SUB2_SCHPO
ID SUB2_SCHPO Reviewed; 434 AA.
AC O13792; P78919;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent RNA helicase uap56;
DE EC=3.6.4.13;
GN Name=uap56; Synonyms=sub2; ORFNames=SPAC17G6.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-434.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP FUNCTION.
RX PubMed=11156603; DOI=10.1101/gad.852101;
RA Libri D., Graziani N., Saguez C., Boulay J.;
RT "Multiple roles for the yeast SUB2/yUAP56 gene in splicing.";
RL Genes Dev. 15:36-41(2001).
RN [4]
RP FUNCTION, INTERACTION WITH MLO3 AND RAE1, AND SUBCELLULAR LOCATION.
RX PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT mRNA export in fission yeast.";
RL EMBO J. 24:2512-2523(2005).
CC -!- FUNCTION: ATP-binding RNA helicase involved in transcription elongation
CC and required for the export of mRNA out of the nucleus. SUB2 also plays
CC a role in pre-mRNA splicing and spliceosome assembly. May be involved
CC in rDNA and telomeric silencing, and maintenance of genome integrity.
CC Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex
CC to the proteins of the nucleoporin complex (NPC).
CC {ECO:0000269|PubMed:11156603, ECO:0000269|PubMed:15990877}.
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 -!- SUBUNIT: Interacts with mlo3 and rae1. {ECO:0000269|PubMed:15990877}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15990877}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16225.1; -; Genomic_DNA.
DR EMBL; D89270; BAA13931.1; -; mRNA.
DR PIR; T37846; T37846.
DR PIR; T43199; T43199.
DR RefSeq; NP_594261.1; NM_001019684.2.
DR AlphaFoldDB; O13792; -.
DR SMR; O13792; -.
DR BioGRID; 278895; 13.
DR IntAct; O13792; 1.
DR STRING; 4896.SPAC17G6.14c.1; -.
DR iPTMnet; O13792; -.
DR MaxQB; O13792; -.
DR PaxDb; O13792; -.
DR PRIDE; O13792; -.
DR EnsemblFungi; SPAC17G6.14c.1; SPAC17G6.14c.1:pep; SPAC17G6.14c.
DR GeneID; 2542433; -.
DR KEGG; spo:SPAC17G6.14c; -.
DR PomBase; SPAC17G6.14c; uap56.
DR VEuPathDB; FungiDB:SPAC17G6.14c; -.
DR eggNOG; KOG0329; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; O13792; -.
DR OMA; IKPICRK; -.
DR PhylomeDB; O13792; -.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR PRO; PR:O13792; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000346; C:transcription export complex; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IGI:PomBase.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISO:PomBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; mRNA transport; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..434
FT /note="ATP-dependent RNA helicase uap56"
FT /id="PRO_0000055081"
FT DOMAIN 82..257
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 269..430
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..79
FT /note="Q motif"
FT MOTIF 204..207
FT /note="DECD box"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 192
FT /note="I -> N (in Ref. 2; BAA13931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 49231 MW; 7DBBC7EDE01FC3DB CRC64;
MASAQEDLID YEEEEELVQD QPAQEITPAA DTAENGEKSD KKGSYVGIHS TGFRDFLLKP
ELLRAITDSG FEHPSEVQQV CIPQSILGTD VLCQAKSGMG KTAVFVLSTL QQIEPVDGEV
SVLVLCHTRE LAFQIKNEYA RFSKYLPDVR TAVFYGGINI KQDMEAFKDK SKSPHIVVAT
PGRLNALVRE KILKVNSVKH FVLDECDKLL ESVDMRRDIQ EVFRATPPQK QVMMFSATLS
NEIRPICKKF MQNPLEIYVD DETKLTLHGL QQHYVKLEEK AKNRKINDLL DSLEFNQVVI
FVKSVSRANE LDRLLRECNF PSICIHGGLP QEERIKRYKA FKDFDKRICV ATDVFGRGID
IERVNIVINY DMPDSPDSYL HRVGRAGRFG TKGLAITFSS SEEDSQILDK IQERFEVNIT
ELPDEIDVGS YMNA
