ID   SUB2_YARLI              Reviewed;         441 AA.
AC   Q6CH90; Q6CH89;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ATP-dependent RNA helicase SUB2;
DE            EC=3.6.4.13;
GN   Name=SUB2; OrderedLocusNames=YALI0A11157g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., 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 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       (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 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; CR382127; CAG83901.2; -; Genomic_DNA.
DR   RefSeq; XP_499972.2; XM_499972.2.
DR   AlphaFoldDB; Q6CH90; -.
DR   SMR; Q6CH90; -.
DR   STRING; 4952.CAG83901; -.
DR   EnsemblFungi; CAG83901; CAG83901; YALI0_A11157g.
DR   GeneID; 2905851; -.
DR   KEGG; yli:YALI0A11157g; -.
DR   VEuPathDB; FungiDB:YALI0_A11157g; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q6CH90; -.
DR   OMA; IKPICRK; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding; Spliceosome; Transport.
FT   CHAIN           1..441
FT                   /note="ATP-dependent RNA helicase SUB2"
FT                   /id="PRO_0000232267"
FT   DOMAIN          88..263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          275..436
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           57..85
FT                   /note="Q motif"
FT   MOTIF           210..213
FT                   /note="DECD box"
FT   COMPBIAS        17..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   441 AA;  49381 MW;  D427479AD9C16454 CRC64;
     MSHEGEEELL DYSDSEEIAL PSTTVESGSN GDAKAETTTV KEENTEQKGS YVGIHSTGFR
     DFLLKPELLR AIVDCGFEHP SEVQQVCIPQ SILGTDVLCQ AKAGVGKTAV FVLSTLQQLE
     PVPGECSVVV LCHTRELAYQ IMNEYARFSK YLPDVKTAVF YGGSPIQKDI ELIQNKETSP
     HVIVATPGRL HALVRDKHLR LGNVKTFVID ECDKVLDQID MRRDVQEIFR VTPRQKQVMM
     FSATLSQEIR PICKKFMSSP LEILVDDEGK LTLHGLQQYY VDVEEKSKNR KLGDLLDNLE
     FNQVIIFVKS TSRANGLSQV LNANGFPCTA VHSGIPQEER IARYKEFKEF KKRICVSTDV
     FGRGIDIERI NLAINYDLPA EADQYLHRVG RAGRFGTKGL AISFVSTPED KEVLAKIQER
     FEVNIAPYPA EGVDPSTYMN S