-terminal 511 - 525 IPR004358-1
domain Signal transduction histidine kinase-related protein, C-terminal 529 - 539 IPR004358-2
domain Signal transduction histidine kinase-related protein, C-terminal 546 - 564 IPR004358-3
domain Histidine kinase domain 350 - 589 IPR005467

Functions

Description
EC Number 2.7.13.3 Protein-histidine kinases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ethylene binding Binding to ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
ethylene receptor activity Combining with ethylene and transmitting the signal in the cell to initiate a change in cell activity.
metal ion binding Binding to a metal ion.
phosphorelay sensor kinase activity Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.

2 GO annotations of biological process

Name Definition
anatomical structure development The biological process whose specific outcome is the progression of an anatomical structure from an initial condition to its mature state. This process begins with the formation of the structure and ends with the mature structure, whatever form that may be including its natural destruction. An anatomical structure is any biological entity that occupies space and is distinguished from its surroundings. Anatomical structures can be macroscopic such as a carpel, or microscopic such as an acrosome.
negative regulation of ethylene-activated signaling pathway Any process that stops or prevents ethylene (ethene) signal transduction.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MESCNCIEPQ WPADELLMKY QYISDFFIAI AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
70 80 90 100 110 120
FIVLCGATHL INLWTFNMHS KTVEIVMTTA KIMTAVVSCA TALMLVHIIP DLLSVKTREL
130 140 150 160 170 180
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
190 200 210 220 230 240
LWMPTRTGLE LQLSYTLRQQ NPVGFTVPIH LPVINQVFSS NHAIKISPNS PIARLRPIAG
250 260 270 280 290 300
KYMPGEVVGV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA
310 320 330 340 350 360
DQVAVALSHA AILEESMRAR DLLMEQNVAL DMARREAETA IRARNDFLAV MNHEMRTPMH
370 380 390 400 410 420
AIIALSSLLQ ETELTPEQRL MVETVLKSSN LLATLINDVL DLSRLEDGSL QLDIGTFNLH
430 440 450 460 470 480
ALLREVHNLI KPIASVKKLC ISLNVATDLP EYAVGDEKRL VQIILNVVGN AVKFSKEGNI
490 500 510 520 530 540
SITAFVAKSE SLRDPRAPDF FPICGENQFY LRVQVKDSGL GINPQDIPRL FTKFAQTQPV
550 560 570 580 590 600
ATKNSGGSGL GLAICKRFVN LMEGHIWIDS EGPGKGCTAT FVVKLGIPER SSEPKLLLMP
610 620 630 640 650 660
KVPANHGQTN FSGLKVLLLD DNGVSRAVTR GLLAHLGCDV TTVSSSDELL RVVSQDYKVV
670 680 690 700 710 720
FMDVCMPEVD GFEIAVRIHE KFMTRHERPL IVALTGNIDQ VTKDNCTRVG MEGVVLKPVS
730 740
IDKMRNVLSN LLEHRVLFEA I