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 Q0VC82

Entry ID Method Resolution Chain Position Source
AF-Q0VC82-F1 Predicted AlphaFoldDB

30 variants for Q0VC82

Variant ID(s) Position Change Description Diseaes Association Provenance
rs456064355 2 S>A No EVA
rs435996558 6 S>P No EVA
rs467153658 10 E>A No EVA
rs454015392 11 S>R No EVA
rs433844397 11 S>R No EVA
rs445027870 48 N>T No EVA
rs482808479 50 F>L No EVA
rs469524465 51 Q>K No EVA
rs449356036 53 D>N No EVA
rs460464715 57 L>R No EVA
rs480620674 57 L>V No EVA
rs440709165 61 M>V No EVA
rs467684023 101 R>G No EVA
rs453953177 106 N>D No EVA
rs433780996 110 D>V No EVA
rs465127941 133 T>A No EVA
rs434023654 134 D>Y No EVA
rs453333922 184 E>Q No EVA
rs433149803 186 I>L No EVA
rs476822182 187 M>I No EVA
rs456710853 188 P>S No EVA
rs478425639 207 V>E No EVA
rs454562980 216 D>G No EVA
rs451841666 244 M>I No EVA
rs438115378 248 N>K No EVA
rs441751764 302 V>E No EVA
rs473345561 303 S>I No EVA
rs459679733 305 A>D No EVA
rs439571555 316 T>I No EVA
rs445838152 368 D>E No EVA

No associated diseases with Q0VC82

2 regional properties for Q0VC82

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 193 - 367 IPR010918
domain PurM-like, N-terminal domain 82 - 169 IPR016188

Functions

Description
EC Number 2.7.9.3 Phosphotransferases with paired acceptors
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Nucleus membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
protein heterodimerization activity Binding to a nonidentical protein to form a heterodimer.
protein homodimerization activity Binding to an identical protein to form a homodimer.
selenide, water dikinase activity Catalysis of the reaction: ATP + H(2)O + hydrogen selenide = AMP + 3 H(+) + phosphate + selenophosphorate.

2 GO annotations of biological process

Name Definition
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
selenocysteine biosynthetic process The chemical reactions and pathways resulting in the formation of selenocysteine, an essential component of glutathione peroxidase and some other proteins.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P49903 SEPHS1 Selenide, water dikinase 1 Homo sapiens (Human) PR
Q8BH69 Sephs1 Selenide, water dikinase 1 Mus musculus (Mouse) PR
Q6GL12 sephs1 Selenide, water dikinase 1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q7ZW38 sephs1 Selenide, water dikinase 1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSARESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV
70 80 90 100 110 120
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD
130 140 150 160 170 180
NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC
190 200 210 220 230 240
QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA
250 260 270 280 290 300
MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA
310 320 330 340 350 360
AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG
370 380 390
NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS