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 P54824

Entry ID Method Resolution Chain Position Source
AF-P54824-F1 Predicted AlphaFoldDB

No variants for P54824

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P54824

No associated diseases with P54824

5 regional properties for P54824

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 243 - 251 IPR000629
domain Helicase, C-terminal 307 - 467 IPR001650
domain DEAD/DEAH box helicase domain 120 - 285 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 114 - 311 IPR014001
domain RNA helicase, DEAD-box type, Q motif 95 - 123 IPR014014

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm, P-body
  • Cytoplasm
  • Nucleus
  • Mostly cytoplasmic
  • Upon cellular stress, relocalizes to stress granules
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
P-body A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing.
ribonucleoprotein complex A macromolecular complex that contains both RNA and protein molecules.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

3 GO annotations of biological process

Name Definition
miRNA-mediated gene silencing by inhibition of translation An RNA interference pathway in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs.
negative regulation of translation Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
P-body assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSTARTENPV LMGMSSQNGQ LRGPLKPSAG PGGGGTQTQQ INQLKNASTI NSGSQQQAQS
70 80 90 100 110 120
MSSIIKPGDD WKKTLKLPPK DLRIKTSDVT STKGNEFEDY CLKRELLMGI FEMGWEKPSP
130 140 150 160 170 180
IQEESIPIAL SGRDILARAK NGTGKSGAYL IPLLERLDLK KDCIQAMVIV PTRELALQVS
190 200 210 220 230 240
QICIQVSKHM GGAKVMATTG GTNLRDDIMR LDDTVHVVIA TPGRILDLIK KGVAKVDHIQ
250 260 270 280 290 300
MIVLDEADKL LSQDFMQIME DIIMTLPKNR QILLYSATFP LSVQKFMTLH LQKPYEINLM
310 320 330 340 350 360
EELTLKGVTQ YYAYVTERQK VHCLNTLFSR LQINQSIIFC NSSQRVELLA KKISQLGYSC
370 380 390 400 410 420
FYIHAKMRQE HRNRVFHDFR NGLCRNLVCT DLFTRGIDIQ AVNVVINFDF PKLAETYLHR
430 440 450 460 470 480
IGRSGRFGHL GLAINLITYD DRFNLKSIEE QLGTEIKPIP SSIDKNLYVA EYHSESGEDK
P