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Protein

Putative ATP-dependent RNA helicase ste13

Gene

ste13

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 95ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: PomBase
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA transport, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ATP-dependent RNA helicase ste13 (EC:3.6.4.13)
Gene namesi
Name:ste13
Synonyms:dhh1
ORF Names:SPBC776.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC776.09.
PomBaseiSPBC776.09. ste13.

Subcellular locationi

  • CytoplasmP-body By similarity

  • Note: 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.By similarity

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytoplasmic mRNA processing body Source: PomBase
  • cytoplasmic stress granule Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000550661 – 485Putative ATP-dependent RNA helicase ste13Add BLAST485

Proteomic databases

MaxQBiQ09181.
PRIDEiQ09181.

Interactioni

Protein-protein interaction databases

BioGridi277730. 14 interactors.
MINTiMINT-4693807.

Structurei

3D structure databases

ProteinModelPortaliQ09181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 245Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini255 – 415Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi44 – 72Q motifAdd BLAST29
Motifi193 – 196DEAD box4

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiQ09181.
KOiK12614.
OMAiKKSGQNR.
OrthoDBiEOG092C2B1L.
PhylomeDBiQ09181.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09181-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESLIQKLE NANLNDRESF KGQMKAQPVD MRPKTEDVTK TRGTEFEDYY
60 70 80 90 100
LKRELLMGIF EAGFERPSPI QEESIPIALS GRDILARAKN GTGKTAAFVI
110 120 130 140 150
PSLEKVDTKK SKIQTLILVP TRELALQTSQ VCKTLGKHMN VKVMVTTGGT
160 170 180 190 200
TLRDDIIRLN DTVHIVVGTP GRVLDLAGKG VADFSECTTF VMDEADKLLS
210 220 230 240 250
PEFTPIIEQL LSYFPKNRQI SLYSATFPLI VKNFMDKHLN KPYEINLMDE
260 270 280 290 300
LTLRGVTQYY AFVDESQKVH CLNTLFSKLQ INQSIIFCNS TNRVELLAKK
310 320 330 340 350
ITELGYSCFY SHAKMLQSHR NRVFHNFRNG VCRNLVCSDL LTRGIDIQAV
360 370 380 390 400
NVVINFDFPK NAETYLHRIG RSGRFGHRGL AISFISWADR FNLYRIENEL
410 420 430 440 450
GTEIQPIPPS IDPSLYVFPN GDYQIPRPLT ASADQVLAAQ QAKGQEGYHN
460 470 480
RPNNNRGGHP RGGGNRGGYR QSNRQPRYRG QQKAD
Length:485
Mass (Da):54,795
Last modified:November 1, 1995 - v1
Checksum:i41205089B17773F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29795 Genomic DNA. Translation: BAA06178.1.
CU329671 Genomic DNA. Translation: CAA22882.1.
PIRiS46654.
RefSeqiNP_596324.1. NM_001022246.2.

Genome annotation databases

EnsemblFungiiSPBC776.09.1; SPBC776.09.1:pep; SPBC776.09.
GeneIDi2541216.
KEGGispo:SPBC776.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29795 Genomic DNA. Translation: BAA06178.1.
CU329671 Genomic DNA. Translation: CAA22882.1.
PIRiS46654.
RefSeqiNP_596324.1. NM_001022246.2.

3D structure databases

ProteinModelPortaliQ09181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277730. 14 interactors.
MINTiMINT-4693807.

Proteomic databases

MaxQBiQ09181.
PRIDEiQ09181.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC776.09.1; SPBC776.09.1:pep; SPBC776.09.
GeneIDi2541216.
KEGGispo:SPBC776.09.

Organism-specific databases

EuPathDBiFungiDB:SPBC776.09.
PomBaseiSPBC776.09. ste13.

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiQ09181.
KOiK12614.
OMAiKKSGQNR.
OrthoDBiEOG092C2B1L.
PhylomeDBiQ09181.

Miscellaneous databases

PROiQ09181.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHH1_SCHPO
AccessioniPrimary (citable) accession number: Q09181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.