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Protein

ATP-dependent RNA helicase uap56

Gene

uap56

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 plays also a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity. Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC).2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi95 – 102ATPPROSITE-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

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase uap56 (EC:3.6.4.13)
Gene namesi
Name:uap56
Synonyms:sub2
ORF Names:SPAC17G6.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17G6.14c
PomBaseiSPAC17G6.14c uap56

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000550811 – 434ATP-dependent RNA helicase uap56Add BLAST434

Proteomic databases

MaxQBiO13792
PaxDbiO13792
PRIDEiO13792

PTM databases

iPTMnetiO13792

Interactioni

Subunit structurei

Interacts with mlo3 and rae1.1 Publication

Protein-protein interaction databases

BioGridi278895, 11 interactors
STRINGi4896.SPAC17G6.14c.1

Structurei

3D structure databases

ProteinModelPortaliO13792
SMRiO13792
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 257Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST176
Domaini269 – 430Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi51 – 79Q motifAdd BLAST29
Motifi204 – 207DECD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi12 – 16Poly-Glu5

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

Phylogenomic databases

HOGENOMiHOG000268797
InParanoidiO13792
KOiK12812
OMAiCRKFMQN
OrthoDBiEOG092C2V3O
PhylomeDBiO13792

Family and domain databases

CDDicd00079 HELICc, 1 hit
InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR014014 RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51195 Q_MOTIF, 1 hit

Sequencei

Sequence statusi: Complete.

O13792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAQEDLID YEEEEELVQD QPAQEITPAA DTAENGEKSD KKGSYVGIHS
60 70 80 90 100
TGFRDFLLKP ELLRAITDSG FEHPSEVQQV CIPQSILGTD VLCQAKSGMG
110 120 130 140 150
KTAVFVLSTL QQIEPVDGEV SVLVLCHTRE LAFQIKNEYA RFSKYLPDVR
160 170 180 190 200
TAVFYGGINI KQDMEAFKDK SKSPHIVVAT PGRLNALVRE KILKVNSVKH
210 220 230 240 250
FVLDECDKLL ESVDMRRDIQ EVFRATPPQK QVMMFSATLS NEIRPICKKF
260 270 280 290 300
MQNPLEIYVD DETKLTLHGL QQHYVKLEEK AKNRKINDLL DSLEFNQVVI
310 320 330 340 350
FVKSVSRANE LDRLLRECNF PSICIHGGLP QEERIKRYKA FKDFDKRICV
360 370 380 390 400
ATDVFGRGID IERVNIVINY DMPDSPDSYL HRVGRAGRFG TKGLAITFSS
410 420 430
SEEDSQILDK IQERFEVNIT ELPDEIDVGS YMNA
Length:434
Mass (Da):49,231
Last modified:February 1, 2005 - v3
Checksum:i7DBBC7EDE01FC3DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti192I → N in BAA13931 (PubMed:9501991).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAB16225.1
D89270 mRNA Translation: BAA13931.1
PIRiT37846
T43199
RefSeqiNP_594261.1, NM_001019684.2

Genome annotation databases

EnsemblFungiiSPAC17G6.14c.1; SPAC17G6.14c.1:pep; SPAC17G6.14c
GeneIDi2542433
KEGGispo:SPAC17G6.14c

Similar proteinsi

Entry informationi

Entry nameiSUB2_SCHPO
AccessioniPrimary (citable) accession number: O13792
Secondary accession number(s): P78919
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: March 28, 2018
This is version 129 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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