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 P96614

Entry ID Method Resolution Chain Position Source
AF-P96614-F1 Predicted AlphaFoldDB

No variants for P96614

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P96614

No associated diseases with P96614

5 regional properties for P96614

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 150 - 158 IPR000629
domain Helicase, C-terminal 215 - 375 IPR001650
domain DEAD/DEAH box helicase domain 27 - 192 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 22 - 219 IPR014001
domain RNA helicase, DEAD-box type, Q motif 3 - 31 IPR014014

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm, nucleoid
  • Cell membrane
  • Shows transcription-dependent localization at subcellular sites surrounding the nucleoid (PubMed:16352840)
  • Associated with free 50S ribosomal subunit, 70S ribosome and polysomes (PubMed:16861794)
  • Cell membrane association shown in (PubMed:20572937)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
bacterial nucleoid The region of a bacterial cell to which the DNA is confined.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
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.
RNA strand annealing activity An activity that facilitates the formation of a complementary double-stranded RNA molecule.

4 GO annotations of biological process

Name Definition
response to cold Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.
ribosomal large subunit assembly The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit.
RNA catabolic process The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
RNA secondary structure unwinding The process in which a secondary structure of RNA are broken or 'melted'.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTITFQDFNL SSDLMKAINR MGFEEATPIQ AQTIPLGLSN KDVIGQAQTG TGKTAAFGIP
70 80 90 100 110 120
LVEKINPESP NIQAIVIAPT RELAIQVSEE LYKIGQDKRA KVLPIYGGQD IGRQIRALKK
130 140 150 160 170 180
NPNIIVGTPG RLLDHINRRT IRLNNVNTVV MDEADEMLNM GFIDDIESIL SNVPSEHQTL
190 200 210 220 230 240
LFSATMPAPI KRIAERFMTE PEHVKVKAKE MTVSNIQQFY LEVQERKKFD TLTRLLDIQS
250 260 270 280 290 300
PELAIVFGRT KRRVDELAEA LNLRGYAAEG IHGDLTQAKR MVALRKFKEG AIEVLVATDV
310 320 330 340 350 360
AARGLDISGV THVYNFDVPQ DPESYVHRIG RTGRAGKTGM AMTFITPREK SMLRAIEQTT
370 380 390 400 410 420
KRKMDRMKEP TLDEALEGQQ QVTVERLRTT ISENNLNFYM TAAAELLEDH DAVTVVAAAI
430 440 450 460 470 480
KMATKEPDDT PVRLTDEAPM VSKRYKNQRS SKRRDGQGGG YRGGKGKSNN RSSYDKKRSN
490
DRRSSGDRRQ KKSY