Q0U7S9

PR
Gene name
DHH1 (SNOG_12185)
Protein name
ATP-dependent RNA helicase DHH1
Names
Species
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
KEGG Pathway
pno:SNOG_12185
EC number
3.6.4.13: Acting on ATP; involved in cellular and subcellular movement
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-68 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q0U7S9

Entry ID Method Resolution Chain Position Source
AF-Q0U7S9-F1 Predicted AlphaFoldDB

No variants for Q0U7S9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0U7S9

No associated diseases with Q0U7S9

5 regional properties for Q0U7S9

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
  • Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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.
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.

5 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.
mRNA transport The directed movement of mRNA, messenger ribonucleic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
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
MTSEITNQMA STKLSDASAS TLADWKEGLK APAKDARPQT EDVTATKGLE FEDFFIKREL
70 80 90 100 110 120
MMGIFEAGFE KPSPIQEETI PVALTGRDIL ARAKNGTGKT AAFVIPTLER VNPKISKTQA
130 140 150 160 170 180
LILVPTRELA LQTSQVCKTL GKHLGINVMV STGGTGLKDD IIRLSDPVHI IVGTPGRILD
190 200 210 220 230 240
LAGKGVADLS TCQTFVMDEA DKLLSPEFTP VVEQLLGFHP KDRQVMLFSA TFPIVVKTFK
250 260 270 280 290 300
DKHMNSPYEI NLMDELTLRG ITQYYAFVEE KQKVHCLNTL FNKLQINQSI IFCNSTNRVE
310 320 330 340 350 360
LLAKKITELG YSCFYSHARM LQHNRNRVFH DFRNGVCRNL VCSDLLTRGI DIQAVNVVIN
370 380 390 400 410 420
FDFPKNAETY LHRIGRSGRF GHLGLAINLI NWEDRFNLYR IEQELGTEIQ PIPQVIEKNL
430 440 450 460 470 480
YVYESPENIP RPISSSQRQP GQQQEQDGTV VRNNQGQNPR GNFRGGRGGG GGGQFQGQRR
490 500 510 520
NPPPGQGQPQ QGQGMGQVQQ PRQNGQQAQR NPQRQPTGPP QA