(data stored in ACNUC6288 zone)

SWISSPROT: SUB2_DEBHA

ID   SUB2_DEBHA              Reviewed;         435 AA.
AC   Q6BME5; Q6BME4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=ATP-dependent RNA helicase SUB2;
DE            EC=3.6.4.13;
GN   Name=SUB2; OrderedLocusNames=DEHA2F06138g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in transcription
CC       elongation and required for the export of mRNA out of the nucleus.
CC       SUB2 plays also a role in pre-mRNA splicing and spliceosome
CC       assembly. May be involved in rDNA and telomeric silencing, and
CC       maintenance of genome integrity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR382138; CAG88955.2; -; Genomic_DNA.
DR   RefSeq; XP_460627.2; XM_460627.2.
DR   SMR; Q6BME5; -.
DR   STRING; 4959.XP_460627.2; -.
DR   PRIDE; Q6BME5; -.
DR   EnsemblFungi; CAG88955; CAG88955; DEHA2F06138g.
DR   GeneID; 2903132; -.
DR   KEGG; dha:DEHA2F06138g; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q6BME5; -.
DR   KO; K12812; -.
DR   OMA; RTAVFYG; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000346; C:transcription export complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004004; F:ATP-dependent RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:EnsemblFungi.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BME5.
DR   SWISS-2DPAGE; Q6BME5.
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; Spliceosome; Transport.
FT   CHAIN         1    435       ATP-dependent RNA helicase SUB2.
FT                                /FTId=PRO_0000232264.
FT   DOMAIN       82    257       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      269    430       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      95    102       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        51     79       Q motif.
FT   MOTIF       204    207       DECD box.
SQ   SEQUENCE   435 AA;  49118 MW;  5D146243B903B726 CRC64;
     MSHEGQEELL DYSDSEEIAV PTTTAPSAAA GEGANDKEAD KKGSYVGIHA TGFRDFLLKP
     ELLRAIGDCG FEHPSEVQQV CIPQSILGTD VLCQAKSGLG KTAVFVLSTL QQLDPVPGEI
     STLVICHTRE LAYQIRNEYA RFSKYMPDVK TEVFYGGTPI TRDLEKLKNK DTCPHIVVAT
     PGRLHALVTE KSIRLNNIKS FVIDECDKVL EAVDMRRDVQ DIFRNTPHQK QVMMFSATLS
     QEIRPVCKKF MQNPLEIYVD DEAKLTLHGL QQYYIKLDEK EKNRKLSDLL DSLEFNQVII
     FVRSTQRANE LNKLLCSSNF PSIAVHSGLP QEERIERYKS FKEFNKRICV STDVFGRGID
     IERINLAINY DLPNEADQYL HRVGRAGRFG TKGLAVSLVS TKDDEEVLEK IQSRFDVKIT
     EFPEEGVDPS TYMNT
//

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