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Database: UniProt
Entry: N1PYJ1_DOTSN
LinkDB: N1PYJ1_DOTSN
Original site: N1PYJ1_DOTSN 
ID   N1PYJ1_DOTSN            Unreviewed;       461 AA.
AC   N1PYJ1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=ATP-dependent RNA helicase SUB2 {ECO:0000256|ARBA:ARBA00040177};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=ATP-dependent RNA helicase sub2 {ECO:0000256|ARBA:ARBA00040402};
GN   ORFNames=DOTSEDRAFT_67510 {ECO:0000313|EMBL:EME48497.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME48497.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME48497.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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       {ECO:0000256|ARBA:ARBA00037698}.
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         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC       {ECO:0000256|ARBA:ARBA00038213}.
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DR   EMBL; KB446535; EME48497.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1PYJ1; -.
DR   STRING; 675120.N1PYJ1; -.
DR   EnsemblFungi; EME48497; EME48497; DOTSEDRAFT_67510.
DR   eggNOG; KOG0329; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   OMA; PRDHQMI; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; 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:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR   CDD; cd17950; DEADc_DDX39; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF104; ATP-DEPENDENT RNA HELICASE WM6; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT   DOMAIN          61..89
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          92..267
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          295..456
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           61..89
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   461 AA;  50958 MW;  488AF20E39959C26 CRC64;
     MSAGEEDLID YSDEELQPTD GATATGAPGA AANGDAKKGD LSVSGSGAAQ AKGSYVGINS
     ASFRDFLLKP ELLKAITDCG FEHPSEVQQV CIPQAILGTD VLCQAKSGLG KTAVFVLSTL
     QQIEPVAGEA SVLVMCHTRE LAFQIKNEYA RFSKYMPEVK TAVFYGGTDI NKDKALLKDK
     ETHPHIIVAT PGRLNGLVRE KALRLGSVSR FVLDECDKML DQIDMRRDVQ EIFRATPTQK
     QVMMFSATLS QATRPICKKF MQNPLEIYVD DEEKLTLHGL QQYYIKCDEG EKNRKLNDLL
     DTLQYNQVII FVKNTLRCGE LDRLLRECNF PSIAVHSGVS QEERIKRYQA FKNYDKRICV
     STDVFGRGID IERINLAINY DMPESVEKGA DPEAKDALAS SADTYLHRVG RAGRFGTKGV
     AISFVTNDRD KKVIAEIEGR FGKAIDEYPE DGKVDVNGGD Q
//
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