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 Q0CDT1

Entry ID Method Resolution Chain Position Source
AF-Q0CDT1-F1 Predicted AlphaFoldDB

No variants for Q0CDT1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0CDT1

No associated diseases with Q0CDT1

5 regional properties for Q0CDT1

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 229 - 237 IPR000629
domain Helicase, C-terminal 295 - 468 IPR001650
domain DEAD/DEAH box helicase domain 103 - 271 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 97 - 299 IPR014001
domain RNA helicase, DEAD-box type, Q motif 78 - 106 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
MSSEQPTEAP AGGSLADRIS KPEESKPADS TQQPTDNGQT DGAPAQLGGS ELHEPEYNVE
70 80 90 100 110 120
VKLSDLQADP NNPLFSVKNF EDLGLDPRIL QGLSAMNFRK PSKIQERALP LLLSNPPKNL
130 140 150 160 170 180
VGQSQSGTGK TAAFVLNILS RLDLSTEQMQ KTPQALILAP TRELARQIVG VIQVMGQFLD
190 200 210 220 230 240
NLIIGTAVPA DTNNRPARME ASVVVGTPGT VMDMIKKRIM VPAKLQVLVL DEADNMLDQQ
250 260 270 280 290 300
GLGDQCIRVK ALLPRTIQVV LFSATFPTHV HQYASKFAPQ ANELTLQHEE LTVEGIKQLY
310 320 330 340 350 360
LDCSDEEDKY RTLVSLYGLL TVGSSIIFVK TRQSAMEIEK RMVAEGHTVA SLTGGIEGSQ
370 380 390 400 410 420
RDAVIDQFRA GAAKVLITTN VLARGIDVST VSMVINYDIP ELHLPPNQPR QADFQTYLHR
430 440 450 460 470 480
IGRTGRFGRV GVSISFVSNR DEWNMLNQIQ KYFNTSIQRI DTKDWDEVED IIKKTIKNPR
SQATFGK