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 Q54E49

Entry ID Method Resolution Chain Position Source
AF-Q54E49-F1 Predicted AlphaFoldDB

No variants for Q54E49

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54E49

No associated diseases with Q54E49

5 regional properties for Q54E49

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 196 - 204 IPR000629
domain Helicase, C-terminal 260 - 420 IPR001650
domain DEAD/DEAH box helicase domain 74 - 237 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 68 - 264 IPR014001
domain RNA helicase, DEAD-box type, Q motif 49 - 77 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
  • Upon cellular stress, relocalizes to stress granules
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
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.

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.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

4 GO annotations of biological process

Name Definition
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
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.
stress granule assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNSQQNKLPQ QPQQPPSSIV DDDNWKSQLK LPPRDERRQT EDVTATEGND FDDLHLKRDL
70 80 90 100 110 120
LRGIFEKGYV KPSPIQEKAI PIALAGRDIM ARAKNGTGKT ASFLIPALEK TDPTKDVIQV
130 140 150 160 170 180
LILVPTRELA LQTSQVCKEL GKYMNVQVMA STGGTSLKDD IMRLYNPVHI LVATPGRVLD
190 200 210 220 230 240
LAQKNVANLS NCHTMIMDEA DKLLSQEFQP LVEQLINFLP QQRQILLFSA TFPVTVKSFK
250 260 270 280 290 300
EHYLQQAFEI NLMEELTLKG VTQYYAFVEE RQKIHCLNTL FSKLQINQSI IFCNSVNRVE
310 320 330 340 350 360
LLAKKITELG YSCFFIHAKM VQAHRNRVFH DFRNGACRNL VSSDLFTRGI DIQDVNVVIN
370 380 390 400 410 420
FDFPKHSETY LHRIGRSGRF GHLGLAINLI TYEDRFSLYK IEQELGTEIK PIPPVIDKSL
YAA