(data stored in ACNUC9543 zone)

SWISSPROT: YK99_SCHPO

ID   YK99_SCHPO              Reviewed;         647 AA.
AC   Q9HE06;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 117.
DE   RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase C20H4.09;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH-box helicase C20H4.09;
GN   ORFNames=SPAC20H4.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC       spliceosomes after the release of mature mRNA.
CC       {ECO:0000250|UniProtKB:P53131}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000255}.
DR   EMBL; CU329670; CAC19739.1; -; Genomic_DNA.
DR   RefSeq; NP_593629.1; NM_001019060.1.
DR   SMR; Q9HE06; -.
DR   BioGrid; 279319; 16.
DR   STRING; 4896.SPAC20H4.09.1; -.
DR   MaxQB; Q9HE06; -.
DR   PaxDb; Q9HE06; -.
DR   PRIDE; Q9HE06; -.
DR   EnsemblFungi; SPAC20H4.09.1; SPAC20H4.09.1:pep; SPAC20H4.09.
DR   GeneID; 2542874; -.
DR   KEGG; spo:SPAC20H4.09; -.
DR   EuPathDB; FungiDB:SPAC20H4.09; -.
DR   PomBase; SPAC20H4.09; -.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; Q9HE06; -.
DR   KO; K13117; -.
DR   OMA; LEAGWCK; -.
DR   PhylomeDB; Q9HE06; -.
DR   PRO; PR:Q9HE06; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034459; F:ATP-dependent 3'-5' RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0004004; F:ATP-dependent RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9HE06.
DR   SWISS-2DPAGE; Q9HE06.
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    647       Putative pre-mRNA-splicing factor ATP-
FT                                dependent RNA helicase C20H4.09.
FT                                /FTId=PRO_0000055171.
FT   DOMAIN       35    199       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      219    398       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      48     55       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       146    149       DEAH box.
SQ   SEQUENCE   647 AA;  73033 MW;  175C96A560E93969 CRC64;
     MPNEFISQSL STLTNTPLNI QKKLLPITKY RNQLLYAVEQ NQITIVLGHT GCGKTTQIPQ
     FLYEAGWASQ NGIIGCTQPR RLVAKSVSER VSLELNSPPG SLCGYSIQFD HNVSEKTKIK
     YMTDGILLNE IFFDPLLERY SIVILDEVHE RTLSTDLLLG VLKRILEKRN DFRLVLSSAS
     VDANKLSQFF GQDKVCTMSI EGKLFPVETL FLQKPTENYV DSAIETVINI NSTYPPGDIL
     VFLSGRKEIE YCIKKIEDSL IHASEDCQTL VPLPLHAGLT VDEQMRVFNI YDGDFRKVIF
     STNIAETSIT IDGIVYVVDS GFNKQRIYNP YTRTSKLINV PISKSSAIQR SGRAGRTMRG
     KVFRLYTEKA YSLMKEEFEA DILNCDMSPL VLFLKGLGLK NILQFPFFVR PPTVHLMAAL
     EDLYLLGVLD ESGNLTDPLG IQISNSFLDA NISKALLTSN QFGCTHEILS IASILTAGEV
     FYNPTSSSKN DAFVAHSSFF ANEGDIITAL NVFESFVGNK KDLQWCRKNY LNYQTLRQAL
     DIRTHLVRFL NKFSIPTAQR LPSSDCSKIL KCLLDGFVRN VAHLQNDGSY KTIGGKQVWL
     DSSSVLHEKK TPWIMYSSAV ESETQIFVKN ISKIESFWLD KYYKREK
//

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