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

3 structures for P93527

Entry ID Method Resolution Chain Position Source
6TBY X-ray 180 A AAA 113-451 PDB
6TC5 X-ray 210 A AAA 113-459 PDB
AF-P93527-F1 Predicted AlphaFoldDB

No variants for P93527

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P93527

No associated diseases with P93527

12 regional properties for P93527

Type Name Position InterPro Accession
domain PAS domain 668 - 790 IPR000014-1
domain PAS domain 801 - 921 IPR000014-2
domain GAF domain 267 - 459 IPR003018
domain Histidine kinase/HSP90-like ATPase 1055 - 1170 IPR003594
domain Signal transduction histidine kinase, dimerisation/phosphoacceptor domain 943 - 1007 IPR003661
domain Histidine kinase domain 950 - 1170 IPR005467
domain Phytochrome, central region 462 - 636 IPR013515
binding_site Phytochrome chromophore binding site 367 - 376 IPR013516
domain PAS fold-2 114 - 234 IPR013654
domain PAS fold 671 - 786 IPR013767-1
domain PAS fold 802 - 921 IPR013767-2
domain Phytochrome chromophore attachment domain 267 - 439 IPR016132

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
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.
photoreceptor activity The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation.
protein homodimerization activity Binding to an identical protein to form a homodimer.

4 GO annotations of biological process

Name Definition
detection of visible light The series of events in which a visible light stimulus is received by a cell and converted into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm.
protein-phytochromobilin linkage The linkage of the chromophore phytochromobilin to phycocyanin or allophycocyanin.
red, far-red light phototransduction The sequence of reactions within a cell required to convert absorbed photons from red or far-red light into a molecular signal; the red, far-red light range is defined as having a wavelength within the range 660-730 nm.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q10MG9 PHYB Phytochrome B Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MASGSRATPT RSPSSARPEA PRHAHHHHHH HSQSSGGSTS RAGGGGGGGG GGGGTAATAT
70 80 90 100 110 120
ATATESVSKA VAQYTLDARL HAVFEQSGAS GRSFDYSQSL RAPPTPSSEQ QIAAYLSRIQ
130 140 150 160 170 180
RGGHIQPFGC TLAVADDSSF RLLAFSENAA DLLDLSPHHS VPSLDSAAPP PVSLGADARL
190 200 210 220 230 240
LFSPSSAVLL ERAFAAREIS LLNPLWIHSR VSSKPFYAIL HRIDVGVVID LEPARTEDPA
250 260 270 280 290 300
LSIAGAVQSQ KLAVRAISRL QALPGGDIKL LCDTVVEHVR ELTGYDRVMV YRFHEDEHGE
310 320 330 340 350 360
VVAESRRDNL EPYLGLHYPA TDIPQASRFL FRQNRVRMIA DCHATPVRVI QDPGMSQPLC
370 380 390 400 410 420
LVGSTLRAPH GCHAQYMANM GSIASLVMAV IISSGGDDEQ TGRGGISSAM KLWGLVVCHH
430 440 450 460 470 480
TSPRCIPFPL RYACEFLMQA FGLQLNMELQ LAHQLSEKHI LRTQTLLCDM LLRDSPTGIV
490 500 510 520 530 540
TQSPSIMDLV KCDGAALYYH GKYYPLGVTP TESQIKDIIE WLTVCHGDST GLSTDSLADA
550 560 570 580 590 600
GYLGAAALGD AVCGMAVAYI TPSDYLFWFR SHTAKEIKWG GAKHHPEDKD DGQRMHPRSS
610 620 630 640 650 660
FKAFLEVVKS RSLPWENAEM DAIHSLQLIL RDSFRDAAEG TSNSKAIVNG QVQLGELELR
670 680 690 700 710 720
GINELSSVAR EMVRLIETAT VPIFAVDTDG CINGWNAKIA ELTGLSVEEA MGKSLVNDLI
730 740 750 760 770 780
FKESEEIVEK LLSRALRGEE DKNVEIKLKT FGSEQSNGAI FVIVNACSSR DYTQNIVGVC
790 800 810 820 830 840
FVGQDVTGQK VVMDKFINIQ GDYKAIVHNP NPLIPPIFAS DENTSCSEWN TAMEKLTGWS
850 860 870 880 890 900
RGEVVGKFLI GEVFGSFCRL KGPDALTKFM VVIHNAIGGQ DYEKFPFSFF DKNGKYVQAL
910 920 930 940 950 960
LTANTRSKMD GKSIGAFCFL QIASAEIQQA FEIQRQQEKK CYARMKELAY ICQEIKNPLS
970 980 990 1000 1010 1020
GIRFTNSLLQ MTDLNDDQRQ FLETCSACEK QMSKIVKDAT LQSIEDGSLV LEKSEFSFGD
1030 1040 1050 1060 1070 1080
VMNAVVSQAM LLLRERDLQL IRDIPDEIKD ASAYGDQFRI QQVLADFLLS MVRSAPSENG
1090 1100 1110 1120 1130 1140
WVEIQVRPNV KQNSDGTDTE LFIFRFACPG EGLPADIVQD MFSNSQWSTQ EGVGLSTCRK
1150 1160 1170
ILKLMGGEVQ YIRESERSFF LIVLELPQPR PAADREIS