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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: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 1028ATPPROSITE-ProRule annotation

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 splicing, mRNA transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-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

GO - Cellular componenti

  • nucleus Source: PomBase
  • spliceosomal complex Source: PomBase
  • transcription export complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434ATP-dependent RNA helicase uap56PRO_0000055081Add
BLAST

Proteomic databases

MaxQBiO13792.

Interactioni

Subunit structurei

Interacts with mlo3 and rae1.1 Publication

Protein-protein interaction databases

BioGridi278895. 11 interactions.
MINTiMINT-4668002.

Structurei

3D structure databases

ProteinModelPortaliO13792.
SMRiO13792. Positions 52-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 257176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini269 – 430162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 7929Q motifAdd
BLAST
Motifi204 – 2074DECD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 165Poly-Glu

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.
InParanoidiO13792.
KOiK12812.
OMAiVAHEANE.
OrthoDBiEOG74J9JF.
PhylomeDBiO13792.

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.
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.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921I → N in BAA13931 (PubMed:9501991).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO13792.
SMRiO13792. Positions 52-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278895. 11 interactions.
MINTiMINT-4668002.

Proteomic databases

MaxQBiO13792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPAC17G6.14c.
PomBaseiSPAC17G6.14c. uap56.

Phylogenomic databases

HOGENOMiHOG000268797.
InParanoidiO13792.
KOiK12812.
OMAiVAHEANE.
OrthoDBiEOG74J9JF.
PhylomeDBiO13792.

Miscellaneous databases

PROiO13792.

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.
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.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-434.
    Strain: PR745.
  3. "Multiple roles for the yeast SUB2/yUAP56 gene in splicing."
    Libri D., Graziani N., Saguez C., Boulay J.
    Genes Dev. 15:36-41(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for mRNA export in fission yeast."
    Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.
    EMBO J. 24:2512-2523(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLO3 AND RAE1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSUB2_SCHPO
AccessioniPrimary (citable) accession number: O13792
Secondary accession number(s): P78919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 115 of the entry and version 3 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.