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 Q6FKN8

Entry ID Method Resolution Chain Position Source
AF-Q6FKN8-F1 Predicted AlphaFoldDB

No variants for Q6FKN8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FKN8

No associated diseases with Q6FKN8

5 regional properties for Q6FKN8

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 259 - 267 IPR000629
domain Helicase, C-terminal 325 - 502 IPR001650
domain DEAD/DEAH box helicase domain 139 - 301 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 133 - 329 IPR014001
domain RNA helicase, DEAD-box type, Q motif 114 - 142 IPR014014

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm
  • Nucleus, nuclear pore complex
  • Nucleus membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Nuclear pore complex cytoplasmic fibrils
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cellular bud tip The end of a cellular bud distal to the site of attachment to the mother cell.
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
nuclear pore cytoplasmic filaments Filamentous extensions on cytoplasmic face of the nuclear pore complex (NPC). In S. cerevisiae, Nup159p, Nup82p, and Nup42p contribute to the cytoplasmic filaments. In vertebrates, Nup358 is a major component.
polysome A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro.

5 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.
inositol hexakisphosphate binding Binding to inositol hexakisphosphate.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

4 GO annotations of biological process

Name Definition
poly(A)+ mRNA export from nucleus The directed movement of poly(A)+ mRNA out of the nucleus into the cytoplasm.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
translational termination The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
tRNA export from nucleus The directed movement of tRNA from the nucleus to the cytoplasm.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSATEDKKDP ASMLAELKLD KDEGNKTPET KTPESNSAET KTTEEVKELK NPFTQKKEDV
70 80 90 100 110 120
ENDAAEEKTN EVNKDDAKDE RENKDTNLIK SEYEVKVNLA DLQADPNSPL YSVKSFDELG
130 140 150 160 170 180
LSPELLKGIY AMKFQKPSKI QERALPLLLS NPPRNMIAQS QSGTGKTAAF SLTMLSRVDE
190 200 210 220 230 240
TQNVPQAICL APSRELARQT LEVIQEMGKY TKITTQLIVP DSFEKNTKIN ANVVVGTPGT
250 260 270 280 290 300
LLDLIRRKLI QLQNVKIFVL DEADNMLDKQ GLGDQCIRVK KFLPKDTQLV LFSATFADAV
310 320 330 340 350 360
KAYAQKVIPN ANTLELQRNE VNVKAIKQLY MDCNDEAHKY EVLCELYGLL TIGSSIIFVA
370 380 390 400 410 420
KKDTANLLYG KLKHEGHQVS ILHSDLRTDE RDRLIDDFRE GRSKVLITTN VLARGIDIPS
430 440 450 460 470 480
VSMVVNYDLP TLPNGMPDYA TYVHRIGRTG RFGRTGVAIS FVHDKKSFKI LSAIQDYFKD
490 500
IELTRVPTDD WDEVEDIVKK VLKQ